*** 4fdo v/s 4p8l ***
Job options:
ID = 20122614375822011
JOBID = 4fdo v/s 4p8l
USERID = tweety.dec6
PRIVAT = 0
NMODES = 5
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = on
DORMSD = on
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
HEADER 4fdo v/s 4p8l
HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 29-MAY-12 4FDO
TITLE MYCOBACTERIUM TUBERCULOSIS DPRE1 IN COMPLEX WITH CT319
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXIDOREDUCTASE DPRE1;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.-.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: DPRE1, MT3898, RV3790;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ALPHA+BETA, OXIDOREDUCTASE, DECAPRENYLPHOSPHORYL-BETA-D-RIBOSE,
KEYWDS 2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.BATT,G.S.BESRA,K.FUTTERER
REVDAT 2 31-OCT-12 4FDO 1 JRNL
REVDAT 1 04-JUL-12 4FDO 0
JRNL AUTH S.M.BATT,T.JABEEN,V.BHOWRUTH,L.QUILL,P.A.LUND,L.EGGELING,
JRNL AUTH 2 L.J.ALDERWICK,K.FUTTERER,G.S.BESRA
JRNL TITL STRUCTURAL BASIS OF INHIBITION OF MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 2 DPRE1 BY BENZOTHIAZINONE INHIBITORS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 11354 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22733761
JRNL DOI 10.1073/PNAS.1205735109
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.410
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23489
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1206
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.8662 - 4.9957 1.00 2552 134 0.1743 0.1961
REMARK 3 2 4.9957 - 3.9662 1.00 2494 135 0.1353 0.1632
REMARK 3 3 3.9662 - 3.4651 1.00 2508 113 0.1727 0.1982
REMARK 3 4 3.4651 - 3.1484 1.00 2492 122 0.1717 0.2060
REMARK 3 5 3.1484 - 2.9228 1.00 2439 129 0.1646 0.2059
REMARK 3 6 2.9228 - 2.7505 1.00 2444 159 0.1747 0.2485
REMARK 3 7 2.7505 - 2.6128 1.00 2472 136 0.1697 0.2202
REMARK 3 8 2.6128 - 2.4991 1.00 2446 149 0.1921 0.2349
REMARK 3 9 2.4991 - 2.4030 0.99 2436 129 0.1937 0.2477
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 26.35
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40550
REMARK 3 B22 (A**2) : -0.40550
REMARK 3 B33 (A**2) : 0.81110
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 3380
REMARK 3 ANGLE : 1.138 4609
REMARK 3 CHIRALITY : 0.077 512
REMARK 3 PLANARITY : 0.005 590
REMARK 3 DIHEDRAL : 14.067 1193
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: all
REMARK 3 ORIGIN FOR THE GROUP (A): 39.4006 8.9742 4.3822
REMARK 3 T TENSOR
REMARK 3 T11: 0.0684 T22: 0.0552
REMARK 3 T33: 0.0539 T12: 0.0013
REMARK 3 T13: -0.0006 T23: -0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 0.7880 L22: 0.6757
REMARK 3 L33: 0.6115 L12: -0.2259
REMARK 3 L13: -0.0025 L23: -0.0339
REMARK 3 S TENSOR
REMARK 3 S11: 0.0054 S12: -0.0555 S13: 0.0767
REMARK 3 S21: 0.0114 S22: -0.0020 S23: -0.0365
REMARK 3 S31: -0.0774 S32: -0.0289 S33: -0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FDO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072770.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VARIMAX
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23613
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 45.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : 0.08800
REMARK 200 FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.33800
REMARK 200 R SYM FOR SHELL (I) : 0.33800
REMARK 200 FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: DPRE1 - MONOCLINIC CRYSTAL FORM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE, 36% ETHYLENE
REMARK 280 GLYCOL, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 21.39233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 42.78467
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 21.39233
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.78467
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 SER A 3
REMARK 465 VAL A 4
REMARK 465 GLY A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 269
REMARK 465 PRO A 270
REMARK 465 GLN A 271
REMARK 465 LEU A 272
REMARK 465 LEU A 273
REMARK 465 THR A 274
REMARK 465 LEU A 275
REMARK 465 PRO A 276
REMARK 465 ASP A 277
REMARK 465 VAL A 278
REMARK 465 PHE A 279
REMARK 465 PRO A 280
REMARK 465 ASN A 281
REMARK 465 GLY A 282
REMARK 465 LEU A 283
REMARK 465 ALA A 284
REMARK 465 ASN A 285
REMARK 465 LYS A 286
REMARK 465 TYR A 287
REMARK 465 THR A 288
REMARK 465 PHE A 289
REMARK 465 GLY A 290
REMARK 465 PRO A 291
REMARK 465 ILE A 292
REMARK 465 GLY A 293
REMARK 465 GLU A 294
REMARK 465 LEU A 295
REMARK 465 TRP A 296
REMARK 465 TYR A 297
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR A 7 OG1 CG2
REMARK 470 LYS A 37 CE NZ
REMARK 470 ARG A 41 NE CZ NH1 NH2
REMARK 470 GLU A 44 CD OE1 OE2
REMARK 470 GLU A 157 CG CD OE1 OE2
REMARK 470 GLU A 166 CG CD OE1 OE2
REMARK 470 GLU A 254 CG CD OE1 OE2
REMARK 470 LYS A 259 CG CD CE NZ
REMARK 470 LYS A 266 NZ
REMARK 470 ASP A 268 CG OD1 OD2
REMARK 470 ARG A 298 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 299 CG CD CE NZ
REMARK 470 GLU A 342 CG CD OE1 OE2
REMARK 470 LYS A 349 CE NZ
REMARK 470 ARG A 405 NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 1018 O HOH A 1019 1.92
REMARK 500 O HOH A 1045 O HOH A 1090 1.94
REMARK 500 O HOH A 1075 O HOH A 1147 1.95
REMARK 500 O HOH A 1077 O HOH A 1149 2.00
REMARK 500 ND2 ASN A 25 O HOH A 1158 2.10
REMARK 500 O HOH A 1111 O HOH A 1176 2.12
REMARK 500 OE1 GLN A 334 O HOH A 1122 2.14
REMARK 500 OE2 GLU A 221 O HOH A 1029 2.14
REMARK 500 O HOH A 1074 O HOH A 1113 2.17
REMARK 500 OD2 ASP A 167 O HOH A 1187 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 66 87.48 -153.13
REMARK 500 ALA A 343 41.22 -99.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T5 A 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FDN RELATED DB: PDB
REMARK 900 RELATED ID: 4FDP RELATED DB: PDB
DBREF 4FDO A 1 461 UNP P72056 DPRE1_MYCTU 1 461
SEQADV 4FDO MET A -19 UNP P72056 EXPRESSION TAG
SEQADV 4FDO GLY A -18 UNP P72056 EXPRESSION TAG
SEQADV 4FDO SER A -17 UNP P72056 EXPRESSION TAG
SEQADV 4FDO SER A -16 UNP P72056 EXPRESSION TAG
SEQADV 4FDO HIS A -15 UNP P72056 EXPRESSION TAG
SEQADV 4FDO HIS A -14 UNP P72056 EXPRESSION TAG
SEQADV 4FDO HIS A -13 UNP P72056 EXPRESSION TAG
SEQADV 4FDO HIS A -12 UNP P72056 EXPRESSION TAG
SEQADV 4FDO HIS A -11 UNP P72056 EXPRESSION TAG
SEQADV 4FDO HIS A -10 UNP P72056 EXPRESSION TAG
SEQADV 4FDO SER A -9 UNP P72056 EXPRESSION TAG
SEQADV 4FDO SER A -8 UNP P72056 EXPRESSION TAG
SEQADV 4FDO GLY A -7 UNP P72056 EXPRESSION TAG
SEQADV 4FDO LEU A -6 UNP P72056 EXPRESSION TAG
SEQADV 4FDO VAL A -5 UNP P72056 EXPRESSION TAG
SEQADV 4FDO PRO A -4 UNP P72056 EXPRESSION TAG
SEQADV 4FDO ARG A -3 UNP P72056 EXPRESSION TAG
SEQADV 4FDO GLY A -2 UNP P72056 EXPRESSION TAG
SEQADV 4FDO SER A -1 UNP P72056 EXPRESSION TAG
SEQADV 4FDO HIS A 0 UNP P72056 EXPRESSION TAG
SEQRES 1 A 481 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 481 LEU VAL PRO ARG GLY SER HIS MET LEU SER VAL GLY ALA
SEQRES 3 A 481 THR THR THR ALA THR ARG LEU THR GLY TRP GLY ARG THR
SEQRES 4 A 481 ALA PRO SER VAL ALA ASN VAL LEU ARG THR PRO ASP ALA
SEQRES 5 A 481 GLU MET ILE VAL LYS ALA VAL ALA ARG VAL ALA GLU SER
SEQRES 6 A 481 GLY GLY GLY ARG GLY ALA ILE ALA ARG GLY LEU GLY ARG
SEQRES 7 A 481 SER TYR GLY ASP ASN ALA GLN ASN GLY GLY GLY LEU VAL
SEQRES 8 A 481 ILE ASP MET THR PRO LEU ASN THR ILE HIS SER ILE ASP
SEQRES 9 A 481 ALA ASP THR LYS LEU VAL ASP ILE ASP ALA GLY VAL ASN
SEQRES 10 A 481 LEU ASP GLN LEU MET LYS ALA ALA LEU PRO PHE GLY LEU
SEQRES 11 A 481 TRP VAL PRO VAL LEU PRO GLY THR ARG GLN VAL THR VAL
SEQRES 12 A 481 GLY GLY ALA ILE ALA CYS ASP ILE HIS GLY LYS ASN HIS
SEQRES 13 A 481 HIS SER ALA GLY SER PHE GLY ASN HIS VAL ARG SER MET
SEQRES 14 A 481 ASP LEU LEU THR ALA ASP GLY GLU ILE ARG HIS LEU THR
SEQRES 15 A 481 PRO THR GLY GLU ASP ALA GLU LEU PHE TRP ALA THR VAL
SEQRES 16 A 481 GLY GLY ASN GLY LEU THR GLY ILE ILE MET ARG ALA THR
SEQRES 17 A 481 ILE GLU MET THR PRO THR SER THR ALA TYR PHE ILE ALA
SEQRES 18 A 481 ASP GLY ASP VAL THR ALA SER LEU ASP GLU THR ILE ALA
SEQRES 19 A 481 LEU HIS SER ASP GLY SER GLU ALA ARG TYR THR TYR SER
SEQRES 20 A 481 SER ALA TRP PHE ASP ALA ILE SER ALA PRO PRO LYS LEU
SEQRES 21 A 481 GLY ARG ALA ALA VAL SER ARG GLY ARG LEU ALA THR VAL
SEQRES 22 A 481 GLU GLN LEU PRO ALA LYS LEU ARG SER GLU PRO LEU LYS
SEQRES 23 A 481 PHE ASP ALA PRO GLN LEU LEU THR LEU PRO ASP VAL PHE
SEQRES 24 A 481 PRO ASN GLY LEU ALA ASN LYS TYR THR PHE GLY PRO ILE
SEQRES 25 A 481 GLY GLU LEU TRP TYR ARG LYS SER GLY THR TYR ARG GLY
SEQRES 26 A 481 LYS VAL GLN ASN LEU THR GLN PHE TYR HIS PRO LEU ASP
SEQRES 27 A 481 MET PHE GLY GLU TRP ASN ARG ALA TYR GLY PRO ALA GLY
SEQRES 28 A 481 PHE LEU GLN TYR GLN PHE VAL ILE PRO THR GLU ALA VAL
SEQRES 29 A 481 ASP GLU PHE LYS LYS ILE ILE GLY VAL ILE GLN ALA SER
SEQRES 30 A 481 GLY HIS TYR SER PHE LEU ASN VAL PHE LYS LEU PHE GLY
SEQRES 31 A 481 PRO ARG ASN GLN ALA PRO LEU SER PHE PRO ILE PRO GLY
SEQRES 32 A 481 TRP ASN ILE CYS VAL ASP PHE PRO ILE LYS ASP GLY LEU
SEQRES 33 A 481 GLY LYS PHE VAL SER GLU LEU ASP ARG ARG VAL LEU GLU
SEQRES 34 A 481 PHE GLY GLY ARG LEU TYR THR ALA LYS ASP SER ARG THR
SEQRES 35 A 481 THR ALA GLU THR PHE HIS ALA MET TYR PRO ARG VAL ASP
SEQRES 36 A 481 GLU TRP ILE SER VAL ARG ARG LYS VAL ASP PRO LEU ARG
SEQRES 37 A 481 VAL PHE ALA SER ASP MET ALA ARG ARG LEU GLU LEU LEU
HET FAD A 900 53
HET 0T5 A 901 24
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM 0T5 3-NITRO-N-[(1R)-1-PHENYLETHYL]-5-(TRIFLUOROMETHYL)
HETNAM 2 0T5 BENZAMIDE
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 0T5 C16 H13 F3 N2 O3
FORMUL 4 HOH *194(H2 O)
HELIX 1 1 ASP A 31 SER A 45 1 15
HELIX 2 2 ASN A 97 LEU A 106 1 10
HELIX 3 3 THR A 122 CYS A 129 1 8
HELIX 4 4 ASN A 135 GLY A 140 1 6
HELIX 5 5 SER A 141 ASN A 144 5 4
HELIX 6 6 ASP A 167 VAL A 175 1 9
HELIX 7 7 SER A 208 HIS A 216 1 9
HELIX 8 8 GLY A 219 TYR A 224 5 6
HELIX 9 9 THR A 252 LEU A 256 5 5
HELIX 10 10 PRO A 257 SER A 262 5 6
HELIX 11 11 LEU A 310 HIS A 315 1 6
HELIX 12 12 GLU A 322 GLY A 328 1 7
HELIX 13 13 ALA A 343 SER A 357 1 15
HELIX 14 14 GLY A 395 PHE A 410 1 16
HELIX 15 15 THR A 416 ASP A 419 5 4
HELIX 16 16 THR A 423 TYR A 431 1 9
HELIX 17 17 ARG A 433 ASP A 445 1 13
HELIX 18 18 SER A 452 LEU A 458 1 7
SHEET 1 A 4 THR A 8 LEU A 13 0
SHEET 2 A 4 SER A 22 LEU A 27 -1 O SER A 22 N LEU A 13
SHEET 3 A 4 LEU A 70 ASP A 73 1 O VAL A 71 N ASN A 25
SHEET 4 A 4 ALA A 51 ARG A 54 1 N ILE A 52 O ILE A 72
SHEET 1 B 5 ILE A 80 ILE A 83 0
SHEET 2 B 5 LEU A 89 ASP A 93 -1 O ASP A 91 N SER A 82
SHEET 3 B 5 ILE A 183 GLU A 190 -1 O ALA A 187 N ILE A 92
SHEET 4 B 5 VAL A 146 LEU A 152 -1 N LEU A 152 O ILE A 183
SHEET 5 B 5 ILE A 158 LEU A 161 -1 O LEU A 161 N MET A 149
SHEET 1 C 2 LEU A 110 TRP A 111 0
SHEET 2 C 2 THR A 192 PRO A 193 -1 O THR A 192 N TRP A 111
SHEET 1 D 8 TYR A 303 ASN A 309 0
SHEET 2 D 8 TYR A 198 VAL A 205 -1 N PHE A 199 O GLN A 308
SHEET 3 D 8 ALA A 243 LEU A 250 -1 O ARG A 247 N ASP A 202
SHEET 4 D 8 TYR A 226 PHE A 231 -1 N TRP A 230 O ALA A 244
SHEET 5 D 8 VAL A 365 PHE A 369 -1 O PHE A 366 N ALA A 229
SHEET 6 D 8 GLY A 383 PRO A 391 -1 O ASN A 385 N LYS A 367
SHEET 7 D 8 PHE A 332 PRO A 340 -1 N LEU A 333 O PHE A 390
SHEET 8 D 8 ARG A 413 LEU A 414 -1 O ARG A 413 N VAL A 338
CISPEP 1 PRO A 237 PRO A 238 0 6.05
CISPEP 2 HIS A 315 PRO A 316 0 7.82
CISPEP 3 GLY A 328 PRO A 329 0 3.55
SITE 1 AC1 33 TRP A 16 ILE A 52 ALA A 53 ARG A 54
SITE 2 AC1 33 GLY A 55 LEU A 56 GLY A 57 ARG A 58
SITE 3 AC1 33 SER A 59 TYR A 60 ASN A 63 ALA A 64
SITE 4 AC1 33 MET A 74 ALA A 94 PRO A 116 GLY A 117
SITE 5 AC1 33 THR A 118 VAL A 121 THR A 122 GLY A 124
SITE 6 AC1 33 GLY A 125 ALA A 128 CYS A 129 ILE A 131
SITE 7 AC1 33 HIS A 132 ASN A 178 GLY A 179 GLY A 182
SITE 8 AC1 33 ILE A 184 TYR A 415 ALA A 417 0T5 A 901
SITE 9 AC1 33 HOH A1009
SITE 1 AC2 11 TYR A 60 GLY A 117 HIS A 132 GLY A 133
SITE 2 AC2 11 LYS A 134 LEU A 317 PHE A 320 GLN A 336
SITE 3 AC2 11 ASN A 385 CYS A 387 FAD A 900
CRYST1 127.884 127.884 64.177 90.00 90.00 120.00 P 64 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007820 0.004515 0.000000 0.00000
SCALE2 0.000000 0.009029 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015582 0.00000
ATOM 1 N THR A 7 38.491 -22.938 2.928 1.00 50.91 N
ANISOU 1 N THR A 7 6700 5539 7105 -183 -69 61 N
ATOM 2 CA THR A 7 39.075 -21.689 2.433 1.00 55.97 C
ANISOU 2 CA THR A 7 7331 6237 7696 -151 -76 26 C
ATOM 3 C THR A 7 38.417 -20.425 3.042 1.00 57.47 C
ANISOU 3 C THR A 7 7484 6519 7834 -174 -67 54 C
ATOM 4 O THR A 7 39.117 -19.547 3.570 1.00 63.98 O
ANISOU 4 O THR A 7 8299 7407 8603 -141 -55 78 O
ATOM 5 CB THR A 7 39.067 -21.629 0.880 1.00 26.46 C
ANISOU 5 CB THR A 7 3611 2497 3948 -143 -99 -67 C
ATOM 6 N THR A 8 37.083 -20.341 2.988 1.00 46.32 N
ANISOU 6 N THR A 8 6049 5111 6441 -228 -73 50 N
ATOM 7 CA THR A 8 36.357 -19.175 3.525 1.00 38.46 C
ANISOU 7 CA THR A 8 5016 4198 5399 -247 -62 72 C
ATOM 8 C THR A 8 35.607 -19.403 4.858 1.00 30.82 C
ANISOU 8 C THR A 8 4026 3234 4450 -280 -37 151 C
ATOM 9 O THR A 8 35.239 -20.523 5.198 1.00 26.89 O
ANISOU 9 O THR A 8 3534 2668 4015 -309 -31 184 O
ATOM 10 CB THR A 8 35.383 -18.554 2.479 1.00 35.56 C
ANISOU 10 CB THR A 8 4629 3860 5021 -274 -86 10 C
ATOM 11 OG1 THR A 8 34.243 -19.397 2.302 1.00 39.95 O
ANISOU 11 OG1 THR A 8 5172 4365 5644 -329 -98 3 O
ATOM 12 CG2 THR A 8 36.074 -18.364 1.133 1.00 35.65 C
ANISOU 12 CG2 THR A 8 4667 3870 5009 -240 -108 -64 C
ATOM 13 N THR A 9 35.382 -18.314 5.592 1.00 25.05 N
ANISOU 13 N THR A 9 3270 2584 3664 -275 -21 180 N
ATOM 14 CA THR A 9 34.652 -18.330 6.861 1.00 23.65 C
ANISOU 14 CA THR A 9 3069 2429 3487 -300 9 251 C
ATOM 15 C THR A 9 33.463 -17.355 6.835 1.00 29.96 C
ANISOU 15 C THR A 9 3827 3292 4264 -328 13 238 C
ATOM 16 O THR A 9 33.650 -16.142 6.650 1.00 21.98 O
ANISOU 16 O THR A 9 2810 2348 3195 -303 8 209 O
ATOM 17 CB THR A 9 35.569 -17.922 8.030 1.00 22.12 C
ANISOU 17 CB THR A 9 2887 2280 3239 -257 28 305 C
ATOM 18 OG1 THR A 9 36.652 -18.849 8.131 1.00 33.91 O
ANISOU 18 OG1 THR A 9 4413 3715 4754 -226 24 325 O
ATOM 19 CG2 THR A 9 34.800 -17.910 9.332 1.00 26.07 C
ANISOU 19 CG2 THR A 9 3366 2810 3728 -277 62 379 C
ATOM 20 N ALA A 10 32.252 -17.884 7.022 1.00 23.35 N
ANISOU 20 N ALA A 10 2960 2434 3478 -380 23 260 N
ATOM 21 CA ALA A 10 31.056 -17.051 7.102 1.00 19.15 C
ANISOU 21 CA ALA A 10 2381 1962 2931 -406 32 256 C
ATOM 22 C ALA A 10 31.194 -16.180 8.331 1.00 20.17 C
ANISOU 22 C ALA A 10 2503 2165 2995 -378 65 306 C
ATOM 23 O ALA A 10 31.540 -16.660 9.402 1.00 21.53 O
ANISOU 23 O ALA A 10 2689 2331 3162 -370 92 371 O
ATOM 24 CB ALA A 10 29.766 -17.904 7.170 1.00 11.64 C
ANISOU 24 CB ALA A 10 1394 972 2056 -470 40 278 C
ATOM 25 N THR A 11 30.936 -14.891 8.165 1.00 19.09 N
ANISOU 25 N THR A 11 2347 2098 2806 -361 62 274 N
ATOM 26 CA THR A 11 31.259 -13.923 9.193 1.00 14.25 C
ANISOU 26 CA THR A 11 1736 1554 2123 -326 86 303 C
ATOM 27 C THR A 11 30.313 -12.746 9.104 1.00 17.29 C
ANISOU 27 C THR A 11 2084 2006 2480 -327 91 279 C
ATOM 28 O THR A 11 30.083 -12.198 8.014 1.00 16.01 O
ANISOU 28 O THR A 11 1913 1849 2320 -327 63 221 O
ATOM 29 CB THR A 11 32.710 -13.398 9.019 1.00 23.92 C
ANISOU 29 CB THR A 11 2999 2788 3300 -276 67 277 C
ATOM 30 OG1 THR A 11 33.602 -14.502 8.826 1.00 23.69 O
ANISOU 30 OG1 THR A 11 3002 2694 3305 -270 56 287 O
ATOM 31 CG2 THR A 11 33.157 -12.589 10.238 1.00 16.86 C
ANISOU 31 CG2 THR A 11 2111 1957 2339 -242 88 310 C
ATOM 32 N ARG A 12 29.761 -12.379 10.259 1.00 16.04 N
ANISOU 32 N ARG A 12 1905 1897 2293 -325 128 326 N
ATOM 33 CA ARG A 12 28.977 -11.161 10.425 1.00 17.51 C
ANISOU 33 CA ARG A 12 2059 2152 2443 -314 140 309 C
ATOM 34 C ARG A 12 29.923 -9.959 10.330 1.00 18.11 C
ANISOU 34 C ARG A 12 2163 2263 2453 -266 124 270 C
ATOM 35 O ARG A 12 30.876 -9.860 11.103 1.00 14.83 O
ANISOU 35 O ARG A 12 1778 1859 1997 -237 130 291 O
ATOM 36 CB ARG A 12 28.272 -11.181 11.791 1.00 10.02 C
ANISOU 36 CB ARG A 12 1086 1246 1474 -319 190 372 C
ATOM 37 CG ARG A 12 27.363 -9.988 12.055 1.00 19.77 C
ANISOU 37 CG ARG A 12 2285 2552 2675 -304 209 357 C
ATOM 38 CD ARG A 12 26.739 -10.062 13.452 1.00 19.21 C
ANISOU 38 CD ARG A 12 2193 2527 2578 -303 265 421 C
ATOM 39 NE ARG A 12 25.752 -9.004 13.696 1.00 20.65 N
ANISOU 39 NE ARG A 12 2335 2776 2735 -289 288 406 N
ATOM 40 CZ ARG A 12 26.053 -7.808 14.204 1.00 24.00 C
ANISOU 40 CZ ARG A 12 2776 3255 3088 -241 295 384 C
ATOM 41 NH1 ARG A 12 27.312 -7.515 14.510 1.00 14.85 N
ANISOU 41 NH1 ARG A 12 1670 2094 1879 -207 277 373 N
ATOM 42 NH2 ARG A 12 25.103 -6.896 14.402 1.00 18.38 N
ANISOU 42 NH2 ARG A 12 2027 2598 2359 -225 317 370 N
ATOM 43 N LEU A 13 29.676 -9.064 9.373 1.00 17.16 N
ANISOU 43 N LEU A 13 2034 2159 2327 -257 100 215 N
ATOM 44 CA LEU A 13 30.485 -7.855 9.226 1.00 12.90 C
ANISOU 44 CA LEU A 13 1518 1649 1735 -216 87 180 C
ATOM 45 C LEU A 13 29.681 -6.575 9.474 1.00 20.85 C
ANISOU 45 C LEU A 13 2500 2713 2710 -199 100 164 C
ATOM 46 O LEU A 13 28.486 -6.493 9.158 1.00 19.20 O
ANISOU 46 O LEU A 13 2251 2518 2526 -217 104 160 O
ATOM 47 CB LEU A 13 31.140 -7.795 7.840 1.00 16.41 C
ANISOU 47 CB LEU A 13 1983 2059 2193 -211 49 130 C
ATOM 48 CG LEU A 13 32.078 -8.952 7.451 1.00 18.86 C
ANISOU 48 CG LEU A 13 2323 2311 2533 -218 35 133 C
ATOM 49 CD1 LEU A 13 32.554 -8.842 5.982 1.00 14.12 C
ANISOU 49 CD1 LEU A 13 1740 1684 1941 -211 2 80 C
ATOM 50 CD2 LEU A 13 33.279 -9.036 8.416 1.00 17.18 C
ANISOU 50 CD2 LEU A 13 2138 2101 2288 -192 45 163 C
ATOM 51 N THR A 14 30.354 -5.576 10.041 1.00 13.34 N
ANISOU 51 N THR A 14 1570 1794 1705 -163 104 155 N
ATOM 52 CA THR A 14 29.815 -4.231 10.153 1.00 18.07 C
ANISOU 52 CA THR A 14 2156 2438 2273 -138 111 129 C
ATOM 53 C THR A 14 30.913 -3.223 9.813 1.00 20.50 C
ANISOU 53 C THR A 14 2498 2744 2550 -108 89 92 C
ATOM 54 O THR A 14 32.097 -3.566 9.775 1.00 17.95 O
ANISOU 54 O THR A 14 2203 2396 2221 -105 74 92 O
ATOM 55 CB THR A 14 29.338 -3.914 11.587 1.00 15.35 C
ANISOU 55 CB THR A 14 1800 2143 1890 -123 149 160 C
ATOM 56 OG1 THR A 14 30.454 -3.980 12.484 1.00 20.14 O
ANISOU 56 OG1 THR A 14 2443 2755 2456 -105 151 175 O
ATOM 57 CG2 THR A 14 28.271 -4.896 12.057 1.00 15.93 C
ANISOU 57 CG2 THR A 14 1837 2222 1995 -154 181 207 C
ATOM 58 N GLY A 15 30.515 -1.976 9.576 1.00 23.75 N
ANISOU 58 N GLY A 15 2902 3178 2943 -87 87 61 N
ATOM 59 CA GLY A 15 31.455 -0.874 9.556 1.00 22.44 C
ANISOU 59 CA GLY A 15 2766 3015 2747 -59 74 32 C
ATOM 60 C GLY A 15 32.044 -0.634 10.940 1.00 19.19 C
ANISOU 60 C GLY A 15 2371 2628 2291 -41 88 44 C
ATOM 61 O GLY A 15 31.701 -1.310 11.906 1.00 18.33 O
ANISOU 61 O GLY A 15 2254 2540 2171 -47 111 79 O
ATOM 62 N TRP A 16 32.918 0.355 11.035 1.00 20.53 N
ANISOU 62 N TRP A 16 2565 2799 2437 -21 74 14 N
ATOM 63 CA TRP A 16 33.634 0.651 12.267 1.00 17.68 C
ANISOU 63 CA TRP A 16 2223 2461 2032 -3 77 15 C
ATOM 64 C TRP A 16 32.735 0.861 13.481 1.00 23.09 C
ANISOU 64 C TRP A 16 2898 3194 2680 13 107 29 C
ATOM 65 O TRP A 16 33.027 0.350 14.565 1.00 29.70 O
ANISOU 65 O TRP A 16 3745 4056 3484 18 118 55 O
ATOM 66 CB TRP A 16 34.504 1.884 12.072 1.00 18.18 C
ANISOU 66 CB TRP A 16 2307 2516 2085 13 56 -27 C
ATOM 67 CG TRP A 16 35.385 2.199 13.262 1.00 22.98 C
ANISOU 67 CG TRP A 16 2935 3146 2651 29 47 -35 C
ATOM 68 CD1 TRP A 16 35.308 3.298 14.078 1.00 15.96 C
ANISOU 68 CD1 TRP A 16 2057 2282 1724 53 49 -66 C
ATOM 69 CD2 TRP A 16 36.468 1.403 13.761 1.00 20.08 C
ANISOU 69 CD2 TRP A 16 2579 2778 2274 25 32 -14 C
ATOM 70 NE1 TRP A 16 36.286 3.235 15.041 1.00 27.44 N
ANISOU 70 NE1 TRP A 16 3529 3754 3144 61 32 -69 N
ATOM 71 CE2 TRP A 16 37.008 2.082 14.871 1.00 23.97 C
ANISOU 71 CE2 TRP A 16 3087 3301 2720 45 21 -35 C
ATOM 72 CE3 TRP A 16 37.034 0.180 13.376 1.00 22.65 C
ANISOU 72 CE3 TRP A 16 2902 3079 2625 8 25 17 C
ATOM 73 CZ2 TRP A 16 38.085 1.581 15.598 1.00 30.02 C
ANISOU 73 CZ2 TRP A 16 3864 4078 3464 49 1 -22 C
ATOM 74 CZ3 TRP A 16 38.098 -0.325 14.107 1.00 25.76 C
ANISOU 74 CZ3 TRP A 16 3306 3480 2999 15 8 33 C
ATOM 75 CH2 TRP A 16 38.613 0.377 15.205 1.00 30.30 C
ANISOU 75 CH2 TRP A 16 3895 4091 3527 36 -5 15 C
ATOM 76 N GLY A 17 31.660 1.623 13.299 1.00 14.30 N
ANISOU 76 N GLY A 17 1766 2098 1570 25 123 11 N
ATOM 77 CA GLY A 17 30.750 1.918 14.385 1.00 25.26 C
ANISOU 77 CA GLY A 17 3141 3534 2921 46 157 20 C
ATOM 78 C GLY A 17 29.691 0.844 14.573 1.00 31.39 C
ANISOU 78 C GLY A 17 3882 4327 3716 25 189 68 C
ATOM 79 O GLY A 17 28.648 1.100 15.189 1.00 26.92 O
ANISOU 79 O GLY A 17 3292 3803 3134 39 224 77 O
ATOM 80 N ARG A 18 29.954 -0.338 14.010 1.00 25.48 N
ANISOU 80 N ARG A 18 3129 3545 3007 -9 178 97 N
ATOM 81 CA ARG A 18 29.187 -1.556 14.288 1.00 27.15 C
ANISOU 81 CA ARG A 18 3313 3761 3243 -37 205 149 C
ATOM 82 C ARG A 18 27.740 -1.527 13.785 1.00 29.91 C
ANISOU 82 C ARG A 18 3613 4123 3630 -50 223 151 C
ATOM 83 O ARG A 18 26.867 -2.200 14.330 1.00 28.93 O
ANISOU 83 O ARG A 18 3456 4019 3517 -66 258 193 O
ATOM 84 CB ARG A 18 29.207 -1.888 15.785 1.00 27.55 C
ANISOU 84 CB ARG A 18 3373 3854 3243 -23 239 189 C
ATOM 85 CG ARG A 18 30.600 -2.065 16.403 1.00 28.88 C
ANISOU 85 CG ARG A 18 3585 4017 3371 -9 218 194 C
ATOM 86 CD ARG A 18 30.425 -2.520 17.848 1.00 34.82 C
ANISOU 86 CD ARG A 18 4343 4815 4070 5 254 243 C
ATOM 87 NE ARG A 18 31.651 -2.477 18.643 1.00 41.48 N
ANISOU 87 NE ARG A 18 5228 5671 4862 28 233 242 N
ATOM 88 CZ ARG A 18 32.600 -3.407 18.615 1.00 41.54 C
ANISOU 88 CZ ARG A 18 5254 5648 4882 18 211 272 C
ATOM 89 NH1 ARG A 18 32.493 -4.452 17.802 1.00 39.49 N
ANISOU 89 NH1 ARG A 18 4981 5338 4687 -17 208 300 N
ATOM 90 NH2 ARG A 18 33.669 -3.281 19.389 1.00 43.11 N
ANISOU 90 NH2 ARG A 18 5484 5866 5029 43 189 270 N
ATOM 91 N THR A 19 27.487 -0.751 12.742 1.00 26.70 N
ANISOU 91 N THR A 19 3197 3703 3245 -43 199 110 N
ATOM 92 CA THR A 19 26.137 -0.654 12.218 1.00 31.29 C
ANISOU 92 CA THR A 19 3727 4299 3861 -51 209 108 C
ATOM 93 C THR A 19 25.936 -1.468 10.919 1.00 24.86 C
ANISOU 93 C THR A 19 2896 3444 3107 -89 178 106 C
ATOM 94 O THR A 19 26.902 -1.927 10.293 1.00 26.27 O
ANISOU 94 O THR A 19 3107 3580 3296 -103 148 97 O
ATOM 95 CB THR A 19 25.750 0.825 12.007 1.00 38.97 C
ANISOU 95 CB THR A 19 4698 5295 4816 -10 206 66 C
ATOM 96 OG1 THR A 19 24.391 0.899 11.564 1.00 55.58 O
ANISOU 96 OG1 THR A 19 6745 7419 6954 -13 216 68 O
ATOM 97 CG2 THR A 19 26.648 1.463 10.973 1.00 25.69 C
ANISOU 97 CG2 THR A 19 3051 3573 3137 -1 164 27 C
ATOM 98 N ALA A 20 24.676 -1.649 10.538 1.00 21.19 N
ANISOU 98 N ALA A 20 2377 2993 2680 -105 184 112 N
ATOM 99 CA ALA A 20 24.310 -2.343 9.300 1.00 25.54 C
ANISOU 99 CA ALA A 20 2906 3511 3286 -140 150 101 C
ATOM 100 C ALA A 20 25.054 -3.674 9.050 1.00 23.50 C
ANISOU 100 C ALA A 20 2672 3201 3055 -179 134 118 C
ATOM 101 O ALA A 20 25.796 -3.809 8.080 1.00 18.41 O
ANISOU 101 O ALA A 20 2058 2518 2417 -182 97 90 O
ATOM 102 CB ALA A 20 24.455 -1.404 8.108 1.00 20.92 C
ANISOU 102 CB ALA A 20 2335 2918 2697 -116 110 54 C
ATOM 103 N PRO A 21 24.835 -4.667 9.919 1.00 20.18 N
ANISOU 103 N PRO A 21 2238 2779 2651 -207 166 166 N
ATOM 104 CA PRO A 21 25.496 -5.968 9.767 1.00 15.04 C
ANISOU 104 CA PRO A 21 1610 2074 2031 -241 154 186 C
ATOM 105 C PRO A 21 24.986 -6.774 8.560 1.00 20.14 C
ANISOU 105 C PRO A 21 2232 2678 2742 -282 120 166 C
ATOM 106 O PRO A 21 23.810 -6.731 8.232 1.00 21.33 O
ANISOU 106 O PRO A 21 2330 2848 2927 -300 118 161 O
ATOM 107 CB PRO A 21 25.111 -6.698 11.056 1.00 14.22 C
ANISOU 107 CB PRO A 21 1489 1985 1930 -258 203 249 C
ATOM 108 CG PRO A 21 23.780 -6.108 11.447 1.00 14.23 C
ANISOU 108 CG PRO A 21 1433 2042 1932 -254 235 257 C
ATOM 109 CD PRO A 21 23.840 -4.660 11.012 1.00 21.62 C
ANISOU 109 CD PRO A 21 2377 3008 2829 -208 216 205 C
ATOM 110 N SER A 22 25.878 -7.493 7.894 1.00 20.92 N
ANISOU 110 N SER A 22 2370 2723 2858 -293 90 151 N
ATOM 111 CA SER A 22 25.460 -8.535 6.964 1.00 19.23 C
ANISOU 111 CA SER A 22 2139 2462 2707 -337 61 137 C
ATOM 112 C SER A 22 26.517 -9.638 6.992 1.00 19.58 C
ANISOU 112 C SER A 22 2228 2444 2767 -349 55 150 C
ATOM 113 O SER A 22 27.620 -9.424 7.486 1.00 20.17 O
ANISOU 113 O SER A 22 2345 2518 2799 -318 64 161 O
ATOM 114 CB SER A 22 25.220 -7.988 5.548 1.00 12.15 C
ANISOU 114 CB SER A 22 1237 1566 1812 -328 14 77 C
ATOM 115 OG SER A 22 26.443 -7.589 4.958 1.00 19.85 O
ANISOU 115 OG SER A 22 2268 2526 2749 -295 -7 47 O
ATOM 116 N VAL A 23 26.169 -10.823 6.495 1.00 18.56 N
ANISOU 116 N VAL A 23 2088 2262 2702 -393 39 149 N
ATOM 117 CA VAL A 23 27.052 -11.980 6.573 1.00 15.72 C
ANISOU 117 CA VAL A 23 1768 1837 2368 -405 36 166 C
ATOM 118 C VAL A 23 27.684 -12.286 5.223 1.00 19.70 C
ANISOU 118 C VAL A 23 2306 2296 2884 -400 -10 106 C
ATOM 119 O VAL A 23 26.991 -12.383 4.207 1.00 20.90 O
ANISOU 119 O VAL A 23 2436 2439 3065 -421 -44 63 O
ATOM 120 CB VAL A 23 26.288 -13.252 7.061 1.00 20.09 C
ANISOU 120 CB VAL A 23 2293 2348 2993 -460 56 212 C
ATOM 121 CG1 VAL A 23 27.212 -14.465 7.058 1.00 14.85 C
ANISOU 121 CG1 VAL A 23 1674 1606 2361 -468 50 227 C
ATOM 122 CG2 VAL A 23 25.685 -13.027 8.441 1.00 13.84 C
ANISOU 122 CG2 VAL A 23 1470 1604 2186 -463 110 279 C
ATOM 123 N ALA A 24 29.003 -12.442 5.211 1.00 16.21 N
ANISOU 123 N ALA A 24 1914 1828 2416 -369 -13 104 N
ATOM 124 CA ALA A 24 29.704 -12.778 3.981 1.00 14.11 C
ANISOU 124 CA ALA A 24 1682 1521 2157 -359 -50 50 C
ATOM 125 C ALA A 24 30.613 -13.968 4.218 1.00 19.57 C
ANISOU 125 C ALA A 24 2411 2146 2878 -360 -45 70 C
ATOM 126 O ALA A 24 31.014 -14.234 5.351 1.00 18.50 O
ANISOU 126 O ALA A 24 2282 2008 2737 -353 -15 126 O
ATOM 127 CB ALA A 24 30.528 -11.581 3.485 1.00 11.44 C
ANISOU 127 CB ALA A 24 1369 1223 1754 -310 -59 17 C
ATOM 128 N ASN A 25 30.934 -14.686 3.146 1.00 16.42 N
ANISOU 128 N ASN A 25 2036 1693 2508 -364 -76 23 N
ATOM 129 CA ASN A 25 32.057 -15.617 3.186 1.00 25.37 C
ANISOU 129 CA ASN A 25 3212 2767 3659 -347 -74 31 C
ATOM 130 C ASN A 25 33.353 -14.821 3.107 1.00 17.62 C
ANISOU 130 C ASN A 25 2260 1819 2616 -292 -70 21 C
ATOM 131 O ASN A 25 33.585 -14.121 2.136 1.00 22.93 O
ANISOU 131 O ASN A 25 2941 2517 3256 -271 -88 -29 O
ATOM 132 CB ASN A 25 31.983 -16.612 2.028 1.00 22.54 C
ANISOU 132 CB ASN A 25 2872 2341 3350 -365 -107 -24 C
ATOM 133 CG ASN A 25 30.678 -17.370 2.011 1.00 35.28 C
ANISOU 133 CG ASN A 25 4452 3920 5033 -426 -118 -22 C
ATOM 134 OD1 ASN A 25 29.906 -17.270 1.054 1.00 42.75 O
ANISOU 134 OD1 ASN A 25 5379 4871 5991 -448 -152 -76 O
ATOM 135 ND2 ASN A 25 30.405 -18.108 3.084 1.00 30.62 N
ANISOU 135 ND2 ASN A 25 3849 3297 4487 -455 -89 43 N
ATOM 136 N VAL A 26 34.182 -14.914 4.136 1.00 19.68 N
ANISOU 136 N VAL A 26 2534 2081 2862 -269 -46 70 N
ATOM 137 CA VAL A 26 35.430 -14.162 4.169 1.00 18.14 C
ANISOU 137 CA VAL A 26 2359 1919 2615 -221 -43 63 C
ATOM 138 C VAL A 26 36.607 -15.049 3.780 1.00 25.36 C
ANISOU 138 C VAL A 26 3307 2779 3550 -195 -49 53 C
ATOM 139 O VAL A 26 36.842 -16.099 4.387 1.00 24.08 O
ANISOU 139 O VAL A 26 3157 2568 3425 -199 -41 91 O
ATOM 140 CB VAL A 26 35.688 -13.536 5.558 1.00 19.12 C
ANISOU 140 CB VAL A 26 2473 2091 2699 -206 -18 118 C
ATOM 141 CG1 VAL A 26 37.092 -12.904 5.623 1.00 17.40 C
ANISOU 141 CG1 VAL A 26 2273 1898 2440 -161 -20 110 C
ATOM 142 CG2 VAL A 26 34.608 -12.506 5.887 1.00 18.89 C
ANISOU 142 CG2 VAL A 26 2412 2121 2644 -222 -9 120 C
ATOM 143 N LEU A 27 37.322 -14.642 2.738 1.00 24.86 N
ANISOU 143 N LEU A 27 3261 2723 3464 -166 -62 3 N
ATOM 144 CA LEU A 27 38.577 -15.287 2.402 1.00 21.62 C
ANISOU 144 CA LEU A 27 2878 2274 3063 -131 -63 -8 C
ATOM 145 C LEU A 27 39.686 -14.505 3.074 1.00 26.03 C
ANISOU 145 C LEU A 27 3433 2879 3580 -94 -50 19 C
ATOM 146 O LEU A 27 39.753 -13.272 2.975 1.00 21.78 O
ANISOU 146 O LEU A 27 2881 2397 2997 -87 -48 7 O
ATOM 147 CB LEU A 27 38.801 -15.323 0.898 1.00 19.25 C
ANISOU 147 CB LEU A 27 2597 1960 2759 -117 -79 -76 C
ATOM 148 CG LEU A 27 40.150 -15.893 0.433 1.00 25.00 C
ANISOU 148 CG LEU A 27 3351 2656 3493 -73 -75 -93 C
ATOM 149 CD1 LEU A 27 40.293 -17.369 0.796 1.00 15.78 C
ANISOU 149 CD1 LEU A 27 2202 1410 2385 -75 -76 -74 C
ATOM 150 CD2 LEU A 27 40.316 -15.687 -1.068 1.00 23.94 C
ANISOU 150 CD2 LEU A 27 3234 2525 3337 -55 -86 -160 C
ATOM 151 N ARG A 28 40.544 -15.228 3.779 1.00 25.62 N
ANISOU 151 N ARG A 28 3391 2799 3544 -72 -43 55 N
ATOM 152 CA ARG A 28 41.665 -14.619 4.466 1.00 22.02 C
ANISOU 152 CA ARG A 28 2929 2385 3055 -37 -36 79 C
ATOM 153 C ARG A 28 42.929 -15.439 4.205 1.00 26.56 C
ANISOU 153 C ARG A 28 3519 2919 3652 3 -38 77 C
ATOM 154 O ARG A 28 43.229 -16.382 4.935 1.00 32.91 O
ANISOU 154 O ARG A 28 4333 3688 4485 13 -36 119 O
ATOM 155 CB ARG A 28 41.379 -14.538 5.966 1.00 21.27 C
ANISOU 155 CB ARG A 28 2822 2314 2945 -46 -28 141 C
ATOM 156 CG ARG A 28 42.474 -13.826 6.723 1.00 29.27 C
ANISOU 156 CG ARG A 28 3826 3376 3918 -13 -29 161 C
ATOM 157 CD ARG A 28 42.244 -13.751 8.228 1.00 29.31 C
ANISOU 157 CD ARG A 28 3825 3412 3899 -15 -23 219 C
ATOM 158 NE ARG A 28 43.517 -13.478 8.890 1.00 44.37 N
ANISOU 158 NE ARG A 28 5729 5351 5781 23 -32 236 N
ATOM 159 CZ ARG A 28 44.083 -12.276 8.957 1.00 52.83 C
ANISOU 159 CZ ARG A 28 6784 6476 6814 35 -40 212 C
ATOM 160 NH1 ARG A 28 43.476 -11.223 8.420 1.00 49.26 N
ANISOU 160 NH1 ARG A 28 6324 6051 6343 14 -37 174 N
ATOM 161 NH2 ARG A 28 45.255 -12.124 9.564 1.00 54.13 N
ANISOU 161 NH2 ARG A 28 6941 6665 6962 67 -54 227 N
ATOM 162 N THR A 29 43.665 -15.094 3.157 1.00 24.57 N
ANISOU 162 N THR A 29 3270 2675 3389 28 -38 31 N
ATOM 163 CA THR A 29 44.898 -15.814 2.844 1.00 29.22 C
ANISOU 163 CA THR A 29 3870 3232 3999 72 -35 25 C
ATOM 164 C THR A 29 46.022 -14.867 2.458 1.00 28.12 C
ANISOU 164 C THR A 29 3713 3142 3827 103 -28 7 C
ATOM 165 O THR A 29 45.781 -13.856 1.809 1.00 29.18 O
ANISOU 165 O THR A 29 3841 3316 3931 92 -25 -23 O
ATOM 166 CB THR A 29 44.702 -16.856 1.702 1.00 20.12 C
ANISOU 166 CB THR A 29 2747 2014 2885 75 -38 -21 C
ATOM 167 OG1 THR A 29 45.976 -17.383 1.333 1.00 26.99 O
ANISOU 167 OG1 THR A 29 3624 2863 3770 126 -31 -32 O
ATOM 168 CG2 THR A 29 44.084 -16.210 0.469 1.00 20.63 C
ANISOU 168 CG2 THR A 29 2815 2099 2923 59 -42 -79 C
ATOM 169 N PRO A 30 47.262 -15.198 2.846 1.00 29.05 N
ANISOU 169 N PRO A 30 3822 3259 3957 143 -25 27 N
ATOM 170 CA PRO A 30 48.408 -14.393 2.406 1.00 28.05 C
ANISOU 170 CA PRO A 30 3673 3176 3810 172 -16 9 C
ATOM 171 C PRO A 30 48.827 -14.773 0.990 1.00 24.07 C
ANISOU 171 C PRO A 30 3184 2647 3316 198 -2 -40 C
ATOM 172 O PRO A 30 49.727 -14.149 0.437 1.00 24.42 O
ANISOU 172 O PRO A 30 3209 2724 3345 221 13 -57 O
ATOM 173 CB PRO A 30 49.502 -14.792 3.394 1.00 21.41 C
ANISOU 173 CB PRO A 30 2814 2339 2983 207 -23 51 C
ATOM 174 CG PRO A 30 49.186 -16.226 3.695 1.00 22.72 C
ANISOU 174 CG PRO A 30 3006 2437 3189 215 -27 73 C
ATOM 175 CD PRO A 30 47.670 -16.287 3.753 1.00 23.54 C
ANISOU 175 CD PRO A 30 3131 2522 3292 164 -31 72 C
ATOM 176 N ASP A 31 48.164 -15.774 0.413 1.00 24.62 N
ANISOU 176 N ASP A 31 3285 2658 3410 192 -5 -64 N
ATOM 177 CA ASP A 31 48.528 -16.300 -0.905 1.00 27.00 C
ANISOU 177 CA ASP A 31 3609 2931 3719 222 7 -117 C
ATOM 178 C ASP A 31 47.806 -15.564 -2.032 1.00 27.49 C
ANISOU 178 C ASP A 31 3682 3019 3744 201 9 -163 C
ATOM 179 O ASP A 31 46.641 -15.837 -2.314 1.00 25.25 O
ANISOU 179 O ASP A 31 3419 2711 3464 168 -7 -183 O
ATOM 180 CB ASP A 31 48.232 -17.811 -0.966 1.00 30.81 C
ANISOU 180 CB ASP A 31 4124 3331 4252 230 -2 -125 C
ATOM 181 CG ASP A 31 48.658 -18.463 -2.291 1.00 39.31 C
ANISOU 181 CG ASP A 31 5227 4373 5335 267 9 -186 C
ATOM 182 OD1 ASP A 31 49.293 -17.804 -3.135 1.00 42.70 O
ANISOU 182 OD1 ASP A 31 5649 4846 5730 292 29 -215 O
ATOM 183 OD2 ASP A 31 48.369 -19.662 -2.483 1.00 46.50 O
ANISOU 183 OD2 ASP A 31 6170 5211 6288 272 0 -205 O
ATOM 184 N ALA A 32 48.512 -14.651 -2.690 1.00 27.27 N
ANISOU 184 N ALA A 32 3639 3040 3681 221 29 -178 N
ATOM 185 CA ALA A 32 47.924 -13.873 -3.778 1.00 22.16 C
ANISOU 185 CA ALA A 32 3005 2424 2993 207 33 -215 C
ATOM 186 C ALA A 32 47.239 -14.729 -4.855 1.00 30.59 C
ANISOU 186 C ALA A 32 4113 3449 4062 210 23 -270 C
ATOM 187 O ALA A 32 46.198 -14.337 -5.402 1.00 32.60 O
ANISOU 187 O ALA A 32 4380 3715 4291 182 8 -294 O
ATOM 188 CB ALA A 32 48.953 -12.958 -4.390 1.00 20.83 C
ANISOU 188 CB ALA A 32 2817 2304 2794 235 63 -218 C
ATOM 189 N GLU A 33 47.794 -15.904 -5.134 1.00 33.89 N
ANISOU 189 N GLU A 33 4550 3817 4511 244 28 -291 N
ATOM 190 CA GLU A 33 47.209 -16.799 -6.142 1.00 39.26 C
ANISOU 190 CA GLU A 33 5272 4451 5196 249 14 -351 C
ATOM 191 C GLU A 33 45.841 -17.351 -5.721 1.00 28.05 C
ANISOU 191 C GLU A 33 3865 2987 3808 197 -21 -352 C
ATOM 192 O GLU A 33 44.979 -17.592 -6.566 1.00 27.34 O
ANISOU 192 O GLU A 33 3799 2882 3708 180 -42 -402 O
ATOM 193 CB GLU A 33 48.162 -17.953 -6.487 1.00 44.91 C
ANISOU 193 CB GLU A 33 6006 5116 5942 301 29 -376 C
ATOM 194 CG GLU A 33 49.348 -17.560 -7.366 1.00 61.97 C
ANISOU 194 CG GLU A 33 8161 7317 8066 356 67 -397 C
ATOM 195 CD GLU A 33 48.972 -17.341 -8.831 1.00 77.99 C
ANISOU 195 CD GLU A 33 10219 9372 10042 362 73 -455 C
ATOM 196 OE1 GLU A 33 47.956 -17.913 -9.287 1.00 80.63 O
ANISOU 196 OE1 GLU A 33 10579 9680 10377 330 47 -487 O
ATOM 197 OE2 GLU A 33 49.698 -16.598 -9.528 1.00 83.05 O
ANISOU 197 OE2 GLU A 33 10849 10069 10639 392 107 -459 O
ATOM 198 N MET A 34 45.652 -17.572 -4.424 1.00 22.93 N
ANISOU 198 N MET A 34 3197 2320 3196 172 -28 -297 N
ATOM 199 CA MET A 34 44.343 -17.983 -3.922 1.00 28.96 C
ANISOU 199 CA MET A 34 3963 3049 3990 119 -55 -287 C
ATOM 200 C MET A 34 43.326 -16.854 -4.120 1.00 32.30 C
ANISOU 200 C MET A 34 4370 3529 4372 81 -66 -292 C
ATOM 201 O MET A 34 42.149 -17.092 -4.414 1.00 27.19 O
ANISOU 201 O MET A 34 3730 2865 3737 43 -91 -316 O
ATOM 202 CB MET A 34 44.421 -18.365 -2.447 1.00 28.83 C
ANISOU 202 CB MET A 34 3931 3012 4013 106 -52 -219 C
ATOM 203 CG MET A 34 45.048 -19.729 -2.195 1.00 46.18 C
ANISOU 203 CG MET A 34 6149 5133 6266 134 -50 -211 C
ATOM 204 SD MET A 34 44.220 -21.048 -3.121 1.00 85.17 S
ANISOU 204 SD MET A 34 11129 9984 11250 115 -71 -273 S
ATOM 205 CE MET A 34 45.441 -21.416 -4.384 1.00 52.87 C
ANISOU 205 CE MET A 34 7061 5896 7130 182 -49 -330 C
ATOM 206 N ILE A 35 43.799 -15.622 -3.964 1.00 26.84 N
ANISOU 206 N ILE A 35 3657 2905 3637 92 -49 -269 N
ATOM 207 CA ILE A 35 42.954 -14.456 -4.150 1.00 24.39 C
ANISOU 207 CA ILE A 35 3332 2649 3287 65 -57 -270 C
ATOM 208 C ILE A 35 42.568 -14.340 -5.622 1.00 28.33 C
ANISOU 208 C ILE A 35 3855 3158 3753 73 -68 -330 C
ATOM 209 O ILE A 35 41.395 -14.160 -5.952 1.00 24.98 O
ANISOU 209 O ILE A 35 3430 2740 3320 42 -93 -350 O
ATOM 210 CB ILE A 35 43.651 -13.194 -3.641 1.00 23.03 C
ANISOU 210 CB ILE A 35 3133 2535 3082 76 -36 -233 C
ATOM 211 CG1 ILE A 35 43.838 -13.290 -2.119 1.00 19.43 C
ANISOU 211 CG1 ILE A 35 2655 2075 2651 64 -34 -176 C
ATOM 212 CG2 ILE A 35 42.872 -11.955 -4.036 1.00 20.03 C
ANISOU 212 CG2 ILE A 35 2744 2205 2659 57 -42 -239 C
ATOM 213 CD1 ILE A 35 44.649 -12.165 -1.511 1.00 23.49 C
ANISOU 213 CD1 ILE A 35 3143 2641 3140 76 -18 -145 C
ATOM 214 N VAL A 36 43.553 -14.483 -6.504 1.00 30.15 N
ANISOU 214 N VAL A 36 4105 3390 3962 118 -49 -360 N
ATOM 215 CA VAL A 36 43.288 -14.503 -7.937 1.00 26.17 C
ANISOU 215 CA VAL A 36 3630 2895 3418 135 -58 -421 C
ATOM 216 C VAL A 36 42.307 -15.626 -8.278 1.00 31.15 C
ANISOU 216 C VAL A 36 4284 3470 4083 111 -95 -467 C
ATOM 217 O VAL A 36 41.332 -15.407 -8.997 1.00 33.76 O
ANISOU 217 O VAL A 36 4620 3820 4386 90 -121 -498 O
ATOM 218 CB VAL A 36 44.585 -14.670 -8.751 1.00 29.42 C
ANISOU 218 CB VAL A 36 4059 3313 3806 192 -25 -444 C
ATOM 219 CG1 VAL A 36 44.276 -14.922 -10.228 1.00 25.11 C
ANISOU 219 CG1 VAL A 36 3547 2775 3217 210 -33 -506 C
ATOM 220 CG2 VAL A 36 45.484 -13.452 -8.580 1.00 23.47 C
ANISOU 220 CG2 VAL A 36 3279 2619 3021 210 10 -402 C
ATOM 221 N LYS A 37 42.541 -16.817 -7.733 1.00 30.13 N
ANISOU 221 N LYS A 37 4162 3274 4011 109 -97 -463 N
ATOM 222 CA LYS A 37 41.664 -17.958 -8.025 1.00 34.66 C
ANISOU 222 CA LYS A 37 4750 3802 4619 76 -121 -489 C
ATOM 223 C LYS A 37 40.249 -17.681 -7.559 1.00 27.54 C
ANISOU 223 C LYS A 37 3825 2905 3735 18 -152 -476 C
ATOM 224 O LYS A 37 39.288 -18.018 -8.253 1.00 31.59 O
ANISOU 224 O LYS A 37 4342 3418 4243 -9 -178 -511 O
ATOM 225 CB LYS A 37 42.166 -19.273 -7.394 1.00 39.30 C
ANISOU 225 CB LYS A 37 5347 4317 5268 82 -111 -473 C
ATOM 226 CG LYS A 37 43.413 -19.881 -8.041 1.00 55.32 C
ANISOU 226 CG LYS A 37 7400 6331 7288 138 -82 -497 C
ATOM 227 CD LYS A 37 43.203 -20.186 -9.517 1.00 63.65 C
ANISOU 227 CD LYS A 37 8482 7400 8303 148 -87 -561 C
ATOM 228 N ALA A 38 40.116 -17.070 -6.384 1.00 23.05 N
ANISOU 228 N ALA A 38 3228 2344 3184 -1 -149 -424 N
ATOM 229 CA ALA A 38 38.785 -16.836 -5.812 1.00 28.38 C
ANISOU 229 CA ALA A 38 3874 3029 3880 -57 -170 -402 C
ATOM 230 C ALA A 38 37.950 -15.887 -6.671 1.00 23.69 C
ANISOU 230 C ALA A 38 3272 2493 3236 -65 -192 -435 C
ATOM 231 O ALA A 38 36.764 -16.118 -6.898 1.00 23.60 O
ANISOU 231 O ALA A 38 3247 2477 3241 -104 -222 -453 O
ATOM 232 CB ALA A 38 38.883 -16.330 -4.371 1.00 21.86 C
ANISOU 232 CB ALA A 38 3016 2225 3064 -70 -146 -325 C
ATOM 233 N VAL A 39 38.587 -14.829 -7.158 1.00 23.57 N
ANISOU 233 N VAL A 39 3261 2536 3158 -29 -173 -434 N
ATOM 234 CA VAL A 39 37.930 -13.874 -8.045 1.00 25.65 C
ANISOU 234 CA VAL A 39 3522 2855 3368 -27 -191 -459 C
ATOM 235 C VAL A 39 37.508 -14.554 -9.344 1.00 30.94 C
ANISOU 235 C VAL A 39 4216 3518 4021 -23 -217 -519 C
ATOM 236 O VAL A 39 36.393 -14.342 -9.838 1.00 28.50 O
ANISOU 236 O VAL A 39 3896 3235 3700 -47 -248 -537 O
ATOM 237 CB VAL A 39 38.861 -12.685 -8.358 1.00 23.22 C
ANISOU 237 CB VAL A 39 3218 2604 3000 15 -159 -440 C
ATOM 238 CG1 VAL A 39 38.301 -11.825 -9.477 1.00 16.16 C
ANISOU 238 CG1 VAL A 39 2333 1762 2045 27 -176 -468 C
ATOM 239 CG2 VAL A 39 39.091 -11.865 -7.098 1.00 17.52 C
ANISOU 239 CG2 VAL A 39 2463 1906 2286 3 -133 -374 C
ATOM 240 N ALA A 40 38.402 -15.384 -9.879 1.00 28.98 N
ANISOU 240 N ALA A 40 3997 3241 3771 7 -199 -543 N
ATOM 241 CA ALA A 40 38.131 -16.144 -11.095 1.00 31.26 C
ANISOU 241 CA ALA A 40 4310 3524 4042 12 -215 -594 C
ATOM 242 C ALA A 40 36.924 -17.071 -10.928 1.00 35.02 C
ANISOU 242 C ALA A 40 4775 3960 4570 -40 -252 -610 C
ATOM 243 O ALA A 40 36.068 -17.171 -11.805 1.00 37.82 O
ANISOU 243 O ALA A 40 5132 4334 4905 -54 -283 -647 O
ATOM 244 CB ALA A 40 39.367 -16.946 -11.490 1.00 40.13 C
ANISOU 244 CB ALA A 40 5465 4617 5167 53 -185 -613 C
ATOM 245 N ARG A 41 36.864 -17.742 -9.786 1.00 34.59 N
ANISOU 245 N ARG A 41 4708 3852 4585 -69 -246 -578 N
ATOM 246 CA ARG A 41 35.770 -18.643 -9.468 1.00 30.64 C
ANISOU 246 CA ARG A 41 4192 3308 4142 -122 -273 -582 C
ATOM 247 C ARG A 41 34.437 -17.894 -9.357 1.00 35.92 C
ANISOU 247 C ARG A 41 4821 4020 4807 -162 -302 -574 C
ATOM 248 O ARG A 41 33.397 -18.412 -9.756 1.00 38.77 O
ANISOU 248 O ARG A 41 5170 4372 5187 -197 -334 -600 O
ATOM 249 CB ARG A 41 36.102 -19.397 -8.173 1.00 37.59 C
ANISOU 249 CB ARG A 41 5066 4125 5091 -140 -252 -534 C
ATOM 250 CG ARG A 41 35.021 -20.336 -7.653 1.00 48.40 C
ANISOU 250 CG ARG A 41 6416 5447 6526 -198 -270 -523 C
ATOM 251 CD ARG A 41 35.362 -20.823 -6.240 1.00 50.54 C
ANISOU 251 CD ARG A 41 6678 5668 6855 -211 -244 -459 C
ATOM 252 N VAL A 42 34.465 -16.675 -8.819 1.00 34.02 N
ANISOU 252 N VAL A 42 4557 3825 4542 -155 -293 -539 N
ATOM 253 CA VAL A 42 33.256 -15.856 -8.739 1.00 27.79 C
ANISOU 253 CA VAL A 42 3730 3083 3746 -184 -318 -531 C
ATOM 254 C VAL A 42 32.827 -15.462 -10.148 1.00 28.00 C
ANISOU 254 C VAL A 42 3767 3158 3712 -165 -346 -578 C
ATOM 255 O VAL A 42 31.648 -15.502 -10.482 1.00 26.40 O
ANISOU 255 O VAL A 42 3540 2972 3518 -195 -380 -594 O
ATOM 256 CB VAL A 42 33.471 -14.597 -7.859 1.00 30.71 C
ANISOU 256 CB VAL A 42 4078 3490 4101 -175 -299 -486 C
ATOM 257 CG1 VAL A 42 32.336 -13.583 -8.045 1.00 24.36 C
ANISOU 257 CG1 VAL A 42 3238 2745 3273 -189 -325 -486 C
ATOM 258 CG2 VAL A 42 33.610 -14.989 -6.386 1.00 25.53 C
ANISOU 258 CG2 VAL A 42 3402 2790 3508 -203 -278 -434 C
ATOM 259 N ALA A 43 33.804 -15.105 -10.978 1.00 30.38 N
ANISOU 259 N ALA A 43 4106 3483 3954 -114 -330 -596 N
ATOM 260 CA ALA A 43 33.550 -14.739 -12.372 1.00 32.11 C
ANISOU 260 CA ALA A 43 4343 3750 4109 -89 -351 -635 C
ATOM 261 C ALA A 43 32.978 -15.902 -13.182 1.00 41.80 C
ANISOU 261 C ALA A 43 5582 4947 5352 -108 -383 -686 C
ATOM 262 O ALA A 43 32.105 -15.709 -14.030 1.00 42.66 O
ANISOU 262 O ALA A 43 5685 5091 5433 -114 -419 -714 O
ATOM 263 CB ALA A 43 34.825 -14.213 -13.029 1.00 22.63 C
ANISOU 263 CB ALA A 43 3177 2575 2845 -31 -317 -637 C
ATOM 264 N GLU A 44 33.479 -17.106 -12.916 1.00 45.33 N
ANISOU 264 N GLU A 44 6049 5330 5846 -116 -370 -698 N
ATOM 265 CA GLU A 44 33.034 -18.299 -13.626 1.00 50.52 C
ANISOU 265 CA GLU A 44 6722 5949 6524 -135 -398 -749 C
ATOM 266 C GLU A 44 31.671 -18.795 -13.146 1.00 53.96 C
ANISOU 266 C GLU A 44 7119 6361 7021 -198 -433 -747 C
ATOM 267 O GLU A 44 31.050 -19.614 -13.800 1.00 52.38 O
ANISOU 267 O GLU A 44 6926 6140 6837 -220 -465 -791 O
ATOM 268 CB GLU A 44 34.086 -19.410 -13.546 1.00 49.97 C
ANISOU 268 CB GLU A 44 6690 5815 6482 -117 -370 -762 C
ATOM 269 CG GLU A 44 35.204 -19.272 -14.578 1.00 52.82 C
ANISOU 269 CG GLU A 44 7093 6200 6778 -56 -346 -792 C
ATOM 270 N SER A 45 31.212 -18.296 -12.003 1.00 57.90 N
ANISOU 270 N SER A 45 7576 6865 7556 -227 -425 -695 N
ATOM 271 CA SER A 45 29.852 -18.568 -11.550 1.00 56.37 C
ANISOU 271 CA SER A 45 7337 6665 7418 -286 -454 -686 C
ATOM 272 C SER A 45 28.934 -17.504 -12.152 1.00 60.29 C
ANISOU 272 C SER A 45 7804 7235 7867 -283 -486 -696 C
ATOM 273 O SER A 45 27.736 -17.449 -11.860 1.00 56.77 O
ANISOU 273 O SER A 45 7311 6802 7456 -325 -511 -687 O
ATOM 274 CB SER A 45 29.759 -18.588 -10.015 1.00 51.86 C
ANISOU 274 CB SER A 45 6732 6065 6908 -318 -425 -623 C
ATOM 275 OG SER A 45 29.815 -17.280 -9.462 1.00 52.27 O
ANISOU 275 OG SER A 45 6760 6170 6931 -303 -411 -584 O
ATOM 276 N GLY A 46 29.525 -16.658 -12.997 1.00 64.35 N
ANISOU 276 N GLY A 46 8346 7799 8304 -230 -483 -710 N
ATOM 277 CA GLY A 46 28.797 -15.657 -13.759 1.00 62.25 C
ANISOU 277 CA GLY A 46 8063 7604 7983 -216 -514 -720 C
ATOM 278 C GLY A 46 28.391 -14.405 -13.001 1.00 60.70 C
ANISOU 278 C GLY A 46 7827 7454 7783 -216 -506 -671 C
ATOM 279 O GLY A 46 27.450 -13.721 -13.409 1.00 62.36 O
ANISOU 279 O GLY A 46 8009 7714 7971 -217 -538 -674 O
ATOM 280 N GLY A 47 29.096 -14.100 -11.910 1.00 58.05 N
ANISOU 280 N GLY A 47 7488 7101 7467 -213 -466 -628 N
ATOM 281 CA GLY A 47 28.744 -12.978 -11.051 1.00 53.54 C
ANISOU 281 CA GLY A 47 6879 6566 6898 -216 -456 -583 C
ATOM 282 C GLY A 47 28.220 -13.383 -9.676 1.00 56.72 C
ANISOU 282 C GLY A 47 7238 6936 7379 -267 -444 -546 C
ATOM 283 O GLY A 47 28.922 -13.225 -8.677 1.00 50.04 O
ANISOU 283 O GLY A 47 6393 6068 6551 -264 -409 -510 O
ATOM 284 N GLY A 48 26.991 -13.907 -9.621 1.00 62.51 N
ANISOU 284 N GLY A 48 7929 7665 8158 -312 -471 -553 N
ATOM 285 CA GLY A 48 26.362 -14.282 -8.360 1.00 56.83 C
ANISOU 285 CA GLY A 48 7161 6919 7511 -363 -456 -512 C
ATOM 286 C GLY A 48 26.181 -13.074 -7.450 1.00 50.02 C
ANISOU 286 C GLY A 48 6262 6101 6644 -356 -436 -466 C
ATOM 287 O GLY A 48 25.688 -12.033 -7.884 1.00 47.63 O
ANISOU 287 O GLY A 48 5940 5857 6301 -334 -455 -472 O
ATOM 288 N ARG A 49 26.586 -13.185 -6.190 1.00 36.64 N
ANISOU 288 N ARG A 49 4556 4377 4988 -372 -397 -420 N
ATOM 289 CA ARG A 49 26.532 -12.016 -5.324 1.00 31.38 C
ANISOU 289 CA ARG A 49 3861 3755 4309 -360 -373 -377 C
ATOM 290 C ARG A 49 27.866 -11.307 -5.185 1.00 24.38 C
ANISOU 290 C ARG A 49 3021 2880 3361 -307 -335 -356 C
ATOM 291 O ARG A 49 28.019 -10.392 -4.384 1.00 32.04 O
ANISOU 291 O ARG A 49 3981 3886 4309 -289 -299 -310 O
ATOM 292 CB ARG A 49 25.886 -12.320 -3.974 1.00 39.83 C
ANISOU 292 CB ARG A 49 4881 4815 5437 -402 -340 -320 C
ATOM 293 CG ARG A 49 24.409 -12.004 -4.021 1.00 44.41 C
ANISOU 293 CG ARG A 49 5392 5437 6045 -431 -365 -323 C
ATOM 294 CD ARG A 49 23.723 -12.250 -2.725 1.00 48.08 C
ANISOU 294 CD ARG A 49 5804 5900 6564 -471 -326 -265 C
ATOM 295 NE ARG A 49 23.667 -11.069 -1.865 1.00 46.05 N
ANISOU 295 NE ARG A 49 5528 5701 6266 -439 -284 -217 N
ATOM 296 CZ ARG A 49 22.833 -10.047 -2.025 1.00 37.22 C
ANISOU 296 CZ ARG A 49 4369 4647 5127 -422 -294 -219 C
ATOM 297 NH1 ARG A 49 21.999 -10.018 -3.053 1.00 36.62 N
ANISOU 297 NH1 ARG A 49 4265 4590 5061 -430 -348 -265 N
ATOM 298 NH2 ARG A 49 22.845 -9.041 -1.154 1.00 35.28 N
ANISOU 298 NH2 ARG A 49 4112 4445 4848 -392 -251 -177 N
ATOM 299 N GLY A 50 28.823 -11.738 -5.991 1.00 20.52 N
ANISOU 299 N GLY A 50 2586 2363 2849 -282 -344 -392 N
ATOM 300 CA GLY A 50 30.049 -11.001 -6.179 1.00 22.76 C
ANISOU 300 CA GLY A 50 2911 2665 3072 -231 -315 -383 C
ATOM 301 C GLY A 50 31.058 -11.051 -5.054 1.00 20.82 C
ANISOU 301 C GLY A 50 2677 2399 2834 -223 -266 -333 C
ATOM 302 O GLY A 50 31.020 -11.916 -4.174 1.00 22.74 O
ANISOU 302 O GLY A 50 2909 2601 3129 -253 -252 -307 O
ATOM 303 N ALA A 51 31.973 -10.096 -5.104 1.00 16.25 N
ANISOU 303 N ALA A 51 2120 1851 2204 -181 -241 -318 N
ATOM 304 CA ALA A 51 33.117 -10.058 -4.216 1.00 15.63 C
ANISOU 304 CA ALA A 51 2056 1759 2124 -166 -201 -279 C
ATOM 305 C ALA A 51 33.485 -8.611 -3.960 1.00 20.28 C
ANISOU 305 C ALA A 51 2642 2398 2666 -137 -179 -253 C
ATOM 306 O ALA A 51 33.292 -7.752 -4.824 1.00 19.28 O
ANISOU 306 O ALA A 51 2521 2306 2500 -116 -191 -272 O
ATOM 307 CB ALA A 51 34.308 -10.813 -4.843 1.00 9.37 C
ANISOU 307 CB ALA A 51 1306 928 1327 -142 -197 -305 C
ATOM 308 N ILE A 52 33.998 -8.340 -2.765 1.00 17.47 N
ANISOU 308 N ILE A 52 2277 2045 2315 -136 -148 -210 N
ATOM 309 CA ILE A 52 34.577 -7.042 -2.467 1.00 13.79 C
ANISOU 309 CA ILE A 52 1813 1615 1810 -110 -127 -189 C
ATOM 310 C ILE A 52 35.786 -7.236 -1.559 1.00 17.00 C
ANISOU 310 C ILE A 52 2230 2007 2223 -100 -100 -161 C
ATOM 311 O ILE A 52 35.849 -8.198 -0.798 1.00 18.28 O
ANISOU 311 O ILE A 52 2388 2140 2417 -117 -95 -142 O
ATOM 312 CB ILE A 52 33.546 -6.080 -1.799 1.00 15.49 C
ANISOU 312 CB ILE A 52 1996 1870 2021 -118 -124 -168 C
ATOM 313 CG1 ILE A 52 33.946 -4.624 -2.035 1.00 10.50 C
ANISOU 313 CG1 ILE A 52 1372 1270 1346 -88 -113 -165 C
ATOM 314 CG2 ILE A 52 33.360 -6.394 -0.307 1.00 11.29 C
ANISOU 314 CG2 ILE A 52 1442 1334 1512 -138 -103 -129 C
ATOM 315 CD1 ILE A 52 33.842 -4.188 -3.504 1.00 9.63 C
ANISOU 315 CD1 ILE A 52 1280 1172 1206 -67 -133 -195 C
ATOM 316 N ALA A 53 36.744 -6.322 -1.642 1.00 16.83 N
ANISOU 316 N ALA A 53 2219 2004 2170 -74 -85 -155 N
ATOM 317 CA ALA A 53 37.897 -6.349 -0.750 1.00 14.41 C
ANISOU 317 CA ALA A 53 1916 1693 1868 -64 -64 -130 C
ATOM 318 C ALA A 53 37.571 -5.730 0.601 1.00 16.51 C
ANISOU 318 C ALA A 53 2160 1982 2130 -73 -54 -98 C
ATOM 319 O ALA A 53 36.682 -4.892 0.727 1.00 13.51 O
ANISOU 319 O ALA A 53 1766 1629 1737 -78 -56 -97 O
ATOM 320 CB ALA A 53 39.078 -5.626 -1.381 1.00 11.68 C
ANISOU 320 CB ALA A 53 1584 1358 1497 -36 -52 -138 C
ATOM 321 N ARG A 54 38.311 -6.142 1.616 1.00 12.54 N
ANISOU 321 N ARG A 54 1657 1471 1636 -71 -44 -72 N
ATOM 322 CA ARG A 54 38.196 -5.509 2.908 1.00 9.99 C
ANISOU 322 CA ARG A 54 1320 1176 1300 -73 -35 -45 C
ATOM 323 C ARG A 54 39.586 -5.279 3.466 1.00 15.30 C
ANISOU 323 C ARG A 54 1997 1852 1962 -55 -29 -34 C
ATOM 324 O ARG A 54 40.441 -6.151 3.377 1.00 14.26 O
ANISOU 324 O ARG A 54 1874 1697 1848 -46 -30 -29 O
ATOM 325 CB ARG A 54 37.370 -6.372 3.861 1.00 5.87 C
ANISOU 325 CB ARG A 54 786 648 797 -95 -31 -17 C
ATOM 326 CG ARG A 54 37.211 -5.795 5.254 1.00 7.76 C
ANISOU 326 CG ARG A 54 1014 921 1014 -93 -19 11 C
ATOM 327 CD ARG A 54 36.198 -6.612 6.030 1.00 16.95 C
ANISOU 327 CD ARG A 54 2163 2082 2195 -115 -9 43 C
ATOM 328 NE ARG A 54 35.991 -6.140 7.392 1.00 21.05 N
ANISOU 328 NE ARG A 54 2674 2639 2686 -110 7 71 N
ATOM 329 CZ ARG A 54 34.950 -5.424 7.799 1.00 20.24 C
ANISOU 329 CZ ARG A 54 2553 2571 2567 -114 19 72 C
ATOM 330 NH1 ARG A 54 33.990 -5.083 6.951 1.00 24.05 N
ANISOU 330 NH1 ARG A 54 3019 3055 3063 -124 14 49 N
ATOM 331 NH2 ARG A 54 34.873 -5.054 9.066 1.00 16.65 N
ANISOU 331 NH2 ARG A 54 2095 2151 2081 -103 35 95 N
ATOM 332 N GLY A 55 39.802 -4.102 4.043 1.00 17.38 N
ANISOU 332 N GLY A 55 2254 2146 2203 -48 -26 -32 N
ATOM 333 CA GLY A 55 41.062 -3.808 4.702 1.00 20.85 C
ANISOU 333 CA GLY A 55 2693 2595 2636 -35 -26 -24 C
ATOM 334 C GLY A 55 40.932 -3.976 6.199 1.00 18.07 C
ANISOU 334 C GLY A 55 2334 2261 2270 -36 -27 3 C
ATOM 335 O GLY A 55 40.555 -5.042 6.685 1.00 16.60 O
ANISOU 335 O GLY A 55 2149 2064 2095 -43 -24 28 O
ATOM 336 N LEU A 56 41.216 -2.911 6.936 1.00 12.53 N
ANISOU 336 N LEU A 56 1628 1588 1544 -31 -29 -2 N
ATOM 337 CA LEU A 56 41.154 -2.984 8.389 1.00 14.83 C
ANISOU 337 CA LEU A 56 1916 1905 1812 -27 -32 20 C
ATOM 338 C LEU A 56 39.777 -2.637 8.963 1.00 17.90 C
ANISOU 338 C LEU A 56 2303 2318 2182 -34 -19 25 C
ATOM 339 O LEU A 56 39.590 -2.593 10.180 1.00 18.61 O
ANISOU 339 O LEU A 56 2392 2435 2243 -28 -16 42 O
ATOM 340 CB LEU A 56 42.247 -2.116 8.999 1.00 17.35 C
ANISOU 340 CB LEU A 56 2232 2245 2114 -15 -46 7 C
ATOM 341 CG LEU A 56 43.602 -2.820 9.091 1.00 18.42 C
ANISOU 341 CG LEU A 56 2363 2371 2264 -4 -59 19 C
ATOM 342 CD1 LEU A 56 44.698 -1.815 9.393 1.00 14.19 C
ANISOU 342 CD1 LEU A 56 1815 1853 1722 2 -76 -2 C
ATOM 343 CD2 LEU A 56 43.528 -3.909 10.178 1.00 9.36 C
ANISOU 343 CD2 LEU A 56 1219 1232 1104 5 -62 58 C
ATOM 344 N GLY A 57 38.815 -2.408 8.077 1.00 15.69 N
ANISOU 344 N GLY A 57 2018 2028 1914 -44 -12 10 N
ATOM 345 CA GLY A 57 37.446 -2.131 8.471 1.00 15.32 C
ANISOU 345 CA GLY A 57 1962 2004 1857 -50 1 15 C
ATOM 346 C GLY A 57 37.250 -0.796 9.180 1.00 22.79 C
ANISOU 346 C GLY A 57 2907 2982 2770 -36 5 -2 C
ATOM 347 O GLY A 57 36.359 -0.676 10.022 1.00 15.73 O
ANISOU 347 O GLY A 57 2004 2115 1856 -33 20 9 O
ATOM 348 N ARG A 58 38.069 0.209 8.864 1.00 14.21 N
ANISOU 348 N ARG A 58 1829 1890 1679 -26 -7 -29 N
ATOM 349 CA ARG A 58 37.930 1.489 9.561 1.00 17.55 C
ANISOU 349 CA ARG A 58 2256 2337 2076 -13 -6 -51 C
ATOM 350 C ARG A 58 36.850 2.376 8.953 1.00 14.64 C
ANISOU 350 C ARG A 58 1882 1968 1712 -7 3 -69 C
ATOM 351 O ARG A 58 36.443 3.372 9.545 1.00 14.16 O
ANISOU 351 O ARG A 58 1824 1925 1631 7 8 -86 O
ATOM 352 CB ARG A 58 39.268 2.237 9.696 1.00 13.15 C
ANISOU 352 CB ARG A 58 1707 1772 1516 -8 -23 -72 C
ATOM 353 CG ARG A 58 39.928 2.047 11.067 1.00 11.54 C
ANISOU 353 CG ARG A 58 1507 1595 1282 0 -35 -67 C
ATOM 354 CD ARG A 58 40.296 0.581 11.343 1.00 10.58 C
ANISOU 354 CD ARG A 58 1382 1473 1164 -4 -36 -29 C
ATOM 355 NE ARG A 58 41.034 0.448 12.595 1.00 17.55 N
ANISOU 355 NE ARG A 58 2269 2383 2015 9 -52 -21 N
ATOM 356 CZ ARG A 58 41.319 -0.707 13.194 1.00 23.70 C
ANISOU 356 CZ ARG A 58 3049 3171 2786 14 -54 16 C
ATOM 357 NH1 ARG A 58 40.924 -1.866 12.669 1.00 24.32 N
ANISOU 357 NH1 ARG A 58 3124 3224 2891 4 -40 48 N
ATOM 358 NH2 ARG A 58 42.005 -0.704 14.333 1.00 25.75 N
ANISOU 358 NH2 ARG A 58 3313 3461 3010 29 -73 21 N
ATOM 359 N SER A 59 36.381 2.009 7.772 1.00 18.39 N
ANISOU 359 N SER A 59 2352 2425 2211 -16 3 -66 N
ATOM 360 CA SER A 59 35.261 2.720 7.173 1.00 15.98 C
ANISOU 360 CA SER A 59 2038 2124 1910 -8 8 -77 C
ATOM 361 C SER A 59 34.016 2.520 8.056 1.00 19.67 C
ANISOU 361 C SER A 59 2485 2623 2365 -5 25 -65 C
ATOM 362 O SER A 59 33.758 1.412 8.549 1.00 11.48 O
ANISOU 362 O SER A 59 1437 1594 1331 -19 33 -39 O
ATOM 363 CB SER A 59 35.046 2.247 5.731 1.00 10.41 C
ANISOU 363 CB SER A 59 1330 1397 1228 -17 -1 -77 C
ATOM 364 OG SER A 59 33.824 2.719 5.210 1.00 22.58 O
ANISOU 364 OG SER A 59 2857 2949 2772 -8 0 -84 O
ATOM 365 N TYR A 60 33.282 3.603 8.302 1.00 15.37 N
ANISOU 365 N TYR A 60 1936 2095 1809 15 34 -81 N
ATOM 366 CA TYR A 60 32.063 3.528 9.104 1.00 17.87 C
ANISOU 366 CA TYR A 60 2229 2447 2114 23 55 -71 C
ATOM 367 C TYR A 60 30.904 2.951 8.311 1.00 24.23 C
ANISOU 367 C TYR A 60 3003 3256 2947 11 57 -58 C
ATOM 368 O TYR A 60 29.886 2.576 8.880 1.00 28.65 O
ANISOU 368 O TYR A 60 3534 3844 3508 8 76 -42 O
ATOM 369 CB TYR A 60 31.671 4.906 9.636 1.00 14.75 C
ANISOU 369 CB TYR A 60 1838 2068 1697 55 65 -97 C
ATOM 370 CG TYR A 60 32.556 5.415 10.760 1.00 26.78 C
ANISOU 370 CG TYR A 60 3388 3600 3189 66 65 -113 C
ATOM 371 CD1 TYR A 60 32.080 5.472 12.067 1.00 25.42 C
ANISOU 371 CD1 TYR A 60 3211 3467 2979 83 86 -111 C
ATOM 372 CD2 TYR A 60 33.874 5.838 10.515 1.00 24.79 C
ANISOU 372 CD2 TYR A 60 3161 3318 2941 61 42 -131 C
ATOM 373 CE1 TYR A 60 32.873 5.946 13.100 1.00 36.24 C
ANISOU 373 CE1 TYR A 60 4607 4849 4314 96 80 -132 C
ATOM 374 CE2 TYR A 60 34.677 6.312 11.544 1.00 27.27 C
ANISOU 374 CE2 TYR A 60 3494 3641 3227 69 35 -151 C
ATOM 375 CZ TYR A 60 34.169 6.363 12.839 1.00 36.05 C
ANISOU 375 CZ TYR A 60 4606 4793 4297 88 52 -153 C
ATOM 376 OH TYR A 60 34.941 6.825 13.883 1.00 31.24 O
ANISOU 376 OH TYR A 60 4018 4197 3654 99 39 -178 O
ATOM 377 N GLY A 61 31.066 2.878 6.996 1.00 21.18 N
ANISOU 377 N GLY A 61 2621 2842 2583 4 35 -67 N
ATOM 378 CA GLY A 61 29.988 2.455 6.134 1.00 20.27 C
ANISOU 378 CA GLY A 61 2478 2732 2493 -6 27 -64 C
ATOM 379 C GLY A 61 29.882 0.964 5.866 1.00 19.60 C
ANISOU 379 C GLY A 61 2379 2634 2433 -40 21 -46 C
ATOM 380 O GLY A 61 30.452 0.125 6.569 1.00 14.73 O
ANISOU 380 O GLY A 61 1771 2009 1815 -56 30 -27 O
ATOM 381 N ASP A 62 29.140 0.651 4.816 1.00 12.71 N
ANISOU 381 N ASP A 62 1487 1757 1584 -50 2 -54 N
ATOM 382 CA ASP A 62 28.889 -0.718 4.413 1.00 17.09 C
ANISOU 382 CA ASP A 62 2028 2295 2170 -84 -9 -45 C
ATOM 383 C ASP A 62 29.598 -1.025 3.080 1.00 13.97 C
ANISOU 383 C ASP A 62 1661 1868 1779 -86 -38 -67 C
ATOM 384 O ASP A 62 29.195 -1.923 2.330 1.00 15.18 O
ANISOU 384 O ASP A 62 1804 2007 1957 -108 -58 -76 O
ATOM 385 CB ASP A 62 27.369 -0.960 4.308 1.00 18.88 C
ANISOU 385 CB ASP A 62 2205 2546 2424 -97 -11 -41 C
ATOM 386 CG ASP A 62 26.678 0.006 3.330 1.00 18.46 C
ANISOU 386 CG ASP A 62 2138 2510 2366 -72 -33 -65 C
ATOM 387 OD1 ASP A 62 27.302 1.014 2.937 1.00 14.32 O
ANISOU 387 OD1 ASP A 62 1645 1980 1815 -42 -38 -79 O
ATOM 388 OD2 ASP A 62 25.513 -0.250 2.952 1.00 17.68 O
ANISOU 388 OD2 ASP A 62 1996 2429 2294 -84 -46 -68 O
ATOM 389 N ASN A 63 30.674 -0.297 2.802 1.00 11.17 N
ANISOU 389 N ASN A 63 1341 1502 1399 -65 -39 -77 N
ATOM 390 CA ASN A 63 31.424 -0.504 1.558 1.00 13.64 C
ANISOU 390 CA ASN A 63 1682 1791 1710 -61 -59 -95 C
ATOM 391 C ASN A 63 32.428 -1.664 1.598 1.00 11.48 C
ANISOU 391 C ASN A 63 1428 1486 1448 -78 -58 -91 C
ATOM 392 O ASN A 63 32.860 -2.150 0.557 1.00 17.84 O
ANISOU 392 O ASN A 63 2250 2271 2256 -78 -73 -108 O
ATOM 393 CB ASN A 63 32.095 0.798 1.090 1.00 7.56 C
ANISOU 393 CB ASN A 63 937 1021 914 -32 -57 -104 C
ATOM 394 CG ASN A 63 32.871 1.489 2.207 1.00 20.18 C
ANISOU 394 CG ASN A 63 2546 2621 2500 -23 -36 -95 C
ATOM 395 OD1 ASN A 63 32.698 1.176 3.394 1.00 19.22 O
ANISOU 395 OD1 ASN A 63 2411 2510 2380 -32 -22 -81 O
ATOM 396 ND2 ASN A 63 33.722 2.433 1.835 1.00 17.06 N
ANISOU 396 ND2 ASN A 63 2174 2216 2092 -6 -33 -101 N
ATOM 397 N ALA A 64 32.785 -2.114 2.796 1.00 12.87 N
ANISOU 397 N ALA A 64 1601 1660 1629 -88 -40 -68 N
ATOM 398 CA ALA A 64 33.720 -3.235 2.940 1.00 14.99 C
ANISOU 398 CA ALA A 64 1886 1897 1911 -99 -39 -59 C
ATOM 399 C ALA A 64 33.026 -4.507 3.408 1.00 21.28 C
ANISOU 399 C ALA A 64 2665 2681 2741 -128 -37 -40 C
ATOM 400 O ALA A 64 33.601 -5.298 4.157 1.00 20.60 O
ANISOU 400 O ALA A 64 2587 2577 2664 -135 -27 -16 O
ATOM 401 CB ALA A 64 34.833 -2.876 3.897 1.00 14.59 C
ANISOU 401 CB ALA A 64 1850 1852 1843 -86 -25 -44 C
ATOM 402 N GLN A 65 31.781 -4.689 2.987 1.00 20.64 N
ANISOU 402 N GLN A 65 2558 2607 2680 -145 -47 -48 N
ATOM 403 CA GLN A 65 31.069 -5.918 3.275 1.00 18.53 C
ANISOU 403 CA GLN A 65 2269 2319 2453 -180 -47 -32 C
ATOM 404 C GLN A 65 30.186 -6.239 2.087 1.00 15.59 C
ANISOU 404 C GLN A 65 1881 1938 2105 -196 -77 -63 C
ATOM 405 O GLN A 65 29.953 -5.391 1.239 1.00 19.38 O
ANISOU 405 O GLN A 65 2361 2440 2564 -177 -94 -90 O
ATOM 406 CB GLN A 65 30.255 -5.805 4.558 1.00 14.17 C
ANISOU 406 CB GLN A 65 1686 1797 1903 -190 -19 5 C
ATOM 407 CG GLN A 65 29.332 -4.624 4.592 1.00 17.86 C
ANISOU 407 CG GLN A 65 2125 2309 2351 -175 -15 -4 C
ATOM 408 CD GLN A 65 28.822 -4.340 5.981 1.00 21.74 C
ANISOU 408 CD GLN A 65 2594 2836 2830 -172 21 30 C
ATOM 409 OE1 GLN A 65 29.348 -3.479 6.681 1.00 28.45 O
ANISOU 409 OE1 GLN A 65 3461 3708 3640 -144 36 33 O
ATOM 410 NE2 GLN A 65 27.790 -5.064 6.391 1.00 27.72 N
ANISOU 410 NE2 GLN A 65 3313 3599 3621 -202 35 55 N
ATOM 411 N ASN A 66 29.726 -7.476 2.012 1.00 10.93 N
ANISOU 411 N ASN A 66 1277 1314 1560 -232 -85 -61 N
ATOM 412 CA ASN A 66 28.971 -7.925 0.856 1.00 14.50 C
ANISOU 412 CA ASN A 66 1717 1754 2039 -251 -121 -98 C
ATOM 413 C ASN A 66 28.043 -9.052 1.280 1.00 17.92 C
ANISOU 413 C ASN A 66 2114 2162 2531 -300 -121 -81 C
ATOM 414 O ASN A 66 28.418 -10.233 1.198 1.00 14.04 O
ANISOU 414 O ASN A 66 1641 1617 2076 -322 -126 -82 O
ATOM 415 CB ASN A 66 29.923 -8.420 -0.234 1.00 12.98 C
ANISOU 415 CB ASN A 66 1568 1524 1838 -239 -144 -135 C
ATOM 416 CG ASN A 66 29.200 -8.763 -1.520 1.00 16.08 C
ANISOU 416 CG ASN A 66 1954 1911 2246 -251 -188 -183 C
ATOM 417 OD1 ASN A 66 28.101 -8.272 -1.771 1.00 14.85 O
ANISOU 417 OD1 ASN A 66 1761 1789 2092 -259 -205 -192 O
ATOM 418 ND2 ASN A 66 29.811 -9.613 -2.340 1.00 16.38 N
ANISOU 418 ND2 ASN A 66 2026 1907 2291 -251 -207 -217 N
ATOM 419 N GLY A 67 26.847 -8.687 1.742 1.00 18.44 N
ANISOU 419 N GLY A 67 2129 2265 2612 -315 -112 -64 N
ATOM 420 CA GLY A 67 25.930 -9.648 2.336 1.00 16.75 C
ANISOU 420 CA GLY A 67 1873 2034 2458 -364 -101 -36 C
ATOM 421 C GLY A 67 25.641 -10.772 1.366 1.00 17.79 C
ANISOU 421 C GLY A 67 2003 2114 2642 -402 -141 -72 C
ATOM 422 O GLY A 67 25.287 -10.507 0.234 1.00 17.92 O
ANISOU 422 O GLY A 67 2015 2141 2651 -397 -183 -121 O
ATOM 423 N GLY A 68 25.854 -12.016 1.788 1.00 16.77 N
ANISOU 423 N GLY A 68 1884 1927 2562 -436 -131 -50 N
ATOM 424 CA GLY A 68 25.546 -13.169 0.955 1.00 14.71 C
ANISOU 424 CA GLY A 68 1622 1608 2360 -476 -168 -87 C
ATOM 425 C GLY A 68 26.568 -13.482 -0.126 1.00 23.59 C
ANISOU 425 C GLY A 68 2805 2693 3464 -451 -201 -140 C
ATOM 426 O GLY A 68 26.375 -14.398 -0.942 1.00 20.44 O
ANISOU 426 O GLY A 68 2414 2246 3108 -478 -238 -183 O
ATOM 427 N GLY A 69 27.659 -12.724 -0.140 1.00 19.84 N
ANISOU 427 N GLY A 69 2372 2241 2925 -399 -187 -139 N
ATOM 428 CA GLY A 69 28.677 -12.904 -1.154 1.00 12.88 C
ANISOU 428 CA GLY A 69 1543 1333 2017 -369 -209 -186 C
ATOM 429 C GLY A 69 30.056 -13.099 -0.561 1.00 11.79 C
ANISOU 429 C GLY A 69 1448 1171 1861 -339 -178 -157 C
ATOM 430 O GLY A 69 30.188 -13.469 0.599 1.00 12.97 O
ANISOU 430 O GLY A 69 1591 1306 2032 -351 -146 -103 O
ATOM 431 N LEU A 70 31.078 -12.829 -1.365 1.00 14.06 N
ANISOU 431 N LEU A 70 1777 1458 2108 -299 -186 -191 N
ATOM 432 CA LEU A 70 32.459 -12.991 -0.946 1.00 12.64 C
ANISOU 432 CA LEU A 70 1632 1258 1911 -267 -161 -170 C
ATOM 433 C LEU A 70 33.081 -11.661 -0.499 1.00 18.39 C
ANISOU 433 C LEU A 70 2363 2045 2582 -230 -137 -146 C
ATOM 434 O LEU A 70 32.903 -10.633 -1.146 1.00 21.06 O
ANISOU 434 O LEU A 70 2698 2426 2880 -212 -147 -169 O
ATOM 435 CB LEU A 70 33.290 -13.596 -2.082 1.00 11.65 C
ANISOU 435 CB LEU A 70 1549 1094 1782 -244 -179 -221 C
ATOM 436 CG LEU A 70 34.789 -13.799 -1.790 1.00 24.92 C
ANISOU 436 CG LEU A 70 3264 2755 3449 -205 -155 -204 C
ATOM 437 CD1 LEU A 70 35.000 -14.865 -0.726 1.00 21.00 C
ANISOU 437 CD1 LEU A 70 2768 2207 3004 -222 -138 -159 C
ATOM 438 CD2 LEU A 70 35.569 -14.156 -3.052 1.00 27.14 C
ANISOU 438 CD2 LEU A 70 3583 3014 3715 -174 -168 -260 C
ATOM 439 N VAL A 71 33.794 -11.692 0.623 1.00 16.97 N
ANISOU 439 N VAL A 71 2187 1863 2399 -220 -108 -100 N
ATOM 440 CA VAL A 71 34.620 -10.575 1.061 1.00 19.89 C
ANISOU 440 CA VAL A 71 2562 2275 2719 -186 -89 -83 C
ATOM 441 C VAL A 71 36.046 -11.091 1.207 1.00 22.79 C
ANISOU 441 C VAL A 71 2959 2614 3086 -159 -79 -75 C
ATOM 442 O VAL A 71 36.272 -12.132 1.819 1.00 17.97 O
ANISOU 442 O VAL A 71 2354 1962 2510 -168 -73 -48 O
ATOM 443 CB VAL A 71 34.162 -9.993 2.413 1.00 15.87 C
ANISOU 443 CB VAL A 71 2027 1804 2199 -193 -67 -36 C
ATOM 444 CG1 VAL A 71 35.300 -9.185 3.063 1.00 7.89 C
ANISOU 444 CG1 VAL A 71 1029 820 1147 -160 -50 -19 C
ATOM 445 CG2 VAL A 71 32.891 -9.139 2.244 1.00 12.13 C
ANISOU 445 CG2 VAL A 71 1522 1372 1715 -206 -72 -46 C
ATOM 446 N ILE A 72 37.009 -10.379 0.632 1.00 21.58 N
ANISOU 446 N ILE A 72 2821 2481 2898 -126 -77 -95 N
ATOM 447 CA ILE A 72 38.394 -10.809 0.728 1.00 19.17 C
ANISOU 447 CA ILE A 72 2536 2153 2594 -97 -67 -88 C
ATOM 448 C ILE A 72 39.191 -9.922 1.664 1.00 12.58 C
ANISOU 448 C ILE A 72 1692 1356 1731 -79 -51 -57 C
ATOM 449 O ILE A 72 39.458 -8.770 1.356 1.00 19.21 O
ANISOU 449 O ILE A 72 2528 2232 2538 -66 -48 -69 O
ATOM 450 CB ILE A 72 39.049 -10.896 -0.655 1.00 16.74 C
ANISOU 450 CB ILE A 72 2251 1833 2275 -73 -74 -135 C
ATOM 451 CG1 ILE A 72 38.228 -11.842 -1.527 1.00 13.94 C
ANISOU 451 CG1 ILE A 72 1908 1440 1949 -92 -96 -172 C
ATOM 452 CG2 ILE A 72 40.491 -11.393 -0.533 1.00 18.06 C
ANISOU 452 CG2 ILE A 72 2433 1980 2451 -40 -60 -126 C
ATOM 453 CD1 ILE A 72 38.778 -12.081 -2.889 1.00 17.80 C
ANISOU 453 CD1 ILE A 72 2424 1916 2422 -65 -103 -222 C
ATOM 454 N ASP A 73 39.515 -10.465 2.834 1.00 12.96 N
ANISOU 454 N ASP A 73 1737 1395 1793 -79 -43 -16 N
ATOM 455 CA ASP A 73 40.340 -9.779 3.813 1.00 16.54 C
ANISOU 455 CA ASP A 73 2182 1882 2220 -61 -35 11 C
ATOM 456 C ASP A 73 41.733 -9.649 3.231 1.00 15.88 C
ANISOU 456 C ASP A 73 2106 1795 2131 -29 -34 -6 C
ATOM 457 O ASP A 73 42.428 -10.642 3.097 1.00 14.31 O
ANISOU 457 O ASP A 73 1919 1561 1957 -13 -34 -3 O
ATOM 458 CB ASP A 73 40.422 -10.610 5.090 1.00 26.30 C
ANISOU 458 CB ASP A 73 3418 3105 3470 -63 -29 60 C
ATOM 459 CG ASP A 73 41.291 -9.965 6.184 1.00 32.53 C
ANISOU 459 CG ASP A 73 4200 3934 4227 -42 -27 86 C
ATOM 460 OD1 ASP A 73 42.010 -8.972 5.927 1.00 19.81 O
ANISOU 460 OD1 ASP A 73 2582 2351 2592 -26 -30 64 O
ATOM 461 OD2 ASP A 73 41.254 -10.481 7.326 1.00 39.21 O
ANISOU 461 OD2 ASP A 73 5046 4781 5072 -41 -23 130 O
ATOM 462 N MET A 74 42.134 -8.420 2.917 1.00 19.35 N
ANISOU 462 N MET A 74 2539 2271 2541 -20 -31 -23 N
ATOM 463 CA MET A 74 43.433 -8.130 2.311 1.00 15.81 C
ANISOU 463 CA MET A 74 2091 1827 2089 7 -25 -38 C
ATOM 464 C MET A 74 44.565 -7.893 3.324 1.00 16.35 C
ANISOU 464 C MET A 74 2144 1915 2155 23 -25 -12 C
ATOM 465 O MET A 74 45.726 -7.742 2.931 1.00 16.88 O
ANISOU 465 O MET A 74 2202 1984 2225 44 -20 -20 O
ATOM 466 CB MET A 74 43.313 -6.916 1.382 1.00 10.09 C
ANISOU 466 CB MET A 74 1366 1127 1339 7 -19 -64 C
ATOM 467 CG MET A 74 42.376 -7.143 0.206 1.00 8.03 C
ANISOU 467 CG MET A 74 1121 853 1076 -1 -24 -93 C
ATOM 468 SD MET A 74 42.981 -8.486 -0.836 1.00 20.32 S
ANISOU 468 SD MET A 74 2699 2367 2654 20 -22 -119 S
ATOM 469 CE MET A 74 44.489 -7.770 -1.470 1.00 16.19 C
ANISOU 469 CE MET A 74 2171 1866 2114 52 0 -125 C
ATOM 470 N THR A 75 44.243 -7.847 4.616 1.00 15.34 N
ANISOU 470 N THR A 75 2008 1802 2017 14 -32 17 N
ATOM 471 CA THR A 75 45.276 -7.653 5.643 1.00 16.68 C
ANISOU 471 CA THR A 75 2164 1995 2179 30 -40 39 C
ATOM 472 C THR A 75 46.435 -8.673 5.669 1.00 18.98 C
ANISOU 472 C THR A 75 2453 2263 2497 59 -43 53 C
ATOM 473 O THR A 75 47.501 -8.351 6.168 1.00 22.57 O
ANISOU 473 O THR A 75 2889 2740 2947 76 -52 61 O
ATOM 474 CB THR A 75 44.697 -7.484 7.086 1.00 19.47 C
ANISOU 474 CB THR A 75 2515 2374 2508 21 -47 70 C
ATOM 475 OG1 THR A 75 44.109 -8.707 7.527 1.00 14.60 O
ANISOU 475 OG1 THR A 75 1910 1729 1907 17 -44 101 O
ATOM 476 CG2 THR A 75 43.671 -6.358 7.143 1.00 14.99 C
ANISOU 476 CG2 THR A 75 1946 1834 1915 1 -42 54 C
ATOM 477 N PRO A 76 46.239 -9.900 5.143 1.00 22.60 N
ANISOU 477 N PRO A 76 2929 2675 2984 65 -38 55 N
ATOM 478 CA PRO A 76 47.446 -10.736 5.131 1.00 14.72 C
ANISOU 478 CA PRO A 76 1925 1655 2010 99 -40 65 C
ATOM 479 C PRO A 76 48.442 -10.417 4.012 1.00 23.93 C
ANISOU 479 C PRO A 76 3081 2825 3185 120 -28 33 C
ATOM 480 O PRO A 76 49.592 -10.854 4.116 1.00 26.14 O
ANISOU 480 O PRO A 76 3347 3103 3483 152 -29 42 O
ATOM 481 CB PRO A 76 46.896 -12.159 4.953 1.00 17.52 C
ANISOU 481 CB PRO A 76 2306 1952 2399 99 -38 75 C
ATOM 482 CG PRO A 76 45.480 -12.088 5.394 1.00 20.86 C
ANISOU 482 CG PRO A 76 2738 2375 2812 62 -38 88 C
ATOM 483 CD PRO A 76 45.026 -10.716 4.957 1.00 19.17 C
ANISOU 483 CD PRO A 76 2514 2204 2566 43 -35 58 C
ATOM 484 N LEU A 77 48.034 -9.708 2.964 1.00 19.09 N
ANISOU 484 N LEU A 77 2474 2221 2559 107 -16 -1 N
ATOM 485 CA LEU A 77 49.003 -9.247 1.969 1.00 19.96 C
ANISOU 485 CA LEU A 77 2571 2342 2669 126 0 -25 C
ATOM 486 C LEU A 77 49.647 -7.962 2.485 1.00 25.52 C
ANISOU 486 C LEU A 77 3245 3092 3359 119 -2 -17 C
ATOM 487 O LEU A 77 49.199 -6.853 2.156 1.00 17.91 O
ANISOU 487 O LEU A 77 2281 2149 2375 98 3 -31 O
ATOM 488 CB LEU A 77 48.327 -8.954 0.633 1.00 25.72 C
ANISOU 488 CB LEU A 77 3323 3066 3384 117 14 -60 C
ATOM 489 CG LEU A 77 48.022 -10.061 -0.354 1.00 33.17 C
ANISOU 489 CG LEU A 77 4295 3968 4341 131 20 -87 C
ATOM 490 CD1 LEU A 77 47.696 -9.402 -1.676 1.00 34.01 C
ANISOU 490 CD1 LEU A 77 4415 4089 4419 130 33 -120 C
ATOM 491 CD2 LEU A 77 49.212 -10.976 -0.486 1.00 36.04 C
ANISOU 491 CD2 LEU A 77 4653 4310 4731 171 30 -86 C
ATOM 492 N ASN A 78 50.689 -8.099 3.295 1.00 19.72 N
ANISOU 492 N ASN A 78 2483 2371 2638 137 -13 3 N
ATOM 493 CA ASN A 78 51.251 -6.945 3.985 1.00 16.60 C
ANISOU 493 CA ASN A 78 2058 2017 2233 125 -25 8 C
ATOM 494 C ASN A 78 52.774 -6.830 3.805 1.00 21.76 C
ANISOU 494 C ASN A 78 2671 2687 2911 148 -20 8 C
ATOM 495 O ASN A 78 53.494 -6.393 4.707 1.00 15.89 O
ANISOU 495 O ASN A 78 1896 1972 2171 148 -41 19 O
ATOM 496 CB ASN A 78 50.881 -7.015 5.463 1.00 14.51 C
ANISOU 496 CB ASN A 78 1794 1767 1952 117 -53 33 C
ATOM 497 CG ASN A 78 51.511 -8.209 6.170 1.00 18.85 C
ANISOU 497 CG ASN A 78 2338 2305 2518 148 -67 62 C
ATOM 498 OD1 ASN A 78 51.973 -9.153 5.536 1.00 22.58 O
ANISOU 498 OD1 ASN A 78 2814 2749 3019 174 -56 63 O
ATOM 499 ND2 ASN A 78 51.552 -8.153 7.491 1.00 19.19 N
ANISOU 499 ND2 ASN A 78 2375 2373 2543 149 -94 87 N
ATOM 500 N THR A 79 53.263 -7.242 2.642 1.00 21.16 N
ANISOU 500 N THR A 79 2594 2595 2852 169 8 -5 N
ATOM 501 CA THR A 79 54.680 -7.106 2.352 1.00 21.79 C
ANISOU 501 CA THR A 79 2630 2693 2957 192 21 -5 C
ATOM 502 C THR A 79 55.019 -5.747 1.758 1.00 21.06 C
ANISOU 502 C THR A 79 2514 2625 2862 168 40 -16 C
ATOM 503 O THR A 79 54.390 -5.272 0.803 1.00 18.56 O
ANISOU 503 O THR A 79 2223 2302 2527 155 64 -31 O
ATOM 504 CB THR A 79 55.180 -8.192 1.393 1.00 21.23 C
ANISOU 504 CB THR A 79 2564 2596 2906 232 47 -13 C
ATOM 505 OG1 THR A 79 54.912 -9.458 1.973 1.00 18.16 O
ANISOU 505 OG1 THR A 79 2198 2176 2527 254 29 0 O
ATOM 506 CG2 THR A 79 56.710 -8.063 1.159 1.00 17.98 C
ANISOU 506 CG2 THR A 79 2098 2210 2525 259 64 -9 C
ATOM 507 N ILE A 80 56.016 -5.118 2.353 1.00 17.78 N
ANISOU 507 N ILE A 80 2050 2238 2467 162 28 -8 N
ATOM 508 CA ILE A 80 56.645 -3.952 1.762 1.00 18.21 C
ANISOU 508 CA ILE A 80 2072 2311 2535 143 51 -14 C
ATOM 509 C ILE A 80 57.783 -4.430 0.859 1.00 17.72 C
ANISOU 509 C ILE A 80 1977 2254 2501 175 87 -12 C
ATOM 510 O ILE A 80 58.786 -4.934 1.342 1.00 24.44 O
ANISOU 510 O ILE A 80 2785 3119 3381 199 75 -2 O
ATOM 511 CB ILE A 80 57.194 -3.054 2.859 1.00 21.08 C
ANISOU 511 CB ILE A 80 2396 2701 2913 117 16 -11 C
ATOM 512 CG1 ILE A 80 56.032 -2.515 3.692 1.00 17.16 C
ANISOU 512 CG1 ILE A 80 1936 2202 2383 89 -13 -17 C
ATOM 513 CG2 ILE A 80 58.062 -1.938 2.267 1.00 23.25 C
ANISOU 513 CG2 ILE A 80 2627 2991 3217 95 41 -14 C
ATOM 514 CD1 ILE A 80 56.461 -1.690 4.898 1.00 13.14 C
ANISOU 514 CD1 ILE A 80 1395 1718 1878 66 -54 -22 C
ATOM 515 N HIS A 81 57.622 -4.286 -0.451 1.00 16.92 N
ANISOU 515 N HIS A 81 1895 2146 2389 181 132 -21 N
ATOM 516 CA HIS A 81 58.573 -4.873 -1.399 1.00 12.99 C
ANISOU 516 CA HIS A 81 1374 1653 1909 220 174 -22 C
ATOM 517 C HIS A 81 59.838 -4.029 -1.580 1.00 20.13 C
ANISOU 517 C HIS A 81 2210 2588 2848 211 198 -9 C
ATOM 518 O HIS A 81 60.942 -4.561 -1.641 1.00 20.28 O
ANISOU 518 O HIS A 81 2183 2622 2900 242 211 -3 O
ATOM 519 CB HIS A 81 57.899 -5.124 -2.758 1.00 15.34 C
ANISOU 519 CB HIS A 81 1723 1936 2172 235 212 -39 C
ATOM 520 CG HIS A 81 56.716 -6.042 -2.688 1.00 29.76 C
ANISOU 520 CG HIS A 81 3608 3729 3971 243 189 -55 C
ATOM 521 ND1 HIS A 81 56.828 -7.413 -2.810 1.00 32.72 N
ANISOU 521 ND1 HIS A 81 4000 4079 4355 284 189 -65 N
ATOM 522 CD2 HIS A 81 55.396 -5.790 -2.512 1.00 26.47 C
ANISOU 522 CD2 HIS A 81 3235 3297 3525 215 167 -62 C
ATOM 523 CE1 HIS A 81 55.632 -7.963 -2.707 1.00 31.63 C
ANISOU 523 CE1 HIS A 81 3912 3910 4196 275 166 -78 C
ATOM 524 NE2 HIS A 81 54.746 -7.000 -2.523 1.00 33.84 N
ANISOU 524 NE2 HIS A 81 4207 4199 4452 234 153 -75 N
ATOM 525 N SER A 82 59.678 -2.713 -1.685 1.00 13.84 N
ANISOU 525 N SER A 82 1408 1800 2052 167 204 -5 N
ATOM 526 CA SER A 82 60.827 -1.852 -1.859 1.00 17.88 C
ANISOU 526 CA SER A 82 1855 2336 2605 149 228 9 C
ATOM 527 C SER A 82 60.595 -0.434 -1.333 1.00 22.29 C
ANISOU 527 C SER A 82 2403 2892 3172 93 208 12 C
ATOM 528 O SER A 82 59.477 0.064 -1.313 1.00 23.02 O
ANISOU 528 O SER A 82 2548 2967 3233 71 196 5 O
ATOM 529 CB SER A 82 61.296 -1.841 -3.326 1.00 20.56 C
ANISOU 529 CB SER A 82 2188 2683 2939 172 298 17 C
ATOM 530 OG SER A 82 60.446 -1.082 -4.170 1.00 18.78 O
ANISOU 530 OG SER A 82 2011 2447 2677 152 325 19 O
ATOM 531 N ILE A 83 61.675 0.193 -0.888 1.00 21.77 N
ANISOU 531 N ILE A 83 2269 2846 3158 70 201 20 N
ATOM 532 CA ILE A 83 61.662 1.588 -0.483 1.00 22.39 C
ANISOU 532 CA ILE A 83 2331 2918 3258 15 185 19 C
ATOM 533 C ILE A 83 62.857 2.237 -1.144 1.00 24.76 C
ANISOU 533 C ILE A 83 2564 3232 3610 -2 230 39 C
ATOM 534 O ILE A 83 63.966 1.698 -1.101 1.00 21.88 O
ANISOU 534 O ILE A 83 2137 2894 3283 19 238 46 O
ATOM 535 CB ILE A 83 61.745 1.761 1.057 1.00 24.30 C
ANISOU 535 CB ILE A 83 2551 3167 3512 -6 113 3 C
ATOM 536 CG1 ILE A 83 60.547 1.073 1.733 1.00 22.62 C
ANISOU 536 CG1 ILE A 83 2404 2944 3246 13 75 -10 C
ATOM 537 CG2 ILE A 83 61.827 3.241 1.432 1.00 10.13 C
ANISOU 537 CG2 ILE A 83 738 1362 1747 -63 98 -5 C
ATOM 538 CD1 ILE A 83 60.347 1.435 3.186 1.00 13.43 C
ANISOU 538 CD1 ILE A 83 1237 1788 2077 -9 11 -27 C
ATOM 539 N ASP A 84 62.618 3.383 -1.769 1.00 20.42 N
ANISOU 539 N ASP A 84 2027 2666 3067 -38 263 51 N
ATOM 540 CA ASP A 84 63.633 4.078 -2.540 1.00 20.90 C
ANISOU 540 CA ASP A 84 2031 2735 3176 -59 317 77 C
ATOM 541 C ASP A 84 63.628 5.539 -2.103 1.00 25.71 C
ANISOU 541 C ASP A 84 2624 3319 3824 -123 299 77 C
ATOM 542 O ASP A 84 62.657 6.248 -2.342 1.00 26.20 O
ANISOU 542 O ASP A 84 2746 3351 3858 -141 302 78 O
ATOM 543 CB ASP A 84 63.296 3.958 -4.029 1.00 15.42 C
ANISOU 543 CB ASP A 84 1378 2039 2442 -32 390 100 C
ATOM 544 CG ASP A 84 64.397 4.490 -4.936 1.00 21.29 C
ANISOU 544 CG ASP A 84 2062 2798 3229 -43 459 135 C
ATOM 545 OD1 ASP A 84 64.956 5.570 -4.632 1.00 20.48 O
ANISOU 545 OD1 ASP A 84 1910 2686 3185 -96 458 148 O
ATOM 546 OD2 ASP A 84 64.682 3.832 -5.970 1.00 18.27 O
ANISOU 546 OD2 ASP A 84 1682 2437 2821 2 518 149 O
ATOM 547 N ALA A 85 64.706 5.993 -1.468 1.00 20.11 N
ANISOU 547 N ALA A 85 1837 2621 3183 -157 277 75 N
ATOM 548 CA ALA A 85 64.747 7.361 -0.959 1.00 17.97 C
ANISOU 548 CA ALA A 85 1551 2321 2957 -221 252 67 C
ATOM 549 C ALA A 85 65.023 8.418 -2.036 1.00 24.34 C
ANISOU 549 C ALA A 85 2345 3103 3799 -256 321 105 C
ATOM 550 O ALA A 85 64.723 9.595 -1.833 1.00 27.19 O
ANISOU 550 O ALA A 85 2720 3425 4186 -304 309 102 O
ATOM 551 CB ALA A 85 65.733 7.481 0.189 1.00 16.01 C
ANISOU 551 CB ALA A 85 1224 2092 2769 -248 193 44 C
ATOM 552 N ASP A 86 65.579 8.012 -3.176 1.00 16.10 N
ANISOU 552 N ASP A 86 1280 2082 2756 -229 393 141 N
ATOM 553 CA ASP A 86 65.890 8.975 -4.239 1.00 18.54 C
ANISOU 553 CA ASP A 86 1598 2374 3071 -253 453 180 C
ATOM 554 C ASP A 86 64.622 9.349 -4.986 1.00 25.16 C
ANISOU 554 C ASP A 86 2517 3181 3861 -244 488 198 C
ATOM 555 O ASP A 86 64.317 10.525 -5.168 1.00 26.54 O
ANISOU 555 O ASP A 86 2719 3317 4049 -283 494 213 O
ATOM 556 CB ASP A 86 66.893 8.413 -5.253 1.00 19.61 C
ANISOU 556 CB ASP A 86 1700 2551 3201 -219 514 210 C
ATOM 557 CG ASP A 86 68.244 8.103 -4.641 1.00 25.68 C
ANISOU 557 CG ASP A 86 2384 3352 4020 -226 487 198 C
ATOM 558 OD1 ASP A 86 68.547 8.648 -3.558 1.00 19.33 O
ANISOU 558 OD1 ASP A 86 1546 2537 3261 -269 426 174 O
ATOM 559 OD2 ASP A 86 68.998 7.314 -5.255 1.00 26.83 O
ANISOU 559 OD2 ASP A 86 2500 3538 4158 -185 527 211 O
ATOM 560 N THR A 87 63.894 8.337 -5.434 1.00 18.78 N
ANISOU 560 N THR A 87 1762 2393 2982 -188 499 191 N
ATOM 561 CA THR A 87 62.635 8.571 -6.110 1.00 16.77 C
ANISOU 561 CA THR A 87 1597 2117 2660 -171 514 199 C
ATOM 562 C THR A 87 61.478 8.811 -5.128 1.00 26.32 C
ANISOU 562 C THR A 87 2859 3297 3845 -183 442 162 C
ATOM 563 O THR A 87 60.401 9.228 -5.550 1.00 34.21 O
ANISOU 563 O THR A 87 3925 4273 4800 -177 447 168 O
ATOM 564 CB THR A 87 62.286 7.412 -7.011 1.00 14.89 C
ANISOU 564 CB THR A 87 1398 1909 2349 -106 547 200 C
ATOM 565 OG1 THR A 87 61.970 6.264 -6.204 1.00 18.23 O
ANISOU 565 OG1 THR A 87 1832 2345 2749 -76 491 158 O
ATOM 566 CG2 THR A 87 63.461 7.102 -7.948 1.00 15.57 C
ANISOU 566 CG2 THR A 87 1430 2030 2455 -86 621 233 C
ATOM 567 N LYS A 88 61.713 8.563 -3.835 1.00 24.06 N
ANISOU 567 N LYS A 88 2541 3015 3586 -197 378 125 N
ATOM 568 CA LYS A 88 60.682 8.677 -2.783 1.00 25.98 C
ANISOU 568 CA LYS A 88 2831 3239 3803 -204 310 88 C
ATOM 569 C LYS A 88 59.568 7.630 -2.924 1.00 24.56 C
ANISOU 569 C LYS A 88 2716 3071 3546 -154 298 73 C
ATOM 570 O LYS A 88 58.538 7.719 -2.262 1.00 25.20 O
ANISOU 570 O LYS A 88 2842 3138 3596 -155 255 49 O
ATOM 571 CB LYS A 88 60.057 10.087 -2.723 1.00 25.04 C
ANISOU 571 CB LYS A 88 2743 3072 3698 -244 305 90 C
ATOM 572 CG LYS A 88 60.898 11.164 -2.029 1.00 32.36 C
ANISOU 572 CG LYS A 88 3615 3974 4706 -303 284 83 C
ATOM 573 CD LYS A 88 62.014 11.696 -2.897 1.00 40.48 C
ANISOU 573 CD LYS A 88 4587 4998 5794 -330 346 126 C
ATOM 574 CE LYS A 88 61.472 12.507 -4.056 1.00 52.37 C
ANISOU 574 CE LYS A 88 6141 6472 7286 -333 405 170 C
ATOM 575 NZ LYS A 88 62.575 12.978 -4.950 1.00 54.35 N
ANISOU 575 NZ LYS A 88 6345 6725 7580 -352 467 217 N
ATOM 576 N LEU A 89 59.771 6.650 -3.796 1.00 21.61 N
ANISOU 576 N LEU A 89 2345 2722 3142 -112 337 87 N
ATOM 577 CA LEU A 89 58.747 5.642 -4.060 1.00 25.77 C
ANISOU 577 CA LEU A 89 2933 3257 3604 -68 328 72 C
ATOM 578 C LEU A 89 58.790 4.466 -3.093 1.00 22.37 C
ANISOU 578 C LEU A 89 2492 2842 3167 -46 281 45 C
ATOM 579 O LEU A 89 59.851 3.901 -2.846 1.00 24.46 O
ANISOU 579 O LEU A 89 2702 3128 3465 -35 282 46 O
ATOM 580 CB LEU A 89 58.862 5.121 -5.497 1.00 17.82 C
ANISOU 580 CB LEU A 89 1943 2266 2562 -30 390 93 C
ATOM 581 CG LEU A 89 58.819 6.207 -6.567 1.00 21.83 C
ANISOU 581 CG LEU A 89 2466 2763 3066 -45 443 129 C
ATOM 582 CD1 LEU A 89 59.057 5.613 -7.952 1.00 19.00 C
ANISOU 582 CD1 LEU A 89 2122 2430 2666 -1 506 148 C
ATOM 583 CD2 LEU A 89 57.496 6.965 -6.491 1.00 16.89 C
ANISOU 583 CD2 LEU A 89 1901 2107 2408 -58 418 125 C
ATOM 584 N VAL A 90 57.630 4.099 -2.555 1.00 16.88 N
ANISOU 584 N VAL A 90 1846 2136 2430 -37 241 24 N
ATOM 585 CA VAL A 90 57.489 2.830 -1.840 1.00 17.46 C
ANISOU 585 CA VAL A 90 1923 2221 2488 -9 206 6 C
ATOM 586 C VAL A 90 56.544 1.904 -2.611 1.00 20.79 C
ANISOU 586 C VAL A 90 2402 2638 2859 26 219 0 C
ATOM 587 O VAL A 90 55.531 2.339 -3.145 1.00 20.89 O
ANISOU 587 O VAL A 90 2461 2638 2838 22 227 0 O
ATOM 588 CB VAL A 90 57.027 3.001 -0.361 1.00 21.91 C
ANISOU 588 CB VAL A 90 2491 2782 3053 -29 144 -13 C
ATOM 589 CG1 VAL A 90 58.004 3.885 0.398 1.00 20.81 C
ANISOU 589 CG1 VAL A 90 2295 2647 2964 -64 123 -16 C
ATOM 590 CG2 VAL A 90 55.605 3.565 -0.277 1.00 16.57 C
ANISOU 590 CG2 VAL A 90 1871 2085 2338 -41 131 -23 C
ATOM 591 N ASP A 91 56.919 0.628 -2.689 1.00 26.97 N
ANISOU 591 N ASP A 91 3179 3430 3640 63 222 -5 N
ATOM 592 CA ASP A 91 56.184 -0.386 -3.431 1.00 18.31 C
ANISOU 592 CA ASP A 91 2130 2325 2502 97 233 -17 C
ATOM 593 C ASP A 91 55.675 -1.409 -2.418 1.00 22.70 C
ANISOU 593 C ASP A 91 2701 2872 3054 107 187 -30 C
ATOM 594 O ASP A 91 56.438 -2.231 -1.904 1.00 22.17 O
ANISOU 594 O ASP A 91 2604 2809 3010 128 176 -28 O
ATOM 595 CB ASP A 91 57.119 -1.017 -4.469 1.00 20.75 C
ANISOU 595 CB ASP A 91 2420 2647 2815 134 281 -12 C
ATOM 596 CG ASP A 91 56.457 -2.115 -5.290 1.00 24.87 C
ANISOU 596 CG ASP A 91 2993 3159 3297 172 291 -33 C
ATOM 597 OD1 ASP A 91 55.287 -2.452 -5.017 1.00 26.92 O
ANISOU 597 OD1 ASP A 91 3297 3400 3530 167 258 -48 O
ATOM 598 OD2 ASP A 91 57.123 -2.649 -6.211 1.00 21.64 O
ANISOU 598 OD2 ASP A 91 2578 2761 2883 208 333 -35 O
ATOM 599 N ILE A 92 54.383 -1.339 -2.101 1.00 21.15 N
ANISOU 599 N ILE A 92 2547 2661 2827 93 161 -39 N
ATOM 600 CA ILE A 92 53.845 -2.144 -1.014 1.00 17.74 C
ANISOU 600 CA ILE A 92 2128 2221 2393 96 119 -44 C
ATOM 601 C ILE A 92 52.562 -2.877 -1.363 1.00 16.36 C
ANISOU 601 C ILE A 92 2003 2026 2187 103 112 -57 C
ATOM 602 O ILE A 92 51.793 -2.418 -2.203 1.00 22.66 O
ANISOU 602 O ILE A 92 2831 2821 2959 97 126 -64 O
ATOM 603 CB ILE A 92 53.618 -1.310 0.279 1.00 24.41 C
ANISOU 603 CB ILE A 92 2959 3073 3242 64 83 -41 C
ATOM 604 CG1 ILE A 92 52.369 -0.427 0.171 1.00 26.11 C
ANISOU 604 CG1 ILE A 92 3210 3281 3431 40 79 -48 C
ATOM 605 CG2 ILE A 92 54.855 -0.499 0.621 1.00 19.57 C
ANISOU 605 CG2 ILE A 92 2294 2477 2665 49 84 -34 C
ATOM 606 CD1 ILE A 92 52.506 0.780 -0.752 1.00 6.37 C
ANISOU 606 CD1 ILE A 92 708 780 932 26 109 -44 C
ATOM 607 N ASP A 93 52.346 -4.024 -0.716 1.00 17.01 N
ANISOU 607 N ASP A 93 2094 2094 2274 117 90 -57 N
ATOM 608 CA ASP A 93 51.069 -4.746 -0.815 1.00 24.20 C
ANISOU 608 CA ASP A 93 3047 2983 3165 115 77 -67 C
ATOM 609 C ASP A 93 49.906 -3.861 -0.341 1.00 21.85 C
ANISOU 609 C ASP A 93 2764 2692 2846 84 59 -67 C
ATOM 610 O ASP A 93 50.093 -2.972 0.484 1.00 12.99 O
ANISOU 610 O ASP A 93 1622 1586 1727 66 47 -58 O
ATOM 611 CB ASP A 93 51.088 -6.015 0.037 1.00 18.69 C
ANISOU 611 CB ASP A 93 2351 2267 2485 129 55 -58 C
ATOM 612 CG ASP A 93 51.872 -7.159 -0.595 1.00 17.46 C
ANISOU 612 CG ASP A 93 2195 2091 2348 167 72 -65 C
ATOM 613 OD1 ASP A 93 52.147 -7.148 -1.812 1.00 16.40 O
ANISOU 613 OD1 ASP A 93 2068 1957 2206 184 100 -84 O
ATOM 614 OD2 ASP A 93 52.207 -8.096 0.144 1.00 17.44 O
ANISOU 614 OD2 ASP A 93 2187 2073 2367 184 56 -52 O
ATOM 615 N ALA A 94 48.703 -4.123 -0.841 1.00 19.49 N
ANISOU 615 N ALA A 94 2497 2380 2527 78 56 -79 N
ATOM 616 CA ALA A 94 47.542 -3.303 -0.483 1.00 13.24 C
ANISOU 616 CA ALA A 94 1717 1596 1716 53 42 -79 C
ATOM 617 C ALA A 94 47.115 -3.472 0.972 1.00 13.26 C
ANISOU 617 C ALA A 94 1712 1602 1723 40 17 -65 C
ATOM 618 O ALA A 94 46.402 -2.631 1.524 1.00 18.57 O
ANISOU 618 O ALA A 94 2386 2288 2382 22 8 -64 O
ATOM 619 CB ALA A 94 46.384 -3.608 -1.395 1.00 13.59 C
ANISOU 619 CB ALA A 94 1791 1630 1742 53 41 -96 C
ATOM 620 N GLY A 95 47.532 -4.572 1.585 1.00 15.08 N
ANISOU 620 N GLY A 95 1938 1821 1970 51 8 -54 N
ATOM 621 CA GLY A 95 47.153 -4.848 2.952 1.00 14.99 C
ANISOU 621 CA GLY A 95 1923 1815 1956 42 -12 -35 C
ATOM 622 C GLY A 95 48.077 -4.199 3.961 1.00 17.04 C
ANISOU 622 C GLY A 95 2157 2101 2216 43 -24 -24 C
ATOM 623 O GLY A 95 47.813 -4.266 5.153 1.00 12.30 O
ANISOU 623 O GLY A 95 1555 1514 1605 39 -41 -9 O
ATOM 624 N VAL A 96 49.163 -3.567 3.516 1.00 22.22 N
ANISOU 624 N VAL A 96 2790 2766 2884 48 -15 -32 N
ATOM 625 CA VAL A 96 50.017 -2.925 4.505 1.00 17.22 C
ANISOU 625 CA VAL A 96 2128 2158 2255 45 -34 -27 C
ATOM 626 C VAL A 96 49.323 -1.689 5.033 1.00 14.21 C
ANISOU 626 C VAL A 96 1754 1792 1854 21 -43 -37 C
ATOM 627 O VAL A 96 48.645 -0.986 4.294 1.00 12.69 O
ANISOU 627 O VAL A 96 1576 1591 1653 9 -28 -49 O
ATOM 628 CB VAL A 96 51.510 -2.668 4.067 1.00 17.65 C
ANISOU 628 CB VAL A 96 2146 2220 2339 54 -25 -29 C
ATOM 629 CG1 VAL A 96 51.892 -3.468 2.862 1.00 18.96 C
ANISOU 629 CG1 VAL A 96 2315 2368 2520 76 3 -30 C
ATOM 630 CG2 VAL A 96 51.821 -1.205 3.913 1.00 16.63 C
ANISOU 630 CG2 VAL A 96 2000 2103 2215 31 -21 -42 C
ATOM 631 N ASN A 97 49.447 -1.466 6.335 1.00 11.77 N
ANISOU 631 N ASN A 97 1435 1504 1531 18 -69 -34 N
ATOM 632 CA ASN A 97 48.776 -0.344 6.957 1.00 14.00 C
ANISOU 632 CA ASN A 97 1727 1801 1792 1 -79 -49 C
ATOM 633 C ASN A 97 49.730 0.840 7.129 1.00 16.23 C
ANISOU 633 C ASN A 97 1984 2092 2091 -12 -90 -68 C
ATOM 634 O ASN A 97 50.945 0.690 7.015 1.00 16.00 O
ANISOU 634 O ASN A 97 1924 2067 2087 -8 -95 -65 O
ATOM 635 CB ASN A 97 48.091 -0.762 8.262 1.00 10.54 C
ANISOU 635 CB ASN A 97 1301 1381 1321 6 -97 -37 C
ATOM 636 CG ASN A 97 49.081 -1.083 9.368 1.00 20.97 C
ANISOU 636 CG ASN A 97 2603 2727 2637 19 -126 -27 C
ATOM 637 OD1 ASN A 97 49.735 -0.186 9.900 1.00 22.36 O
ANISOU 637 OD1 ASN A 97 2762 2922 2811 12 -148 -47 O
ATOM 638 ND2 ASN A 97 49.178 -2.364 9.737 1.00 12.85 N
ANISOU 638 ND2 ASN A 97 1579 1698 1607 38 -130 3 N
ATOM 639 N LEU A 98 49.173 2.017 7.376 1.00 15.49 N
ANISOU 639 N LEU A 98 1900 1998 1985 -28 -94 -88 N
ATOM 640 CA LEU A 98 49.947 3.255 7.324 1.00 11.94 C
ANISOU 640 CA LEU A 98 1432 1545 1560 -47 -100 -108 C
ATOM 641 C LEU A 98 50.894 3.397 8.504 1.00 16.14 C
ANISOU 641 C LEU A 98 1938 2102 2094 -49 -138 -120 C
ATOM 642 O LEU A 98 51.938 4.023 8.398 1.00 17.30 O
ANISOU 642 O LEU A 98 2052 2246 2274 -65 -147 -132 O
ATOM 643 CB LEU A 98 49.030 4.456 7.247 1.00 10.38 C
ANISOU 643 CB LEU A 98 1257 1334 1352 -60 -93 -128 C
ATOM 644 CG LEU A 98 48.153 4.525 6.003 1.00 17.65 C
ANISOU 644 CG LEU A 98 2201 2233 2273 -57 -61 -118 C
ATOM 645 CD1 LEU A 98 47.494 5.912 5.905 1.00 14.02 C
ANISOU 645 CD1 LEU A 98 1757 1756 1812 -67 -56 -136 C
ATOM 646 CD2 LEU A 98 48.963 4.200 4.755 1.00 7.32 C
ANISOU 646 CD2 LEU A 98 878 912 992 -56 -36 -102 C
ATOM 647 N ASP A 99 50.513 2.808 9.627 1.00 20.17 N
ANISOU 647 N ASP A 99 2460 2638 2567 -34 -161 -115 N
ATOM 648 CA ASP A 99 51.387 2.710 10.775 1.00 23.75 C
ANISOU 648 CA ASP A 99 2890 3122 3012 -29 -202 -122 C
ATOM 649 C ASP A 99 52.639 1.913 10.404 1.00 20.30 C
ANISOU 649 C ASP A 99 2415 2688 2610 -18 -206 -102 C
ATOM 650 O ASP A 99 53.768 2.367 10.611 1.00 24.60 O
ANISOU 650 O ASP A 99 2920 3243 3182 -28 -230 -116 O
ATOM 651 CB ASP A 99 50.643 2.020 11.913 1.00 36.01 C
ANISOU 651 CB ASP A 99 4469 4703 4511 -8 -217 -108 C
ATOM 652 CG ASP A 99 51.255 2.305 13.254 1.00 48.27 C
ANISOU 652 CG ASP A 99 6010 6294 6037 -1 -263 -125 C
ATOM 653 OD1 ASP A 99 51.508 1.339 14.007 1.00 60.90 O
ANISOU 653 OD1 ASP A 99 7608 7920 7611 23 -282 -99 O
ATOM 654 OD2 ASP A 99 51.476 3.498 13.551 1.00 45.13 O
ANISOU 654 OD2 ASP A 99 5607 5897 5643 -20 -283 -165 O
ATOM 655 N GLN A 100 52.420 0.724 9.850 1.00 15.48 N
ANISOU 655 N GLN A 100 1814 2067 2001 2 -183 -72 N
ATOM 656 CA GLN A 100 53.485 -0.160 9.395 1.00 18.84 C
ANISOU 656 CA GLN A 100 2209 2491 2459 20 -180 -52 C
ATOM 657 C GLN A 100 54.425 0.551 8.421 1.00 28.37 C
ANISOU 657 C GLN A 100 3380 3687 3714 3 -162 -65 C
ATOM 658 O GLN A 100 55.648 0.493 8.553 1.00 29.31 O
ANISOU 658 O GLN A 100 3452 3821 3864 7 -178 -64 O
ATOM 659 CB GLN A 100 52.864 -1.388 8.734 1.00 8.84 C
ANISOU 659 CB GLN A 100 969 1201 1190 40 -151 -26 C
ATOM 660 CG GLN A 100 53.843 -2.369 8.127 1.00 10.18 C
ANISOU 660 CG GLN A 100 1113 1362 1393 65 -140 -9 C
ATOM 661 CD GLN A 100 53.137 -3.473 7.336 1.00 24.52 C
ANISOU 661 CD GLN A 100 2961 3145 3208 81 -111 6 C
ATOM 662 OE1 GLN A 100 51.907 -3.489 7.229 1.00 24.14 O
ANISOU 662 OE1 GLN A 100 2950 3084 3138 70 -100 5 O
ATOM 663 NE2 GLN A 100 53.917 -4.397 6.776 1.00 21.91 N
ANISOU 663 NE2 GLN A 100 2616 2803 2907 108 -99 17 N
ATOM 664 N LEU A 101 53.836 1.234 7.449 1.00 20.21 N
ANISOU 664 N LEU A 101 2365 2628 2686 -15 -129 -73 N
ATOM 665 CA LEU A 101 54.593 1.953 6.437 1.00 14.31 C
ANISOU 665 CA LEU A 101 1589 1867 1981 -32 -103 -78 C
ATOM 666 C LEU A 101 55.355 3.149 7.017 1.00 22.44 C
ANISOU 666 C LEU A 101 2584 2905 3037 -62 -129 -101 C
ATOM 667 O LEU A 101 56.477 3.450 6.603 1.00 20.33 O
ANISOU 667 O LEU A 101 2270 2640 2815 -73 -122 -99 O
ATOM 668 CB LEU A 101 53.649 2.429 5.340 1.00 11.35 C
ANISOU 668 CB LEU A 101 1251 1466 1597 -41 -64 -78 C
ATOM 669 CG LEU A 101 54.206 3.288 4.211 1.00 17.27 C
ANISOU 669 CG LEU A 101 1983 2199 2381 -58 -29 -76 C
ATOM 670 CD1 LEU A 101 55.321 2.532 3.500 1.00 15.88 C
ANISOU 670 CD1 LEU A 101 1771 2031 2234 -40 -6 -59 C
ATOM 671 CD2 LEU A 101 53.085 3.654 3.246 1.00 12.59 C
ANISOU 671 CD2 LEU A 101 1435 1585 1766 -59 2 -73 C
ATOM 672 N MET A 102 54.730 3.845 7.956 1.00 25.12 N
ANISOU 672 N MET A 102 2945 3249 3350 -75 -159 -123 N
ATOM 673 CA MET A 102 55.347 5.017 8.548 1.00 27.32 C
ANISOU 673 CA MET A 102 3198 3530 3653 -105 -189 -153 C
ATOM 674 C MET A 102 56.632 4.592 9.252 1.00 24.36 C
ANISOU 674 C MET A 102 2769 3187 3299 -100 -228 -155 C
ATOM 675 O MET A 102 57.661 5.240 9.129 1.00 24.26 O
ANISOU 675 O MET A 102 2709 3174 3336 -125 -237 -167 O
ATOM 676 CB MET A 102 54.388 5.704 9.521 1.00 24.05 C
ANISOU 676 CB MET A 102 2823 3118 3199 -111 -215 -183 C
ATOM 677 CG MET A 102 55.046 6.802 10.353 1.00 35.01 C
ANISOU 677 CG MET A 102 4186 4509 4606 -139 -258 -223 C
ATOM 678 SD MET A 102 53.889 7.673 11.434 1.00 42.49 S
ANISOU 678 SD MET A 102 5184 5457 5503 -140 -284 -265 S
ATOM 679 CE MET A 102 54.946 8.073 12.826 1.00115.70 C
ANISOU 679 CE MET A 102 14423 14764 14776 -151 -355 -308 C
ATOM 680 N LYS A 103 56.557 3.472 9.960 1.00 21.62 N
ANISOU 680 N LYS A 103 2429 2868 2917 -66 -250 -139 N
ATOM 681 CA LYS A 103 57.687 2.946 10.699 1.00 20.84 C
ANISOU 681 CA LYS A 103 2284 2805 2830 -52 -292 -136 C
ATOM 682 C LYS A 103 58.814 2.483 9.781 1.00 22.60 C
ANISOU 682 C LYS A 103 2453 3025 3108 -45 -267 -115 C
ATOM 683 O LYS A 103 59.987 2.712 10.066 1.00 24.93 O
ANISOU 683 O LYS A 103 2689 3342 3442 -54 -295 -123 O
ATOM 684 CB LYS A 103 57.234 1.802 11.589 1.00 20.05 C
ANISOU 684 CB LYS A 103 2211 2730 2677 -12 -314 -115 C
ATOM 685 CG LYS A 103 58.362 1.058 12.231 1.00 31.20 C
ANISOU 685 CG LYS A 103 3579 4178 4099 14 -353 -101 C
ATOM 686 CD LYS A 103 57.863 0.123 13.301 1.00 37.18 C
ANISOU 686 CD LYS A 103 4368 4960 4797 50 -380 -78 C
ATOM 687 CE LYS A 103 59.022 -0.667 13.878 1.00 42.64 C
ANISOU 687 CE LYS A 103 5014 5687 5499 83 -420 -58 C
ATOM 688 NZ LYS A 103 58.603 -1.473 15.050 1.00 42.49 N
ANISOU 688 NZ LYS A 103 5028 5697 5418 119 -451 -33 N
ATOM 689 N ALA A 104 58.451 1.843 8.675 1.00 19.50 N
ANISOU 689 N ALA A 104 2081 2610 2719 -28 -215 -90 N
ATOM 690 CA ALA A 104 59.426 1.319 7.735 1.00 18.86 C
ANISOU 690 CA ALA A 104 1956 2527 2682 -14 -183 -70 C
ATOM 691 C ALA A 104 60.098 2.415 6.895 1.00 22.68 C
ANISOU 691 C ALA A 104 2400 2998 3219 -51 -154 -79 C
ATOM 692 O ALA A 104 61.257 2.279 6.495 1.00 19.68 O
ANISOU 692 O ALA A 104 1960 2632 2887 -48 -143 -69 O
ATOM 693 CB ALA A 104 58.767 0.282 6.826 1.00 16.68 C
ANISOU 693 CB ALA A 104 1721 2230 2388 17 -138 -48 C
ATOM 694 N ALA A 105 59.374 3.503 6.639 1.00 18.71 N
ANISOU 694 N ALA A 105 1929 2470 2710 -85 -141 -94 N
ATOM 695 CA ALA A 105 59.859 4.540 5.733 1.00 21.92 C
ANISOU 695 CA ALA A 105 2309 2855 3165 -120 -105 -94 C
ATOM 696 C ALA A 105 60.606 5.695 6.412 1.00 19.82 C
ANISOU 696 C ALA A 105 1997 2591 2943 -165 -143 -120 C
ATOM 697 O ALA A 105 61.466 6.330 5.792 1.00 21.46 O
ANISOU 697 O ALA A 105 2155 2789 3209 -193 -118 -113 O
ATOM 698 CB ALA A 105 58.716 5.072 4.865 1.00 13.97 C
ANISOU 698 CB ALA A 105 1361 1813 2134 -129 -63 -89 C
ATOM 699 N LEU A 106 60.262 5.967 7.669 1.00 15.40 N
ANISOU 699 N LEU A 106 1453 2042 2355 -171 -201 -151 N
ATOM 700 CA LEU A 106 60.923 7.017 8.455 1.00 25.93 C
ANISOU 700 CA LEU A 106 2748 3378 3726 -212 -248 -187 C
ATOM 701 C LEU A 106 62.461 7.010 8.383 1.00 31.69 C
ANISOU 701 C LEU A 106 3388 4129 4524 -228 -260 -182 C
ATOM 702 O LEU A 106 63.057 8.046 8.091 1.00 34.35 O
ANISOU 702 O LEU A 106 3685 4443 4922 -275 -254 -193 O
ATOM 703 CB LEU A 106 60.453 6.995 9.912 1.00 20.39 C
ANISOU 703 CB LEU A 106 2074 2700 2973 -202 -314 -220 C
ATOM 704 CG LEU A 106 59.334 7.977 10.273 1.00 19.44 C
ANISOU 704 CG LEU A 106 2014 2551 2821 -220 -320 -252 C
ATOM 705 CD1 LEU A 106 58.867 7.789 11.718 1.00 16.53 C
ANISOU 705 CD1 LEU A 106 1675 2216 2389 -200 -379 -282 C
ATOM 706 CD2 LEU A 106 59.768 9.410 10.037 1.00 16.15 C
ANISOU 706 CD2 LEU A 106 1574 2095 2466 -274 -321 -280 C
ATOM 707 N PRO A 107 63.103 5.842 8.607 1.00 25.11 N
ANISOU 707 N PRO A 107 2520 3336 3686 -188 -274 -163 N
ATOM 708 CA PRO A 107 64.571 5.834 8.571 1.00 30.60 C
ANISOU 708 CA PRO A 107 3121 4056 4448 -200 -287 -159 C
ATOM 709 C PRO A 107 65.143 6.240 7.220 1.00 33.88 C
ANISOU 709 C PRO A 107 3498 4449 4927 -223 -217 -133 C
ATOM 710 O PRO A 107 66.322 6.597 7.137 1.00 33.46 O
ANISOU 710 O PRO A 107 3368 4410 4937 -248 -221 -132 O
ATOM 711 CB PRO A 107 64.928 4.374 8.860 1.00 28.42 C
ANISOU 711 CB PRO A 107 2831 3821 4148 -140 -301 -135 C
ATOM 712 CG PRO A 107 63.692 3.783 9.505 1.00 25.67 C
ANISOU 712 CG PRO A 107 2565 3471 3717 -108 -319 -137 C
ATOM 713 CD PRO A 107 62.557 4.491 8.866 1.00 16.55 C
ANISOU 713 CD PRO A 107 1474 2271 2541 -132 -276 -142 C
ATOM 714 N PHE A 108 64.324 6.191 6.178 1.00 27.27 N
ANISOU 714 N PHE A 108 2717 3581 4065 -213 -153 -110 N
ATOM 715 CA PHE A 108 64.756 6.646 4.865 1.00 20.31 C
ANISOU 715 CA PHE A 108 1808 2678 3230 -233 -81 -82 C
ATOM 716 C PHE A 108 64.517 8.141 4.680 1.00 25.32 C
ANISOU 716 C PHE A 108 2453 3268 3897 -293 -72 -94 C
ATOM 717 O PHE A 108 64.771 8.673 3.603 1.00 24.54 O
ANISOU 717 O PHE A 108 2342 3148 3836 -313 -10 -66 O
ATOM 718 CB PHE A 108 64.022 5.890 3.767 1.00 14.90 C
ANISOU 718 CB PHE A 108 1180 1984 2499 -191 -18 -51 C
ATOM 719 CG PHE A 108 64.457 4.467 3.610 1.00 30.33 C
ANISOU 719 CG PHE A 108 3116 3970 4440 -134 -8 -34 C
ATOM 720 CD1 PHE A 108 65.365 4.111 2.607 1.00 32.00 C
ANISOU 720 CD1 PHE A 108 3276 4196 4689 -118 48 -7 C
ATOM 721 CD2 PHE A 108 63.957 3.474 4.444 1.00 27.38 C
ANISOU 721 CD2 PHE A 108 2776 3611 4016 -95 -52 -43 C
ATOM 722 CE1 PHE A 108 65.763 2.791 2.434 1.00 25.34 C
ANISOU 722 CE1 PHE A 108 2417 3376 3834 -60 59 6 C
ATOM 723 CE2 PHE A 108 64.360 2.141 4.286 1.00 25.76 C
ANISOU 723 CE2 PHE A 108 2557 3428 3804 -41 -43 -26 C
ATOM 724 CZ PHE A 108 65.262 1.800 3.277 1.00 26.00 C
ANISOU 724 CZ PHE A 108 2537 3468 3872 -22 12 -4 C
ATOM 725 N GLY A 109 64.018 8.817 5.714 1.00 24.37 N
ANISOU 725 N GLY A 109 2361 3135 3763 -317 -130 -134 N
ATOM 726 CA GLY A 109 63.607 10.208 5.573 1.00 23.18 C
ANISOU 726 CA GLY A 109 2236 2933 3639 -367 -123 -150 C
ATOM 727 C GLY A 109 62.371 10.374 4.680 1.00 28.73 C
ANISOU 727 C GLY A 109 3019 3600 4296 -351 -69 -127 C
ATOM 728 O GLY A 109 62.218 11.373 3.970 1.00 26.13 O
ANISOU 728 O GLY A 109 2702 3227 3998 -383 -30 -114 O
ATOM 729 N LEU A 110 61.487 9.382 4.705 1.00 26.95 N
ANISOU 729 N LEU A 110 2847 3393 3998 -301 -67 -121 N
ATOM 730 CA LEU A 110 60.247 9.447 3.945 1.00 21.76 C
ANISOU 730 CA LEU A 110 2264 2711 3294 -283 -26 -105 C
ATOM 731 C LEU A 110 59.030 9.480 4.868 1.00 24.77 C
ANISOU 731 C LEU A 110 2707 3087 3617 -270 -68 -136 C
ATOM 732 O LEU A 110 58.979 8.774 5.874 1.00 27.01 O
ANISOU 732 O LEU A 110 2991 3404 3869 -249 -114 -155 O
ATOM 733 CB LEU A 110 60.149 8.270 2.982 1.00 13.28 C
ANISOU 733 CB LEU A 110 1201 1657 2188 -237 21 -70 C
ATOM 734 CG LEU A 110 61.292 8.150 1.985 1.00 16.56 C
ANISOU 734 CG LEU A 110 1559 2083 2652 -241 73 -37 C
ATOM 735 CD1 LEU A 110 61.011 7.010 1.020 1.00 18.23 C
ANISOU 735 CD1 LEU A 110 1796 2310 2820 -190 119 -11 C
ATOM 736 CD2 LEU A 110 61.519 9.456 1.235 1.00 14.49 C
ANISOU 736 CD2 LEU A 110 1287 1783 2438 -285 114 -19 C
ATOM 737 N TRP A 111 58.052 10.301 4.500 1.00 23.52 N
ANISOU 737 N TRP A 111 2601 2890 3444 -279 -49 -138 N
ATOM 738 CA TRP A 111 56.868 10.549 5.318 1.00 23.28 C
ANISOU 738 CA TRP A 111 2627 2854 3366 -269 -82 -168 C
ATOM 739 C TRP A 111 55.616 10.161 4.535 1.00 20.84 C
ANISOU 739 C TRP A 111 2377 2537 3006 -236 -44 -145 C
ATOM 740 O TRP A 111 55.493 10.493 3.359 1.00 14.68 O
ANISOU 740 O TRP A 111 1607 1733 2237 -238 3 -116 O
ATOM 741 CB TRP A 111 56.804 12.040 5.656 1.00 22.59 C
ANISOU 741 CB TRP A 111 2547 2722 3316 -309 -98 -197 C
ATOM 742 CG TRP A 111 55.751 12.436 6.645 1.00 25.48 C
ANISOU 742 CG TRP A 111 2962 3082 3638 -299 -135 -238 C
ATOM 743 CD1 TRP A 111 54.613 13.154 6.394 1.00 25.43 C
ANISOU 743 CD1 TRP A 111 3009 3040 3612 -293 -118 -242 C
ATOM 744 CD2 TRP A 111 55.748 12.163 8.050 1.00 21.16 C
ANISOU 744 CD2 TRP A 111 2414 2568 3059 -291 -194 -279 C
ATOM 745 NE1 TRP A 111 53.899 13.331 7.551 1.00 24.32 N
ANISOU 745 NE1 TRP A 111 2900 2909 3432 -281 -159 -284 N
ATOM 746 CE2 TRP A 111 54.575 12.734 8.583 1.00 24.69 C
ANISOU 746 CE2 TRP A 111 2915 2998 3466 -279 -205 -308 C
ATOM 747 CE3 TRP A 111 56.617 11.484 8.907 1.00 21.13 C
ANISOU 747 CE3 TRP A 111 2367 2609 3052 -287 -238 -292 C
ATOM 748 CZ2 TRP A 111 54.256 12.651 9.937 1.00 25.42 C
ANISOU 748 CZ2 TRP A 111 3024 3121 3514 -266 -255 -350 C
ATOM 749 CZ3 TRP A 111 56.297 11.403 10.253 1.00 25.29 C
ANISOU 749 CZ3 TRP A 111 2912 3164 3531 -274 -291 -332 C
ATOM 750 CH2 TRP A 111 55.128 11.979 10.753 1.00 23.35 C
ANISOU 750 CH2 TRP A 111 2723 2904 3244 -263 -297 -361 C
ATOM 751 N VAL A 112 54.695 9.452 5.174 1.00 15.93 N
ANISOU 751 N VAL A 112 1789 1937 2326 -207 -67 -157 N
ATOM 752 CA VAL A 112 53.446 9.093 4.510 1.00 19.04 C
ANISOU 752 CA VAL A 112 2234 2325 2675 -180 -38 -140 C
ATOM 753 C VAL A 112 52.723 10.384 4.090 1.00 18.97 C
ANISOU 753 C VAL A 112 2258 2275 2675 -194 -22 -144 C
ATOM 754 O VAL A 112 52.456 11.247 4.919 1.00 22.62 O
ANISOU 754 O VAL A 112 2731 2721 3143 -208 -50 -176 O
ATOM 755 CB VAL A 112 52.561 8.196 5.407 1.00 16.21 C
ANISOU 755 CB VAL A 112 1902 1996 2262 -152 -66 -152 C
ATOM 756 CG1 VAL A 112 51.247 7.910 4.746 1.00 16.10 C
ANISOU 756 CG1 VAL A 112 1933 1975 2210 -130 -41 -138 C
ATOM 757 CG2 VAL A 112 53.275 6.886 5.713 1.00 11.50 C
ANISOU 757 CG2 VAL A 112 1277 1433 1660 -133 -78 -140 C
ATOM 758 N PRO A 113 52.440 10.525 2.785 1.00 17.52 N
ANISOU 758 N PRO A 113 2091 2073 2492 -187 23 -112 N
ATOM 759 CA PRO A 113 52.066 11.817 2.191 1.00 17.30 C
ANISOU 759 CA PRO A 113 2086 2001 2486 -202 45 -104 C
ATOM 760 C PRO A 113 50.672 12.317 2.592 1.00 16.02 C
ANISOU 760 C PRO A 113 1971 1824 2290 -186 30 -123 C
ATOM 761 O PRO A 113 50.430 13.521 2.605 1.00 23.26 O
ANISOU 761 O PRO A 113 2905 2701 3232 -200 31 -131 O
ATOM 762 CB PRO A 113 52.161 11.550 0.681 1.00 19.81 C
ANISOU 762 CB PRO A 113 2409 2318 2799 -188 97 -59 C
ATOM 763 CG PRO A 113 51.948 10.097 0.546 1.00 24.83 C
ANISOU 763 CG PRO A 113 3047 2994 3392 -157 96 -56 C
ATOM 764 CD PRO A 113 52.570 9.469 1.765 1.00 17.56 C
ANISOU 764 CD PRO A 113 2094 2099 2479 -163 57 -81 C
ATOM 765 N VAL A 114 49.779 11.397 2.926 1.00 20.67 N
ANISOU 765 N VAL A 114 2580 2446 2828 -157 17 -130 N
ATOM 766 CA VAL A 114 48.459 11.740 3.434 1.00 19.35 C
ANISOU 766 CA VAL A 114 2448 2274 2628 -139 3 -149 C
ATOM 767 C VAL A 114 48.164 10.848 4.641 1.00 23.66 C
ANISOU 767 C VAL A 114 2991 2859 3138 -127 -29 -172 C
ATOM 768 O VAL A 114 48.168 9.626 4.532 1.00 21.97 O
ANISOU 768 O VAL A 114 2770 2675 2902 -113 -27 -157 O
ATOM 769 CB VAL A 114 47.370 11.576 2.342 1.00 14.57 C
ANISOU 769 CB VAL A 114 1875 1667 1994 -113 30 -122 C
ATOM 770 CG1 VAL A 114 45.963 11.720 2.933 1.00 9.67 C
ANISOU 770 CG1 VAL A 114 1281 1053 1339 -91 15 -141 C
ATOM 771 CG2 VAL A 114 47.584 12.592 1.198 1.00 14.73 C
ANISOU 771 CG2 VAL A 114 1905 1648 2043 -121 62 -95 C
ATOM 772 N LEU A 115 47.940 11.467 5.795 1.00 24.70 N
ANISOU 772 N LEU A 115 3130 2990 3266 -131 -57 -207 N
ATOM 773 CA LEU A 115 47.650 10.737 7.025 1.00 24.97 C
ANISOU 773 CA LEU A 115 3164 3063 3259 -118 -86 -227 C
ATOM 774 C LEU A 115 46.285 11.107 7.603 1.00 24.43 C
ANISOU 774 C LEU A 115 3128 3000 3155 -96 -89 -245 C
ATOM 775 O LEU A 115 46.036 12.263 7.946 1.00 31.88 O
ANISOU 775 O LEU A 115 4087 3918 4110 -99 -96 -274 O
ATOM 776 CB LEU A 115 48.751 10.979 8.058 1.00 29.81 C
ANISOU 776 CB LEU A 115 3752 3686 3889 -137 -123 -256 C
ATOM 777 CG LEU A 115 50.060 10.257 7.722 1.00 34.37 C
ANISOU 777 CG LEU A 115 4288 4277 4495 -150 -124 -236 C
ATOM 778 CD1 LEU A 115 51.231 10.840 8.494 1.00 37.12 C
ANISOU 778 CD1 LEU A 115 4604 4624 4877 -177 -160 -266 C
ATOM 779 CD2 LEU A 115 49.922 8.749 7.979 1.00 23.97 C
ANISOU 779 CD2 LEU A 115 2967 3001 3140 -126 -127 -214 C
ATOM 780 N PRO A 116 45.393 10.118 7.707 1.00 19.56 N
ANISOU 780 N PRO A 116 2519 2414 2498 -74 -82 -229 N
ATOM 781 CA PRO A 116 44.062 10.347 8.262 1.00 20.97 C
ANISOU 781 CA PRO A 116 2721 2605 2642 -52 -79 -242 C
ATOM 782 C PRO A 116 44.132 10.341 9.797 1.00 23.02 C
ANISOU 782 C PRO A 116 2983 2896 2870 -46 -106 -273 C
ATOM 783 O PRO A 116 45.226 10.189 10.358 1.00 21.81 O
ANISOU 783 O PRO A 116 2813 2752 2723 -60 -131 -284 O
ATOM 784 CB PRO A 116 43.282 9.133 7.760 1.00 22.38 C
ANISOU 784 CB PRO A 116 2899 2807 2798 -38 -62 -209 C
ATOM 785 CG PRO A 116 44.319 8.024 7.736 1.00 16.50 C
ANISOU 785 CG PRO A 116 2133 2076 2059 -48 -70 -191 C
ATOM 786 CD PRO A 116 45.635 8.693 7.410 1.00 17.30 C
ANISOU 786 CD PRO A 116 2220 2154 2201 -69 -76 -199 C
ATOM 787 N GLY A 117 42.984 10.476 10.457 1.00 16.25 N
ANISOU 787 N GLY A 117 2142 2057 1976 -23 -101 -285 N
ATOM 788 CA GLY A 117 42.922 10.462 11.910 1.00 17.42 C
ANISOU 788 CA GLY A 117 2297 2241 2082 -11 -121 -313 C
ATOM 789 C GLY A 117 43.356 9.187 12.623 1.00 20.51 C
ANISOU 789 C GLY A 117 2675 2676 2441 -8 -134 -291 C
ATOM 790 O GLY A 117 43.514 9.182 13.844 1.00 26.85 O
ANISOU 790 O GLY A 117 3484 3512 3205 2 -156 -312 O
ATOM 791 N THR A 118 43.535 8.102 11.881 1.00 18.85 N
ANISOU 791 N THR A 118 2451 2467 2245 -15 -122 -250 N
ATOM 792 CA THR A 118 44.073 6.872 12.448 1.00 15.33 C
ANISOU 792 CA THR A 118 1993 2052 1779 -12 -135 -224 C
ATOM 793 C THR A 118 44.999 6.205 11.427 1.00 21.97 C
ANISOU 793 C THR A 118 2814 2873 2662 -27 -132 -199 C
ATOM 794 O THR A 118 44.704 6.200 10.236 1.00 29.15 O
ANISOU 794 O THR A 118 3723 3755 3597 -32 -109 -185 O
ATOM 795 CB THR A 118 42.934 5.895 12.878 1.00 19.08 C
ANISOU 795 CB THR A 118 2476 2557 2215 6 -114 -194 C
ATOM 796 OG1 THR A 118 43.497 4.684 13.402 1.00 20.74 O
ANISOU 796 OG1 THR A 118 2678 2792 2411 9 -126 -164 O
ATOM 797 CG2 THR A 118 42.032 5.541 11.696 1.00 22.78 C
ANISOU 797 CG2 THR A 118 2943 3004 2707 2 -84 -170 C
ATOM 798 N ARG A 119 46.112 5.641 11.885 1.00 27.78 N
ANISOU 798 N ARG A 119 3531 3625 3400 -29 -156 -192 N
ATOM 799 CA ARG A 119 47.066 4.974 10.985 1.00 30.21 C
ANISOU 799 CA ARG A 119 3816 3917 3747 -37 -152 -169 C
ATOM 800 C ARG A 119 46.705 3.521 10.755 1.00 26.20 C
ANISOU 800 C ARG A 119 3310 3415 3229 -24 -137 -130 C
ATOM 801 O ARG A 119 47.369 2.819 9.997 1.00 23.10 O
ANISOU 801 O ARG A 119 2903 3008 2864 -24 -130 -111 O
ATOM 802 CB ARG A 119 48.475 5.021 11.559 1.00 36.92 C
ANISOU 802 CB ARG A 119 4638 4779 4609 -43 -186 -181 C
ATOM 803 CG ARG A 119 49.113 6.385 11.563 1.00 45.10 C
ANISOU 803 CG ARG A 119 5664 5799 5675 -65 -203 -220 C
ATOM 804 CD ARG A 119 50.281 6.397 12.539 1.00 48.42 C
ANISOU 804 CD ARG A 119 6056 6245 6094 -69 -249 -238 C
ATOM 805 NE ARG A 119 49.894 6.905 13.854 1.00 52.12 N
ANISOU 805 NE ARG A 119 6545 6741 6515 -60 -279 -272 N
ATOM 806 CZ ARG A 119 50.724 7.003 14.888 1.00 60.74 C
ANISOU 806 CZ ARG A 119 7621 7864 7591 -58 -327 -296 C
ATOM 807 NH1 ARG A 119 51.987 6.615 14.770 1.00 63.34 N
ANISOU 807 NH1 ARG A 119 7909 8201 7955 -66 -350 -287 N
ATOM 808 NH2 ARG A 119 50.292 7.490 16.041 1.00 66.04 N
ANISOU 808 NH2 ARG A 119 8317 8563 8212 -46 -352 -331 N
ATOM 809 N GLN A 120 45.659 3.065 11.432 1.00 22.69 N
ANISOU 809 N GLN A 120 2883 2990 2746 -12 -130 -118 N
ATOM 810 CA GLN A 120 45.200 1.701 11.260 1.00 21.54 C
ANISOU 810 CA GLN A 120 2742 2844 2598 -4 -115 -79 C
ATOM 811 C GLN A 120 44.270 1.562 10.059 1.00 21.26 C
ANISOU 811 C GLN A 120 2714 2782 2581 -11 -87 -74 C
ATOM 812 O GLN A 120 43.144 1.095 10.191 1.00 19.28 O
ANISOU 812 O GLN A 120 2473 2537 2316 -9 -72 -59 O
ATOM 813 CB GLN A 120 44.541 1.194 12.542 1.00 26.24 C
ANISOU 813 CB GLN A 120 3349 3473 3147 10 -118 -61 C
ATOM 814 CG GLN A 120 45.544 0.912 13.645 1.00 24.42 C
ANISOU 814 CG GLN A 120 3112 3272 2893 23 -150 -56 C
ATOM 815 CD GLN A 120 46.560 -0.145 13.229 1.00 39.46 C
ANISOU 815 CD GLN A 120 5000 5162 4829 28 -158 -29 C
ATOM 816 OE1 GLN A 120 46.202 -1.300 12.971 1.00 46.12 O
ANISOU 816 OE1 GLN A 120 5850 5992 5683 34 -141 7 O
ATOM 817 NE2 GLN A 120 47.833 0.248 13.149 1.00 37.85 N
ANISOU 817 NE2 GLN A 120 4774 4960 4647 26 -183 -47 N
ATOM 818 N VAL A 121 44.756 1.990 8.891 1.00 19.45 N
ANISOU 818 N VAL A 121 2478 2526 2384 -19 -80 -85 N
ATOM 819 CA VAL A 121 44.075 1.763 7.625 1.00 17.56 C
ANISOU 819 CA VAL A 121 2248 2265 2161 -22 -58 -79 C
ATOM 820 C VAL A 121 45.052 1.143 6.637 1.00 16.82 C
ANISOU 820 C VAL A 121 2145 2152 2096 -21 -53 -71 C
ATOM 821 O VAL A 121 46.254 1.385 6.707 1.00 17.66 O
ANISOU 821 O VAL A 121 2234 2258 2217 -22 -61 -75 O
ATOM 822 CB VAL A 121 43.455 3.063 7.021 1.00 18.34 C
ANISOU 822 CB VAL A 121 2354 2352 2260 -27 -48 -100 C
ATOM 823 CG1 VAL A 121 42.652 3.830 8.067 1.00 14.96 C
ANISOU 823 CG1 VAL A 121 1934 1943 1806 -22 -53 -115 C
ATOM 824 CG2 VAL A 121 44.506 3.953 6.449 1.00 18.60 C
ANISOU 824 CG2 VAL A 121 2380 2368 2318 -34 -49 -113 C
ATOM 825 N THR A 122 44.537 0.334 5.718 1.00 14.68 N
ANISOU 825 N THR A 122 1882 1865 1832 -19 -39 -62 N
ATOM 826 CA THR A 122 45.388 -0.270 4.711 1.00 14.10 C
ANISOU 826 CA THR A 122 1804 1774 1780 -12 -30 -59 C
ATOM 827 C THR A 122 45.575 0.679 3.539 1.00 15.43 C
ANISOU 827 C THR A 122 1974 1932 1955 -15 -14 -72 C
ATOM 828 O THR A 122 44.727 1.534 3.294 1.00 14.57 O
ANISOU 828 O THR A 122 1877 1823 1835 -20 -10 -80 O
ATOM 829 CB THR A 122 44.808 -1.607 4.181 1.00 15.79 C
ANISOU 829 CB THR A 122 2031 1971 1999 -7 -24 -50 C
ATOM 830 OG1 THR A 122 43.592 -1.356 3.465 1.00 14.49 O
ANISOU 830 OG1 THR A 122 1880 1802 1825 -13 -18 -60 O
ATOM 831 CG2 THR A 122 44.551 -2.588 5.335 1.00 10.56 C
ANISOU 831 CG2 THR A 122 1367 1312 1332 -5 -35 -29 C
ATOM 832 N VAL A 123 46.683 0.516 2.819 1.00 15.98 N
ANISOU 832 N VAL A 123 2033 1994 2044 -9 -2 -70 N
ATOM 833 CA VAL A 123 46.910 1.220 1.561 1.00 16.37 C
ANISOU 833 CA VAL A 123 2087 2035 2098 -8 20 -73 C
ATOM 834 C VAL A 123 45.743 1.047 0.569 1.00 18.14 C
ANISOU 834 C VAL A 123 2338 2253 2302 -2 28 -78 C
ATOM 835 O VAL A 123 45.320 2.011 -0.078 1.00 16.77 O
ANISOU 835 O VAL A 123 2176 2077 2120 -3 38 -80 O
ATOM 836 CB VAL A 123 48.239 0.785 0.913 1.00 19.44 C
ANISOU 836 CB VAL A 123 2458 2422 2508 3 38 -68 C
ATOM 837 CG1 VAL A 123 48.390 1.414 -0.486 1.00 12.63 C
ANISOU 837 CG1 VAL A 123 1603 1553 1641 7 68 -66 C
ATOM 838 CG2 VAL A 123 49.408 1.177 1.820 1.00 15.00 C
ANISOU 838 CG2 VAL A 123 1861 1869 1969 -6 26 -65 C
ATOM 839 N GLY A 124 45.215 -0.172 0.474 1.00 10.00 N
ANISOU 839 N GLY A 124 1317 1217 1266 5 22 -80 N
ATOM 840 CA GLY A 124 44.049 -0.443 -0.347 1.00 7.33 C
ANISOU 840 CA GLY A 124 999 874 911 8 20 -89 C
ATOM 841 C GLY A 124 42.833 0.364 0.064 1.00 17.18 C
ANISOU 841 C GLY A 124 2251 2131 2146 -2 10 -90 C
ATOM 842 O GLY A 124 42.160 0.955 -0.782 1.00 15.01 O
ANISOU 842 O GLY A 124 1987 1858 1856 3 13 -95 O
ATOM 843 N GLY A 125 42.554 0.405 1.367 1.00 19.45 N
ANISOU 843 N GLY A 125 2528 2428 2436 -12 -1 -85 N
ATOM 844 CA GLY A 125 41.481 1.234 1.888 1.00 16.03 C
ANISOU 844 CA GLY A 125 2095 2006 1991 -16 -7 -87 C
ATOM 845 C GLY A 125 41.739 2.720 1.692 1.00 18.81 C
ANISOU 845 C GLY A 125 2449 2356 2340 -14 0 -92 C
ATOM 846 O GLY A 125 40.803 3.509 1.495 1.00 16.89 O
ANISOU 846 O GLY A 125 2213 2117 2088 -10 0 -97 O
ATOM 847 N ALA A 126 43.013 3.105 1.747 1.00 12.27 N
ANISOU 847 N ALA A 126 1614 1522 1525 -17 6 -91 N
ATOM 848 CA ALA A 126 43.393 4.504 1.571 1.00 13.39 C
ANISOU 848 CA ALA A 126 1758 1655 1676 -20 14 -94 C
ATOM 849 C ALA A 126 43.117 4.967 0.138 1.00 15.86 C
ANISOU 849 C ALA A 126 2087 1958 1983 -10 30 -87 C
ATOM 850 O ALA A 126 42.643 6.076 -0.086 1.00 16.64 O
ANISOU 850 O ALA A 126 2195 2047 2079 -7 34 -86 O
ATOM 851 CB ALA A 126 44.862 4.716 1.933 1.00 13.02 C
ANISOU 851 CB ALA A 126 1692 1603 1652 -30 15 -93 C
ATOM 852 N ILE A 127 43.406 4.097 -0.822 1.00 11.00 N
ANISOU 852 N ILE A 127 1476 1343 1361 -2 39 -82 N
ATOM 853 CA ILE A 127 43.189 4.399 -2.223 1.00 14.16 C
ANISOU 853 CA ILE A 127 1894 1741 1746 12 54 -75 C
ATOM 854 C ILE A 127 41.698 4.317 -2.587 1.00 15.87 C
ANISOU 854 C ILE A 127 2125 1967 1939 22 39 -81 C
ATOM 855 O ILE A 127 41.144 5.226 -3.210 1.00 14.50 O
ANISOU 855 O ILE A 127 1964 1791 1753 33 42 -74 O
ATOM 856 CB ILE A 127 43.988 3.436 -3.115 1.00 14.48 C
ANISOU 856 CB ILE A 127 1937 1784 1782 22 69 -74 C
ATOM 857 CG1 ILE A 127 45.480 3.582 -2.841 1.00 15.74 C
ANISOU 857 CG1 ILE A 127 2074 1938 1967 14 87 -65 C
ATOM 858 CG2 ILE A 127 43.653 3.664 -4.595 1.00 19.71 C
ANISOU 858 CG2 ILE A 127 2624 2451 2415 41 83 -68 C
ATOM 859 CD1 ILE A 127 46.365 2.649 -3.694 1.00 7.64 C
ANISOU 859 CD1 ILE A 127 1047 917 940 30 107 -64 C
ATOM 860 N ALA A 128 41.059 3.224 -2.184 1.00 10.71 N
ANISOU 860 N ALA A 128 1466 1321 1283 18 21 -93 N
ATOM 861 CA ALA A 128 39.649 2.998 -2.462 1.00 11.47 C
ANISOU 861 CA ALA A 128 1566 1428 1365 23 4 -101 C
ATOM 862 C ALA A 128 38.717 4.100 -1.933 1.00 14.68 C
ANISOU 862 C ALA A 128 1968 1840 1770 26 -2 -98 C
ATOM 863 O ALA A 128 37.682 4.361 -2.523 1.00 17.71 O
ANISOU 863 O ALA A 128 2355 2233 2140 38 -13 -100 O
ATOM 864 CB ALA A 128 39.223 1.645 -1.937 1.00 4.96 C
ANISOU 864 CB ALA A 128 731 604 549 11 -10 -109 C
ATOM 865 N CYS A 129 39.062 4.735 -0.821 1.00 16.23 N
ANISOU 865 N CYS A 129 2155 2031 1979 18 3 -96 N
ATOM 866 CA CYS A 129 38.238 5.830 -0.309 1.00 5.87 C
ANISOU 866 CA CYS A 129 841 722 666 26 0 -98 C
ATOM 867 C CYS A 129 38.877 7.195 -0.563 1.00 6.31 C
ANISOU 867 C CYS A 129 911 757 731 32 12 -92 C
ATOM 868 O CYS A 129 38.360 8.213 -0.097 1.00 12.92 O
ANISOU 868 O CYS A 129 1751 1587 1572 41 12 -97 O
ATOM 869 CB CYS A 129 37.958 5.667 1.198 1.00 9.40 C
ANISOU 869 CB CYS A 129 1274 1181 1117 17 -5 -106 C
ATOM 870 SG CYS A 129 36.684 4.453 1.604 1.00 18.96 S
ANISOU 870 SG CYS A 129 2466 2415 2323 12 -15 -106 S
ATOM 871 N ASP A 130 39.982 7.191 -1.311 1.00 12.77 N
ANISOU 871 N ASP A 130 1736 1561 1554 28 26 -82 N
ATOM 872 CA ASP A 130 40.761 8.391 -1.638 1.00 10.37 C
ANISOU 872 CA ASP A 130 1442 1233 1266 27 43 -70 C
ATOM 873 C ASP A 130 40.874 9.316 -0.431 1.00 10.27 C
ANISOU 873 C ASP A 130 1424 1205 1274 17 38 -83 C
ATOM 874 O ASP A 130 40.519 10.491 -0.500 1.00 9.77 O
ANISOU 874 O ASP A 130 1372 1120 1219 26 42 -81 O
ATOM 875 CB ASP A 130 40.149 9.113 -2.837 1.00 12.96 C
ANISOU 875 CB ASP A 130 1791 1555 1579 49 51 -52 C
ATOM 876 CG ASP A 130 41.068 10.180 -3.420 1.00 19.64 C
ANISOU 876 CG ASP A 130 2648 2371 2441 46 75 -29 C
ATOM 877 OD1 ASP A 130 42.283 10.188 -3.109 1.00 21.15 O
ANISOU 877 OD1 ASP A 130 2827 2550 2657 24 88 -28 O
ATOM 878 OD2 ASP A 130 40.566 11.012 -4.208 1.00 21.04 O
ANISOU 878 OD2 ASP A 130 2847 2538 2610 66 82 -9 O
ATOM 879 N ILE A 131 41.364 8.764 0.676 1.00 13.70 N
ANISOU 879 N ILE A 131 1841 1649 1715 1 28 -98 N
ATOM 880 CA ILE A 131 41.304 9.441 1.974 1.00 13.41 C
ANISOU 880 CA ILE A 131 1800 1607 1686 -5 17 -119 C
ATOM 881 C ILE A 131 42.043 10.777 1.998 1.00 15.22 C
ANISOU 881 C ILE A 131 2036 1800 1945 -15 22 -124 C
ATOM 882 O ILE A 131 42.981 10.998 1.221 1.00 14.57 O
ANISOU 882 O ILE A 131 1951 1700 1883 -27 37 -107 O
ATOM 883 CB ILE A 131 41.854 8.564 3.107 1.00 10.44 C
ANISOU 883 CB ILE A 131 1407 1252 1306 -17 3 -131 C
ATOM 884 CG1 ILE A 131 43.353 8.306 2.908 1.00 13.35 C
ANISOU 884 CG1 ILE A 131 1762 1613 1698 -35 6 -124 C
ATOM 885 CG2 ILE A 131 41.060 7.261 3.219 1.00 13.92 C
ANISOU 885 CG2 ILE A 131 1843 1721 1724 -10 -1 -124 C
ATOM 886 CD1 ILE A 131 43.987 7.566 4.071 1.00 14.09 C
ANISOU 886 CD1 ILE A 131 1838 1727 1788 -44 -12 -134 C
ATOM 887 N HIS A 132 41.602 11.654 2.900 1.00 13.47 N
ANISOU 887 N HIS A 132 1822 1569 1728 -10 12 -147 N
ATOM 888 CA HIS A 132 42.173 12.989 3.058 1.00 14.45 C
ANISOU 888 CA HIS A 132 1953 1650 1885 -22 13 -159 C
ATOM 889 C HIS A 132 42.761 13.130 4.442 1.00 16.39 C
ANISOU 889 C HIS A 132 2190 1900 2138 -38 -8 -194 C
ATOM 890 O HIS A 132 42.414 12.382 5.346 1.00 13.33 O
ANISOU 890 O HIS A 132 1796 1550 1721 -31 -22 -209 O
ATOM 891 CB HIS A 132 41.096 14.066 2.859 1.00 18.67 C
ANISOU 891 CB HIS A 132 2511 2160 2421 4 18 -162 C
ATOM 892 CG HIS A 132 39.864 13.841 3.675 1.00 18.29 C
ANISOU 892 CG HIS A 132 2465 2142 2343 28 8 -182 C
ATOM 893 ND1 HIS A 132 38.834 13.019 3.259 1.00 16.03 N
ANISOU 893 ND1 HIS A 132 2173 1891 2029 48 11 -166 N
ATOM 894 CD2 HIS A 132 39.508 14.298 4.898 1.00 12.58 C
ANISOU 894 CD2 HIS A 132 1746 1423 1613 37 -3 -218 C
ATOM 895 CE1 HIS A 132 37.891 13.001 4.182 1.00 15.18 C
ANISOU 895 CE1 HIS A 132 2061 1806 1901 65 5 -187 C
ATOM 896 NE2 HIS A 132 38.277 13.766 5.191 1.00 13.38 N
ANISOU 896 NE2 HIS A 132 1841 1561 1682 62 -1 -218 N
ATOM 897 N GLY A 133 43.640 14.106 4.613 1.00 18.73 N
ANISOU 897 N GLY A 133 2485 2159 2473 -59 -13 -209 N
ATOM 898 CA GLY A 133 44.240 14.331 5.903 1.00 13.22 C
ANISOU 898 CA GLY A 133 1778 1464 1780 -75 -40 -249 C
ATOM 899 C GLY A 133 44.304 15.803 6.227 1.00 20.01 C
ANISOU 899 C GLY A 133 2655 2273 2674 -82 -47 -279 C
ATOM 900 O GLY A 133 43.782 16.640 5.497 1.00 22.13 O
ANISOU 900 O GLY A 133 2944 2502 2961 -71 -29 -265 O
ATOM 901 N LYS A 134 44.966 16.108 7.335 1.00 20.14 N
ANISOU 901 N LYS A 134 2664 2290 2700 -100 -77 -322 N
ATOM 902 CA LYS A 134 45.105 17.461 7.832 1.00 17.15 C
ANISOU 902 CA LYS A 134 2302 1860 2355 -110 -91 -363 C
ATOM 903 C LYS A 134 45.830 18.365 6.820 1.00 18.02 C
ANISOU 903 C LYS A 134 2409 1906 2533 -140 -73 -340 C
ATOM 904 O LYS A 134 45.714 19.593 6.862 1.00 20.02 O
ANISOU 904 O LYS A 134 2684 2100 2823 -144 -74 -361 O
ATOM 905 CB LYS A 134 45.839 17.401 9.173 1.00 18.09 C
ANISOU 905 CB LYS A 134 2408 2001 2466 -127 -133 -414 C
ATOM 906 CG LYS A 134 45.789 18.655 9.989 1.00 28.47 C
ANISOU 906 CG LYS A 134 3745 3274 3800 -129 -156 -474 C
ATOM 907 CD LYS A 134 46.222 18.364 11.413 1.00 34.35 C
ANISOU 907 CD LYS A 134 4481 4061 4509 -132 -200 -527 C
ATOM 908 CE LYS A 134 46.395 19.647 12.218 1.00 30.74 C
ANISOU 908 CE LYS A 134 4045 3569 4065 -139 -220 -572 C
ATOM 909 NZ LYS A 134 46.870 19.353 13.600 1.00 29.17 N
ANISOU 909 NZ LYS A 134 3839 3423 3820 -138 -258 -607 N
ATOM 910 N ASN A 135 46.555 17.749 5.893 1.00 11.10 N
ANISOU 910 N ASN A 135 1508 1039 1671 -158 -53 -294 N
ATOM 911 CA ASN A 135 47.293 18.500 4.883 1.00 13.01 C
ANISOU 911 CA ASN A 135 1743 1227 1973 -187 -29 -262 C
ATOM 912 C ASN A 135 46.646 18.536 3.499 1.00 16.70 C
ANISOU 912 C ASN A 135 2231 1682 2432 -163 13 -206 C
ATOM 913 O ASN A 135 47.338 18.779 2.514 1.00 22.08 O
ANISOU 913 O ASN A 135 2903 2339 3149 -183 41 -165 O
ATOM 914 CB ASN A 135 48.713 17.936 4.751 1.00 16.81 C
ANISOU 914 CB ASN A 135 2177 1726 2483 -224 -30 -249 C
ATOM 915 CG ASN A 135 48.719 16.496 4.263 1.00 25.09 C
ANISOU 915 CG ASN A 135 3210 2835 3488 -205 -16 -215 C
ATOM 916 OD1 ASN A 135 47.693 15.802 4.331 1.00 23.15 O
ANISOU 916 OD1 ASN A 135 2985 2624 3189 -170 -16 -212 O
ATOM 917 ND2 ASN A 135 49.868 16.037 3.773 1.00 19.77 N
ANISOU 917 ND2 ASN A 135 2498 2172 2841 -229 -3 -190 N
ATOM 918 N HIS A 136 45.339 18.292 3.416 1.00 16.36 N
ANISOU 918 N HIS A 136 2214 1661 2341 -121 16 -203 N
ATOM 919 CA HIS A 136 44.672 18.210 2.115 1.00 12.31 C
ANISOU 919 CA HIS A 136 1719 1147 1811 -94 47 -152 C
ATOM 920 C HIS A 136 44.800 19.456 1.240 1.00 20.85 C
ANISOU 920 C HIS A 136 2822 2162 2939 -100 72 -120 C
ATOM 921 O HIS A 136 44.938 19.357 0.018 1.00 24.13 O
ANISOU 921 O HIS A 136 3241 2576 3352 -95 103 -68 O
ATOM 922 CB HIS A 136 43.187 17.878 2.243 1.00 12.53 C
ANISOU 922 CB HIS A 136 1766 1206 1789 -49 41 -159 C
ATOM 923 CG HIS A 136 42.523 17.712 0.917 1.00 19.37 C
ANISOU 923 CG HIS A 136 2646 2079 2633 -22 64 -111 C
ATOM 924 ND1 HIS A 136 41.968 18.771 0.222 1.00 21.80 N
ANISOU 924 ND1 HIS A 136 2983 2343 2957 0 79 -87 N
ATOM 925 CD2 HIS A 136 42.399 16.628 0.112 1.00 14.31 C
ANISOU 925 CD2 HIS A 136 1998 1483 1957 -12 74 -83 C
ATOM 926 CE1 HIS A 136 41.505 18.339 -0.936 1.00 18.99 C
ANISOU 926 CE1 HIS A 136 2634 2010 2570 23 94 -45 C
ATOM 927 NE2 HIS A 136 41.756 17.042 -1.030 1.00 18.25 N
ANISOU 927 NE2 HIS A 136 2520 1970 2446 15 91 -45 N
ATOM 928 N HIS A 137 44.722 20.627 1.857 1.00 19.26 N
ANISOU 928 N HIS A 137 2636 1904 2776 -106 60 -151 N
ATOM 929 CA HIS A 137 44.789 21.870 1.098 1.00 27.43 C
ANISOU 929 CA HIS A 137 3696 2867 3861 -110 84 -119 C
ATOM 930 C HIS A 137 46.181 22.053 0.470 1.00 29.91 C
ANISOU 930 C HIS A 137 3985 3152 4226 -159 108 -84 C
ATOM 931 O HIS A 137 46.349 22.862 -0.441 1.00 33.21 O
ANISOU 931 O HIS A 137 4420 3519 4681 -164 139 -36 O
ATOM 932 CB HIS A 137 44.433 23.071 1.984 1.00 22.79 C
ANISOU 932 CB HIS A 137 3132 2217 3309 -107 63 -167 C
ATOM 933 CG HIS A 137 45.439 23.330 3.060 1.00 30.16 C
ANISOU 933 CG HIS A 137 4044 3131 4283 -154 35 -222 C
ATOM 934 ND1 HIS A 137 45.572 22.512 4.163 1.00 23.61 N
ANISOU 934 ND1 HIS A 137 3194 2360 3418 -157 2 -271 N
ATOM 935 CD2 HIS A 137 46.391 24.285 3.181 1.00 30.99 C
ANISOU 935 CD2 HIS A 137 4144 3167 4464 -200 32 -233 C
ATOM 936 CE1 HIS A 137 46.554 22.962 4.923 1.00 28.84 C
ANISOU 936 CE1 HIS A 137 3838 2993 4125 -200 -24 -314 C
ATOM 937 NE2 HIS A 137 47.066 24.038 4.351 1.00 30.27 N
ANISOU 937 NE2 HIS A 137 4028 3106 4369 -227 -8 -289 N
ATOM 938 N SER A 138 47.171 21.298 0.946 1.00 25.99 N
ANISOU 938 N SER A 138 3448 2693 3735 -192 95 -103 N
ATOM 939 CA SER A 138 48.518 21.368 0.369 1.00 22.66 C
ANISOU 939 CA SER A 138 2992 2255 3363 -238 120 -69 C
ATOM 940 C SER A 138 48.963 20.107 -0.382 1.00 26.74 C
ANISOU 940 C SER A 138 3482 2837 3841 -231 143 -32 C
ATOM 941 O SER A 138 49.810 20.187 -1.261 1.00 26.79 O
ANISOU 941 O SER A 138 3469 2833 3876 -253 180 14 O
ATOM 942 CB SER A 138 49.564 21.733 1.437 1.00 21.72 C
ANISOU 942 CB SER A 138 2839 2113 3301 -288 88 -119 C
ATOM 943 OG SER A 138 49.757 20.687 2.377 1.00 25.90 O
ANISOU 943 OG SER A 138 3342 2707 3792 -286 52 -161 O
ATOM 944 N ALA A 139 48.407 18.948 -0.037 1.00 24.83 N
ANISOU 944 N ALA A 139 3239 2658 3536 -202 123 -52 N
ATOM 945 CA ALA A 139 48.878 17.687 -0.613 1.00 18.65 C
ANISOU 945 CA ALA A 139 2431 1933 2721 -196 140 -27 C
ATOM 946 C ALA A 139 47.834 16.959 -1.456 1.00 23.00 C
ANISOU 946 C ALA A 139 3010 2521 3207 -150 154 -2 C
ATOM 947 O ALA A 139 48.127 15.912 -2.035 1.00 24.67 O
ANISOU 947 O ALA A 139 3208 2776 3389 -140 168 17 O
ATOM 948 CB ALA A 139 49.388 16.758 0.494 1.00 17.84 C
ANISOU 948 CB ALA A 139 2294 1874 2610 -208 104 -70 C
ATOM 949 N GLY A 140 46.622 17.502 -1.514 1.00 15.83 N
ANISOU 949 N GLY A 140 2140 1596 2278 -120 147 -3 N
ATOM 950 CA GLY A 140 45.507 16.787 -2.103 1.00 17.13 C
ANISOU 950 CA GLY A 140 2326 1800 2382 -77 147 9 C
ATOM 951 C GLY A 140 45.171 15.565 -1.263 1.00 17.52 C
ANISOU 951 C GLY A 140 2360 1903 2395 -70 118 -28 C
ATOM 952 O GLY A 140 45.501 15.499 -0.067 1.00 19.32 O
ANISOU 952 O GLY A 140 2570 2133 2638 -88 92 -66 O
ATOM 953 N SER A 141 44.521 14.588 -1.880 1.00 12.35 N
ANISOU 953 N SER A 141 1711 1289 1692 -43 120 -16 N
ATOM 954 CA SER A 141 44.179 13.361 -1.168 1.00 14.35 C
ANISOU 954 CA SER A 141 1950 1587 1915 -37 96 -43 C
ATOM 955 C SER A 141 45.133 12.209 -1.516 1.00 19.32 C
ANISOU 955 C SER A 141 2557 2245 2539 -47 106 -34 C
ATOM 956 O SER A 141 46.086 12.389 -2.274 1.00 17.37 O
ANISOU 956 O SER A 141 2301 1987 2310 -59 133 -9 O
ATOM 957 CB SER A 141 42.723 12.972 -1.421 1.00 18.72 C
ANISOU 957 CB SER A 141 2521 2164 2426 -4 85 -45 C
ATOM 958 OG SER A 141 42.435 12.972 -2.805 1.00 19.78 O
ANISOU 958 OG SER A 141 2674 2303 2539 17 104 -11 O
ATOM 959 N PHE A 142 44.867 11.030 -0.957 1.00 19.79 N
ANISOU 959 N PHE A 142 2605 2339 2574 -42 87 -53 N
ATOM 960 CA PHE A 142 45.791 9.907 -1.067 1.00 18.95 C
ANISOU 960 CA PHE A 142 2477 2255 2467 -49 92 -50 C
ATOM 961 C PHE A 142 46.034 9.515 -2.522 1.00 19.90 C
ANISOU 961 C PHE A 142 2606 2383 2571 -34 122 -22 C
ATOM 962 O PHE A 142 47.165 9.204 -2.918 1.00 14.94 O
ANISOU 962 O PHE A 142 1959 1759 1959 -42 143 -10 O
ATOM 963 CB PHE A 142 45.279 8.712 -0.269 1.00 12.23 C
ANISOU 963 CB PHE A 142 1620 1434 1592 -41 67 -70 C
ATOM 964 CG PHE A 142 46.339 7.710 0.065 1.00 16.45 C
ANISOU 964 CG PHE A 142 2128 1984 2137 -49 65 -72 C
ATOM 965 CD1 PHE A 142 46.589 6.645 -0.776 1.00 16.78 C
ANISOU 965 CD1 PHE A 142 2169 2039 2166 -36 79 -61 C
ATOM 966 CD2 PHE A 142 47.091 7.838 1.219 1.00 16.37 C
ANISOU 966 CD2 PHE A 142 2095 1976 2149 -67 46 -87 C
ATOM 967 CE1 PHE A 142 47.557 5.713 -0.472 1.00 13.08 C
ANISOU 967 CE1 PHE A 142 1677 1583 1710 -38 77 -62 C
ATOM 968 CE2 PHE A 142 48.069 6.917 1.527 1.00 16.75 C
ANISOU 968 CE2 PHE A 142 2117 2041 2208 -69 41 -86 C
ATOM 969 CZ PHE A 142 48.303 5.844 0.675 1.00 10.93 C
ANISOU 969 CZ PHE A 142 1377 1313 1461 -54 58 -72 C
ATOM 970 N GLY A 143 44.970 9.559 -3.315 1.00 15.43 N
ANISOU 970 N GLY A 143 2068 1822 1972 -10 124 -13 N
ATOM 971 CA GLY A 143 45.069 9.295 -4.739 1.00 15.62 C
ANISOU 971 CA GLY A 143 2108 1857 1970 9 150 11 C
ATOM 972 C GLY A 143 46.073 10.151 -5.488 1.00 15.76 C
ANISOU 972 C GLY A 143 2124 1855 2008 1 188 44 C
ATOM 973 O GLY A 143 46.661 9.684 -6.459 1.00 20.88 O
ANISOU 973 O GLY A 143 2774 2519 2639 12 217 62 O
ATOM 974 N ASN A 144 46.281 11.391 -5.041 1.00 17.08 N
ANISOU 974 N ASN A 144 2288 1987 2213 -19 192 52 N
ATOM 975 CA ASN A 144 47.213 12.301 -5.716 1.00 23.61 C
ANISOU 975 CA ASN A 144 3112 2788 3070 -32 231 89 C
ATOM 976 C ASN A 144 48.649 11.778 -5.652 1.00 27.17 C
ANISOU 976 C ASN A 144 3523 3250 3550 -54 252 92 C
ATOM 977 O ASN A 144 49.509 12.252 -6.374 1.00 20.07 O
ANISOU 977 O ASN A 144 2614 2341 2671 -64 292 127 O
ATOM 978 CB ASN A 144 47.176 13.734 -5.130 1.00 17.38 C
ANISOU 978 CB ASN A 144 2326 1949 2328 -54 226 92 C
ATOM 979 CG ASN A 144 45.789 14.384 -5.205 1.00 22.43 C
ANISOU 979 CG ASN A 144 3003 2575 2945 -28 209 92 C
ATOM 980 OD1 ASN A 144 44.788 13.799 -4.786 1.00 16.84 O
ANISOU 980 OD1 ASN A 144 2302 1891 2205 -9 179 65 O
ATOM 981 ND2 ASN A 144 45.736 15.609 -5.740 1.00 20.03 N
ANISOU 981 ND2 ASN A 144 2720 2229 2661 -27 230 126 N
ATOM 982 N HIS A 145 48.901 10.798 -4.790 1.00 24.35 N
ANISOU 982 N HIS A 145 3141 2915 3195 -59 226 59 N
ATOM 983 CA HIS A 145 50.268 10.372 -4.527 1.00 24.25 C
ANISOU 983 CA HIS A 145 3084 2911 3217 -79 238 59 C
ATOM 984 C HIS A 145 50.501 8.939 -4.972 1.00 25.20 C
ANISOU 984 C HIS A 145 3199 3069 3306 -53 245 53 C
ATOM 985 O HIS A 145 51.574 8.372 -4.758 1.00 18.89 O
ANISOU 985 O HIS A 145 2363 2284 2532 -60 253 51 O
ATOM 986 CB HIS A 145 50.613 10.566 -3.045 1.00 19.80 C
ANISOU 986 CB HIS A 145 2492 2338 2692 -107 199 27 C
ATOM 987 CG HIS A 145 50.398 11.972 -2.571 1.00 21.39 C
ANISOU 987 CG HIS A 145 2702 2498 2927 -131 190 23 C
ATOM 988 ND1 HIS A 145 51.394 12.921 -2.589 1.00 17.46 N
ANISOU 988 ND1 HIS A 145 2178 1970 2487 -166 207 37 N
ATOM 989 CD2 HIS A 145 49.288 12.595 -2.105 1.00 17.89 C
ANISOU 989 CD2 HIS A 145 2290 2035 2471 -125 166 7 C
ATOM 990 CE1 HIS A 145 50.912 14.069 -2.140 1.00 22.44 C
ANISOU 990 CE1 HIS A 145 2827 2558 3140 -180 192 27 C
ATOM 991 NE2 HIS A 145 49.640 13.897 -1.836 1.00 23.01 N
ANISOU 991 NE2 HIS A 145 2935 2639 3169 -153 168 8 N
ATOM 992 N VAL A 146 49.494 8.356 -5.607 1.00 19.14 N
ANISOU 992 N VAL A 146 2469 2317 2487 -23 241 49 N
ATOM 993 CA VAL A 146 49.650 7.014 -6.137 1.00 14.24 C
ANISOU 993 CA VAL A 146 1850 1725 1836 3 248 40 C
ATOM 994 C VAL A 146 50.319 7.118 -7.493 1.00 21.04 C
ANISOU 994 C VAL A 146 2715 2597 2682 20 299 70 C
ATOM 995 O VAL A 146 49.827 7.797 -8.395 1.00 22.54 O
ANISOU 995 O VAL A 146 2936 2784 2844 32 318 94 O
ATOM 996 CB VAL A 146 48.302 6.288 -6.264 1.00 12.82 C
ANISOU 996 CB VAL A 146 1705 1556 1611 25 218 18 C
ATOM 997 CG1 VAL A 146 48.496 4.921 -6.915 1.00 9.96 C
ANISOU 997 CG1 VAL A 146 1348 1215 1221 51 226 5 C
ATOM 998 CG2 VAL A 146 47.665 6.137 -4.906 1.00 12.41 C
ANISOU 998 CG2 VAL A 146 1645 1498 1573 10 175 -6 C
ATOM 999 N ARG A 147 51.458 6.456 -7.630 1.00 19.65 N
ANISOU 999 N ARG A 147 2507 2436 2522 24 323 72 N
ATOM 1000 CA ARG A 147 52.205 6.512 -8.871 1.00 23.80 C
ANISOU 1000 CA ARG A 147 3032 2977 3033 42 379 101 C
ATOM 1001 C ARG A 147 51.883 5.324 -9.767 1.00 21.21 C
ANISOU 1001 C ARG A 147 2734 2676 2648 85 387 83 C
ATOM 1002 O ARG A 147 51.878 5.438 -10.988 1.00 29.62 O
ANISOU 1002 O ARG A 147 3825 3759 3670 111 424 102 O
ATOM 1003 CB ARG A 147 53.694 6.627 -8.566 1.00 37.22 C
ANISOU 1003 CB ARG A 147 4673 4679 4788 22 408 115 C
ATOM 1004 CG ARG A 147 54.045 8.026 -8.031 1.00 56.26 C
ANISOU 1004 CG ARG A 147 7061 7060 7255 -23 410 138 C
ATOM 1005 CD ARG A 147 54.351 8.971 -9.182 1.00 56.65 C
ANISOU 1005 CD ARG A 147 7120 7103 7300 -24 468 188 C
ATOM 1006 NE ARG A 147 55.444 8.401 -9.969 1.00 50.07 N
ANISOU 1006 NE ARG A 147 6257 6301 6465 -5 522 206 N
ATOM 1007 CZ ARG A 147 56.722 8.749 -9.839 1.00 42.92 C
ANISOU 1007 CZ ARG A 147 5292 5395 5620 -32 555 228 C
ATOM 1008 NH1 ARG A 147 57.075 9.698 -8.978 1.00 23.37 N
ANISOU 1008 NH1 ARG A 147 2783 2886 3211 -81 537 233 N
ATOM 1009 NH2 ARG A 147 57.645 8.157 -10.587 1.00 48.55 N
ANISOU 1009 NH2 ARG A 147 5979 6142 6327 -8 607 244 N
ATOM 1010 N SER A 148 51.580 4.187 -9.158 1.00 17.10 N
ANISOU 1010 N SER A 148 2213 2158 2125 93 350 45 N
ATOM 1011 CA SER A 148 51.042 3.071 -9.922 1.00 20.69 C
ANISOU 1011 CA SER A 148 2703 2629 2529 130 345 19 C
ATOM 1012 C SER A 148 50.302 2.133 -9.000 1.00 17.56 C
ANISOU 1012 C SER A 148 2312 2222 2140 125 293 -17 C
ATOM 1013 O SER A 148 50.465 2.180 -7.781 1.00 25.42 O
ANISOU 1013 O SER A 148 3279 3204 3176 100 267 -19 O
ATOM 1014 CB SER A 148 52.145 2.322 -10.696 1.00 22.33 C
ANISOU 1014 CB SER A 148 2897 2857 2729 160 390 19 C
ATOM 1015 OG SER A 148 52.912 1.495 -9.840 1.00 24.82 O
ANISOU 1015 OG SER A 148 3175 3168 3088 158 380 3 O
ATOM 1016 N MET A 149 49.469 1.288 -9.578 1.00 21.98 N
ANISOU 1016 N MET A 149 2907 2786 2658 148 275 -44 N
ATOM 1017 CA MET A 149 48.819 0.259 -8.787 1.00 21.02 C
ANISOU 1017 CA MET A 149 2788 2650 2548 143 231 -75 C
ATOM 1018 C MET A 149 48.486 -0.962 -9.617 1.00 21.39 C
ANISOU 1018 C MET A 149 2865 2700 2561 173 226 -109 C
ATOM 1019 O MET A 149 48.252 -0.860 -10.819 1.00 23.48 O
ANISOU 1019 O MET A 149 3161 2982 2779 197 242 -114 O
ATOM 1020 CB MET A 149 47.581 0.793 -8.073 1.00 22.81 C
ANISOU 1020 CB MET A 149 3024 2868 2776 119 192 -76 C
ATOM 1021 CG MET A 149 46.458 1.292 -8.964 1.00 29.17 C
ANISOU 1021 CG MET A 149 3864 3683 3536 129 183 -77 C
ATOM 1022 SD MET A 149 45.148 1.886 -7.869 1.00 27.17 S
ANISOU 1022 SD MET A 149 3607 3419 3298 101 140 -78 S
ATOM 1023 CE MET A 149 44.547 3.337 -8.717 1.00 16.43 C
ANISOU 1023 CE MET A 149 2269 2067 1906 111 150 -52 C
ATOM 1024 N ASP A 150 48.508 -2.119 -8.963 1.00 18.26 N
ANISOU 1024 N ASP A 150 2462 2285 2190 174 204 -131 N
ATOM 1025 CA ASP A 150 48.149 -3.376 -9.588 1.00 15.52 C
ANISOU 1025 CA ASP A 150 2144 1929 1822 198 192 -170 C
ATOM 1026 C ASP A 150 46.751 -3.743 -9.164 1.00 16.74 C
ANISOU 1026 C ASP A 150 2315 2068 1977 176 144 -189 C
ATOM 1027 O ASP A 150 46.481 -3.977 -7.983 1.00 18.74 O
ANISOU 1027 O ASP A 150 2550 2304 2267 152 120 -182 O
ATOM 1028 CB ASP A 150 49.128 -4.484 -9.191 1.00 26.78 C
ANISOU 1028 CB ASP A 150 3552 3338 3283 214 202 -180 C
ATOM 1029 CG ASP A 150 50.520 -4.273 -9.774 1.00 27.83 C
ANISOU 1029 CG ASP A 150 3666 3491 3417 241 253 -166 C
ATOM 1030 OD1 ASP A 150 50.680 -3.364 -10.616 1.00 31.11 O
ANISOU 1030 OD1 ASP A 150 4088 3933 3800 248 285 -149 O
ATOM 1031 OD2 ASP A 150 51.446 -5.027 -9.401 1.00 29.42 O
ANISOU 1031 OD2 ASP A 150 3844 3683 3651 258 264 -168 O
ATOM 1032 N LEU A 151 45.857 -3.786 -10.141 1.00 24.01 N
ANISOU 1032 N LEU A 151 3269 2999 2855 187 129 -212 N
ATOM 1033 CA LEU A 151 44.460 -4.073 -9.886 1.00 21.15 C
ANISOU 1033 CA LEU A 151 2917 2626 2492 166 84 -231 C
ATOM 1034 C LEU A 151 44.087 -5.440 -10.426 1.00 22.90 C
ANISOU 1034 C LEU A 151 3164 2829 2710 178 62 -278 C
ATOM 1035 O LEU A 151 44.205 -5.701 -11.624 1.00 23.07 O
ANISOU 1035 O LEU A 151 3214 2863 2688 209 70 -306 O
ATOM 1036 CB LEU A 151 43.587 -2.999 -10.527 1.00 20.27 C
ANISOU 1036 CB LEU A 151 2819 2542 2340 167 74 -222 C
ATOM 1037 CG LEU A 151 42.074 -3.105 -10.375 1.00 17.41 C
ANISOU 1037 CG LEU A 151 2461 2178 1975 148 27 -239 C
ATOM 1038 CD1 LEU A 151 41.669 -2.879 -8.930 1.00 17.66 C
ANISOU 1038 CD1 LEU A 151 2462 2196 2053 114 14 -218 C
ATOM 1039 CD2 LEU A 151 41.411 -2.089 -11.292 1.00 17.11 C
ANISOU 1039 CD2 LEU A 151 2440 2172 1888 163 22 -230 C
ATOM 1040 N LEU A 152 43.646 -6.317 -9.531 1.00 21.29 N
ANISOU 1040 N LEU A 152 2949 2591 2548 155 34 -287 N
ATOM 1041 CA LEU A 152 43.056 -7.585 -9.939 1.00 16.22 C
ANISOU 1041 CA LEU A 152 2330 1921 1913 156 6 -333 C
ATOM 1042 C LEU A 152 41.626 -7.325 -10.404 1.00 21.12 C
ANISOU 1042 C LEU A 152 2959 2555 2509 139 -33 -353 C
ATOM 1043 O LEU A 152 40.756 -6.949 -9.604 1.00 16.41 O
ANISOU 1043 O LEU A 152 2341 1961 1934 108 -54 -333 O
ATOM 1044 CB LEU A 152 43.064 -8.590 -8.780 1.00 14.78 C
ANISOU 1044 CB LEU A 152 2131 1694 1790 134 -7 -327 C
ATOM 1045 CG LEU A 152 42.333 -9.919 -9.017 1.00 18.37 C
ANISOU 1045 CG LEU A 152 2605 2106 2267 124 -40 -371 C
ATOM 1046 CD1 LEU A 152 42.892 -10.649 -10.258 1.00 13.80 C
ANISOU 1046 CD1 LEU A 152 2063 1518 1662 164 -32 -420 C
ATOM 1047 CD2 LEU A 152 42.429 -10.789 -7.771 1.00 15.02 C
ANISOU 1047 CD2 LEU A 152 2165 1638 1904 103 -45 -349 C
ATOM 1048 N THR A 153 41.396 -7.521 -11.701 1.00 15.55 N
ANISOU 1048 N THR A 153 2286 1865 1757 164 -44 -392 N
ATOM 1049 CA THR A 153 40.103 -7.243 -12.316 1.00 14.85 C
ANISOU 1049 CA THR A 153 2207 1798 1638 156 -85 -414 C
ATOM 1050 C THR A 153 39.309 -8.516 -12.504 1.00 17.64 C
ANISOU 1050 C THR A 153 2571 2118 2015 139 -129 -468 C
ATOM 1051 O THR A 153 39.816 -9.609 -12.262 1.00 17.85 O
ANISOU 1051 O THR A 153 2604 2101 2077 138 -124 -487 O
ATOM 1052 CB THR A 153 40.241 -6.487 -13.661 1.00 14.31 C
ANISOU 1052 CB THR A 153 2168 1776 1493 195 -74 -421 C
ATOM 1053 OG1 THR A 153 41.315 -7.048 -14.423 1.00 21.51 O
ANISOU 1053 OG1 THR A 153 3101 2687 2386 227 -41 -437 O
ATOM 1054 CG2 THR A 153 40.543 -5.028 -13.403 1.00 10.77 C
ANISOU 1054 CG2 THR A 153 1704 1357 1031 198 -43 -363 C
ATOM 1055 N ALA A 154 38.061 -8.357 -12.931 1.00 19.75 N
ANISOU 1055 N ALA A 154 2832 2404 2268 122 -171 -483 N
ATOM 1056 CA ALA A 154 37.093 -9.448 -13.009 1.00 18.52 C
ANISOU 1056 CA ALA A 154 2668 2220 2149 89 -213 -518 C
ATOM 1057 C ALA A 154 37.508 -10.542 -13.979 1.00 23.24 C
ANISOU 1057 C ALA A 154 3294 2800 2737 105 -211 -559 C
ATOM 1058 O ALA A 154 37.103 -11.693 -13.832 1.00 23.48 O
ANISOU 1058 O ALA A 154 3322 2787 2812 79 -233 -587 O
ATOM 1059 CB ALA A 154 35.718 -8.897 -13.388 1.00 18.53 C
ANISOU 1059 CB ALA A 154 2651 2257 2132 73 -255 -522 C
ATOM 1060 N ASP A 155 38.320 -10.176 -14.967 1.00 26.40 N
ANISOU 1060 N ASP A 155 3720 3232 3080 147 -182 -562 N
ATOM 1061 CA ASP A 155 38.853 -11.143 -15.926 1.00 30.36 C
ANISOU 1061 CA ASP A 155 4250 3721 3566 169 -174 -602 C
ATOM 1062 C ASP A 155 39.959 -12.028 -15.332 1.00 33.43 C
ANISOU 1062 C ASP A 155 4643 4060 3998 178 -142 -604 C
ATOM 1063 O ASP A 155 40.439 -12.949 -15.987 1.00 37.94 O
ANISOU 1063 O ASP A 155 5236 4612 4566 196 -133 -639 O
ATOM 1064 CB ASP A 155 39.328 -10.446 -17.219 1.00 30.98 C
ANISOU 1064 CB ASP A 155 4351 3853 3565 212 -152 -600 C
ATOM 1065 CG ASP A 155 40.331 -9.328 -16.963 1.00 39.52 C
ANISOU 1065 CG ASP A 155 5429 4963 4624 239 -102 -551 C
ATOM 1066 OD1 ASP A 155 40.392 -8.382 -17.789 1.00 49.28 O
ANISOU 1066 OD1 ASP A 155 6677 6247 5800 264 -89 -531 O
ATOM 1067 OD2 ASP A 155 41.056 -9.393 -15.943 1.00 35.10 O
ANISOU 1067 OD2 ASP A 155 4856 4375 4106 235 -75 -529 O
ATOM 1068 N GLY A 156 40.357 -11.744 -14.095 1.00 31.45 N
ANISOU 1068 N GLY A 156 4372 3790 3788 168 -124 -568 N
ATOM 1069 CA GLY A 156 41.389 -12.516 -13.421 1.00 29.16 C
ANISOU 1069 CA GLY A 156 4083 3454 3543 179 -96 -563 C
ATOM 1070 C GLY A 156 42.785 -12.039 -13.761 1.00 31.41 C
ANISOU 1070 C GLY A 156 4374 3766 3796 225 -44 -546 C
ATOM 1071 O GLY A 156 43.764 -12.628 -13.319 1.00 36.92 O
ANISOU 1071 O GLY A 156 5069 4432 4526 244 -17 -541 O
ATOM 1072 N GLU A 157 42.878 -10.979 -14.557 1.00 34.90 N
ANISOU 1072 N GLU A 157 4821 4264 4176 245 -28 -533 N
ATOM 1073 CA GLU A 157 44.163 -10.363 -14.876 1.00 42.68 C
ANISOU 1073 CA GLU A 157 5805 5279 5130 284 27 -507 C
ATOM 1074 C GLU A 157 44.546 -9.288 -13.855 1.00 42.00 C
ANISOU 1074 C GLU A 157 5695 5204 5057 279 49 -457 C
ATOM 1075 O GLU A 157 43.693 -8.541 -13.367 1.00 36.80 O
ANISOU 1075 O GLU A 157 5027 4556 4398 252 25 -438 O
ATOM 1076 CB GLU A 157 44.126 -9.729 -16.272 1.00 44.11 C
ANISOU 1076 CB GLU A 157 6006 5515 5239 308 39 -511 C
ATOM 1077 N ILE A 158 45.836 -9.207 -13.550 1.00 34.73 N
ANISOU 1077 N ILE A 158 4763 4284 4151 305 95 -435 N
ATOM 1078 CA ILE A 158 46.355 -8.137 -12.720 1.00 30.54 C
ANISOU 1078 CA ILE A 158 4193 3771 3639 288 121 -375 C
ATOM 1079 C ILE A 158 46.863 -7.004 -13.610 1.00 40.37 C
ANISOU 1079 C ILE A 158 5443 5067 4830 312 162 -350 C
ATOM 1080 O ILE A 158 47.858 -7.149 -14.319 1.00 44.14 O
ANISOU 1080 O ILE A 158 5927 5560 5285 350 206 -355 O
ATOM 1081 CB ILE A 158 47.457 -8.644 -11.786 1.00 31.39 C
ANISOU 1081 CB ILE A 158 4269 3853 3803 292 143 -354 C
ATOM 1082 CG1 ILE A 158 46.862 -9.696 -10.841 1.00 31.93 C
ANISOU 1082 CG1 ILE A 158 4336 3871 3926 266 103 -367 C
ATOM 1083 CG2 ILE A 158 48.089 -7.474 -11.014 1.00 28.83 C
ANISOU 1083 CG2 ILE A 158 3904 3553 3498 274 168 -297 C
ATOM 1084 CD1 ILE A 158 47.797 -10.181 -9.762 1.00 31.59 C
ANISOU 1084 CD1 ILE A 158 4263 3803 3939 269 116 -340 C
ATOM 1085 N ARG A 159 46.158 -5.881 -13.569 1.00 39.24 N
ANISOU 1085 N ARG A 159 5295 4946 4667 289 150 -322 N
ATOM 1086 CA ARG A 159 46.392 -4.763 -14.474 1.00 34.47 C
ANISOU 1086 CA ARG A 159 4703 4386 4010 309 184 -294 C
ATOM 1087 C ARG A 159 47.249 -3.694 -13.824 1.00 30.69 C
ANISOU 1087 C ARG A 159 4185 3914 3561 293 222 -237 C
ATOM 1088 O ARG A 159 46.875 -3.147 -12.784 1.00 33.67 O
ANISOU 1088 O ARG A 159 4537 4278 3978 256 201 -212 O
ATOM 1089 CB ARG A 159 45.056 -4.129 -14.823 1.00 35.28 C
ANISOU 1089 CB ARG A 159 4824 4504 4075 297 144 -296 C
ATOM 1090 CG ARG A 159 44.940 -3.663 -16.222 1.00 44.61 C
ANISOU 1090 CG ARG A 159 6037 5726 5185 328 157 -295 C
ATOM 1091 CD ARG A 159 43.866 -4.465 -16.907 1.00 53.14 C
ANISOU 1091 CD ARG A 159 7138 6808 6246 325 103 -343 C
ATOM 1092 NE ARG A 159 42.867 -3.603 -17.518 1.00 55.76 N
ANISOU 1092 NE ARG A 159 7482 7171 6535 326 77 -328 N
ATOM 1093 CZ ARG A 159 41.631 -3.995 -17.785 1.00 61.94 C
ANISOU 1093 CZ ARG A 159 8271 7954 7310 313 20 -361 C
ATOM 1094 NH1 ARG A 159 41.252 -5.236 -17.485 1.00 60.62 N
ANISOU 1094 NH1 ARG A 159 8100 7755 7178 294 -14 -408 N
ATOM 1095 NH2 ARG A 159 40.776 -3.146 -18.341 1.00 64.88 N
ANISOU 1095 NH2 ARG A 159 8651 8358 7644 319 -3 -343 N
ATOM 1096 N HIS A 160 48.382 -3.378 -14.444 1.00 27.29 N
ANISOU 1096 N HIS A 160 3749 3505 3114 320 278 -216 N
ATOM 1097 CA HIS A 160 49.234 -2.290 -13.972 1.00 30.98 C
ANISOU 1097 CA HIS A 160 4178 3981 3613 302 316 -162 C
ATOM 1098 C HIS A 160 48.692 -0.940 -14.448 1.00 32.36 C
ANISOU 1098 C HIS A 160 4366 4175 3752 294 322 -125 C
ATOM 1099 O HIS A 160 48.685 -0.644 -15.648 1.00 41.89 O
ANISOU 1099 O HIS A 160 5605 5413 4899 325 349 -119 O
ATOM 1100 CB HIS A 160 50.668 -2.486 -14.459 1.00 32.47 C
ANISOU 1100 CB HIS A 160 4348 4187 3804 333 377 -151 C
ATOM 1101 CG HIS A 160 51.657 -1.547 -13.836 1.00 34.73 C
ANISOU 1101 CG HIS A 160 4583 4475 4138 308 412 -100 C
ATOM 1102 ND1 HIS A 160 52.195 -1.754 -12.582 1.00 35.15 N
ANISOU 1102 ND1 HIS A 160 4591 4505 4259 283 397 -95 N
ATOM 1103 CD2 HIS A 160 52.216 -0.404 -14.299 1.00 30.24 C
ANISOU 1103 CD2 HIS A 160 4001 3926 3561 304 459 -53 C
ATOM 1104 CE1 HIS A 160 53.046 -0.784 -12.304 1.00 34.36 C
ANISOU 1104 CE1 HIS A 160 4450 4414 4192 263 429 -52 C
ATOM 1105 NE2 HIS A 160 53.077 0.051 -13.328 1.00 32.09 N
ANISOU 1105 NE2 HIS A 160 4180 4149 3864 273 469 -25 N
ATOM 1106 N LEU A 161 48.244 -0.123 -13.501 1.00 20.79 N
ANISOU 1106 N LEU A 161 2881 2694 2325 256 299 -101 N
ATOM 1107 CA LEU A 161 47.627 1.166 -13.816 1.00 23.18 C
ANISOU 1107 CA LEU A 161 3198 3007 2605 248 299 -66 C
ATOM 1108 C LEU A 161 48.499 2.349 -13.410 1.00 24.25 C
ANISOU 1108 C LEU A 161 3300 3134 2779 226 338 -15 C
ATOM 1109 O LEU A 161 49.162 2.335 -12.367 1.00 18.49 O
ANISOU 1109 O LEU A 161 2530 2386 2108 199 338 -11 O
ATOM 1110 CB LEU A 161 46.264 1.288 -13.113 1.00 27.52 C
ANISOU 1110 CB LEU A 161 3752 3541 3164 225 241 -81 C
ATOM 1111 CG LEU A 161 45.274 0.119 -13.225 1.00 28.80 C
ANISOU 1111 CG LEU A 161 3934 3700 3307 232 193 -132 C
ATOM 1112 CD1 LEU A 161 43.957 0.466 -12.577 1.00 24.25 C
ANISOU 1112 CD1 LEU A 161 3355 3116 2744 208 144 -135 C
ATOM 1113 CD2 LEU A 161 45.060 -0.285 -14.681 1.00 30.33 C
ANISOU 1113 CD2 LEU A 161 4170 3922 3430 272 197 -155 C
ATOM 1114 N THR A 162 48.467 3.389 -14.227 1.00 24.62 N
ANISOU 1114 N THR A 162 3366 3195 2794 236 367 24 N
ATOM 1115 CA THR A 162 49.188 4.620 -13.938 1.00 19.66 C
ANISOU 1115 CA THR A 162 2711 2553 2206 211 403 74 C
ATOM 1116 C THR A 162 48.232 5.795 -14.136 1.00 24.71 C
ANISOU 1116 C THR A 162 3377 3184 2828 207 389 103 C
ATOM 1117 O THR A 162 47.239 5.681 -14.859 1.00 25.32 O
ANISOU 1117 O THR A 162 3494 3280 2848 234 366 93 O
ATOM 1118 CB THR A 162 50.455 4.772 -14.838 1.00 32.41 C
ANISOU 1118 CB THR A 162 4316 4190 3809 230 475 108 C
ATOM 1119 OG1 THR A 162 50.077 4.877 -16.215 1.00 24.29 O
ANISOU 1119 OG1 THR A 162 3335 3193 2701 270 497 121 O
ATOM 1120 CG2 THR A 162 51.395 3.574 -14.671 1.00 23.56 C
ANISOU 1120 CG2 THR A 162 3167 3079 2706 242 490 77 C
ATOM 1121 N PRO A 163 48.510 6.926 -13.473 1.00 26.73 N
ANISOU 1121 N PRO A 163 3609 3411 3136 174 398 137 N
ATOM 1122 CA PRO A 163 47.565 8.053 -13.528 1.00 25.01 C
ANISOU 1122 CA PRO A 163 3416 3177 2910 171 381 162 C
ATOM 1123 C PRO A 163 47.543 8.853 -14.849 1.00 27.97 C
ANISOU 1123 C PRO A 163 3826 3565 3235 200 421 213 C
ATOM 1124 O PRO A 163 46.663 9.691 -15.038 1.00 30.07 O
ANISOU 1124 O PRO A 163 4118 3821 3486 208 404 234 O
ATOM 1125 CB PRO A 163 48.007 8.936 -12.357 1.00 21.04 C
ANISOU 1125 CB PRO A 163 2878 2633 2484 127 380 175 C
ATOM 1126 CG PRO A 163 49.455 8.572 -12.125 1.00 17.20 C
ANISOU 1126 CG PRO A 163 2349 2149 2038 109 416 178 C
ATOM 1127 CD PRO A 163 49.558 7.118 -12.451 1.00 18.27 C
ANISOU 1127 CD PRO A 163 2487 2316 2138 136 411 141 C
ATOM 1128 N THR A 164 48.477 8.595 -15.755 1.00 31.57 N
ANISOU 1128 N THR A 164 4284 4048 3664 219 475 234 N
ATOM 1129 CA THR A 164 48.510 9.321 -17.022 1.00 34.13 C
ANISOU 1129 CA THR A 164 4644 4390 3934 249 519 289 C
ATOM 1130 C THR A 164 48.634 8.379 -18.198 1.00 43.24 C
ANISOU 1130 C THR A 164 5827 5596 5007 297 538 272 C
ATOM 1131 O THR A 164 48.665 8.816 -19.343 1.00 55.94 O
ANISOU 1131 O THR A 164 7456 7224 6575 320 555 303 O
ATOM 1132 CB THR A 164 49.707 10.272 -17.105 1.00 33.47 C
ANISOU 1132 CB THR A 164 4533 4286 3898 224 586 350 C
ATOM 1133 OG1 THR A 164 50.920 9.515 -17.010 1.00 37.92 O
ANISOU 1133 OG1 THR A 164 5056 4865 4485 217 623 336 O
ATOM 1134 CG2 THR A 164 49.669 11.302 -15.985 1.00 35.02 C
ANISOU 1134 CG2 THR A 164 4703 4425 4178 175 568 363 C
ATOM 1135 N GLY A 165 48.719 7.086 -17.919 1.00 38.55 N
ANISOU 1135 N GLY A 165 5223 5017 4410 303 515 213 N
ATOM 1136 CA GLY A 165 48.907 6.105 -18.971 1.00 43.47 C
ANISOU 1136 CA GLY A 165 5863 5678 4976 340 517 181 C
ATOM 1137 C GLY A 165 47.683 5.855 -19.831 1.00 46.82 C
ANISOU 1137 C GLY A 165 6332 6127 5331 371 466 156 C
ATOM 1138 O GLY A 165 46.781 6.694 -19.947 1.00 49.15 O
ANISOU 1138 O GLY A 165 6648 6417 5609 374 442 181 O
ATOM 1139 N GLU A 166 47.661 4.684 -20.454 1.00 46.79 N
ANISOU 1139 N GLU A 166 6340 6148 5291 395 448 105 N
ATOM 1140 CA GLU A 166 46.553 4.307 -21.317 1.00 44.92 C
ANISOU 1140 CA GLU A 166 6139 5936 4992 421 395 72 C
ATOM 1141 C GLU A 166 45.362 3.897 -20.460 1.00 43.10 C
ANISOU 1141 C GLU A 166 5911 5688 4777 406 329 29 C
ATOM 1142 O GLU A 166 44.217 3.993 -20.891 1.00 44.03 O
ANISOU 1142 O GLU A 166 6049 5819 4860 418 280 16 O
ATOM 1143 CB GLU A 166 46.969 3.156 -22.244 1.00 41.48 C
ANISOU 1143 CB GLU A 166 5715 5527 4518 448 399 28 C
ATOM 1144 N ASP A 167 45.642 3.445 -19.239 1.00 37.88 N
ANISOU 1144 N ASP A 167 5224 5000 4171 379 328 8 N
ATOM 1145 CA ASP A 167 44.596 3.000 -18.335 1.00 45.14 C
ANISOU 1145 CA ASP A 167 6141 5901 5110 362 269 -33 C
ATOM 1146 C ASP A 167 44.242 4.065 -17.284 1.00 35.92 C
ANISOU 1146 C ASP A 167 4950 4703 3994 328 260 3 C
ATOM 1147 O ASP A 167 43.698 3.742 -16.227 1.00 27.05 O
ANISOU 1147 O ASP A 167 3803 3555 2921 298 219 -23 O
ATOM 1148 CB ASP A 167 44.994 1.681 -17.661 1.00 54.98 C
ANISOU 1148 CB ASP A 167 7370 7129 6392 350 259 -86 C
ATOM 1149 CG ASP A 167 44.288 0.467 -18.266 1.00 66.61 C
ANISOU 1149 CG ASP A 167 8859 8610 7839 361 208 -147 C
ATOM 1150 OD1 ASP A 167 43.105 0.582 -18.669 1.00 67.14 O
ANISOU 1150 OD1 ASP A 167 8941 8690 7878 363 159 -160 O
ATOM 1151 OD2 ASP A 167 44.919 -0.612 -18.329 1.00 70.29 O
ANISOU 1151 OD2 ASP A 167 9320 9068 8318 366 218 -182 O
ATOM 1152 N ALA A 168 44.537 5.327 -17.589 1.00 22.99 N
ANISOU 1152 N ALA A 168 3318 3065 2352 332 297 63 N
ATOM 1153 CA ALA A 168 44.270 6.430 -16.662 1.00 28.24 C
ANISOU 1153 CA ALA A 168 3961 3694 3074 300 290 97 C
ATOM 1154 C ALA A 168 42.817 6.472 -16.194 1.00 23.88 C
ANISOU 1154 C ALA A 168 3411 3138 2526 295 225 72 C
ATOM 1155 O ALA A 168 42.532 6.768 -15.039 1.00 23.03 O
ANISOU 1155 O ALA A 168 3275 2999 2475 263 205 68 O
ATOM 1156 CB ALA A 168 44.648 7.769 -17.300 1.00 23.86 C
ANISOU 1156 CB ALA A 168 3422 3137 2506 311 337 166 C
ATOM 1157 N GLU A 169 41.909 6.186 -17.113 1.00 17.58 N
ANISOU 1157 N GLU A 169 2645 2373 1662 329 192 55 N
ATOM 1158 CA GLU A 169 40.491 6.211 -16.824 1.00 23.95 C
ANISOU 1158 CA GLU A 169 3449 3183 2468 329 130 33 C
ATOM 1159 C GLU A 169 40.147 5.202 -15.728 1.00 23.85 C
ANISOU 1159 C GLU A 169 3404 3152 2506 295 94 -19 C
ATOM 1160 O GLU A 169 39.472 5.529 -14.753 1.00 15.84 O
ANISOU 1160 O GLU A 169 2364 2119 1536 272 68 -21 O
ATOM 1161 CB GLU A 169 39.717 5.913 -18.098 1.00 24.61 C
ANISOU 1161 CB GLU A 169 3570 3312 2469 372 100 17 C
ATOM 1162 CG GLU A 169 38.226 5.928 -17.946 1.00 32.70 C
ANISOU 1162 CG GLU A 169 4588 4347 3490 376 33 -6 C
ATOM 1163 CD GLU A 169 37.535 5.625 -19.259 1.00 36.74 C
ANISOU 1163 CD GLU A 169 5118 4899 3944 407 -2 -23 C
ATOM 1164 OE1 GLU A 169 37.473 4.434 -19.647 1.00 34.02 O
ANISOU 1164 OE1 GLU A 169 4771 4566 3589 401 -26 -76 O
ATOM 1165 OE2 GLU A 169 37.080 6.583 -19.914 1.00 38.22 O
ANISOU 1165 OE2 GLU A 169 5319 5100 4102 434 -6 17 O
ATOM 1166 N LEU A 170 40.641 3.982 -15.887 1.00 21.26 N
ANISOU 1166 N LEU A 170 3077 2830 2171 293 96 -59 N
ATOM 1167 CA LEU A 170 40.396 2.934 -14.920 1.00 19.35 C
ANISOU 1167 CA LEU A 170 2808 2568 1976 263 66 -103 C
ATOM 1168 C LEU A 170 41.114 3.256 -13.601 1.00 25.08 C
ANISOU 1168 C LEU A 170 3499 3260 2772 228 90 -83 C
ATOM 1169 O LEU A 170 40.582 3.032 -12.507 1.00 24.10 O
ANISOU 1169 O LEU A 170 3348 3117 2691 200 63 -97 O
ATOM 1170 CB LEU A 170 40.841 1.586 -15.490 1.00 17.25 C
ANISOU 1170 CB LEU A 170 2558 2310 1688 275 66 -148 C
ATOM 1171 CG LEU A 170 40.691 0.379 -14.562 1.00 20.37 C
ANISOU 1171 CG LEU A 170 2929 2677 2133 246 39 -190 C
ATOM 1172 CD1 LEU A 170 39.279 0.288 -14.006 1.00 8.96 C
ANISOU 1172 CD1 LEU A 170 1466 1228 708 224 -16 -208 C
ATOM 1173 CD2 LEU A 170 41.068 -0.907 -15.287 1.00 16.78 C
ANISOU 1173 CD2 LEU A 170 2497 2226 1653 265 37 -238 C
ATOM 1174 N PHE A 171 42.311 3.812 -13.717 1.00 18.43 N
ANISOU 1174 N PHE A 171 2655 2411 1938 229 142 -48 N
ATOM 1175 CA PHE A 171 43.095 4.185 -12.555 1.00 20.40 C
ANISOU 1175 CA PHE A 171 2870 2632 2250 197 162 -31 C
ATOM 1176 C PHE A 171 42.310 5.170 -11.696 1.00 19.88 C
ANISOU 1176 C PHE A 171 2791 2548 2213 178 140 -15 C
ATOM 1177 O PHE A 171 42.200 5.014 -10.479 1.00 19.39 O
ANISOU 1177 O PHE A 171 2703 2468 2196 151 124 -28 O
ATOM 1178 CB PHE A 171 44.425 4.799 -13.009 1.00 22.04 C
ANISOU 1178 CB PHE A 171 3076 2839 2460 202 221 8 C
ATOM 1179 CG PHE A 171 45.291 5.304 -11.882 1.00 18.22 C
ANISOU 1179 CG PHE A 171 2554 2327 2042 168 239 25 C
ATOM 1180 CD1 PHE A 171 46.357 4.553 -11.424 1.00 13.29 C
ANISOU 1180 CD1 PHE A 171 1902 1698 1449 157 256 13 C
ATOM 1181 CD2 PHE A 171 45.049 6.550 -11.300 1.00 22.12 C
ANISOU 1181 CD2 PHE A 171 3041 2798 2567 148 237 52 C
ATOM 1182 CE1 PHE A 171 47.158 5.021 -10.393 1.00 17.98 C
ANISOU 1182 CE1 PHE A 171 2459 2271 2101 126 266 26 C
ATOM 1183 CE2 PHE A 171 45.832 7.016 -10.270 1.00 20.18 C
ANISOU 1183 CE2 PHE A 171 2762 2527 2379 116 247 61 C
ATOM 1184 CZ PHE A 171 46.903 6.254 -9.823 1.00 19.26 C
ANISOU 1184 CZ PHE A 171 2615 2412 2292 104 260 48 C
ATOM 1185 N TRP A 172 41.767 6.193 -12.333 1.00 16.15 N
ANISOU 1185 N TRP A 172 2340 2083 1714 197 142 13 N
ATOM 1186 CA TRP A 172 41.076 7.228 -11.592 1.00 17.79 C
ANISOU 1186 CA TRP A 172 2538 2270 1951 186 126 29 C
ATOM 1187 C TRP A 172 39.654 6.836 -11.152 1.00 17.22 C
ANISOU 1187 C TRP A 172 2458 2208 1877 186 75 -1 C
ATOM 1188 O TRP A 172 39.083 7.466 -10.263 1.00 17.28 O
ANISOU 1188 O TRP A 172 2449 2200 1915 175 61 1 O
ATOM 1189 CB TRP A 172 41.124 8.555 -12.350 1.00 18.13 C
ANISOU 1189 CB TRP A 172 2606 2308 1977 206 151 78 C
ATOM 1190 CG TRP A 172 42.482 9.181 -12.300 1.00 20.63 C
ANISOU 1190 CG TRP A 172 2915 2601 2324 190 203 112 C
ATOM 1191 CD1 TRP A 172 43.408 9.225 -13.309 1.00 19.46 C
ANISOU 1191 CD1 TRP A 172 2781 2465 2148 204 248 142 C
ATOM 1192 CD2 TRP A 172 43.083 9.841 -11.172 1.00 19.43 C
ANISOU 1192 CD2 TRP A 172 2736 2411 2237 154 214 119 C
ATOM 1193 NE1 TRP A 172 44.539 9.879 -12.881 1.00 19.96 N
ANISOU 1193 NE1 TRP A 172 2823 2499 2263 176 288 169 N
ATOM 1194 CE2 TRP A 172 44.372 10.265 -11.577 1.00 19.44 C
ANISOU 1194 CE2 TRP A 172 2731 2401 2253 145 265 153 C
ATOM 1195 CE3 TRP A 172 42.655 10.122 -9.867 1.00 9.92 C
ANISOU 1195 CE3 TRP A 172 1510 1183 1076 131 187 98 C
ATOM 1196 CZ2 TRP A 172 45.241 10.957 -10.720 1.00 23.72 C
ANISOU 1196 CZ2 TRP A 172 3246 2907 2860 108 283 165 C
ATOM 1197 CZ3 TRP A 172 43.519 10.813 -9.015 1.00 15.05 C
ANISOU 1197 CZ3 TRP A 172 2138 1799 1781 99 204 106 C
ATOM 1198 CH2 TRP A 172 44.797 11.225 -9.446 1.00 21.36 C
ANISOU 1198 CH2 TRP A 172 2930 2585 2601 86 249 138 C
ATOM 1199 N ALA A 173 39.101 5.778 -11.738 1.00 14.39 N
ANISOU 1199 N ALA A 173 2108 1875 1485 198 47 -33 N
ATOM 1200 CA ALA A 173 37.853 5.226 -11.220 1.00 14.56 C
ANISOU 1200 CA ALA A 173 2110 1904 1516 189 0 -64 C
ATOM 1201 C ALA A 173 38.109 4.308 -10.013 1.00 15.76 C
ANISOU 1201 C ALA A 173 2235 2039 1715 154 -4 -89 C
ATOM 1202 O ALA A 173 37.230 4.122 -9.170 1.00 15.95 O
ANISOU 1202 O ALA A 173 2236 2062 1763 139 -29 -102 O
ATOM 1203 CB ALA A 173 37.100 4.491 -12.303 1.00 11.93 C
ANISOU 1203 CB ALA A 173 1795 1602 1135 211 -33 -91 C
ATOM 1204 N THR A 174 39.317 3.750 -9.943 1.00 12.71 N
ANISOU 1204 N THR A 174 1849 1642 1339 146 24 -91 N
ATOM 1205 CA THR A 174 39.759 2.943 -8.807 1.00 14.01 C
ANISOU 1205 CA THR A 174 1989 1788 1545 118 24 -106 C
ATOM 1206 C THR A 174 40.048 3.792 -7.559 1.00 19.28 C
ANISOU 1206 C THR A 174 2636 2439 2252 98 35 -86 C
ATOM 1207 O THR A 174 39.645 3.445 -6.444 1.00 11.96 O
ANISOU 1207 O THR A 174 1687 1505 1351 79 19 -96 O
ATOM 1208 CB THR A 174 41.016 2.130 -9.181 1.00 11.78 C
ANISOU 1208 CB THR A 174 1713 1500 1261 123 50 -113 C
ATOM 1209 OG1 THR A 174 40.718 1.297 -10.312 1.00 11.96 O
ANISOU 1209 OG1 THR A 174 1761 1539 1246 144 37 -139 O
ATOM 1210 CG2 THR A 174 41.456 1.259 -8.026 1.00 5.96 C
ANISOU 1210 CG2 THR A 174 952 745 566 100 46 -124 C
ATOM 1211 N VAL A 175 40.766 4.897 -7.749 1.00 15.30 N
ANISOU 1211 N VAL A 175 2137 1926 1751 103 63 -59 N
ATOM 1212 CA VAL A 175 40.875 5.899 -6.708 1.00 11.64 C
ANISOU 1212 CA VAL A 175 1658 1444 1320 86 68 -45 C
ATOM 1213 C VAL A 175 39.457 6.351 -6.332 1.00 18.82 C
ANISOU 1213 C VAL A 175 2566 2359 2226 92 40 -51 C
ATOM 1214 O VAL A 175 38.680 6.753 -7.207 1.00 10.38 O
ANISOU 1214 O VAL A 175 1513 1301 1129 115 31 -44 O
ATOM 1215 CB VAL A 175 41.659 7.112 -7.209 1.00 15.97 C
ANISOU 1215 CB VAL A 175 2217 1977 1873 91 100 -14 C
ATOM 1216 CG1 VAL A 175 41.561 8.253 -6.216 1.00 5.92 C
ANISOU 1216 CG1 VAL A 175 934 680 634 76 98 -7 C
ATOM 1217 CG2 VAL A 175 43.105 6.724 -7.465 1.00 15.62 C
ANISOU 1217 CG2 VAL A 175 2164 1930 1839 83 132 -6 C
ATOM 1218 N GLY A 176 39.112 6.237 -5.047 1.00 16.93 N
ANISOU 1218 N GLY A 176 2305 2116 2012 74 27 -64 N
ATOM 1219 CA GLY A 176 37.772 6.554 -4.566 1.00 14.74 C
ANISOU 1219 CA GLY A 176 2019 1848 1734 80 5 -71 C
ATOM 1220 C GLY A 176 36.680 5.585 -5.012 1.00 18.24 C
ANISOU 1220 C GLY A 176 2456 2314 2160 85 -21 -87 C
ATOM 1221 O GLY A 176 35.490 5.823 -4.791 1.00 19.65 O
ANISOU 1221 O GLY A 176 2622 2506 2339 93 -39 -91 O
ATOM 1222 N GLY A 177 37.079 4.480 -5.630 1.00 12.69 N
ANISOU 1222 N GLY A 177 1760 1616 1447 81 -24 -98 N
ATOM 1223 CA GLY A 177 36.124 3.556 -6.207 1.00 12.91 C
ANISOU 1223 CA GLY A 177 1784 1660 1460 84 -53 -119 C
ATOM 1224 C GLY A 177 35.519 2.536 -5.257 1.00 16.31 C
ANISOU 1224 C GLY A 177 2188 2091 1917 58 -69 -134 C
ATOM 1225 O GLY A 177 34.738 1.682 -5.682 1.00 15.77 O
ANISOU 1225 O GLY A 177 2113 2031 1847 53 -94 -153 O
ATOM 1226 N ASN A 178 35.883 2.612 -3.981 1.00 10.06 N
ANISOU 1226 N ASN A 178 1382 1289 1150 42 -55 -125 N
ATOM 1227 CA ASN A 178 35.313 1.726 -2.972 1.00 20.28 C
ANISOU 1227 CA ASN A 178 2653 2586 2468 20 -63 -131 C
ATOM 1228 C ASN A 178 35.375 0.232 -3.337 1.00 17.72 C
ANISOU 1228 C ASN A 178 2330 2249 2152 5 -76 -146 C
ATOM 1229 O ASN A 178 34.451 -0.531 -3.044 1.00 10.06 O
ANISOU 1229 O ASN A 178 1340 1282 1200 -13 -92 -153 O
ATOM 1230 CB ASN A 178 33.874 2.141 -2.661 1.00 17.67 C
ANISOU 1230 CB ASN A 178 2299 2275 2141 22 -77 -131 C
ATOM 1231 CG ASN A 178 33.784 3.499 -1.962 1.00 17.71 C
ANISOU 1231 CG ASN A 178 2300 2285 2144 36 -63 -119 C
ATOM 1232 OD1 ASN A 178 33.817 3.577 -0.739 1.00 20.36 O
ANISOU 1232 OD1 ASN A 178 2624 2621 2491 26 -51 -114 O
ATOM 1233 ND2 ASN A 178 33.653 4.568 -2.743 1.00 16.77 N
ANISOU 1233 ND2 ASN A 178 2196 2167 2009 61 -64 -114 N
ATOM 1234 N GLY A 179 36.462 -0.166 -3.998 1.00 11.97 N
ANISOU 1234 N GLY A 179 1624 1508 1417 13 -66 -152 N
ATOM 1235 CA GLY A 179 36.719 -1.559 -4.313 1.00 8.73 C
ANISOU 1235 CA GLY A 179 1221 1080 1018 4 -74 -169 C
ATOM 1236 C GLY A 179 35.922 -2.074 -5.491 1.00 14.07 C
ANISOU 1236 C GLY A 179 1906 1761 1678 8 -102 -198 C
ATOM 1237 O GLY A 179 36.023 -3.236 -5.871 1.00 13.81 O
ANISOU 1237 O GLY A 179 1883 1710 1656 1 -113 -220 O
ATOM 1238 N LEU A 180 35.118 -1.210 -6.083 1.00 14.56 N
ANISOU 1238 N LEU A 180 1966 1848 1717 22 -116 -198 N
ATOM 1239 CA LEU A 180 34.177 -1.676 -7.080 1.00 11.70 C
ANISOU 1239 CA LEU A 180 1607 1498 1342 24 -151 -227 C
ATOM 1240 C LEU A 180 34.745 -1.729 -8.493 1.00 14.03 C
ANISOU 1240 C LEU A 180 1938 1799 1592 53 -154 -246 C
ATOM 1241 O LEU A 180 33.989 -1.919 -9.428 1.00 16.47 O
ANISOU 1241 O LEU A 180 2253 2125 1878 62 -186 -271 O
ATOM 1242 CB LEU A 180 32.896 -0.851 -7.038 1.00 11.48 C
ANISOU 1242 CB LEU A 180 1554 1498 1309 28 -171 -220 C
ATOM 1243 CG LEU A 180 32.065 -1.018 -5.770 1.00 20.06 C
ANISOU 1243 CG LEU A 180 2601 2585 2437 1 -172 -208 C
ATOM 1244 CD1 LEU A 180 30.997 0.093 -5.670 1.00 13.60 C
ANISOU 1244 CD1 LEU A 180 1759 1798 1613 16 -181 -196 C
ATOM 1245 CD2 LEU A 180 31.419 -2.432 -5.709 1.00 8.19 C
ANISOU 1245 CD2 LEU A 180 1078 1067 967 -32 -197 -231 C
ATOM 1246 N THR A 181 36.061 -1.565 -8.656 1.00 19.95 N
ANISOU 1246 N THR A 181 2711 2540 2331 68 -119 -235 N
ATOM 1247 CA THR A 181 36.693 -1.848 -9.960 1.00 24.75 C
ANISOU 1247 CA THR A 181 3354 3154 2897 95 -115 -254 C
ATOM 1248 C THR A 181 37.517 -3.131 -9.914 1.00 22.75 C
ANISOU 1248 C THR A 181 3110 2871 2662 90 -105 -278 C
ATOM 1249 O THR A 181 38.004 -3.606 -10.938 1.00 15.55 O
ANISOU 1249 O THR A 181 2228 1962 1719 113 -102 -303 O
ATOM 1250 CB THR A 181 37.604 -0.710 -10.482 1.00 19.61 C
ANISOU 1250 CB THR A 181 2721 2517 2211 123 -78 -224 C
ATOM 1251 OG1 THR A 181 38.694 -0.490 -9.575 1.00 22.59 O
ANISOU 1251 OG1 THR A 181 3087 2876 2621 112 -41 -198 O
ATOM 1252 CG2 THR A 181 36.813 0.575 -10.691 1.00 17.58 C
ANISOU 1252 CG2 THR A 181 2462 2284 1934 136 -87 -199 C
ATOM 1253 N GLY A 182 37.656 -3.689 -8.718 1.00 18.23 N
ANISOU 1253 N GLY A 182 2515 2272 2138 63 -101 -268 N
ATOM 1254 CA GLY A 182 38.483 -4.857 -8.512 1.00 16.51 C
ANISOU 1254 CA GLY A 182 2305 2022 1946 60 -90 -282 C
ATOM 1255 C GLY A 182 39.321 -4.749 -7.246 1.00 16.86 C
ANISOU 1255 C GLY A 182 2329 2051 2024 50 -63 -248 C
ATOM 1256 O GLY A 182 39.158 -3.830 -6.434 1.00 10.31 O
ANISOU 1256 O GLY A 182 1480 1235 1201 39 -56 -218 O
ATOM 1257 N ILE A 183 40.226 -5.703 -7.085 1.00 12.18 N
ANISOU 1257 N ILE A 183 1743 1431 1452 55 -50 -255 N
ATOM 1258 CA ILE A 183 41.034 -5.788 -5.884 1.00 13.83 C
ANISOU 1258 CA ILE A 183 1932 1627 1694 48 -32 -225 C
ATOM 1259 C ILE A 183 42.396 -5.169 -6.126 1.00 17.88 C
ANISOU 1259 C ILE A 183 2446 2153 2194 72 2 -210 C
ATOM 1260 O ILE A 183 43.126 -5.584 -7.024 1.00 17.04 O
ANISOU 1260 O ILE A 183 2357 2044 2074 98 17 -228 O
ATOM 1261 CB ILE A 183 41.138 -7.251 -5.408 1.00 19.11 C
ANISOU 1261 CB ILE A 183 2603 2255 2402 39 -41 -234 C
ATOM 1262 CG1 ILE A 183 39.736 -7.730 -5.019 1.00 19.76 C
ANISOU 1262 CG1 ILE A 183 2677 2325 2506 7 -71 -240 C
ATOM 1263 CG2 ILE A 183 42.101 -7.389 -4.213 1.00 14.20 C
ANISOU 1263 CG2 ILE A 183 1964 1624 1809 39 -24 -201 C
ATOM 1264 CD1 ILE A 183 39.624 -9.183 -4.918 1.00 27.42 C
ANISOU 1264 CD1 ILE A 183 3656 3249 3514 -4 -84 -257 C
ATOM 1265 N ILE A 184 42.716 -4.134 -5.357 1.00 16.71 N
ANISOU 1265 N ILE A 184 2278 2022 2050 63 14 -179 N
ATOM 1266 CA ILE A 184 44.038 -3.558 -5.437 1.00 13.90 C
ANISOU 1266 CA ILE A 184 1913 1675 1694 78 44 -163 C
ATOM 1267 C ILE A 184 44.960 -4.532 -4.709 1.00 14.00 C
ANISOU 1267 C ILE A 184 1912 1668 1740 83 49 -158 C
ATOM 1268 O ILE A 184 44.707 -4.888 -3.568 1.00 19.08 O
ANISOU 1268 O ILE A 184 2542 2300 2406 66 33 -146 O
ATOM 1269 CB ILE A 184 44.087 -2.159 -4.820 1.00 13.17 C
ANISOU 1269 CB ILE A 184 1803 1599 1601 65 51 -137 C
ATOM 1270 CG1 ILE A 184 43.022 -1.253 -5.465 1.00 13.45 C
ANISOU 1270 CG1 ILE A 184 1853 1650 1608 64 43 -139 C
ATOM 1271 CG2 ILE A 184 45.484 -1.574 -4.976 1.00 7.68 C
ANISOU 1271 CG2 ILE A 184 1094 911 913 75 82 -120 C
ATOM 1272 CD1 ILE A 184 42.618 -0.056 -4.623 1.00 10.25 C
ANISOU 1272 CD1 ILE A 184 1434 1252 1209 48 39 -120 C
ATOM 1273 N MET A 185 45.993 -5.005 -5.399 1.00 12.95 N
ANISOU 1273 N MET A 185 1783 1531 1607 109 71 -167 N
ATOM 1274 CA MET A 185 46.874 -6.029 -4.866 1.00 12.70 C
ANISOU 1274 CA MET A 185 1739 1478 1607 122 75 -164 C
ATOM 1275 C MET A 185 48.100 -5.370 -4.246 1.00 19.46 C
ANISOU 1275 C MET A 185 2561 2351 2480 125 94 -137 C
ATOM 1276 O MET A 185 48.634 -5.819 -3.228 1.00 18.42 O
ANISOU 1276 O MET A 185 2409 2212 2378 124 84 -122 O
ATOM 1277 CB MET A 185 47.309 -6.975 -5.987 1.00 15.92 C
ANISOU 1277 CB MET A 185 2170 1873 2007 155 90 -195 C
ATOM 1278 CG MET A 185 46.168 -7.814 -6.621 1.00 17.04 C
ANISOU 1278 CG MET A 185 2346 1991 2137 152 65 -231 C
ATOM 1279 SD MET A 185 45.329 -8.897 -5.416 1.00 18.60 S
ANISOU 1279 SD MET A 185 2541 2147 2379 123 30 -226 S
ATOM 1280 CE MET A 185 46.469 -10.265 -5.318 1.00 25.05 C
ANISOU 1280 CE MET A 185 3362 2924 3232 157 42 -233 C
ATOM 1281 N ARG A 186 48.506 -4.262 -4.854 1.00 15.83 N
ANISOU 1281 N ARG A 186 2095 1916 2004 126 117 -129 N
ATOM 1282 CA ARG A 186 49.836 -3.738 -4.666 1.00 15.18 C
ANISOU 1282 CA ARG A 186 1978 1848 1941 132 142 -110 C
ATOM 1283 C ARG A 186 49.857 -2.343 -5.262 1.00 19.20 C
ANISOU 1283 C ARG A 186 2485 2377 2432 121 163 -97 C
ATOM 1284 O ARG A 186 49.146 -2.067 -6.229 1.00 23.43 O
ANISOU 1284 O ARG A 186 3052 2918 2932 127 170 -106 O
ATOM 1285 CB ARG A 186 50.817 -4.655 -5.398 1.00 13.54 C
ANISOU 1285 CB ARG A 186 1767 1637 1740 169 168 -121 C
ATOM 1286 CG ARG A 186 52.273 -4.274 -5.286 1.00 15.61 C
ANISOU 1286 CG ARG A 186 1985 1917 2028 179 197 -102 C
ATOM 1287 CD ARG A 186 53.114 -5.482 -5.683 1.00 20.19 C
ANISOU 1287 CD ARG A 186 2561 2488 2622 220 215 -115 C
ATOM 1288 NE ARG A 186 54.523 -5.152 -5.798 1.00 24.33 N
ANISOU 1288 NE ARG A 186 3038 3035 3170 235 249 -97 N
ATOM 1289 CZ ARG A 186 55.495 -6.050 -5.897 1.00 28.95 C
ANISOU 1289 CZ ARG A 186 3602 3618 3779 272 265 -102 C
ATOM 1290 NH1 ARG A 186 55.210 -7.350 -5.878 1.00 23.99 N
ANISOU 1290 NH1 ARG A 186 3002 2960 3154 299 250 -124 N
ATOM 1291 NH2 ARG A 186 56.757 -5.640 -6.003 1.00 20.88 N
ANISOU 1291 NH2 ARG A 186 2529 2622 2782 283 298 -84 N
ATOM 1292 N ALA A 187 50.649 -1.449 -4.683 1.00 13.63 N
ANISOU 1292 N ALA A 187 1745 1681 1751 105 171 -76 N
ATOM 1293 CA ALA A 187 50.704 -0.085 -5.194 1.00 16.42 C
ANISOU 1293 CA ALA A 187 2098 2045 2096 91 193 -59 C
ATOM 1294 C ALA A 187 52.056 0.549 -4.938 1.00 19.00 C
ANISOU 1294 C ALA A 187 2379 2380 2460 82 216 -40 C
ATOM 1295 O ALA A 187 52.778 0.162 -4.014 1.00 13.85 O
ANISOU 1295 O ALA A 187 1692 1729 1841 78 201 -39 O
ATOM 1296 CB ALA A 187 49.576 0.783 -4.585 1.00 8.70 C
ANISOU 1296 CB ALA A 187 1134 1060 1110 65 165 -58 C
ATOM 1297 N THR A 188 52.385 1.523 -5.780 1.00 17.98 N
ANISOU 1297 N THR A 188 2248 2257 2326 78 252 -21 N
ATOM 1298 CA THR A 188 53.577 2.342 -5.603 1.00 18.48 C
ANISOU 1298 CA THR A 188 2265 2325 2431 59 275 2 C
ATOM 1299 C THR A 188 53.185 3.766 -5.222 1.00 18.14 C
ANISOU 1299 C THR A 188 2224 2267 2400 24 266 14 C
ATOM 1300 O THR A 188 52.514 4.450 -5.984 1.00 17.73 O
ANISOU 1300 O THR A 188 2205 2210 2322 25 281 26 O
ATOM 1301 CB THR A 188 54.430 2.349 -6.881 1.00 22.00 C
ANISOU 1301 CB THR A 188 2701 2787 2869 81 334 20 C
ATOM 1302 OG1 THR A 188 54.984 1.042 -7.074 1.00 17.44 O
ANISOU 1302 OG1 THR A 188 2115 2221 2291 116 342 4 O
ATOM 1303 CG2 THR A 188 55.553 3.347 -6.752 1.00 18.47 C
ANISOU 1303 CG2 THR A 188 2204 2343 2471 54 361 48 C
ATOM 1304 N ILE A 189 53.576 4.189 -4.023 1.00 20.55 N
ANISOU 1304 N ILE A 189 2497 2567 2746 -5 237 9 N
ATOM 1305 CA ILE A 189 53.210 5.506 -3.495 1.00 18.59 C
ANISOU 1305 CA ILE A 189 2251 2298 2514 -38 222 12 C
ATOM 1306 C ILE A 189 54.423 6.444 -3.484 1.00 20.07 C
ANISOU 1306 C ILE A 189 2393 2479 2755 -67 244 30 C
ATOM 1307 O ILE A 189 55.506 6.041 -3.080 1.00 17.49 O
ANISOU 1307 O ILE A 189 2018 2166 2463 -71 242 29 O
ATOM 1308 CB ILE A 189 52.698 5.402 -2.037 1.00 17.25 C
ANISOU 1308 CB ILE A 189 2081 2125 2348 -51 168 -13 C
ATOM 1309 CG1 ILE A 189 51.580 4.358 -1.892 1.00 17.00 C
ANISOU 1309 CG1 ILE A 189 2085 2100 2274 -27 146 -28 C
ATOM 1310 CG2 ILE A 189 52.279 6.772 -1.505 1.00 15.71 C
ANISOU 1310 CG2 ILE A 189 1894 1908 2168 -80 153 -17 C
ATOM 1311 CD1 ILE A 189 50.354 4.634 -2.738 1.00 18.58 C
ANISOU 1311 CD1 ILE A 189 2331 2293 2436 -16 155 -26 C
ATOM 1312 N GLU A 190 54.248 7.687 -3.925 1.00 21.26 N
ANISOU 1312 N GLU A 190 2555 2606 2917 -87 264 49 N
ATOM 1313 CA GLU A 190 55.304 8.686 -3.772 1.00 17.70 C
ANISOU 1313 CA GLU A 190 2059 2139 2526 -125 280 65 C
ATOM 1314 C GLU A 190 55.243 9.344 -2.395 1.00 20.87 C
ANISOU 1314 C GLU A 190 2447 2522 2961 -159 228 36 C
ATOM 1315 O GLU A 190 54.287 10.047 -2.066 1.00 19.41 O
ANISOU 1315 O GLU A 190 2299 2312 2763 -165 208 25 O
ATOM 1316 CB GLU A 190 55.254 9.744 -4.876 1.00 14.19 C
ANISOU 1316 CB GLU A 190 1634 1673 2087 -134 329 104 C
ATOM 1317 CG GLU A 190 56.255 10.867 -4.631 1.00 24.49 C
ANISOU 1317 CG GLU A 190 2892 2951 3464 -181 342 120 C
ATOM 1318 CD GLU A 190 56.480 11.781 -5.827 1.00 32.57 C
ANISOU 1318 CD GLU A 190 3924 3953 4498 -190 403 171 C
ATOM 1319 OE1 GLU A 190 57.276 12.738 -5.697 1.00 32.94 O
ANISOU 1319 OE1 GLU A 190 3933 3972 4612 -233 419 189 O
ATOM 1320 OE2 GLU A 190 55.877 11.548 -6.894 1.00 38.61 O
ANISOU 1320 OE2 GLU A 190 4732 4730 5207 -154 435 194 O
ATOM 1321 N MET A 191 56.264 9.095 -1.584 1.00 25.98 N
ANISOU 1321 N MET A 191 3040 3182 3648 -175 206 22 N
ATOM 1322 CA MET A 191 56.322 9.630 -0.229 1.00 15.51 C
ANISOU 1322 CA MET A 191 1698 1845 2349 -204 152 -11 C
ATOM 1323 C MET A 191 56.780 11.088 -0.190 1.00 22.19 C
ANISOU 1323 C MET A 191 2526 2652 3254 -251 158 -7 C
ATOM 1324 O MET A 191 57.244 11.647 -1.188 1.00 25.12 O
ANISOU 1324 O MET A 191 2886 3007 3654 -264 208 28 O
ATOM 1325 CB MET A 191 57.253 8.784 0.614 1.00 12.64 C
ANISOU 1325 CB MET A 191 1284 1515 2003 -201 121 -27 C
ATOM 1326 CG MET A 191 56.929 7.316 0.539 1.00 14.83 C
ANISOU 1326 CG MET A 191 1578 1824 2234 -156 119 -27 C
ATOM 1327 SD MET A 191 55.443 6.900 1.481 1.00 20.13 S
ANISOU 1327 SD MET A 191 2306 2495 2845 -138 73 -53 S
ATOM 1328 CE MET A 191 56.098 6.793 3.142 1.00 14.15 C
ANISOU 1328 CE MET A 191 1510 1759 2106 -151 10 -82 C
ATOM 1329 N THR A 192 56.631 11.705 0.972 1.00 20.69 N
ANISOU 1329 N THR A 192 2335 2446 3080 -275 108 -45 N
ATOM 1330 CA THR A 192 57.096 13.058 1.168 1.00 22.17 C
ANISOU 1330 CA THR A 192 2504 2590 3331 -323 104 -51 C
ATOM 1331 C THR A 192 58.417 13.018 1.945 1.00 29.37 C
ANISOU 1331 C THR A 192 3343 3518 4298 -355 72 -72 C
ATOM 1332 O THR A 192 58.533 12.320 2.965 1.00 22.82 O
ANISOU 1332 O THR A 192 2499 2723 3447 -342 23 -103 O
ATOM 1333 CB THR A 192 56.014 13.907 1.870 1.00 24.86 C
ANISOU 1333 CB THR A 192 2895 2896 3654 -327 71 -85 C
ATOM 1334 OG1 THR A 192 54.854 13.935 1.042 1.00 20.17 O
ANISOU 1334 OG1 THR A 192 2359 2290 3014 -296 102 -61 O
ATOM 1335 CG2 THR A 192 56.474 15.357 2.120 1.00 10.08 C
ANISOU 1335 CG2 THR A 192 1009 968 1853 -378 63 -98 C
ATOM 1336 N PRO A 193 59.432 13.719 1.423 1.00 27.83 N
ANISOU 1336 N PRO A 193 3099 3301 4174 -395 102 -49 N
ATOM 1337 CA PRO A 193 60.738 13.853 2.072 1.00 29.94 C
ANISOU 1337 CA PRO A 193 3288 3580 4508 -433 73 -67 C
ATOM 1338 C PRO A 193 60.590 14.611 3.374 1.00 33.87 C
ANISOU 1338 C PRO A 193 3791 4055 5023 -463 3 -125 C
ATOM 1339 O PRO A 193 59.916 15.646 3.413 1.00 32.45 O
ANISOU 1339 O PRO A 193 3659 3825 4848 -479 1 -137 O
ATOM 1340 CB PRO A 193 61.541 14.711 1.083 1.00 30.27 C
ANISOU 1340 CB PRO A 193 3298 3591 4614 -470 129 -24 C
ATOM 1341 CG PRO A 193 60.832 14.572 -0.218 1.00 35.41 C
ANISOU 1341 CG PRO A 193 3994 4231 5228 -441 198 26 C
ATOM 1342 CD PRO A 193 59.385 14.406 0.123 1.00 32.70 C
ANISOU 1342 CD PRO A 193 3731 3883 4811 -405 170 1 C
ATOM 1343 N THR A 194 61.206 14.099 4.432 1.00 28.67 N
ANISOU 1343 N THR A 194 3093 3437 4363 -462 -55 -160 N
ATOM 1344 CA THR A 194 61.233 14.805 5.702 1.00 27.06 C
ANISOU 1344 CA THR A 194 2902 3226 4153 -480 -123 -214 C
ATOM 1345 C THR A 194 62.574 14.506 6.354 1.00 32.78 C
ANISOU 1345 C THR A 194 3559 3994 4901 -492 -162 -226 C
ATOM 1346 O THR A 194 63.220 13.503 6.028 1.00 35.24 O
ANISOU 1346 O THR A 194 3823 4349 5219 -472 -147 -200 O
ATOM 1347 CB THR A 194 60.106 14.349 6.633 1.00 21.92 C
ANISOU 1347 CB THR A 194 2301 2591 3437 -448 -167 -255 C
ATOM 1348 OG1 THR A 194 60.069 15.183 7.799 1.00 19.26 O
ANISOU 1348 OG1 THR A 194 1985 2244 3088 -463 -224 -306 O
ATOM 1349 CG2 THR A 194 60.317 12.885 7.063 1.00 16.05 C
ANISOU 1349 CG2 THR A 194 1535 1914 2649 -407 -189 -251 C
ATOM 1350 N SER A 195 63.000 15.374 7.265 1.00 26.79 N
ANISOU 1350 N SER A 195 2797 3224 4157 -521 -211 -265 N
ATOM 1351 CA SER A 195 64.263 15.154 7.970 1.00 32.86 C
ANISOU 1351 CA SER A 195 3503 4036 4947 -534 -255 -280 C
ATOM 1352 C SER A 195 63.988 14.885 9.436 1.00 33.62 C
ANISOU 1352 C SER A 195 3620 4167 4988 -514 -331 -333 C
ATOM 1353 O SER A 195 64.882 14.486 10.187 1.00 34.76 O
ANISOU 1353 O SER A 195 3718 4357 5131 -513 -377 -347 O
ATOM 1354 CB SER A 195 65.211 16.348 7.806 1.00 32.37 C
ANISOU 1354 CB SER A 195 3408 3941 4952 -589 -251 -281 C
ATOM 1355 OG SER A 195 64.549 17.578 8.075 1.00 37.14 O
ANISOU 1355 OG SER A 195 4066 4485 5558 -613 -261 -310 O
ATOM 1356 N THR A 196 62.743 15.124 9.843 1.00 31.11 N
ANISOU 1356 N THR A 196 3373 3829 4621 -497 -342 -359 N
ATOM 1357 CA THR A 196 62.306 14.765 11.186 1.00 33.00 C
ANISOU 1357 CA THR A 196 3641 4105 4792 -469 -404 -403 C
ATOM 1358 C THR A 196 60.911 14.174 11.185 1.00 33.18 C
ANISOU 1358 C THR A 196 3724 4132 4752 -427 -391 -402 C
ATOM 1359 O THR A 196 60.169 14.280 10.208 1.00 32.95 O
ANISOU 1359 O THR A 196 3720 4065 4732 -425 -340 -378 O
ATOM 1360 CB THR A 196 62.283 15.958 12.162 1.00 35.26 C
ANISOU 1360 CB THR A 196 3957 4368 5074 -494 -448 -456 C
ATOM 1361 OG1 THR A 196 61.057 16.686 12.005 1.00 36.09 O
ANISOU 1361 OG1 THR A 196 4130 4423 5158 -489 -426 -470 O
ATOM 1362 CG2 THR A 196 63.481 16.880 11.943 1.00 29.32 C
ANISOU 1362 CG2 THR A 196 3155 3589 4397 -547 -450 -457 C
ATOM 1363 N ALA A 197 60.564 13.563 12.309 1.00 34.98 N
ANISOU 1363 N ALA A 197 3973 4406 4912 -394 -439 -428 N
ATOM 1364 CA ALA A 197 59.259 12.956 12.498 1.00 34.69 C
ANISOU 1364 CA ALA A 197 3991 4381 4808 -353 -433 -430 C
ATOM 1365 C ALA A 197 58.379 13.835 13.378 1.00 33.63 C
ANISOU 1365 C ALA A 197 3919 4230 4628 -349 -455 -475 C
ATOM 1366 O ALA A 197 57.447 13.345 14.005 1.00 39.18 O
ANISOU 1366 O ALA A 197 4665 4960 5260 -311 -466 -485 O
ATOM 1367 CB ALA A 197 59.415 11.575 13.119 1.00 29.00 C
ANISOU 1367 CB ALA A 197 3254 3727 4037 -312 -464 -418 C
ATOM 1368 N TYR A 198 58.684 15.129 13.424 1.00 29.78 N
ANISOU 1368 N TYR A 198 3436 3697 4181 -385 -458 -500 N
ATOM 1369 CA TYR A 198 57.953 16.067 14.274 1.00 26.22 C
ANISOU 1369 CA TYR A 198 3042 3227 3694 -381 -478 -546 C
ATOM 1370 C TYR A 198 57.368 17.234 13.487 1.00 28.53 C
ANISOU 1370 C TYR A 198 3367 3445 4029 -402 -438 -547 C
ATOM 1371 O TYR A 198 57.833 17.580 12.398 1.00 30.27 O
ANISOU 1371 O TYR A 198 3560 3625 4317 -433 -402 -515 O
ATOM 1372 CB TYR A 198 58.855 16.618 15.384 1.00 28.01 C
ANISOU 1372 CB TYR A 198 3251 3470 3922 -401 -534 -588 C
ATOM 1373 CG TYR A 198 59.416 15.557 16.301 1.00 29.41 C
ANISOU 1373 CG TYR A 198 3401 3722 4052 -376 -580 -588 C
ATOM 1374 CD1 TYR A 198 58.808 15.267 17.515 1.00 34.65 C
ANISOU 1374 CD1 TYR A 198 4107 4428 4631 -339 -612 -615 C
ATOM 1375 CD2 TYR A 198 60.553 14.845 15.951 1.00 32.59 C
ANISOU 1375 CD2 TYR A 198 3737 4153 4492 -386 -587 -558 C
ATOM 1376 CE1 TYR A 198 59.316 14.289 18.356 1.00 39.80 C
ANISOU 1376 CE1 TYR A 198 4738 5147 5236 -313 -653 -608 C
ATOM 1377 CE2 TYR A 198 61.069 13.864 16.782 1.00 39.78 C
ANISOU 1377 CE2 TYR A 198 4624 5132 5360 -359 -630 -553 C
ATOM 1378 CZ TYR A 198 60.450 13.595 17.981 1.00 41.13 C
ANISOU 1378 CZ TYR A 198 4841 5342 5446 -323 -663 -577 C
ATOM 1379 OH TYR A 198 60.968 12.628 18.800 1.00 46.11 O
ANISOU 1379 OH TYR A 198 5450 6037 6031 -293 -704 -566 O
ATOM 1380 N PHE A 199 56.339 17.841 14.061 1.00 28.32 N
ANISOU 1380 N PHE A 199 3400 3402 3960 -383 -442 -580 N
ATOM 1381 CA PHE A 199 55.731 19.026 13.494 1.00 24.68 C
ANISOU 1381 CA PHE A 199 2975 2870 3533 -396 -410 -586 C
ATOM 1382 C PHE A 199 56.106 20.232 14.340 1.00 33.57 C
ANISOU 1382 C PHE A 199 4114 3968 4674 -419 -445 -636 C
ATOM 1383 O PHE A 199 56.310 20.116 15.557 1.00 36.07 O
ANISOU 1383 O PHE A 199 4434 4326 4945 -409 -492 -676 O
ATOM 1384 CB PHE A 199 54.202 18.887 13.492 1.00 24.49 C
ANISOU 1384 CB PHE A 199 3009 2845 3452 -351 -386 -588 C
ATOM 1385 CG PHE A 199 53.685 17.815 12.575 1.00 28.28 C
ANISOU 1385 CG PHE A 199 3483 3342 3920 -330 -350 -542 C
ATOM 1386 CD1 PHE A 199 53.344 18.115 11.260 1.00 25.30 C
ANISOU 1386 CD1 PHE A 199 3111 2914 3588 -340 -300 -505 C
ATOM 1387 CD2 PHE A 199 53.532 16.514 13.027 1.00 25.69 C
ANISOU 1387 CD2 PHE A 199 3146 3080 3535 -300 -364 -534 C
ATOM 1388 CE1 PHE A 199 52.873 17.139 10.416 1.00 29.59 C
ANISOU 1388 CE1 PHE A 199 3650 3472 4119 -322 -268 -467 C
ATOM 1389 CE2 PHE A 199 53.055 15.536 12.190 1.00 32.15 C
ANISOU 1389 CE2 PHE A 199 3959 3910 4344 -283 -333 -496 C
ATOM 1390 CZ PHE A 199 52.727 15.843 10.880 1.00 32.29 C
ANISOU 1390 CZ PHE A 199 3985 3881 4403 -292 -281 -459 C
ATOM 1391 N ILE A 200 56.192 21.390 13.700 1.00 34.49 N
ANISOU 1391 N ILE A 200 4239 4013 4853 -451 -423 -634 N
ATOM 1392 CA ILE A 200 56.178 22.640 14.437 1.00 34.56 C
ANISOU 1392 CA ILE A 200 4277 3982 4873 -466 -449 -686 C
ATOM 1393 C ILE A 200 54.826 23.323 14.220 1.00 34.81 C
ANISOU 1393 C ILE A 200 4373 3968 4886 -437 -417 -693 C
ATOM 1394 O ILE A 200 54.458 23.681 13.100 1.00 30.83 O
ANISOU 1394 O ILE A 200 3879 3413 4422 -442 -372 -654 O
ATOM 1395 CB ILE A 200 57.375 23.549 14.087 1.00 40.42 C
ANISOU 1395 CB ILE A 200 4981 4676 5700 -526 -455 -686 C
ATOM 1396 CG1 ILE A 200 57.206 24.918 14.742 1.00 43.83 C
ANISOU 1396 CG1 ILE A 200 5453 5055 6148 -541 -477 -740 C
ATOM 1397 CG2 ILE A 200 57.552 23.670 12.583 1.00 39.15 C
ANISOU 1397 CG2 ILE A 200 4801 4471 5605 -549 -399 -622 C
ATOM 1398 CD1 ILE A 200 58.426 25.804 14.602 1.00 53.28 C
ANISOU 1398 CD1 ILE A 200 6610 6207 7426 -603 -493 -749 C
ATOM 1399 N ALA A 201 54.089 23.489 15.313 1.00 36.93 N
ANISOU 1399 N ALA A 201 4684 4257 5092 -403 -440 -741 N
ATOM 1400 CA ALA A 201 52.680 23.861 15.256 1.00 33.65 C
ANISOU 1400 CA ALA A 201 4326 3818 4642 -362 -411 -747 C
ATOM 1401 C ALA A 201 52.378 25.263 15.783 1.00 42.45 C
ANISOU 1401 C ALA A 201 5482 4876 5772 -366 -421 -797 C
ATOM 1402 O ALA A 201 53.009 25.735 16.732 1.00 46.83 O
ANISOU 1402 O ALA A 201 6034 5435 6325 -385 -463 -847 O
ATOM 1403 CB ALA A 201 51.849 22.827 16.019 1.00 26.63 C
ANISOU 1403 CB ALA A 201 3453 3003 3660 -310 -417 -755 C
ATOM 1404 N ASP A 202 51.402 25.919 15.159 1.00 40.37 N
ANISOU 1404 N ASP A 202 5259 4558 5522 -346 -382 -785 N
ATOM 1405 CA ASP A 202 50.835 27.156 15.692 1.00 42.16 C
ANISOU 1405 CA ASP A 202 5534 4734 5751 -335 -385 -833 C
ATOM 1406 C ASP A 202 49.354 26.938 16.021 1.00 47.65 C
ANISOU 1406 C ASP A 202 6273 5454 6378 -271 -362 -841 C
ATOM 1407 O ASP A 202 48.596 26.451 15.179 1.00 47.43 O
ANISOU 1407 O ASP A 202 6249 5429 6342 -245 -324 -796 O
ATOM 1408 CB ASP A 202 50.964 28.317 14.693 1.00 40.32 C
ANISOU 1408 CB ASP A 202 5313 4405 5600 -364 -359 -810 C
ATOM 1409 CG ASP A 202 52.410 28.709 14.409 1.00 43.51 C
ANISOU 1409 CG ASP A 202 5674 4778 6079 -431 -378 -804 C
ATOM 1410 OD1 ASP A 202 53.322 28.302 15.164 1.00 44.39 O
ANISOU 1410 OD1 ASP A 202 5751 4937 6180 -454 -420 -831 O
ATOM 1411 OD2 ASP A 202 52.629 29.442 13.422 1.00 41.21 O
ANISOU 1411 OD2 ASP A 202 5383 4417 5856 -459 -349 -768 O
ATOM 1412 N GLY A 203 48.947 27.310 17.236 1.00 47.74 N
ANISOU 1412 N GLY A 203 6314 5485 6340 -246 -384 -900 N
ATOM 1413 CA GLY A 203 47.557 27.216 17.660 1.00 41.44 C
ANISOU 1413 CA GLY A 203 5555 4712 5479 -185 -360 -912 C
ATOM 1414 C GLY A 203 46.824 28.548 17.801 1.00 42.79 C
ANISOU 1414 C GLY A 203 5774 4815 5668 -166 -345 -948 C
ATOM 1415 O GLY A 203 47.396 29.550 18.224 1.00 45.22 O
ANISOU 1415 O GLY A 203 6095 5075 6011 -193 -370 -993 O
ATOM 1416 N ASP A 204 45.546 28.558 17.436 1.00 40.31 N
ANISOU 1416 N ASP A 204 5485 4498 5333 -117 -304 -930 N
ATOM 1417 CA ASP A 204 44.701 29.734 17.603 1.00 35.94 C
ANISOU 1417 CA ASP A 204 4978 3888 4791 -87 -285 -962 C
ATOM 1418 C ASP A 204 43.295 29.327 17.998 1.00 42.45 C
ANISOU 1418 C ASP A 204 5820 4763 5548 -21 -256 -964 C
ATOM 1419 O ASP A 204 42.777 28.308 17.545 1.00 46.28 O
ANISOU 1419 O ASP A 204 6284 5296 6002 0 -235 -918 O
ATOM 1420 CB ASP A 204 44.654 30.551 16.320 1.00 38.12 C
ANISOU 1420 CB ASP A 204 5265 4074 5146 -102 -258 -923 C
ATOM 1421 CG ASP A 204 45.986 31.159 15.983 1.00 50.03 C
ANISOU 1421 CG ASP A 204 6759 5525 6727 -168 -282 -923 C
ATOM 1422 OD1 ASP A 204 46.532 31.872 16.849 1.00 61.21 O
ANISOU 1422 OD1 ASP A 204 8186 6919 8151 -190 -315 -982 O
ATOM 1423 OD2 ASP A 204 46.499 30.911 14.871 1.00 50.78 O
ANISOU 1423 OD2 ASP A 204 6828 5597 6869 -199 -268 -866 O
ATOM 1424 N VAL A 205 42.678 30.128 18.851 1.00 42.29 N
ANISOU 1424 N VAL A 205 5835 4729 5505 12 -254 -1017 N
ATOM 1425 CA VAL A 205 41.314 29.874 19.266 1.00 38.58 C
ANISOU 1425 CA VAL A 205 5379 4305 4976 76 -222 -1021 C
ATOM 1426 C VAL A 205 40.449 31.038 18.822 1.00 43.51 C
ANISOU 1426 C VAL A 205 6037 4854 5640 107 -190 -1029 C
ATOM 1427 O VAL A 205 40.802 32.197 19.041 1.00 49.95 O
ANISOU 1427 O VAL A 205 6882 5600 6496 92 -202 -1071 O
ATOM 1428 CB VAL A 205 41.219 29.697 20.779 1.00 45.38 C
ANISOU 1428 CB VAL A 205 6252 5230 5762 97 -243 -1076 C
ATOM 1429 CG1 VAL A 205 39.785 29.404 21.186 1.00 52.71 C
ANISOU 1429 CG1 VAL A 205 7189 6208 6630 163 -204 -1074 C
ATOM 1430 CG2 VAL A 205 42.142 28.576 21.228 1.00 43.13 C
ANISOU 1430 CG2 VAL A 205 5934 5015 5439 68 -277 -1066 C
ATOM 1431 N THR A 206 39.336 30.720 18.166 1.00 40.87 N
ANISOU 1431 N THR A 206 5698 4533 5298 150 -149 -987 N
ATOM 1432 CA THR A 206 38.390 31.721 17.697 1.00 35.00 C
ANISOU 1432 CA THR A 206 4982 3726 4590 189 -116 -986 C
ATOM 1433 C THR A 206 37.200 31.748 18.634 1.00 36.11 C
ANISOU 1433 C THR A 206 5134 3916 4672 252 -95 -1020 C
ATOM 1434 O THR A 206 37.031 30.849 19.459 1.00 37.49 O
ANISOU 1434 O THR A 206 5292 4177 4776 264 -100 -1029 O
ATOM 1435 CB THR A 206 37.886 31.406 16.287 1.00 34.62 C
ANISOU 1435 CB THR A 206 4917 3660 4576 201 -86 -915 C
ATOM 1436 OG1 THR A 206 37.182 30.155 16.305 1.00 34.54 O
ANISOU 1436 OG1 THR A 206 4876 3739 4508 230 -71 -884 O
ATOM 1437 CG2 THR A 206 39.057 31.338 15.303 1.00 30.94 C
ANISOU 1437 CG2 THR A 206 4440 3149 4166 141 -102 -875 C
ATOM 1438 N ALA A 207 36.363 32.769 18.493 1.00 35.33 N
ANISOU 1438 N ALA A 207 5062 3763 4601 292 -68 -1035 N
ATOM 1439 CA ALA A 207 35.286 32.995 19.443 1.00 37.27 C
ANISOU 1439 CA ALA A 207 5319 4045 4796 351 -46 -1076 C
ATOM 1440 C ALA A 207 33.938 32.819 18.775 1.00 39.90 C
ANISOU 1440 C ALA A 207 5635 4394 5132 407 -3 -1032 C
ATOM 1441 O ALA A 207 32.896 32.854 19.431 1.00 40.66 O
ANISOU 1441 O ALA A 207 5731 4532 5187 461 21 -1053 O
ATOM 1442 CB ALA A 207 35.405 34.385 20.041 1.00 38.17 C
ANISOU 1442 CB ALA A 207 5478 4086 4938 358 -53 -1142 C
ATOM 1443 N SER A 208 33.961 32.611 17.465 1.00 41.64 N
ANISOU 1443 N SER A 208 5838 4585 5398 395 6 -970 N
ATOM 1444 CA SER A 208 32.729 32.553 16.703 1.00 40.18 C
ANISOU 1444 CA SER A 208 5636 4407 5225 447 41 -927 C
ATOM 1445 C SER A 208 32.944 31.926 15.347 1.00 39.20 C
ANISOU 1445 C SER A 208 5487 4276 5131 425 42 -857 C
ATOM 1446 O SER A 208 34.063 31.888 14.841 1.00 40.34 O
ANISOU 1446 O SER A 208 5636 4383 5308 371 21 -841 O
ATOM 1447 CB SER A 208 32.192 33.960 16.487 1.00 39.69 C
ANISOU 1447 CB SER A 208 5605 4259 5216 483 61 -946 C
ATOM 1448 OG SER A 208 33.032 34.660 15.589 1.00 46.48 O
ANISOU 1448 OG SER A 208 6487 5025 6147 443 51 -925 O
ATOM 1449 N LEU A 209 31.845 31.464 14.759 1.00 34.88 N
ANISOU 1449 N LEU A 209 4912 3766 4576 469 66 -815 N
ATOM 1450 CA LEU A 209 31.843 30.915 13.414 1.00 33.77 C
ANISOU 1450 CA LEU A 209 4749 3621 4462 460 68 -748 C
ATOM 1451 C LEU A 209 32.445 31.892 12.411 1.00 37.81 C
ANISOU 1451 C LEU A 209 5287 4030 5050 440 67 -725 C
ATOM 1452 O LEU A 209 33.270 31.503 11.588 1.00 38.88 O
ANISOU 1452 O LEU A 209 5418 4147 5207 397 55 -686 O
ATOM 1453 CB LEU A 209 30.415 30.538 13.009 1.00 29.78 C
ANISOU 1453 CB LEU A 209 4212 3164 3940 520 92 -715 C
ATOM 1454 CG LEU A 209 30.160 29.964 11.617 1.00 32.56 C
ANISOU 1454 CG LEU A 209 4539 3521 4312 524 93 -647 C
ATOM 1455 CD1 LEU A 209 31.131 28.834 11.285 1.00 33.77 C
ANISOU 1455 CD1 LEU A 209 4679 3705 4446 470 73 -623 C
ATOM 1456 CD2 LEU A 209 28.737 29.472 11.551 1.00 29.16 C
ANISOU 1456 CD2 LEU A 209 4073 3158 3850 581 111 -627 C
ATOM 1457 N ASP A 210 32.042 33.158 12.489 1.00 44.60 N
ANISOU 1457 N ASP A 210 6175 4821 5948 470 81 -746 N
ATOM 1458 CA ASP A 210 32.530 34.177 11.554 1.00 41.22 C
ANISOU 1458 CA ASP A 210 5777 4290 5595 454 86 -718 C
ATOM 1459 C ASP A 210 34.035 34.358 11.654 1.00 32.44 C
ANISOU 1459 C ASP A 210 4690 3132 4503 382 62 -731 C
ATOM 1460 O ASP A 210 34.704 34.576 10.655 1.00 37.08 O
ANISOU 1460 O ASP A 210 5289 3665 5136 350 62 -684 O
ATOM 1461 CB ASP A 210 31.832 35.520 11.774 1.00 40.13 C
ANISOU 1461 CB ASP A 210 5669 4085 5495 501 107 -744 C
ATOM 1462 CG ASP A 210 30.388 35.503 11.327 1.00 46.39 C
ANISOU 1462 CG ASP A 210 6433 4905 6287 572 129 -715 C
ATOM 1463 OD1 ASP A 210 29.983 34.520 10.676 1.00 47.91 O
ANISOU 1463 OD1 ASP A 210 6587 5160 6457 582 127 -667 O
ATOM 1464 OD2 ASP A 210 29.659 36.476 11.617 1.00 49.17 O
ANISOU 1464 OD2 ASP A 210 6802 5218 6664 620 147 -739 O
ATOM 1465 N GLU A 211 34.557 34.256 12.867 1.00 31.96 N
ANISOU 1465 N GLU A 211 4635 3100 4407 357 40 -793 N
ATOM 1466 CA GLU A 211 35.991 34.368 13.119 1.00 37.20 C
ANISOU 1466 CA GLU A 211 5313 3735 5087 288 8 -813 C
ATOM 1467 C GLU A 211 36.748 33.140 12.575 1.00 38.53 C
ANISOU 1467 C GLU A 211 5446 3954 5240 244 -8 -770 C
ATOM 1468 O GLU A 211 37.805 33.270 11.947 1.00 35.80 O
ANISOU 1468 O GLU A 211 5103 3563 4936 191 -21 -743 O
ATOM 1469 CB GLU A 211 36.206 34.521 14.623 1.00 43.31 C
ANISOU 1469 CB GLU A 211 6097 4538 5820 283 -13 -892 C
ATOM 1470 CG GLU A 211 37.577 34.985 15.053 1.00 55.64 C
ANISOU 1470 CG GLU A 211 7676 6057 7407 219 -50 -928 C
ATOM 1471 CD GLU A 211 37.591 35.389 16.518 1.00 63.10 C
ANISOU 1471 CD GLU A 211 8640 7019 8315 227 -69 -1011 C
ATOM 1472 OE1 GLU A 211 36.548 35.881 17.003 1.00 67.38 O
ANISOU 1472 OE1 GLU A 211 9201 7562 8839 284 -45 -1041 O
ATOM 1473 OE2 GLU A 211 38.633 35.208 17.185 1.00 64.34 O
ANISOU 1473 OE2 GLU A 211 8792 7193 8460 180 -107 -1045 O
ATOM 1474 N THR A 212 36.191 31.954 12.816 1.00 26.25 N
ANISOU 1474 N THR A 212 3856 2491 3626 265 -5 -761 N
ATOM 1475 CA THR A 212 36.735 30.714 12.274 1.00 28.75 C
ANISOU 1475 CA THR A 212 4139 2859 3927 233 -16 -720 C
ATOM 1476 C THR A 212 36.879 30.807 10.751 1.00 36.19 C
ANISOU 1476 C THR A 212 5081 3750 4921 224 -2 -652 C
ATOM 1477 O THR A 212 37.928 30.464 10.185 1.00 35.42 O
ANISOU 1477 O THR A 212 4974 3639 4846 174 -16 -624 O
ATOM 1478 CB THR A 212 35.826 29.515 12.618 1.00 30.16 C
ANISOU 1478 CB THR A 212 4285 3136 4038 270 -8 -713 C
ATOM 1479 OG1 THR A 212 35.779 29.332 14.039 1.00 25.14 O
ANISOU 1479 OG1 THR A 212 3651 2554 3348 276 -20 -768 O
ATOM 1480 CG2 THR A 212 36.330 28.240 11.956 1.00 29.49 C
ANISOU 1480 CG2 THR A 212 4169 3096 3941 240 -17 -669 C
ATOM 1481 N ILE A 213 35.824 31.286 10.095 1.00 30.43 N
ANISOU 1481 N ILE A 213 4359 2994 4209 276 25 -624 N
ATOM 1482 CA ILE A 213 35.817 31.428 8.647 1.00 28.28 C
ANISOU 1482 CA ILE A 213 4090 2676 3979 279 41 -555 C
ATOM 1483 C ILE A 213 36.765 32.524 8.172 1.00 36.15 C
ANISOU 1483 C ILE A 213 5126 3575 5036 240 39 -539 C
ATOM 1484 O ILE A 213 37.370 32.411 7.103 1.00 37.76 O
ANISOU 1484 O ILE A 213 5333 3750 5266 213 39 -482 O
ATOM 1485 CB ILE A 213 34.410 31.725 8.146 1.00 32.65 C
ANISOU 1485 CB ILE A 213 4637 3230 4539 348 65 -530 C
ATOM 1486 CG1 ILE A 213 33.488 30.550 8.486 1.00 32.76 C
ANISOU 1486 CG1 ILE A 213 4611 3346 4489 383 62 -534 C
ATOM 1487 CG2 ILE A 213 34.422 31.995 6.646 1.00 32.01 C
ANISOU 1487 CG2 ILE A 213 4560 3098 4505 354 79 -456 C
ATOM 1488 CD1 ILE A 213 32.063 30.798 8.124 1.00 37.17 C
ANISOU 1488 CD1 ILE A 213 5157 3919 5046 452 78 -514 C
ATOM 1489 N ALA A 214 36.897 33.577 8.977 1.00 30.02 N
ANISOU 1489 N ALA A 214 4380 2748 4277 237 34 -590 N
ATOM 1490 CA ALA A 214 37.789 34.687 8.648 1.00 36.68 C
ANISOU 1490 CA ALA A 214 5263 3497 5178 199 26 -582 C
ATOM 1491 C ALA A 214 39.235 34.221 8.687 1.00 37.31 C
ANISOU 1491 C ALA A 214 5321 3585 5268 122 -4 -582 C
ATOM 1492 O ALA A 214 40.033 34.552 7.808 1.00 41.56 O
ANISOU 1492 O ALA A 214 5865 4072 5853 83 -7 -535 O
ATOM 1493 CB ALA A 214 37.579 35.861 9.620 1.00 32.98 C
ANISOU 1493 CB ALA A 214 4829 2977 4724 213 25 -647 C
ATOM 1494 N LEU A 215 39.557 33.449 9.719 1.00 30.14 N
ANISOU 1494 N LEU A 215 4385 2748 4319 103 -26 -632 N
ATOM 1495 CA LEU A 215 40.887 32.890 9.883 1.00 33.55 C
ANISOU 1495 CA LEU A 215 4788 3203 4759 36 -55 -637 C
ATOM 1496 C LEU A 215 41.239 31.922 8.754 1.00 36.08 C
ANISOU 1496 C LEU A 215 5075 3550 5082 17 -46 -568 C
ATOM 1497 O LEU A 215 42.412 31.741 8.433 1.00 45.14 O
ANISOU 1497 O LEU A 215 6200 4690 6262 -41 -59 -549 O
ATOM 1498 CB LEU A 215 41.001 32.205 11.253 1.00 38.28 C
ANISOU 1498 CB LEU A 215 5366 3879 5300 32 -80 -700 C
ATOM 1499 CG LEU A 215 42.268 31.426 11.618 1.00 38.88 C
ANISOU 1499 CG LEU A 215 5405 3999 5371 -27 -113 -710 C
ATOM 1500 CD1 LEU A 215 42.543 31.573 13.091 1.00 40.65 C
ANISOU 1500 CD1 LEU A 215 5632 4253 5560 -33 -145 -785 C
ATOM 1501 CD2 LEU A 215 42.142 29.946 11.265 1.00 38.77 C
ANISOU 1501 CD2 LEU A 215 5352 4065 5314 -20 -109 -674 C
ATOM 1502 N HIS A 216 40.230 31.303 8.148 1.00 33.63 N
ANISOU 1502 N HIS A 216 4760 3275 4743 66 -24 -531 N
ATOM 1503 CA HIS A 216 40.483 30.369 7.053 1.00 35.17 C
ANISOU 1503 CA HIS A 216 4928 3497 4940 54 -15 -468 C
ATOM 1504 C HIS A 216 40.442 31.035 5.687 1.00 39.18 C
ANISOU 1504 C HIS A 216 5457 3938 5493 60 4 -398 C
ATOM 1505 O HIS A 216 40.732 30.398 4.680 1.00 43.64 O
ANISOU 1505 O HIS A 216 6000 4517 6064 47 14 -341 O
ATOM 1506 CB HIS A 216 39.511 29.191 7.092 1.00 27.63 C
ANISOU 1506 CB HIS A 216 3950 2621 3926 98 -7 -465 C
ATOM 1507 CG HIS A 216 39.842 28.176 8.136 1.00 27.44 C
ANISOU 1507 CG HIS A 216 3896 2675 3855 79 -29 -510 C
ATOM 1508 ND1 HIS A 216 39.464 28.314 9.456 1.00 35.50 N
ANISOU 1508 ND1 HIS A 216 4923 3729 4838 97 -41 -571 N
ATOM 1509 CD2 HIS A 216 40.530 27.012 8.063 1.00 26.80 C
ANISOU 1509 CD2 HIS A 216 3780 2646 3756 47 -42 -498 C
ATOM 1510 CE1 HIS A 216 39.902 27.280 10.148 1.00 31.63 C
ANISOU 1510 CE1 HIS A 216 4404 3308 4305 77 -62 -592 C
ATOM 1511 NE2 HIS A 216 40.550 26.472 9.324 1.00 32.85 N
ANISOU 1511 NE2 HIS A 216 4534 3474 4473 47 -63 -549 N
ATOM 1512 N SER A 217 40.102 32.318 5.653 1.00 39.79 N
ANISOU 1512 N SER A 217 5575 3942 5599 80 10 -401 N
ATOM 1513 CA SER A 217 40.004 33.032 4.385 1.00 43.03 C
ANISOU 1513 CA SER A 217 6009 4290 6050 92 22 -331 C
ATOM 1514 C SER A 217 40.936 34.244 4.333 1.00 47.51 C
ANISOU 1514 C SER A 217 6598 4772 6680 45 17 -329 C
ATOM 1515 O SER A 217 40.825 35.082 3.438 1.00 49.84 O
ANISOU 1515 O SER A 217 6918 5005 7012 56 27 -277 O
ATOM 1516 CB SER A 217 38.565 33.495 4.131 1.00 45.57 C
ANISOU 1516 CB SER A 217 6363 4599 6353 174 33 -320 C
ATOM 1517 OG SER A 217 37.607 32.606 4.681 1.00 45.15 O
ANISOU 1517 OG SER A 217 6290 4622 6244 217 45 -349 O
ATOM 1518 N ASP A 218 41.851 34.351 5.288 1.00 41.08 N
ANISOU 1518 N ASP A 218 5771 3957 5879 -8 0 -385 N
ATOM 1519 CA ASP A 218 42.682 35.546 5.358 1.00 38.64 C
ANISOU 1519 CA ASP A 218 5483 3565 5632 -53 -7 -393 C
ATOM 1520 C ASP A 218 44.044 35.352 4.710 1.00 41.45 C
ANISOU 1520 C ASP A 218 5801 3915 6033 -126 -5 -349 C
ATOM 1521 O ASP A 218 44.922 36.204 4.836 1.00 48.07 O
ANISOU 1521 O ASP A 218 6643 4694 6926 -176 -12 -357 O
ATOM 1522 CB ASP A 218 42.833 36.039 6.802 1.00 34.45 C
ANISOU 1522 CB ASP A 218 4966 3026 5098 -65 -31 -484 C
ATOM 1523 CG ASP A 218 43.574 35.060 7.689 1.00 46.31 C
ANISOU 1523 CG ASP A 218 6423 4603 6570 -104 -56 -530 C
ATOM 1524 OD1 ASP A 218 44.141 34.070 7.176 1.00 47.75 O
ANISOU 1524 OD1 ASP A 218 6562 4836 6746 -131 -54 -492 O
ATOM 1525 OD2 ASP A 218 43.597 35.290 8.917 1.00 52.57 O
ANISOU 1525 OD2 ASP A 218 7223 5407 7345 -106 -78 -605 O
ATOM 1526 N GLY A 219 44.218 34.215 4.046 1.00 36.53 N
ANISOU 1526 N GLY A 219 5139 3354 5387 -131 8 -303 N
ATOM 1527 CA GLY A 219 45.462 33.900 3.366 1.00 27.98 C
ANISOU 1527 CA GLY A 219 4014 2276 4340 -193 20 -256 C
ATOM 1528 C GLY A 219 46.486 33.169 4.216 1.00 35.87 C
ANISOU 1528 C GLY A 219 4966 3327 5335 -244 -4 -304 C
ATOM 1529 O GLY A 219 47.541 32.802 3.711 1.00 48.22 O
ANISOU 1529 O GLY A 219 6489 4905 6926 -293 7 -268 O
ATOM 1530 N SER A 220 46.194 32.951 5.497 1.00 30.13 N
ANISOU 1530 N SER A 220 4243 2633 4571 -231 -35 -381 N
ATOM 1531 CA SER A 220 47.161 32.298 6.388 1.00 29.69 C
ANISOU 1531 CA SER A 220 4144 2629 4507 -275 -65 -428 C
ATOM 1532 C SER A 220 47.265 30.783 6.173 1.00 35.42 C
ANISOU 1532 C SER A 220 4826 3440 5190 -271 -61 -407 C
ATOM 1533 O SER A 220 48.298 30.184 6.480 1.00 39.56 O
ANISOU 1533 O SER A 220 5306 4003 5721 -314 -78 -418 O
ATOM 1534 CB SER A 220 46.860 32.589 7.864 1.00 33.50 C
ANISOU 1534 CB SER A 220 4646 3123 4959 -261 -101 -517 C
ATOM 1535 OG SER A 220 45.632 32.012 8.278 1.00 39.76 O
ANISOU 1535 OG SER A 220 5457 3965 5685 -198 -98 -538 O
ATOM 1536 N GLU A 221 46.205 30.165 5.662 1.00 27.02 N
ANISOU 1536 N GLU A 221 3776 2405 4084 -219 -41 -379 N
ATOM 1537 CA GLU A 221 46.243 28.731 5.372 1.00 32.86 C
ANISOU 1537 CA GLU A 221 4479 3219 4787 -214 -34 -357 C
ATOM 1538 C GLU A 221 47.446 28.382 4.480 1.00 40.39 C
ANISOU 1538 C GLU A 221 5392 4175 5782 -265 -14 -302 C
ATOM 1539 O GLU A 221 48.085 27.332 4.651 1.00 36.53 O
ANISOU 1539 O GLU A 221 4859 3742 5277 -286 -22 -306 O
ATOM 1540 CB GLU A 221 44.923 28.258 4.743 1.00 26.51 C
ANISOU 1540 CB GLU A 221 3696 2433 3942 -153 -10 -327 C
ATOM 1541 CG GLU A 221 43.796 28.022 5.748 1.00 32.40 C
ANISOU 1541 CG GLU A 221 4462 3217 4633 -102 -28 -384 C
ATOM 1542 CD GLU A 221 44.013 26.771 6.593 1.00 36.56 C
ANISOU 1542 CD GLU A 221 4955 3826 5111 -109 -50 -421 C
ATOM 1543 OE1 GLU A 221 44.503 26.893 7.732 1.00 34.51 O
ANISOU 1543 OE1 GLU A 221 4690 3583 4840 -129 -81 -476 O
ATOM 1544 OE2 GLU A 221 43.696 25.657 6.115 1.00 33.41 O
ANISOU 1544 OE2 GLU A 221 4537 3475 4683 -93 -38 -395 O
ATOM 1545 N ALA A 222 47.776 29.287 3.562 1.00 38.97 N
ANISOU 1545 N ALA A 222 5222 3932 5651 -283 12 -251 N
ATOM 1546 CA ALA A 222 48.907 29.087 2.653 1.00 37.42 C
ANISOU 1546 CA ALA A 222 4987 3737 5494 -329 40 -193 C
ATOM 1547 C ALA A 222 50.258 28.948 3.363 1.00 33.12 C
ANISOU 1547 C ALA A 222 4394 3211 4980 -388 14 -227 C
ATOM 1548 O ALA A 222 51.223 28.463 2.783 1.00 32.73 O
ANISOU 1548 O ALA A 222 4300 3184 4952 -422 34 -188 O
ATOM 1549 CB ALA A 222 48.965 30.210 1.647 1.00 32.60 C
ANISOU 1549 CB ALA A 222 4402 3057 4929 -335 73 -133 C
ATOM 1550 N ARG A 223 50.319 29.376 4.617 1.00 38.96 N
ANISOU 1550 N ARG A 223 5142 3943 5717 -396 -30 -301 N
ATOM 1551 CA ARG A 223 51.553 29.324 5.392 1.00 38.19 C
ANISOU 1551 CA ARG A 223 5001 3864 5647 -448 -62 -339 C
ATOM 1552 C ARG A 223 51.757 27.984 6.083 1.00 37.35 C
ANISOU 1552 C ARG A 223 4857 3843 5490 -441 -89 -370 C
ATOM 1553 O ARG A 223 52.816 27.736 6.653 1.00 41.01 O
ANISOU 1553 O ARG A 223 5278 4335 5971 -479 -116 -395 O
ATOM 1554 CB ARG A 223 51.569 30.426 6.457 1.00 44.20 C
ANISOU 1554 CB ARG A 223 5790 4580 6426 -460 -100 -406 C
ATOM 1555 CG ARG A 223 51.820 31.836 5.926 1.00 49.69 C
ANISOU 1555 CG ARG A 223 6509 5184 7188 -488 -82 -383 C
ATOM 1556 CD ARG A 223 52.240 32.781 7.052 1.00 51.23 C
ANISOU 1556 CD ARG A 223 6715 5340 7410 -517 -125 -455 C
ATOM 1557 NE ARG A 223 51.140 33.166 7.939 1.00 56.15 N
ANISOU 1557 NE ARG A 223 7393 5953 7990 -469 -146 -515 N
ATOM 1558 CZ ARG A 223 50.267 34.134 7.663 1.00 62.89 C
ANISOU 1558 CZ ARG A 223 8302 6738 8854 -438 -128 -508 C
ATOM 1559 NH1 ARG A 223 50.353 34.803 6.517 1.00 64.52 N
ANISOU 1559 NH1 ARG A 223 8521 6882 9112 -450 -92 -442 N
ATOM 1560 NH2 ARG A 223 49.303 34.434 8.529 1.00 61.12 N
ANISOU 1560 NH2 ARG A 223 8122 6512 8588 -392 -144 -566 N
ATOM 1561 N TYR A 224 50.741 27.131 6.065 1.00 30.57 N
ANISOU 1561 N TYR A 224 4016 3027 4573 -392 -82 -369 N
ATOM 1562 CA TYR A 224 50.852 25.839 6.728 1.00 24.47 C
ANISOU 1562 CA TYR A 224 3214 2334 3751 -383 -107 -396 C
ATOM 1563 C TYR A 224 50.507 24.714 5.771 1.00 28.55 C
ANISOU 1563 C TYR A 224 3717 2886 4244 -361 -72 -344 C
ATOM 1564 O TYR A 224 49.567 24.817 4.993 1.00 36.45 O
ANISOU 1564 O TYR A 224 4750 3865 5233 -328 -40 -310 O
ATOM 1565 CB TYR A 224 49.923 25.772 7.936 1.00 26.01 C
ANISOU 1565 CB TYR A 224 3441 2555 3885 -342 -140 -460 C
ATOM 1566 CG TYR A 224 50.068 26.917 8.909 1.00 26.32 C
ANISOU 1566 CG TYR A 224 3504 2557 3939 -355 -171 -517 C
ATOM 1567 CD1 TYR A 224 51.080 26.924 9.864 1.00 31.99 C
ANISOU 1567 CD1 TYR A 224 4193 3299 4664 -390 -213 -560 C
ATOM 1568 CD2 TYR A 224 49.184 27.977 8.891 1.00 25.07 C
ANISOU 1568 CD2 TYR A 224 3397 2341 3786 -329 -160 -528 C
ATOM 1569 CE1 TYR A 224 51.208 27.960 10.768 1.00 27.47 C
ANISOU 1569 CE1 TYR A 224 3644 2692 4103 -401 -242 -616 C
ATOM 1570 CE2 TYR A 224 49.299 29.021 9.791 1.00 31.38 C
ANISOU 1570 CE2 TYR A 224 4221 3104 4599 -339 -186 -584 C
ATOM 1571 CZ TYR A 224 50.311 29.011 10.727 1.00 34.92 C
ANISOU 1571 CZ TYR A 224 4641 3575 5053 -376 -228 -629 C
ATOM 1572 OH TYR A 224 50.418 30.062 11.619 1.00 38.42 O
ANISOU 1572 OH TYR A 224 5110 3979 5509 -387 -256 -688 O
ATOM 1573 N THR A 225 51.276 23.636 5.830 1.00 31.89 N
ANISOU 1573 N THR A 225 4093 3365 4660 -378 -79 -339 N
ATOM 1574 CA THR A 225 51.006 22.472 5.007 1.00 28.22 C
ANISOU 1574 CA THR A 225 3615 2937 4172 -359 -47 -296 C
ATOM 1575 C THR A 225 49.888 21.645 5.631 1.00 24.72 C
ANISOU 1575 C THR A 225 3195 2538 3661 -313 -65 -330 C
ATOM 1576 O THR A 225 49.184 20.940 4.936 1.00 20.68 O
ANISOU 1576 O THR A 225 2695 2059 3102 -278 -37 -289 O
ATOM 1577 CB THR A 225 52.247 21.604 4.882 1.00 29.12 C
ANISOU 1577 CB THR A 225 3668 3093 4303 -391 -48 -280 C
ATOM 1578 OG1 THR A 225 52.921 21.590 6.146 1.00 31.49 O
ANISOU 1578 OG1 THR A 225 3944 3422 4599 -409 -101 -335 O
ATOM 1579 CG2 THR A 225 53.183 22.176 3.828 1.00 25.61 C
ANISOU 1579 CG2 THR A 225 3198 2613 3919 -427 -8 -224 C
ATOM 1580 N TYR A 226 49.736 21.756 6.946 1.00 21.08 N
ANISOU 1580 N TYR A 226 2741 2100 3166 -304 -110 -390 N
ATOM 1581 CA TYR A 226 48.754 21.001 7.711 1.00 20.70 C
ANISOU 1581 CA TYR A 226 2713 2104 3049 -261 -129 -423 C
ATOM 1582 C TYR A 226 47.874 21.946 8.513 1.00 19.74 C
ANISOU 1582 C TYR A 226 2636 1961 2903 -233 -143 -466 C
ATOM 1583 O TYR A 226 48.382 22.831 9.193 1.00 26.39 O
ANISOU 1583 O TYR A 226 3483 2779 3765 -254 -167 -499 O
ATOM 1584 CB TYR A 226 49.467 20.100 8.719 1.00 24.15 C
ANISOU 1584 CB TYR A 226 3116 2606 3454 -271 -169 -453 C
ATOM 1585 CG TYR A 226 50.171 18.899 8.137 1.00 27.73 C
ANISOU 1585 CG TYR A 226 3527 3106 3904 -281 -155 -408 C
ATOM 1586 CD1 TYR A 226 49.663 17.615 8.329 1.00 22.93 C
ANISOU 1586 CD1 TYR A 226 2920 2566 3227 -246 -154 -391 C
ATOM 1587 CD2 TYR A 226 51.353 19.042 7.412 1.00 24.41 C
ANISOU 1587 CD2 TYR A 226 3066 2662 3548 -323 -141 -378 C
ATOM 1588 CE1 TYR A 226 50.305 16.513 7.810 1.00 21.40 C
ANISOU 1588 CE1 TYR A 226 2690 2411 3028 -250 -141 -350 C
ATOM 1589 CE2 TYR A 226 52.007 17.944 6.884 1.00 19.06 C
ANISOU 1589 CE2 TYR A 226 2349 2030 2861 -325 -124 -336 C
ATOM 1590 CZ TYR A 226 51.481 16.679 7.090 1.00 24.36 C
ANISOU 1590 CZ TYR A 226 3027 2766 3464 -287 -126 -325 C
ATOM 1591 OH TYR A 226 52.120 15.578 6.568 1.00 21.32 O
ANISOU 1591 OH TYR A 226 2607 2421 3073 -285 -110 -287 O
ATOM 1592 N SER A 227 46.562 21.740 8.473 1.00 23.66 N
ANISOU 1592 N SER A 227 3164 2470 3357 -185 -129 -467 N
ATOM 1593 CA SER A 227 45.642 22.533 9.292 1.00 21.55 C
ANISOU 1593 CA SER A 227 2936 2193 3061 -151 -138 -508 C
ATOM 1594 C SER A 227 44.306 21.815 9.479 1.00 22.07 C
ANISOU 1594 C SER A 227 3017 2306 3063 -97 -127 -511 C
ATOM 1595 O SER A 227 43.737 21.299 8.516 1.00 21.07 O
ANISOU 1595 O SER A 227 2888 2190 2927 -79 -98 -462 O
ATOM 1596 CB SER A 227 45.403 23.907 8.657 1.00 22.10 C
ANISOU 1596 CB SER A 227 3035 2180 3181 -152 -117 -494 C
ATOM 1597 OG SER A 227 44.249 24.534 9.197 1.00 25.91 O
ANISOU 1597 OG SER A 227 3557 2654 3634 -106 -115 -524 O
ATOM 1598 N SER A 228 43.822 21.780 10.720 1.00 18.08 N
ANISOU 1598 N SER A 228 2525 1843 2504 -72 -145 -554 N
ATOM 1599 CA SER A 228 42.481 21.290 11.037 1.00 21.83 C
ANISOU 1599 CA SER A 228 3013 2363 2918 -20 -131 -557 C
ATOM 1600 C SER A 228 41.985 21.991 12.296 1.00 25.01 C
ANISOU 1600 C SER A 228 3440 2777 3287 5 -140 -605 C
ATOM 1601 O SER A 228 42.768 22.604 13.012 1.00 26.36 O
ANISOU 1601 O SER A 228 3615 2932 3470 -21 -165 -639 O
ATOM 1602 CB SER A 228 42.457 19.771 11.229 1.00 16.88 C
ANISOU 1602 CB SER A 228 2360 1812 2240 -15 -135 -541 C
ATOM 1603 OG SER A 228 43.262 19.381 12.322 1.00 21.77 O
ANISOU 1603 OG SER A 228 2966 2472 2832 -33 -167 -568 O
ATOM 1604 N ALA A 229 40.691 21.901 12.579 1.00 20.88 N
ANISOU 1604 N ALA A 229 2931 2283 2721 54 -120 -609 N
ATOM 1605 CA ALA A 229 40.160 22.587 13.745 1.00 16.21 C
ANISOU 1605 CA ALA A 229 2362 1701 2097 80 -123 -654 C
ATOM 1606 C ALA A 229 39.146 21.761 14.513 1.00 21.72 C
ANISOU 1606 C ALA A 229 3054 2476 2722 122 -109 -655 C
ATOM 1607 O ALA A 229 38.367 21.016 13.937 1.00 26.85 O
ANISOU 1607 O ALA A 229 3691 3156 3356 144 -87 -620 O
ATOM 1608 CB ALA A 229 39.562 23.922 13.345 1.00 17.93 C
ANISOU 1608 CB ALA A 229 2607 1849 2355 101 -104 -663 C
ATOM 1609 N TRP A 230 39.180 21.904 15.830 1.00 27.52 N
ANISOU 1609 N TRP A 230 3799 3245 3413 131 -122 -694 N
ATOM 1610 CA TRP A 230 38.160 21.353 16.698 1.00 29.79 C
ANISOU 1610 CA TRP A 230 4086 3601 3634 172 -103 -696 C
ATOM 1611 C TRP A 230 37.090 22.433 16.869 1.00 33.02 C
ANISOU 1611 C TRP A 230 4517 3982 4048 213 -79 -720 C
ATOM 1612 O TRP A 230 37.393 23.571 17.208 1.00 37.66 O
ANISOU 1612 O TRP A 230 5129 4520 4661 209 -90 -760 O
ATOM 1613 CB TRP A 230 38.770 20.981 18.039 1.00 38.71 C
ANISOU 1613 CB TRP A 230 5217 4780 4711 164 -129 -723 C
ATOM 1614 CG TRP A 230 37.998 19.933 18.743 1.00 55.14 C
ANISOU 1614 CG TRP A 230 7287 6941 6721 194 -110 -703 C
ATOM 1615 CD1 TRP A 230 37.109 20.114 19.781 1.00 60.53 C
ANISOU 1615 CD1 TRP A 230 7983 7663 7352 233 -91 -723 C
ATOM 1616 CD2 TRP A 230 38.014 18.534 18.469 1.00 57.46 C
ANISOU 1616 CD2 TRP A 230 7555 7285 6990 187 -104 -656 C
ATOM 1617 NE1 TRP A 230 36.592 18.915 20.167 1.00 63.24 N
ANISOU 1617 NE1 TRP A 230 8309 8077 7642 249 -72 -688 N
ATOM 1618 CE2 TRP A 230 37.126 17.923 19.381 1.00 64.41 C
ANISOU 1618 CE2 TRP A 230 8434 8232 7805 221 -81 -646 C
ATOM 1619 CE3 TRP A 230 38.695 17.732 17.548 1.00 52.63 C
ANISOU 1619 CE3 TRP A 230 6923 6668 6406 156 -115 -622 C
ATOM 1620 CZ2 TRP A 230 36.901 16.535 19.393 1.00 64.60 C
ANISOU 1620 CZ2 TRP A 230 8437 8314 7793 222 -68 -600 C
ATOM 1621 CZ3 TRP A 230 38.472 16.368 17.559 1.00 53.69 C
ANISOU 1621 CZ3 TRP A 230 7037 6859 6502 160 -105 -581 C
ATOM 1622 CH2 TRP A 230 37.582 15.779 18.469 1.00 56.55 C
ANISOU 1622 CH2 TRP A 230 7399 7285 6803 192 -81 -569 C
ATOM 1623 N PHE A 231 35.837 22.058 16.663 1.00 29.35 N
ANISOU 1623 N PHE A 231 4041 3549 3560 254 -46 -696 N
ATOM 1624 CA PHE A 231 34.770 22.998 16.339 1.00 24.25 C
ANISOU 1624 CA PHE A 231 3407 2869 2938 294 -19 -703 C
ATOM 1625 C PHE A 231 33.583 22.848 17.311 1.00 23.67 C
ANISOU 1625 C PHE A 231 3330 2856 2809 342 9 -714 C
ATOM 1626 O PHE A 231 33.182 21.735 17.656 1.00 27.11 O
ANISOU 1626 O PHE A 231 3741 3362 3196 349 21 -689 O
ATOM 1627 CB PHE A 231 34.373 22.658 14.896 1.00 30.97 C
ANISOU 1627 CB PHE A 231 4240 3701 3825 298 -5 -654 C
ATOM 1628 CG PHE A 231 33.296 23.500 14.306 1.00 28.49 C
ANISOU 1628 CG PHE A 231 3931 3351 3541 341 19 -647 C
ATOM 1629 CD1 PHE A 231 33.606 24.495 13.398 1.00 32.86 C
ANISOU 1629 CD1 PHE A 231 4504 3823 4158 334 15 -643 C
ATOM 1630 CD2 PHE A 231 31.961 23.235 14.573 1.00 31.33 C
ANISOU 1630 CD2 PHE A 231 4273 3762 3868 389 48 -638 C
ATOM 1631 CE1 PHE A 231 32.595 25.255 12.801 1.00 29.97 C
ANISOU 1631 CE1 PHE A 231 4143 3424 3821 378 36 -630 C
ATOM 1632 CE2 PHE A 231 30.954 23.981 13.989 1.00 26.14 C
ANISOU 1632 CE2 PHE A 231 3616 3076 3242 431 68 -629 C
ATOM 1633 CZ PHE A 231 31.270 24.993 13.103 1.00 26.13 C
ANISOU 1633 CZ PHE A 231 3636 2992 3301 428 61 -625 C
ATOM 1634 N ASP A 232 33.029 23.970 17.758 1.00 27.28 N
ANISOU 1634 N ASP A 232 3809 3284 3274 374 20 -751 N
ATOM 1635 CA ASP A 232 31.894 23.971 18.683 1.00 33.36 C
ANISOU 1635 CA ASP A 232 4574 4106 3995 421 50 -765 C
ATOM 1636 C ASP A 232 30.591 23.972 17.894 1.00 27.97 C
ANISOU 1636 C ASP A 232 3868 3428 3332 462 84 -732 C
ATOM 1637 O ASP A 232 30.325 24.904 17.147 1.00 28.93 O
ANISOU 1637 O ASP A 232 3999 3487 3505 477 88 -734 O
ATOM 1638 CB ASP A 232 31.959 25.230 19.562 1.00 36.88 C
ANISOU 1638 CB ASP A 232 5056 4514 4441 438 45 -827 C
ATOM 1639 CG ASP A 232 30.884 25.270 20.661 1.00 34.32 C
ANISOU 1639 CG ASP A 232 4732 4247 4062 488 76 -848 C
ATOM 1640 OD1 ASP A 232 29.798 24.648 20.543 1.00 33.20 O
ANISOU 1640 OD1 ASP A 232 4558 4156 3898 519 110 -813 O
ATOM 1641 OD2 ASP A 232 31.142 25.961 21.662 1.00 29.99 O
ANISOU 1641 OD2 ASP A 232 4213 3690 3491 495 67 -902 O
ATOM 1642 N ALA A 233 29.771 22.946 18.090 1.00 30.17 N
ANISOU 1642 N ALA A 233 4114 3781 3569 480 108 -699 N
ATOM 1643 CA ALA A 233 28.515 22.801 17.344 1.00 32.19 C
ANISOU 1643 CA ALA A 233 4337 4052 3842 516 138 -664 C
ATOM 1644 C ALA A 233 27.306 22.795 18.262 1.00 31.04 C
ANISOU 1644 C ALA A 233 4175 3964 3656 562 175 -672 C
ATOM 1645 O ALA A 233 26.187 22.515 17.834 1.00 31.69 O
ANISOU 1645 O ALA A 233 4221 4075 3745 592 201 -641 O
ATOM 1646 CB ALA A 233 28.534 21.521 16.515 1.00 29.03 C
ANISOU 1646 CB ALA A 233 3903 3687 3439 494 136 -611 C
ATOM 1647 N ILE A 234 27.535 23.089 19.532 1.00 31.59 N
ANISOU 1647 N ILE A 234 4269 4050 3684 568 176 -713 N
ATOM 1648 CA ILE A 234 26.471 23.014 20.518 1.00 34.85 C
ANISOU 1648 CA ILE A 234 4668 4523 4052 610 213 -720 C
ATOM 1649 C ILE A 234 26.103 24.391 21.055 1.00 37.82 C
ANISOU 1649 C ILE A 234 5073 4859 4437 649 223 -775 C
ATOM 1650 O ILE A 234 24.923 24.682 21.266 1.00 36.63 O
ANISOU 1650 O ILE A 234 4904 4732 4283 696 258 -775 O
ATOM 1651 CB ILE A 234 26.862 22.073 21.665 1.00 33.13 C
ANISOU 1651 CB ILE A 234 4452 4372 3765 593 215 -717 C
ATOM 1652 CG1 ILE A 234 27.091 20.665 21.108 1.00 29.55 C
ANISOU 1652 CG1 ILE A 234 3966 3956 3305 558 212 -659 C
ATOM 1653 CG2 ILE A 234 25.787 22.060 22.739 1.00 31.96 C
ANISOU 1653 CG2 ILE A 234 4292 4283 3567 637 258 -725 C
ATOM 1654 CD1 ILE A 234 27.595 19.665 22.132 1.00 32.92 C
ANISOU 1654 CD1 ILE A 234 4396 4444 3669 538 210 -648 C
ATOM 1655 N SER A 235 27.114 25.237 21.249 1.00 36.80 N
ANISOU 1655 N SER A 235 4988 4669 4325 629 191 -821 N
ATOM 1656 CA SER A 235 26.913 26.557 21.842 1.00 36.50 C
ANISOU 1656 CA SER A 235 4984 4588 4295 661 196 -880 C
ATOM 1657 C SER A 235 25.974 27.428 21.027 1.00 40.20 C
ANISOU 1657 C SER A 235 5444 5009 4820 702 217 -874 C
ATOM 1658 O SER A 235 26.030 27.452 19.795 1.00 32.49 O
ANISOU 1658 O SER A 235 4455 3993 3898 690 207 -839 O
ATOM 1659 CB SER A 235 28.247 27.282 22.048 1.00 31.45 C
ANISOU 1659 CB SER A 235 4391 3885 3675 623 154 -926 C
ATOM 1660 OG SER A 235 29.060 26.586 22.976 1.00 30.34 O
ANISOU 1660 OG SER A 235 4259 3793 3477 594 132 -939 O
ATOM 1661 N ALA A 236 25.094 28.128 21.733 1.00 51.78 N
ANISOU 1661 N ALA A 236 6916 6484 6272 754 246 -908 N
ATOM 1662 CA ALA A 236 24.251 29.134 21.113 1.00 55.46 C
ANISOU 1662 CA ALA A 236 7380 6900 6794 798 264 -912 C
ATOM 1663 C ALA A 236 25.159 30.178 20.473 1.00 46.16 C
ANISOU 1663 C ALA A 236 6243 5617 5679 775 233 -936 C
ATOM 1664 O ALA A 236 26.232 30.475 21.012 1.00 40.62 O
ANISOU 1664 O ALA A 236 5580 4886 4968 739 205 -976 O
ATOM 1665 CB ALA A 236 23.349 29.778 22.162 1.00 56.18 C
ANISOU 1665 CB ALA A 236 7479 7012 6855 855 299 -957 C
ATOM 1666 N PRO A 237 24.750 30.720 19.312 1.00 42.30 N
ANISOU 1666 N PRO A 237 5745 5073 5255 792 236 -907 N
ATOM 1667 CA PRO A 237 25.492 31.843 18.732 1.00 44.16 C
ANISOU 1667 CA PRO A 237 6021 5202 5555 775 214 -926 C
ATOM 1668 C PRO A 237 25.539 33.008 19.737 1.00 53.24 C
ANISOU 1668 C PRO A 237 7216 6309 6705 798 220 -999 C
ATOM 1669 O PRO A 237 24.660 33.106 20.602 1.00 55.87 O
ANISOU 1669 O PRO A 237 7542 6688 6999 846 249 -1027 O
ATOM 1670 CB PRO A 237 24.666 32.209 17.483 1.00 35.12 C
ANISOU 1670 CB PRO A 237 4853 4023 4469 810 227 -879 C
ATOM 1671 CG PRO A 237 23.885 31.000 17.160 1.00 33.61 C
ANISOU 1671 CG PRO A 237 4607 3919 4246 821 240 -827 C
ATOM 1672 CD PRO A 237 23.598 30.329 18.482 1.00 42.47 C
ANISOU 1672 CD PRO A 237 5718 5126 5294 828 258 -853 C
ATOM 1673 N PRO A 238 26.563 33.871 19.644 1.00 52.76 N
ANISOU 1673 N PRO A 238 7200 6162 6686 765 195 -1032 N
ATOM 1674 CA PRO A 238 27.584 33.887 18.596 1.00 51.26 C
ANISOU 1674 CA PRO A 238 7018 5910 6548 711 167 -998 C
ATOM 1675 C PRO A 238 28.770 32.967 18.890 1.00 46.77 C
ANISOU 1675 C PRO A 238 6450 5379 5944 646 134 -997 C
ATOM 1676 O PRO A 238 29.738 32.979 18.135 1.00 42.95 O
ANISOU 1676 O PRO A 238 5973 4846 5500 597 110 -975 O
ATOM 1677 CB PRO A 238 28.038 35.348 18.592 1.00 49.56 C
ANISOU 1677 CB PRO A 238 6853 5585 6392 709 161 -1042 C
ATOM 1678 CG PRO A 238 27.777 35.838 20.007 1.00 50.13 C
ANISOU 1678 CG PRO A 238 6951 5676 6419 738 169 -1117 C
ATOM 1679 CD PRO A 238 26.883 34.836 20.710 1.00 54.12 C
ANISOU 1679 CD PRO A 238 7419 6296 6849 772 191 -1109 C
ATOM 1680 N LYS A 239 28.699 32.179 19.958 1.00 49.15 N
ANISOU 1680 N LYS A 239 6740 5766 6170 648 134 -1016 N
ATOM 1681 CA LYS A 239 29.800 31.271 20.287 1.00 49.68 C
ANISOU 1681 CA LYS A 239 6803 5871 6201 592 103 -1013 C
ATOM 1682 C LYS A 239 29.789 30.025 19.393 1.00 42.90 C
ANISOU 1682 C LYS A 239 5903 5059 5339 571 102 -943 C
ATOM 1683 O LYS A 239 30.792 29.322 19.289 1.00 38.54 O
ANISOU 1683 O LYS A 239 5345 4520 4777 520 75 -928 O
ATOM 1684 CB LYS A 239 29.806 30.908 21.782 1.00 49.60 C
ANISOU 1684 CB LYS A 239 6801 5932 6111 601 101 -1057 C
ATOM 1685 CG LYS A 239 30.094 32.103 22.697 1.00 59.57 C
ANISOU 1685 CG LYS A 239 8112 7147 7375 611 91 -1135 C
ATOM 1686 CD LYS A 239 31.419 32.781 22.331 1.00 63.53 C
ANISOU 1686 CD LYS A 239 8643 7564 7932 555 50 -1157 C
ATOM 1687 CE LYS A 239 31.374 34.297 22.524 1.00 64.21 C
ANISOU 1687 CE LYS A 239 8773 7559 8064 573 52 -1215 C
ATOM 1688 NZ LYS A 239 31.654 34.727 23.924 1.00 62.52 N
ANISOU 1688 NZ LYS A 239 8593 7361 7801 580 36 -1293 N
ATOM 1689 N LEU A 240 28.652 29.768 18.749 1.00 40.19 N
ANISOU 1689 N LEU A 240 5528 4738 5003 611 132 -901 N
ATOM 1690 CA LEU A 240 28.548 28.713 17.750 1.00 38.10 C
ANISOU 1690 CA LEU A 240 5226 4507 4744 595 132 -836 C
ATOM 1691 C LEU A 240 29.618 28.893 16.669 1.00 34.49 C
ANISOU 1691 C LEU A 240 4782 3981 4344 548 104 -814 C
ATOM 1692 O LEU A 240 29.831 29.994 16.170 1.00 40.30 O
ANISOU 1692 O LEU A 240 5544 4633 5137 549 101 -824 O
ATOM 1693 CB LEU A 240 27.151 28.705 17.119 1.00 35.39 C
ANISOU 1693 CB LEU A 240 4850 4183 4415 649 163 -801 C
ATOM 1694 CG LEU A 240 26.959 27.692 15.983 1.00 37.98 C
ANISOU 1694 CG LEU A 240 5139 4540 4751 637 160 -735 C
ATOM 1695 CD1 LEU A 240 27.175 26.257 16.476 1.00 38.39 C
ANISOU 1695 CD1 LEU A 240 5166 4676 4744 609 159 -718 C
ATOM 1696 CD2 LEU A 240 25.594 27.840 15.328 1.00 34.85 C
ANISOU 1696 CD2 LEU A 240 4710 4156 4375 691 185 -703 C
ATOM 1697 N GLY A 241 30.319 27.818 16.339 1.00 27.57 N
ANISOU 1697 N GLY A 241 3887 3137 3451 505 87 -782 N
ATOM 1698 CA GLY A 241 31.327 27.872 15.296 1.00 30.81 C
ANISOU 1698 CA GLY A 241 4305 3489 3911 460 64 -757 C
ATOM 1699 C GLY A 241 32.722 28.301 15.723 1.00 29.12 C
ANISOU 1699 C GLY A 241 4120 3232 3713 408 34 -792 C
ATOM 1700 O GLY A 241 33.638 28.297 14.910 1.00 36.20 O
ANISOU 1700 O GLY A 241 5019 4084 4650 366 17 -769 O
ATOM 1701 N ARG A 242 32.894 28.691 16.979 1.00 29.75 N
ANISOU 1701 N ARG A 242 4219 3324 3760 411 26 -848 N
ATOM 1702 CA ARG A 242 34.233 28.975 17.486 1.00 35.28 C
ANISOU 1702 CA ARG A 242 4941 3996 4469 360 -10 -883 C
ATOM 1703 C ARG A 242 35.055 27.700 17.397 1.00 36.44 C
ANISOU 1703 C ARG A 242 5061 4196 4589 317 -31 -854 C
ATOM 1704 O ARG A 242 34.513 26.600 17.473 1.00 35.35 O
ANISOU 1704 O ARG A 242 4895 4131 4404 334 -19 -825 O
ATOM 1705 CB ARG A 242 34.192 29.454 18.938 1.00 38.77 C
ANISOU 1705 CB ARG A 242 5406 4457 4866 376 -17 -949 C
ATOM 1706 CG ARG A 242 33.725 28.401 19.925 1.00 44.48 C
ANISOU 1706 CG ARG A 242 6110 5282 5507 397 -9 -950 C
ATOM 1707 CD ARG A 242 33.824 28.884 21.360 1.00 44.34 C
ANISOU 1707 CD ARG A 242 6120 5283 5443 411 -20 -1016 C
ATOM 1708 NE ARG A 242 33.088 28.007 22.263 1.00 41.74 N
ANISOU 1708 NE ARG A 242 5775 5049 5035 445 0 -1010 N
ATOM 1709 CZ ARG A 242 32.908 28.246 23.557 1.00 43.38 C
ANISOU 1709 CZ ARG A 242 6004 5293 5187 469 1 -1059 C
ATOM 1710 NH1 ARG A 242 33.422 29.337 24.116 1.00 48.96 N
ANISOU 1710 NH1 ARG A 242 6748 5948 5908 464 -22 -1123 N
ATOM 1711 NH2 ARG A 242 32.214 27.389 24.292 1.00 38.18 N
ANISOU 1711 NH2 ARG A 242 5329 4721 4459 499 24 -1044 N
ATOM 1712 N ALA A 243 36.362 27.843 17.247 1.00 30.58 N
ANISOU 1712 N ALA A 243 4324 3416 3878 263 -64 -862 N
ATOM 1713 CA ALA A 243 37.198 26.684 16.997 1.00 26.86 C
ANISOU 1713 CA ALA A 243 3825 2986 3393 223 -84 -830 C
ATOM 1714 C ALA A 243 38.590 26.771 17.615 1.00 32.49 C
ANISOU 1714 C ALA A 243 4542 3693 4110 173 -126 -862 C
ATOM 1715 O ALA A 243 39.143 27.852 17.808 1.00 35.56 O
ANISOU 1715 O ALA A 243 4953 4019 4537 154 -142 -899 O
ATOM 1716 CB ALA A 243 37.310 26.445 15.492 1.00 22.66 C
ANISOU 1716 CB ALA A 243 3278 2418 2913 207 -73 -774 C
ATOM 1717 N ALA A 244 39.142 25.605 17.923 1.00 31.58 N
ANISOU 1717 N ALA A 244 4402 3642 3957 153 -144 -846 N
ATOM 1718 CA ALA A 244 40.532 25.475 18.320 1.00 29.12 C
ANISOU 1718 CA ALA A 244 4080 3330 3652 104 -186 -864 C
ATOM 1719 C ALA A 244 41.289 24.919 17.116 1.00 32.32 C
ANISOU 1719 C ALA A 244 4458 3716 4106 64 -190 -814 C
ATOM 1720 O ALA A 244 41.181 23.734 16.788 1.00 34.65 O
ANISOU 1720 O ALA A 244 4728 4062 4375 67 -183 -775 O
ATOM 1721 CB ALA A 244 40.666 24.552 19.520 1.00 28.69 C
ANISOU 1721 CB ALA A 244 4016 3362 3521 113 -204 -877 C
ATOM 1722 N VAL A 245 42.050 25.798 16.469 1.00 27.96 N
ANISOU 1722 N VAL A 245 3910 3088 3625 27 -200 -816 N
ATOM 1723 CA VAL A 245 42.728 25.516 15.214 1.00 17.73 C
ANISOU 1723 CA VAL A 245 2592 1760 2385 -10 -196 -768 C
ATOM 1724 C VAL A 245 44.177 25.117 15.441 1.00 32.25 C
ANISOU 1724 C VAL A 245 4401 3613 4239 -63 -233 -772 C
ATOM 1725 O VAL A 245 44.937 25.842 16.101 1.00 39.27 O
ANISOU 1725 O VAL A 245 5295 4478 5146 -89 -263 -813 O
ATOM 1726 CB VAL A 245 42.702 26.759 14.330 1.00 20.49 C
ANISOU 1726 CB VAL A 245 2964 2016 2807 -20 -180 -759 C
ATOM 1727 CG1 VAL A 245 43.230 26.447 12.962 1.00 22.37 C
ANISOU 1727 CG1 VAL A 245 3180 2223 3096 -50 -167 -700 C
ATOM 1728 CG2 VAL A 245 41.277 27.296 14.242 1.00 23.48 C
ANISOU 1728 CG2 VAL A 245 3372 2378 3172 37 -146 -761 C
ATOM 1729 N SER A 246 44.550 23.960 14.899 1.00 30.93 N
ANISOU 1729 N SER A 246 4201 3485 4067 -76 -233 -730 N
ATOM 1730 CA SER A 246 45.912 23.447 14.989 1.00 28.08 C
ANISOU 1730 CA SER A 246 3804 3143 3724 -122 -264 -726 C
ATOM 1731 C SER A 246 46.532 23.470 13.599 1.00 23.80 C
ANISOU 1731 C SER A 246 3238 2553 3252 -158 -248 -678 C
ATOM 1732 O SER A 246 46.046 22.813 12.688 1.00 24.61 O
ANISOU 1732 O SER A 246 3334 2663 3354 -144 -220 -635 O
ATOM 1733 CB SER A 246 45.919 22.018 15.557 1.00 27.20 C
ANISOU 1733 CB SER A 246 3670 3118 3546 -106 -276 -715 C
ATOM 1734 OG SER A 246 47.234 21.465 15.570 1.00 33.07 O
ANISOU 1734 OG SER A 246 4375 3881 4310 -146 -306 -707 O
ATOM 1735 N ARG A 247 47.586 24.254 13.424 1.00 23.00 N
ANISOU 1735 N ARG A 247 3124 2401 3212 -204 -263 -685 N
ATOM 1736 CA ARG A 247 48.226 24.364 12.117 1.00 24.32 C
ANISOU 1736 CA ARG A 247 3270 2523 3449 -240 -241 -635 C
ATOM 1737 C ARG A 247 49.741 24.270 12.235 1.00 28.24 C
ANISOU 1737 C ARG A 247 3720 3024 3985 -294 -269 -637 C
ATOM 1738 O ARG A 247 50.317 24.620 13.263 1.00 31.17 O
ANISOU 1738 O ARG A 247 4088 3407 4350 -309 -307 -683 O
ATOM 1739 CB ARG A 247 47.833 25.671 11.422 1.00 21.87 C
ANISOU 1739 CB ARG A 247 2993 2127 3191 -241 -215 -625 C
ATOM 1740 CG ARG A 247 46.335 25.960 11.448 1.00 25.93 C
ANISOU 1740 CG ARG A 247 3551 2632 3667 -184 -192 -631 C
ATOM 1741 CD ARG A 247 45.929 27.038 10.461 1.00 32.24 C
ANISOU 1741 CD ARG A 247 4380 3350 4521 -179 -161 -601 C
ATOM 1742 NE ARG A 247 46.266 28.376 10.927 1.00 33.18 N
ANISOU 1742 NE ARG A 247 4524 3406 4678 -199 -175 -638 N
ATOM 1743 CZ ARG A 247 45.906 29.498 10.306 1.00 38.61 C
ANISOU 1743 CZ ARG A 247 5244 4015 5410 -192 -153 -621 C
ATOM 1744 NH1 ARG A 247 45.187 29.447 9.192 1.00 29.11 N
ANISOU 1744 NH1 ARG A 247 4054 2791 4216 -164 -117 -566 N
ATOM 1745 NH2 ARG A 247 46.261 30.680 10.805 1.00 42.32 N
ANISOU 1745 NH2 ARG A 247 5737 4427 5916 -213 -168 -660 N
ATOM 1746 N GLY A 248 50.387 23.796 11.180 1.00 25.22 N
ANISOU 1746 N GLY A 248 3301 2636 3644 -321 -249 -585 N
ATOM 1747 CA GLY A 248 51.825 23.670 11.200 1.00 26.85 C
ANISOU 1747 CA GLY A 248 3458 2851 3894 -369 -269 -581 C
ATOM 1748 C GLY A 248 52.388 22.978 9.984 1.00 36.21 C
ANISOU 1748 C GLY A 248 4602 4040 5116 -389 -237 -519 C
ATOM 1749 O GLY A 248 51.748 22.890 8.932 1.00 41.23 O
ANISOU 1749 O GLY A 248 5253 4651 5759 -373 -194 -475 O
ATOM 1750 N ARG A 249 53.604 22.475 10.148 1.00 33.68 N
ANISOU 1750 N ARG A 249 4228 3752 4816 -421 -257 -515 N
ATOM 1751 CA ARG A 249 54.346 21.843 9.076 1.00 33.90 C
ANISOU 1751 CA ARG A 249 4210 3788 4883 -443 -226 -459 C
ATOM 1752 C ARG A 249 55.396 20.928 9.688 1.00 32.22 C
ANISOU 1752 C ARG A 249 3942 3638 4662 -456 -261 -470 C
ATOM 1753 O ARG A 249 55.653 20.990 10.890 1.00 31.01 O
ANISOU 1753 O ARG A 249 3788 3513 4481 -455 -310 -519 O
ATOM 1754 CB ARG A 249 55.031 22.904 8.228 1.00 41.55 C
ANISOU 1754 CB ARG A 249 5166 4692 5929 -485 -197 -428 C
ATOM 1755 CG ARG A 249 55.775 23.946 9.039 1.00 50.98 C
ANISOU 1755 CG ARG A 249 6353 5858 7158 -522 -235 -472 C
ATOM 1756 CD ARG A 249 56.731 24.744 8.172 1.00 61.23 C
ANISOU 1756 CD ARG A 249 7622 7106 8537 -571 -207 -433 C
ATOM 1757 NE ARG A 249 56.294 24.783 6.781 1.00 67.90 N
ANISOU 1757 NE ARG A 249 8481 7919 9400 -562 -145 -365 N
ATOM 1758 CZ ARG A 249 55.332 25.577 6.324 1.00 66.46 C
ANISOU 1758 CZ ARG A 249 8354 7681 9218 -543 -120 -352 C
ATOM 1759 NH1 ARG A 249 54.699 26.393 7.160 1.00 76.50 N
ANISOU 1759 NH1 ARG A 249 9671 8921 10476 -531 -149 -404 N
ATOM 1760 NH2 ARG A 249 54.999 25.544 5.038 1.00 49.79 N
ANISOU 1760 NH2 ARG A 249 6253 5548 7117 -532 -64 -286 N
ATOM 1761 N LEU A 250 56.000 20.075 8.867 1.00 29.94 N
ANISOU 1761 N LEU A 250 3609 3374 4395 -464 -235 -424 N
ATOM 1762 CA LEU A 250 57.051 19.198 9.359 1.00 24.86 C
ANISOU 1762 CA LEU A 250 2908 2789 3749 -473 -266 -429 C
ATOM 1763 C LEU A 250 58.257 20.023 9.787 1.00 31.89 C
ANISOU 1763 C LEU A 250 3762 3664 4691 -518 -294 -449 C
ATOM 1764 O LEU A 250 58.654 20.974 9.106 1.00 28.86 O
ANISOU 1764 O LEU A 250 3372 3226 4368 -552 -267 -429 O
ATOM 1765 CB LEU A 250 57.437 18.153 8.306 1.00 24.63 C
ANISOU 1765 CB LEU A 250 2838 2785 3737 -469 -225 -374 C
ATOM 1766 CG LEU A 250 56.384 17.042 8.131 1.00 32.12 C
ANISOU 1766 CG LEU A 250 3813 3764 4628 -425 -212 -364 C
ATOM 1767 CD1 LEU A 250 56.713 16.130 6.958 1.00 33.76 C
ANISOU 1767 CD1 LEU A 250 3988 3989 4849 -419 -163 -306 C
ATOM 1768 CD2 LEU A 250 56.232 16.224 9.404 1.00 33.17 C
ANISOU 1768 CD2 LEU A 250 3947 3957 4697 -397 -266 -403 C
ATOM 1769 N ALA A 251 58.821 19.667 10.934 1.00 35.41 N
ANISOU 1769 N ALA A 251 4185 4158 5110 -516 -350 -488 N
ATOM 1770 CA ALA A 251 59.993 20.357 11.452 1.00 38.83 C
ANISOU 1770 CA ALA A 251 4580 4584 5589 -559 -385 -513 C
ATOM 1771 C ALA A 251 61.277 19.890 10.761 1.00 42.47 C
ANISOU 1771 C ALA A 251 4966 5066 6106 -586 -368 -471 C
ATOM 1772 O ALA A 251 61.431 18.707 10.427 1.00 36.45 O
ANISOU 1772 O ALA A 251 4174 4351 5326 -563 -355 -440 O
ATOM 1773 CB ALA A 251 60.094 20.161 12.956 1.00 33.60 C
ANISOU 1773 CB ALA A 251 3925 3969 4872 -544 -452 -569 C
ATOM 1774 N THR A 252 62.187 20.834 10.537 1.00 42.53 N
ANISOU 1774 N THR A 252 4942 5036 6182 -636 -366 -470 N
ATOM 1775 CA THR A 252 63.552 20.514 10.134 1.00 45.49 C
ANISOU 1775 CA THR A 252 5238 5437 6610 -665 -359 -440 C
ATOM 1776 C THR A 252 64.333 20.219 11.402 1.00 40.26 C
ANISOU 1776 C THR A 252 4541 4827 5930 -669 -431 -486 C
ATOM 1777 O THR A 252 63.886 20.549 12.502 1.00 38.27 O
ANISOU 1777 O THR A 252 4328 4577 5634 -659 -480 -540 O
ATOM 1778 CB THR A 252 64.215 21.682 9.402 1.00 44.00 C
ANISOU 1778 CB THR A 252 5028 5187 6502 -719 -327 -419 C
ATOM 1779 OG1 THR A 252 64.105 22.859 10.206 1.00 43.44 O
ANISOU 1779 OG1 THR A 252 4989 5072 6443 -746 -367 -472 O
ATOM 1780 CG2 THR A 252 63.537 21.925 8.060 1.00 36.75 C
ANISOU 1780 CG2 THR A 252 4142 4222 5600 -712 -253 -363 C
ATOM 1781 N VAL A 253 65.489 19.589 11.267 1.00 35.25 N
ANISOU 1781 N VAL A 253 3833 4237 5324 -680 -436 -464 N
ATOM 1782 CA VAL A 253 66.210 19.168 12.462 1.00 40.95 C
ANISOU 1782 CA VAL A 253 4520 5017 6023 -676 -506 -502 C
ATOM 1783 C VAL A 253 66.741 20.351 13.307 1.00 41.25 C
ANISOU 1783 C VAL A 253 4556 5029 6090 -722 -557 -557 C
ATOM 1784 O VAL A 253 66.737 20.277 14.540 1.00 32.52 O
ANISOU 1784 O VAL A 253 3462 3956 4936 -709 -621 -606 O
ATOM 1785 CB VAL A 253 67.271 18.077 12.155 1.00 52.20 C
ANISOU 1785 CB VAL A 253 5867 6503 7466 -667 -502 -464 C
ATOM 1786 CG1 VAL A 253 67.711 18.152 10.700 1.00 50.29 C
ANISOU 1786 CG1 VAL A 253 5586 6234 7287 -688 -427 -405 C
ATOM 1787 CG2 VAL A 253 68.451 18.168 13.128 1.00 52.76 C
ANISOU 1787 CG2 VAL A 253 5880 6613 7552 -690 -568 -498 C
ATOM 1788 N GLU A 254 67.118 21.451 12.647 1.00 47.30 N
ANISOU 1788 N GLU A 254 5310 5732 6930 -772 -527 -547 N
ATOM 1789 CA GLU A 254 67.534 22.681 13.337 1.00 53.95 C
ANISOU 1789 CA GLU A 254 6154 6535 7809 -820 -571 -599 C
ATOM 1790 C GLU A 254 66.432 23.259 14.223 1.00 57.64 C
ANISOU 1790 C GLU A 254 6705 6976 8220 -799 -602 -656 C
ATOM 1791 O GLU A 254 66.715 24.029 15.144 1.00 55.64 O
ANISOU 1791 O GLU A 254 6459 6710 7973 -824 -655 -713 O
ATOM 1792 CB GLU A 254 67.974 23.753 12.335 1.00 52.49 C
ANISOU 1792 CB GLU A 254 5951 6278 7713 -875 -523 -569 C
ATOM 1793 N GLN A 255 65.182 22.896 13.932 1.00 51.83 N
ANISOU 1793 N GLN A 255 6030 6233 7432 -753 -569 -640 N
ATOM 1794 CA GLN A 255 64.033 23.374 14.704 1.00 47.94 C
ANISOU 1794 CA GLN A 255 5616 5719 6880 -725 -590 -689 C
ATOM 1795 C GLN A 255 63.742 22.497 15.918 1.00 44.47 C
ANISOU 1795 C GLN A 255 5191 5353 6351 -679 -642 -724 C
ATOM 1796 O GLN A 255 62.928 22.855 16.765 1.00 40.52 O
ANISOU 1796 O GLN A 255 4750 4848 5796 -655 -666 -770 O
ATOM 1797 CB GLN A 255 62.785 23.464 13.821 1.00 47.79 C
ANISOU 1797 CB GLN A 255 5653 5657 6847 -697 -528 -655 C
ATOM 1798 CG GLN A 255 62.895 24.466 12.684 1.00 55.05 C
ANISOU 1798 CG GLN A 255 6573 6498 7845 -737 -476 -620 C
ATOM 1799 CD GLN A 255 61.691 24.435 11.763 1.00 54.62 C
ANISOU 1799 CD GLN A 255 6571 6409 7772 -705 -417 -581 C
ATOM 1800 OE1 GLN A 255 61.193 23.365 11.418 1.00 59.21 O
ANISOU 1800 OE1 GLN A 255 7155 7032 8310 -665 -396 -550 O
ATOM 1801 NE2 GLN A 255 61.208 25.611 11.373 1.00 48.98 N
ANISOU 1801 NE2 GLN A 255 5899 5618 7092 -720 -393 -581 N
ATOM 1802 N LEU A 256 64.404 21.347 16.001 1.00 44.70 N
ANISOU 1802 N LEU A 256 5168 5450 6364 -664 -656 -699 N
ATOM 1803 CA LEU A 256 64.159 20.423 17.103 1.00 50.92 C
ANISOU 1803 CA LEU A 256 5971 6311 7067 -617 -702 -721 C
ATOM 1804 C LEU A 256 64.853 20.888 18.378 1.00 63.03 C
ANISOU 1804 C LEU A 256 7493 7868 8587 -635 -776 -781 C
ATOM 1805 O LEU A 256 65.963 21.426 18.322 1.00 64.62 O
ANISOU 1805 O LEU A 256 7640 8057 8855 -685 -797 -790 O
ATOM 1806 CB LEU A 256 64.615 19.000 16.747 1.00 43.24 C
ANISOU 1806 CB LEU A 256 4948 5400 6081 -590 -693 -671 C
ATOM 1807 CG LEU A 256 63.812 18.218 15.701 1.00 44.07 C
ANISOU 1807 CG LEU A 256 5071 5501 6174 -558 -631 -617 C
ATOM 1808 CD1 LEU A 256 64.349 16.800 15.563 1.00 41.37 C
ANISOU 1808 CD1 LEU A 256 4678 5223 5816 -529 -633 -577 C
ATOM 1809 CD2 LEU A 256 62.325 18.201 16.039 1.00 41.77 C
ANISOU 1809 CD2 LEU A 256 4860 5201 5812 -518 -620 -634 C
ATOM 1810 N PRO A 257 64.197 20.681 19.534 1.00 66.86 N
ANISOU 1810 N PRO A 257 8027 8389 8986 -595 -814 -820 N
ATOM 1811 CA PRO A 257 64.852 20.911 20.825 1.00 67.56 C
ANISOU 1811 CA PRO A 257 8106 8516 9047 -603 -888 -875 C
ATOM 1812 C PRO A 257 66.100 20.047 20.911 1.00 71.39 C
ANISOU 1812 C PRO A 257 8513 9063 9550 -610 -920 -849 C
ATOM 1813 O PRO A 257 66.116 18.957 20.331 1.00 70.09 O
ANISOU 1813 O PRO A 257 8322 8930 9377 -583 -891 -794 O
ATOM 1814 CB PRO A 257 63.809 20.438 21.843 1.00 68.24 C
ANISOU 1814 CB PRO A 257 8259 8646 9025 -543 -905 -898 C
ATOM 1815 CG PRO A 257 62.872 19.561 21.072 1.00 69.92 C
ANISOU 1815 CG PRO A 257 8494 8863 9210 -503 -846 -843 C
ATOM 1816 CD PRO A 257 62.838 20.137 19.690 1.00 68.14 C
ANISOU 1816 CD PRO A 257 8255 8566 9069 -539 -788 -812 C
ATOM 1817 N ALA A 258 67.120 20.536 21.610 1.00 70.51 N
ANISOU 1817 N ALA A 258 8363 8966 9464 -645 -979 -889 N
ATOM 1818 CA ALA A 258 68.433 19.898 21.637 1.00 66.99 C
ANISOU 1818 CA ALA A 258 7832 8572 9049 -659 -1012 -867 C
ATOM 1819 C ALA A 258 68.380 18.388 21.873 1.00 60.65 C
ANISOU 1819 C ALA A 258 7018 7846 8181 -600 -1018 -824 C
ATOM 1820 O ALA A 258 69.004 17.625 21.135 1.00 60.72 O
ANISOU 1820 O ALA A 258 6967 7878 8228 -599 -994 -772 O
ATOM 1821 CB ALA A 258 69.325 20.572 22.668 1.00 67.42 C
ANISOU 1821 CB ALA A 258 7861 8643 9114 -694 -1089 -927 C
ATOM 1822 N LYS A 259 67.622 17.971 22.886 1.00 55.10 N
ANISOU 1822 N LYS A 259 6373 7182 7380 -551 -1046 -845 N
ATOM 1823 CA LYS A 259 67.526 16.564 23.271 1.00 55.82 C
ANISOU 1823 CA LYS A 259 6461 7345 7402 -493 -1057 -805 C
ATOM 1824 C LYS A 259 67.116 15.644 22.117 1.00 68.29 C
ANISOU 1824 C LYS A 259 8032 8919 8997 -468 -990 -738 C
ATOM 1825 O LYS A 259 67.600 14.516 22.005 1.00 73.07 O
ANISOU 1825 O LYS A 259 8596 9573 9594 -440 -994 -693 O
ATOM 1826 CB LYS A 259 66.537 16.406 24.429 1.00 51.19 C
ANISOU 1826 CB LYS A 259 5952 6789 6708 -445 -1080 -835 C
ATOM 1827 N LEU A 260 66.235 16.146 21.256 1.00 64.71 N
ANISOU 1827 N LEU A 260 7617 8402 8566 -478 -930 -732 N
ATOM 1828 CA LEU A 260 65.599 15.335 20.222 1.00 52.53 C
ANISOU 1828 CA LEU A 260 6082 6851 7026 -451 -867 -676 C
ATOM 1829 C LEU A 260 66.381 15.284 18.915 1.00 50.88 C
ANISOU 1829 C LEU A 260 5807 6617 6909 -484 -825 -634 C
ATOM 1830 O LEU A 260 66.060 14.486 18.031 1.00 51.02 O
ANISOU 1830 O LEU A 260 5819 6636 6932 -461 -776 -586 O
ATOM 1831 CB LEU A 260 64.185 15.855 19.955 1.00 51.21 C
ANISOU 1831 CB LEU A 260 5991 6635 6831 -441 -824 -688 C
ATOM 1832 CG LEU A 260 63.033 15.197 20.714 1.00 61.80 C
ANISOU 1832 CG LEU A 260 7397 8011 8071 -383 -828 -690 C
ATOM 1833 CD1 LEU A 260 63.473 14.719 22.093 1.00 69.09 C
ANISOU 1833 CD1 LEU A 260 8319 9003 8928 -357 -893 -710 C
ATOM 1834 CD2 LEU A 260 61.862 16.162 20.831 1.00 59.44 C
ANISOU 1834 CD2 LEU A 260 7170 7664 7750 -383 -805 -726 C
ATOM 1835 N ARG A 261 67.399 16.132 18.789 1.00 45.83 N
ANISOU 1835 N ARG A 261 5117 5957 6341 -538 -841 -653 N
ATOM 1836 CA ARG A 261 68.213 16.184 17.573 1.00 52.80 C
ANISOU 1836 CA ARG A 261 5934 6816 7312 -572 -796 -612 C
ATOM 1837 C ARG A 261 69.029 14.906 17.372 1.00 53.93 C
ANISOU 1837 C ARG A 261 6010 7022 7458 -543 -799 -566 C
ATOM 1838 O ARG A 261 69.618 14.691 16.311 1.00 52.05 O
ANISOU 1838 O ARG A 261 5718 6775 7282 -558 -752 -524 O
ATOM 1839 CB ARG A 261 69.166 17.381 17.604 1.00 58.33 C
ANISOU 1839 CB ARG A 261 6593 7484 8087 -637 -817 -642 C
ATOM 1840 CG ARG A 261 68.542 18.743 17.349 1.00 59.93 C
ANISOU 1840 CG ARG A 261 6846 7606 8318 -675 -794 -672 C
ATOM 1841 CD ARG A 261 69.639 19.726 16.964 1.00 61.75 C
ANISOU 1841 CD ARG A 261 7018 7800 8644 -743 -795 -679 C
ATOM 1842 NE ARG A 261 69.158 21.079 16.708 1.00 67.31 N
ANISOU 1842 NE ARG A 261 7767 8422 9386 -782 -775 -705 N
ATOM 1843 CZ ARG A 261 69.116 22.040 17.626 1.00 74.71 C
ANISOU 1843 CZ ARG A 261 8734 9335 10317 -805 -825 -769 C
ATOM 1844 NH1 ARG A 261 69.512 21.794 18.870 1.00 74.61 N
ANISOU 1844 NH1 ARG A 261 8713 9378 10259 -794 -899 -814 N
ATOM 1845 NH2 ARG A 261 68.673 23.247 17.302 1.00 76.04 N
ANISOU 1845 NH2 ARG A 261 8943 9424 10525 -838 -802 -787 N
ATOM 1846 N SER A 262 69.070 14.074 18.408 1.00 57.35 N
ANISOU 1846 N SER A 262 6449 7518 7823 -501 -851 -573 N
ATOM 1847 CA SER A 262 69.779 12.800 18.381 1.00 60.90 C
ANISOU 1847 CA SER A 262 6843 8028 8267 -464 -860 -530 C
ATOM 1848 C SER A 262 69.158 11.802 17.399 1.00 58.96 C
ANISOU 1848 C SER A 262 6610 7779 8015 -424 -798 -477 C
ATOM 1849 O SER A 262 69.830 11.323 16.486 1.00 52.97 O
ANISOU 1849 O SER A 262 5791 7026 7309 -424 -760 -436 O
ATOM 1850 CB SER A 262 69.811 12.204 19.789 1.00 65.73 C
ANISOU 1850 CB SER A 262 7473 8704 8799 -424 -931 -548 C
ATOM 1851 OG SER A 262 70.239 10.855 19.764 1.00 71.03 O
ANISOU 1851 OG SER A 262 8106 9429 9453 -376 -935 -499 O
ATOM 1852 N GLU A 263 67.883 11.475 17.605 1.00 60.58 N
ANISOU 1852 N GLU A 263 6889 7976 8153 -389 -786 -479 N
ATOM 1853 CA GLU A 263 67.122 10.690 16.628 1.00 61.24 C
ANISOU 1853 CA GLU A 263 6993 8045 8232 -358 -725 -436 C
ATOM 1854 C GLU A 263 65.919 11.491 16.120 1.00 46.78 C
ANISOU 1854 C GLU A 263 5226 6151 6397 -375 -683 -453 C
ATOM 1855 O GLU A 263 64.806 11.392 16.644 1.00 40.13 O
ANISOU 1855 O GLU A 263 4452 5310 5488 -348 -689 -468 O
ATOM 1856 CB GLU A 263 66.710 9.327 17.192 1.00 68.00 C
ANISOU 1856 CB GLU A 263 7870 8951 9016 -293 -744 -411 C
ATOM 1857 CG GLU A 263 66.314 9.353 18.654 1.00 79.73 C
ANISOU 1857 CG GLU A 263 9403 10470 10419 -272 -804 -442 C
ATOM 1858 CD GLU A 263 66.016 7.971 19.204 1.00 85.42 C
ANISOU 1858 CD GLU A 263 10142 11242 11073 -209 -820 -407 C
ATOM 1859 OE1 GLU A 263 65.434 7.142 18.466 1.00 85.59 O
ANISOU 1859 OE1 GLU A 263 10175 11254 11091 -179 -776 -369 O
ATOM 1860 OE2 GLU A 263 66.368 7.717 20.376 1.00 85.41 O
ANISOU 1860 OE2 GLU A 263 10142 11287 11021 -188 -877 -415 O
ATOM 1861 N PRO A 264 66.155 12.307 15.091 1.00 36.40 N
ANISOU 1861 N PRO A 264 3892 4785 5155 -419 -638 -446 N
ATOM 1862 CA PRO A 264 65.127 13.222 14.605 1.00 36.08 C
ANISOU 1862 CA PRO A 264 3909 4681 5118 -439 -600 -460 C
ATOM 1863 C PRO A 264 63.999 12.497 13.868 1.00 37.12 C
ANISOU 1863 C PRO A 264 4082 4803 5221 -403 -551 -429 C
ATOM 1864 O PRO A 264 62.920 13.065 13.732 1.00 41.58 O
ANISOU 1864 O PRO A 264 4706 5327 5765 -405 -531 -444 O
ATOM 1865 CB PRO A 264 65.905 14.137 13.656 1.00 35.86 C
ANISOU 1865 CB PRO A 264 3838 4608 5180 -493 -564 -448 C
ATOM 1866 CG PRO A 264 67.026 13.285 13.155 1.00 36.52 C
ANISOU 1866 CG PRO A 264 3843 4731 5301 -486 -551 -408 C
ATOM 1867 CD PRO A 264 67.395 12.380 14.296 1.00 35.92 C
ANISOU 1867 CD PRO A 264 3751 4723 5173 -449 -614 -419 C
ATOM 1868 N LEU A 265 64.247 11.273 13.411 1.00 33.27 N
ANISOU 1868 N LEU A 265 3561 4349 4732 -371 -534 -389 N
ATOM 1869 CA LEU A 265 63.255 10.510 12.663 1.00 31.50 C
ANISOU 1869 CA LEU A 265 3368 4115 4485 -338 -489 -360 C
ATOM 1870 C LEU A 265 62.626 9.415 13.521 1.00 38.05 C
ANISOU 1870 C LEU A 265 4230 4992 5236 -285 -523 -360 C
ATOM 1871 O LEU A 265 62.148 8.407 13.001 1.00 42.15 O
ANISOU 1871 O LEU A 265 4755 5521 5741 -251 -497 -330 O
ATOM 1872 CB LEU A 265 63.882 9.911 11.400 1.00 24.81 C
ANISOU 1872 CB LEU A 265 2466 3265 3694 -336 -435 -312 C
ATOM 1873 CG LEU A 265 64.321 10.952 10.362 1.00 26.34 C
ANISOU 1873 CG LEU A 265 2638 3411 3961 -385 -385 -300 C
ATOM 1874 CD1 LEU A 265 65.355 10.386 9.398 1.00 16.32 C
ANISOU 1874 CD1 LEU A 265 1299 2157 2744 -383 -341 -255 C
ATOM 1875 CD2 LEU A 265 63.118 11.473 9.593 1.00 26.91 C
ANISOU 1875 CD2 LEU A 265 2769 3429 4028 -393 -337 -295 C
ATOM 1876 N LYS A 266 62.617 9.630 14.835 1.00 38.00 N
ANISOU 1876 N LYS A 266 4247 5015 5178 -278 -579 -393 N
ATOM 1877 CA LYS A 266 62.100 8.646 15.782 1.00 39.44 C
ANISOU 1877 CA LYS A 266 4461 5245 5279 -227 -612 -387 C
ATOM 1878 C LYS A 266 60.630 8.313 15.538 1.00 38.53 C
ANISOU 1878 C LYS A 266 4410 5116 5116 -201 -580 -381 C
ATOM 1879 O LYS A 266 59.828 9.192 15.248 1.00 32.63 O
ANISOU 1879 O LYS A 266 3703 4326 4370 -222 -556 -404 O
ATOM 1880 CB LYS A 266 62.266 9.137 17.222 1.00 40.10 C
ANISOU 1880 CB LYS A 266 4567 5358 5313 -228 -670 -426 C
ATOM 1881 CG LYS A 266 62.086 8.028 18.252 1.00 47.23 C
ANISOU 1881 CG LYS A 266 5489 6319 6137 -175 -706 -408 C
ATOM 1882 CD LYS A 266 61.485 8.539 19.554 1.00 51.85 C
ANISOU 1882 CD LYS A 266 6132 6922 6646 -166 -740 -445 C
ATOM 1883 CE LYS A 266 61.376 7.420 20.593 1.00 51.03 C
ANISOU 1883 CE LYS A 266 6047 6878 6463 -113 -772 -419 C
ATOM 1884 N PHE A 267 60.279 7.042 15.692 1.00 42.19 N
ANISOU 1884 N PHE A 267 4882 5614 5535 -154 -582 -349 N
ATOM 1885 CA PHE A 267 58.931 6.577 15.390 1.00 44.90 C
ANISOU 1885 CA PHE A 267 5289 5943 5829 -129 -538 -326 C
ATOM 1886 C PHE A 267 57.929 6.757 16.547 1.00 58.21 C
ANISOU 1886 C PHE A 267 7035 7652 7432 -109 -565 -353 C
ATOM 1887 O PHE A 267 58.243 6.453 17.703 1.00 53.69 O
ANISOU 1887 O PHE A 267 6463 7125 6810 -87 -612 -359 O
ATOM 1888 CB PHE A 267 58.971 5.119 14.894 1.00 42.20 C
ANISOU 1888 CB PHE A 267 4942 5612 5479 -89 -505 -265 C
ATOM 1889 CG PHE A 267 57.605 4.494 14.707 1.00 50.43 C
ANISOU 1889 CG PHE A 267 6051 6643 6468 -63 -461 -235 C
ATOM 1890 CD1 PHE A 267 56.677 5.051 13.828 1.00 48.98 C
ANISOU 1890 CD1 PHE A 267 5902 6414 6294 -81 -410 -237 C
ATOM 1891 CD2 PHE A 267 57.251 3.338 15.404 1.00 51.61 C
ANISOU 1891 CD2 PHE A 267 6224 6825 6561 -20 -472 -203 C
ATOM 1892 CE1 PHE A 267 55.419 4.474 13.658 1.00 47.01 C
ANISOU 1892 CE1 PHE A 267 5706 6156 6000 -60 -373 -212 C
ATOM 1893 CE2 PHE A 267 55.992 2.750 15.237 1.00 46.81 C
ANISOU 1893 CE2 PHE A 267 5670 6203 5912 -1 -431 -174 C
ATOM 1894 CZ PHE A 267 55.079 3.319 14.363 1.00 46.22 C
ANISOU 1894 CZ PHE A 267 5625 6087 5849 -22 -383 -181 C
ATOM 1895 N ASP A 268 56.746 7.281 16.194 1.00 71.02 N
ANISOU 1895 N ASP A 268 8709 9239 9036 -116 -523 -360 N
ATOM 1896 CA ASP A 268 55.534 7.377 17.039 1.00 73.56 C
ANISOU 1896 CA ASP A 268 9093 9577 9280 -92 -525 -375 C
ATOM 1897 C ASP A 268 55.393 8.692 17.820 1.00 76.05 C
ANISOU 1897 C ASP A 268 9431 9884 9581 -112 -552 -435 C
ATOM 1898 O ASP A 268 54.295 9.259 17.914 1.00 74.23 O
ANISOU 1898 O ASP A 268 9248 9635 9320 -107 -528 -454 O
ATOM 1899 CB ASP A 268 55.342 6.150 17.957 1.00 65.89 C
ANISOU 1899 CB ASP A 268 8137 8662 8236 -46 -543 -341 C
ATOM 1900 N ARG A 298 41.156 27.059 28.005 1.00 86.50 N
ANISOU 1900 N ARG A 298 11495 10857 10516 218 -337 -1243 N
ATOM 1901 CA ARG A 298 40.020 27.571 27.246 1.00 89.74 C
ANISOU 1901 CA ARG A 298 11913 11223 10961 246 -285 -1228 C
ATOM 1902 C ARG A 298 40.469 28.417 26.052 1.00 88.35 C
ANISOU 1902 C ARG A 298 11735 10948 10886 207 -290 -1225 C
ATOM 1903 O ARG A 298 40.050 28.170 24.919 1.00 83.67 O
ANISOU 1903 O ARG A 298 11124 10331 10335 205 -259 -1172 O
ATOM 1904 CB ARG A 298 39.095 28.388 28.154 1.00 90.56 C
ANISOU 1904 CB ARG A 298 12055 11330 11023 297 -263 -1285 C
ATOM 1905 N LYS A 299 41.314 29.414 26.317 1.00 89.08 N
ANISOU 1905 N LYS A 299 11847 10984 11017 175 -329 -1282 N
ATOM 1906 CA LYS A 299 41.795 30.335 25.284 1.00 86.06 C
ANISOU 1906 CA LYS A 299 11466 10501 10732 135 -333 -1281 C
ATOM 1907 C LYS A 299 43.292 30.618 25.419 1.00 86.47 C
ANISOU 1907 C LYS A 299 11507 10524 10822 73 -391 -1309 C
ATOM 1908 O LYS A 299 43.854 31.481 24.729 1.00 82.02 O
ANISOU 1908 O LYS A 299 10947 9876 10341 33 -401 -1316 O
ATOM 1909 CB LYS A 299 41.017 31.647 25.314 1.00 83.93 C
ANISOU 1909 CB LYS A 299 11238 10161 10490 165 -309 -1325 C
ATOM 1910 N SER A 300 43.941 29.892 26.319 1.00 87.98 N
ANISOU 1910 N SER A 300 11684 10787 10956 65 -429 -1323 N
ATOM 1911 CA SER A 300 45.392 29.770 26.244 1.00 85.80 C
ANISOU 1911 CA SER A 300 11379 10503 10717 4 -481 -1327 C
ATOM 1912 C SER A 300 45.771 28.531 25.439 1.00 84.64 C
ANISOU 1912 C SER A 300 11186 10395 10579 -15 -474 -1250 C
ATOM 1913 O SER A 300 46.852 27.971 25.623 1.00 86.68 O
ANISOU 1913 O SER A 300 11413 10685 10838 -49 -515 -1244 O
ATOM 1914 CB SER A 300 46.035 29.721 27.635 1.00 83.37 C
ANISOU 1914 CB SER A 300 11080 10247 10349 4 -534 -1386 C
ATOM 1915 OG SER A 300 46.078 30.988 28.241 1.00 80.90 O
ANISOU 1915 OG SER A 300 10805 9882 10050 2 -553 -1464 O
ATOM 1916 N GLY A 301 44.876 28.109 24.549 1.00 73.88 N
ANISOU 1916 N GLY A 301 9818 9029 9224 9 -424 -1194 N
ATOM 1917 CA GLY A 301 45.199 27.094 23.566 1.00 58.99 C
ANISOU 1917 CA GLY A 301 7892 7162 7361 -12 -414 -1124 C
ATOM 1918 C GLY A 301 45.725 27.861 22.372 1.00 52.39 C
ANISOU 1918 C GLY A 301 7047 6235 6624 -56 -410 -1108 C
ATOM 1919 O GLY A 301 45.498 27.467 21.235 1.00 46.37 O
ANISOU 1919 O GLY A 301 6267 5457 5896 -61 -379 -1051 O
ATOM 1920 N THR A 302 46.380 28.992 22.639 1.00 56.17 N
ANISOU 1920 N THR A 302 7540 6654 7148 -88 -439 -1159 N
ATOM 1921 CA THR A 302 46.995 29.828 21.610 1.00 51.12 C
ANISOU 1921 CA THR A 302 6894 5924 6606 -135 -437 -1146 C
ATOM 1922 C THR A 302 48.495 29.804 21.827 1.00 49.33 C
ANISOU 1922 C THR A 302 6632 5697 6413 -195 -488 -1162 C
ATOM 1923 O THR A 302 48.955 30.067 22.932 1.00 55.40 O
ANISOU 1923 O THR A 302 7410 6488 7153 -200 -531 -1220 O
ATOM 1924 CB THR A 302 46.513 31.309 21.689 1.00 59.92 C
ANISOU 1924 CB THR A 302 8055 6954 7758 -127 -426 -1193 C
ATOM 1925 OG1 THR A 302 45.106 31.407 21.408 1.00 60.27 O
ANISOU 1925 OG1 THR A 302 8128 6993 7779 -70 -376 -1176 O
ATOM 1926 CG2 THR A 302 47.267 32.193 20.674 1.00 56.46 C
ANISOU 1926 CG2 THR A 302 7611 6419 7423 -182 -426 -1176 C
ATOM 1927 N TYR A 303 49.255 29.471 20.788 1.00 36.89 N
ANISOU 1927 N TYR A 303 5016 4102 4898 -237 -485 -1109 N
ATOM 1928 CA TYR A 303 50.706 29.303 20.921 1.00 40.40 C
ANISOU 1928 CA TYR A 303 5417 4557 5378 -293 -530 -1115 C
ATOM 1929 C TYR A 303 51.418 29.393 19.573 1.00 41.41 C
ANISOU 1929 C TYR A 303 5508 4632 5593 -341 -512 -1059 C
ATOM 1930 O TYR A 303 50.781 29.349 18.519 1.00 41.35 O
ANISOU 1930 O TYR A 303 5508 4593 5609 -328 -465 -1009 O
ATOM 1931 CB TYR A 303 51.038 27.960 21.583 1.00 43.15 C
ANISOU 1931 CB TYR A 303 5735 5006 5656 -278 -556 -1104 C
ATOM 1932 CG TYR A 303 50.342 26.794 20.914 1.00 53.50 C
ANISOU 1932 CG TYR A 303 7034 6360 6933 -245 -515 -1039 C
ATOM 1933 CD1 TYR A 303 50.830 26.250 19.723 1.00 54.54 C
ANISOU 1933 CD1 TYR A 303 7125 6480 7116 -273 -496 -978 C
ATOM 1934 CD2 TYR A 303 49.193 26.243 21.464 1.00 56.71 C
ANISOU 1934 CD2 TYR A 303 7469 6821 7259 -187 -494 -1039 C
ATOM 1935 CE1 TYR A 303 50.192 25.186 19.104 1.00 52.92 C
ANISOU 1935 CE1 TYR A 303 6912 6314 6883 -244 -462 -923 C
ATOM 1936 CE2 TYR A 303 48.550 25.180 20.856 1.00 57.20 C
ANISOU 1936 CE2 TYR A 303 7520 6921 7294 -160 -458 -982 C
ATOM 1937 CZ TYR A 303 49.053 24.656 19.675 1.00 56.27 C
ANISOU 1937 CZ TYR A 303 7364 6788 7227 -189 -444 -926 C
ATOM 1938 OH TYR A 303 48.413 23.600 19.071 1.00 54.69 O
ANISOU 1938 OH TYR A 303 7155 6624 7001 -163 -412 -874 O
ATOM 1939 N ARG A 304 52.742 29.506 19.615 1.00 40.02 N
ANISOU 1939 N ARG A 304 5291 4450 5466 -397 -549 -1067 N
ATOM 1940 CA ARG A 304 53.538 29.616 18.402 1.00 44.76 C
ANISOU 1940 CA ARG A 304 5851 5004 6152 -446 -531 -1015 C
ATOM 1941 C ARG A 304 54.777 28.729 18.485 1.00 50.47 C
ANISOU 1941 C ARG A 304 6509 5784 6882 -480 -563 -997 C
ATOM 1942 O ARG A 304 55.441 28.669 19.526 1.00 51.66 O
ANISOU 1942 O ARG A 304 6645 5972 7009 -491 -615 -1045 O
ATOM 1943 CB ARG A 304 53.956 31.070 18.170 1.00 41.51 C
ANISOU 1943 CB ARG A 304 5454 4496 5821 -491 -535 -1040 C
ATOM 1944 CG ARG A 304 52.818 32.003 17.810 1.00 41.48 C
ANISOU 1944 CG ARG A 304 5511 4422 5829 -461 -496 -1043 C
ATOM 1945 CD ARG A 304 52.317 31.730 16.398 1.00 46.79 C
ANISOU 1945 CD ARG A 304 6180 5069 6529 -450 -439 -964 C
ATOM 1946 NE ARG A 304 51.146 32.539 16.066 1.00 43.44 N
ANISOU 1946 NE ARG A 304 5813 4584 6107 -412 -403 -963 N
ATOM 1947 CZ ARG A 304 49.901 32.216 16.411 1.00 40.30 C
ANISOU 1947 CZ ARG A 304 5451 4220 5641 -349 -385 -973 C
ATOM 1948 NH1 ARG A 304 49.669 31.102 17.098 1.00 36.69 N
ANISOU 1948 NH1 ARG A 304 4980 3855 5107 -319 -398 -982 N
ATOM 1949 NH2 ARG A 304 48.888 33.004 16.072 1.00 35.24 N
ANISOU 1949 NH2 ARG A 304 4858 3522 5010 -315 -351 -971 N
ATOM 1950 N GLY A 305 55.077 28.042 17.386 1.00 46.39 N
ANISOU 1950 N GLY A 305 5954 5274 6398 -493 -532 -929 N
ATOM 1951 CA GLY A 305 56.297 27.261 17.264 1.00 37.21 C
ANISOU 1951 CA GLY A 305 4725 4157 5257 -526 -554 -905 C
ATOM 1952 C GLY A 305 56.450 26.112 18.245 1.00 43.58 C
ANISOU 1952 C GLY A 305 5515 5058 5986 -497 -592 -921 C
ATOM 1953 O GLY A 305 57.570 25.711 18.566 1.00 47.35 O
ANISOU 1953 O GLY A 305 5942 5573 6477 -525 -629 -925 O
ATOM 1954 N LYS A 306 55.332 25.582 18.734 1.00 38.80 N
ANISOU 1954 N LYS A 306 4951 4494 5299 -440 -581 -928 N
ATOM 1955 CA LYS A 306 55.374 24.407 19.594 1.00 36.15 C
ANISOU 1955 CA LYS A 306 4603 4248 4885 -408 -609 -931 C
ATOM 1956 C LYS A 306 55.790 23.187 18.760 1.00 44.86 C
ANISOU 1956 C LYS A 306 5657 5387 5999 -410 -591 -866 C
ATOM 1957 O LYS A 306 55.408 23.056 17.595 1.00 45.13 O
ANISOU 1957 O LYS A 306 5690 5391 6068 -411 -543 -818 O
ATOM 1958 CB LYS A 306 54.013 24.192 20.265 1.00 44.70 C
ANISOU 1958 CB LYS A 306 5742 5361 5881 -348 -595 -948 C
ATOM 1959 CG LYS A 306 53.941 22.980 21.183 1.00 52.19 C
ANISOU 1959 CG LYS A 306 6685 6401 6742 -310 -618 -945 C
ATOM 1960 CD LYS A 306 52.540 22.778 21.765 1.00 54.93 C
ANISOU 1960 CD LYS A 306 7085 6778 7008 -252 -593 -954 C
ATOM 1961 CE LYS A 306 52.208 23.814 22.834 1.00 58.35 C
ANISOU 1961 CE LYS A 306 7562 7197 7412 -240 -615 -1023 C
ATOM 1962 NZ LYS A 306 50.907 23.526 23.515 1.00 58.52 N
ANISOU 1962 NZ LYS A 306 7628 7259 7348 -180 -590 -1031 N
ATOM 1963 N VAL A 307 56.592 22.308 19.350 1.00 44.75 N
ANISOU 1963 N VAL A 307 5606 5440 5958 -410 -629 -864 N
ATOM 1964 CA VAL A 307 57.112 21.153 18.631 1.00 39.70 C
ANISOU 1964 CA VAL A 307 4916 4835 5332 -413 -616 -807 C
ATOM 1965 C VAL A 307 56.378 19.901 19.098 1.00 44.15 C
ANISOU 1965 C VAL A 307 5498 5469 5809 -358 -613 -789 C
ATOM 1966 O VAL A 307 56.284 19.634 20.300 1.00 49.06 O
ANISOU 1966 O VAL A 307 6137 6142 6362 -332 -649 -819 O
ATOM 1967 CB VAL A 307 58.645 21.021 18.811 1.00 47.80 C
ANISOU 1967 CB VAL A 307 5876 5882 6402 -453 -658 -810 C
ATOM 1968 CG1 VAL A 307 59.014 21.076 20.285 1.00 63.55 C
ANISOU 1968 CG1 VAL A 307 7879 7925 8343 -444 -721 -863 C
ATOM 1969 CG2 VAL A 307 59.176 19.748 18.163 1.00 43.74 C
ANISOU 1969 CG2 VAL A 307 5310 5411 5896 -447 -645 -753 C
ATOM 1970 N GLN A 308 55.823 19.152 18.149 1.00 35.83 N
ANISOU 1970 N GLN A 308 4442 4416 4756 -341 -568 -739 N
ATOM 1971 CA GLN A 308 54.972 18.019 18.495 1.00 35.99 C
ANISOU 1971 CA GLN A 308 4484 4493 4697 -291 -559 -718 C
ATOM 1972 C GLN A 308 55.273 16.808 17.628 1.00 36.62 C
ANISOU 1972 C GLN A 308 4525 4598 4793 -288 -539 -663 C
ATOM 1973 O GLN A 308 55.596 16.949 16.446 1.00 40.10 O
ANISOU 1973 O GLN A 308 4938 4997 5300 -315 -509 -634 O
ATOM 1974 CB GLN A 308 53.494 18.394 18.340 1.00 38.60 C
ANISOU 1974 CB GLN A 308 4872 4799 4997 -260 -519 -723 C
ATOM 1975 CG GLN A 308 53.062 19.605 19.154 1.00 40.54 C
ANISOU 1975 CG GLN A 308 5160 5017 5226 -256 -531 -779 C
ATOM 1976 CD GLN A 308 51.575 19.877 19.054 1.00 42.73 C
ANISOU 1976 CD GLN A 308 5489 5278 5468 -218 -491 -780 C
ATOM 1977 OE1 GLN A 308 51.079 20.328 18.024 1.00 42.64 O
ANISOU 1977 OE1 GLN A 308 5488 5214 5501 -225 -452 -761 O
ATOM 1978 NE2 GLN A 308 50.857 19.603 20.130 1.00 46.63 N
ANISOU 1978 NE2 GLN A 308 6015 5821 5882 -177 -497 -801 N
ATOM 1979 N ASN A 309 55.170 15.617 18.211 1.00 30.33 N
ANISOU 1979 N ASN A 309 3724 3866 3932 -253 -554 -645 N
ATOM 1980 CA ASN A 309 55.176 14.413 17.395 1.00 33.58 C
ANISOU 1980 CA ASN A 309 4111 4300 4350 -241 -531 -594 C
ATOM 1981 C ASN A 309 53.781 14.222 16.812 1.00 34.99 C
ANISOU 1981 C ASN A 309 4330 4461 4502 -215 -484 -577 C
ATOM 1982 O ASN A 309 52.880 15.007 17.112 1.00 36.12 O
ANISOU 1982 O ASN A 309 4519 4582 4623 -204 -471 -603 O
ATOM 1983 CB ASN A 309 55.670 13.179 18.166 1.00 32.82 C
ANISOU 1983 CB ASN A 309 3993 4275 4204 -214 -565 -576 C
ATOM 1984 CG ASN A 309 54.843 12.876 19.400 1.00 42.36 C
ANISOU 1984 CG ASN A 309 5249 5529 5318 -172 -579 -589 C
ATOM 1985 OD1 ASN A 309 53.640 13.136 19.443 1.00 43.34 O
ANISOU 1985 OD1 ASN A 309 5420 5641 5407 -152 -548 -596 O
ATOM 1986 ND2 ASN A 309 55.490 12.306 20.415 1.00 40.34 N
ANISOU 1986 ND2 ASN A 309 4979 5328 5020 -156 -622 -589 N
ATOM 1987 N LEU A 310 53.611 13.192 15.987 1.00 33.90 N
ANISOU 1987 N LEU A 310 4175 4335 4369 -204 -459 -535 N
ATOM 1988 CA LEU A 310 52.368 12.979 15.245 1.00 32.19 C
ANISOU 1988 CA LEU A 310 3991 4101 4138 -185 -414 -517 C
ATOM 1989 C LEU A 310 51.138 12.873 16.148 1.00 37.46 C
ANISOU 1989 C LEU A 310 4710 4799 4724 -145 -410 -530 C
ATOM 1990 O LEU A 310 50.096 13.471 15.874 1.00 40.33 O
ANISOU 1990 O LEU A 310 5109 5133 5081 -135 -379 -539 O
ATOM 1991 CB LEU A 310 52.476 11.735 14.363 1.00 30.67 C
ANISOU 1991 CB LEU A 310 3776 3925 3952 -175 -382 -455 C
ATOM 1992 CG LEU A 310 51.198 11.351 13.615 1.00 34.52 C
ANISOU 1992 CG LEU A 310 4300 4401 4416 -151 -327 -416 C
ATOM 1993 CD1 LEU A 310 50.671 12.514 12.766 1.00 36.14 C
ANISOU 1993 CD1 LEU A 310 4525 4544 4661 -168 -295 -425 C
ATOM 1994 CD2 LEU A 310 51.444 10.125 12.752 1.00 30.48 C
ANISOU 1994 CD2 LEU A 310 3767 3901 3914 -143 -297 -356 C
ATOM 1995 N THR A 311 51.267 12.122 17.229 1.00 35.78 N
ANISOU 1995 N THR A 311 4500 4647 4450 -120 -437 -526 N
ATOM 1996 CA THR A 311 50.157 11.934 18.148 1.00 38.63 C
ANISOU 1996 CA THR A 311 4904 5043 4731 -81 -427 -530 C
ATOM 1997 C THR A 311 49.697 13.251 18.794 1.00 39.20 C
ANISOU 1997 C THR A 311 5011 5090 4793 -80 -428 -578 C
ATOM 1998 O THR A 311 48.497 13.547 18.845 1.00 32.20 O
ANISOU 1998 O THR A 311 4160 4198 3878 -57 -396 -582 O
ATOM 1999 CB THR A 311 50.512 10.885 19.216 1.00 44.77 C
ANISOU 1999 CB THR A 311 5676 5888 5446 -55 -456 -511 C
ATOM 2000 OG1 THR A 311 50.670 9.608 18.583 1.00 47.01 O
ANISOU 2000 OG1 THR A 311 5937 6192 5734 -46 -448 -463 O
ATOM 2001 CG2 THR A 311 49.413 10.791 20.262 1.00 47.06 C
ANISOU 2001 CG2 THR A 311 6012 6215 5655 -17 -442 -514 C
ATOM 2002 N GLN A 312 50.653 14.039 19.278 1.00 37.83 N
ANISOU 2002 N GLN A 312 4825 4903 4646 -105 -465 -613 N
ATOM 2003 CA GLN A 312 50.353 15.322 19.900 1.00 37.68 C
ANISOU 2003 CA GLN A 312 4838 4857 4623 -107 -471 -663 C
ATOM 2004 C GLN A 312 49.748 16.302 18.902 1.00 39.78 C
ANISOU 2004 C GLN A 312 5119 5053 4943 -121 -435 -670 C
ATOM 2005 O GLN A 312 48.768 16.990 19.208 1.00 35.49 O
ANISOU 2005 O GLN A 312 4614 4494 4376 -99 -415 -693 O
ATOM 2006 CB GLN A 312 51.620 15.934 20.493 1.00 37.20 C
ANISOU 2006 CB GLN A 312 4755 4791 4589 -138 -521 -699 C
ATOM 2007 CG GLN A 312 52.281 15.081 21.542 1.00 38.71 C
ANISOU 2007 CG GLN A 312 4931 5050 4727 -123 -562 -694 C
ATOM 2008 CD GLN A 312 53.666 15.580 21.891 1.00 47.27 C
ANISOU 2008 CD GLN A 312 5980 6129 5851 -158 -613 -723 C
ATOM 2009 OE1 GLN A 312 54.346 16.195 21.067 1.00 52.62 O
ANISOU 2009 OE1 GLN A 312 6628 6756 6608 -200 -613 -728 O
ATOM 2010 NE2 GLN A 312 54.088 15.328 23.121 1.00 47.49 N
ANISOU 2010 NE2 GLN A 312 6011 6209 5823 -143 -656 -742 N
ATOM 2011 N PHE A 313 50.342 16.363 17.712 1.00 35.12 N
ANISOU 2011 N PHE A 313 4498 4421 4425 -154 -425 -648 N
ATOM 2012 CA PHE A 313 49.903 17.293 16.684 1.00 30.05 C
ANISOU 2012 CA PHE A 313 3869 3709 3840 -169 -391 -647 C
ATOM 2013 C PHE A 313 48.482 16.989 16.224 1.00 32.29 C
ANISOU 2013 C PHE A 313 4182 3994 4092 -133 -348 -627 C
ATOM 2014 O PHE A 313 47.743 17.891 15.826 1.00 37.66 O
ANISOU 2014 O PHE A 313 4890 4626 4791 -126 -323 -637 O
ATOM 2015 CB PHE A 313 50.853 17.259 15.487 1.00 27.07 C
ANISOU 2015 CB PHE A 313 3450 3294 3542 -210 -384 -618 C
ATOM 2016 CG PHE A 313 50.519 18.264 14.425 1.00 27.18 C
ANISOU 2016 CG PHE A 313 3478 3234 3617 -228 -349 -610 C
ATOM 2017 CD1 PHE A 313 50.463 19.619 14.728 1.00 28.15 C
ANISOU 2017 CD1 PHE A 313 3626 3307 3764 -239 -354 -646 C
ATOM 2018 CD2 PHE A 313 50.256 17.860 13.122 1.00 27.06 C
ANISOU 2018 CD2 PHE A 313 3453 3196 3633 -231 -310 -567 C
ATOM 2019 CE1 PHE A 313 50.154 20.559 13.749 1.00 32.06 C
ANISOU 2019 CE1 PHE A 313 4136 3730 4315 -252 -322 -633 C
ATOM 2020 CE2 PHE A 313 49.952 18.790 12.139 1.00 26.98 C
ANISOU 2020 CE2 PHE A 313 3458 3117 3675 -243 -277 -553 C
ATOM 2021 CZ PHE A 313 49.897 20.148 12.456 1.00 28.57 C
ANISOU 2021 CZ PHE A 313 3685 3268 3901 -253 -283 -584 C
ATOM 2022 N TYR A 314 48.106 15.716 16.285 1.00 27.05 N
ANISOU 2022 N TYR A 314 3514 3385 3381 -108 -340 -597 N
ATOM 2023 CA TYR A 314 46.784 15.295 15.850 1.00 29.95 C
ANISOU 2023 CA TYR A 314 3902 3760 3717 -76 -301 -574 C
ATOM 2024 C TYR A 314 45.789 15.178 17.014 1.00 35.98 C
ANISOU 2024 C TYR A 314 4697 4571 4404 -35 -295 -588 C
ATOM 2025 O TYR A 314 44.615 14.912 16.783 1.00 34.43 O
ANISOU 2025 O TYR A 314 4516 4385 4180 -6 -260 -571 O
ATOM 2026 CB TYR A 314 46.862 13.972 15.068 1.00 27.74 C
ANISOU 2026 CB TYR A 314 3597 3505 3437 -76 -286 -524 C
ATOM 2027 CG TYR A 314 47.070 14.103 13.558 1.00 34.20 C
ANISOU 2027 CG TYR A 314 4401 4274 4322 -100 -253 -483 C
ATOM 2028 CD1 TYR A 314 46.263 13.407 12.662 1.00 35.05 C
ANISOU 2028 CD1 TYR A 314 4511 4385 4420 -84 -211 -431 C
ATOM 2029 CD2 TYR A 314 48.079 14.905 13.028 1.00 42.36 C
ANISOU 2029 CD2 TYR A 314 5414 5257 5424 -138 -264 -495 C
ATOM 2030 CE1 TYR A 314 46.451 13.510 11.279 1.00 36.58 C
ANISOU 2030 CE1 TYR A 314 4695 4540 4664 -101 -182 -394 C
ATOM 2031 CE2 TYR A 314 48.276 15.015 11.635 1.00 36.97 C
ANISOU 2031 CE2 TYR A 314 4719 4534 4795 -157 -228 -452 C
ATOM 2032 CZ TYR A 314 47.459 14.316 10.772 1.00 38.59 C
ANISOU 2032 CZ TYR A 314 4933 4749 4981 -135 -188 -403 C
ATOM 2033 OH TYR A 314 47.642 14.417 9.402 1.00 36.34 O
ANISOU 2033 OH TYR A 314 4640 4429 4739 -148 -154 -362 O
ATOM 2034 N HIS A 315 46.254 15.375 18.251 1.00 40.71 N
ANISOU 2034 N HIS A 315 5302 5199 4968 -31 -326 -616 N
ATOM 2035 CA HIS A 315 45.391 15.303 19.449 1.00 48.27 C
ANISOU 2035 CA HIS A 315 6288 6203 5850 7 -319 -629 C
ATOM 2036 C HIS A 315 44.152 16.204 19.340 1.00 52.67 C
ANISOU 2036 C HIS A 315 6875 6731 6406 31 -283 -647 C
ATOM 2037 O HIS A 315 44.262 17.357 18.901 1.00 47.66 O
ANISOU 2037 O HIS A 315 6249 6035 5823 16 -284 -675 O
ATOM 2038 CB HIS A 315 46.196 15.650 20.713 1.00 52.38 C
ANISOU 2038 CB HIS A 315 6812 6747 6343 3 -362 -667 C
ATOM 2039 CG HIS A 315 45.365 15.781 21.957 1.00 59.72 C
ANISOU 2039 CG HIS A 315 7775 7718 7200 42 -354 -687 C
ATOM 2040 ND1 HIS A 315 45.050 14.707 22.763 1.00 64.60 N
ANISOU 2040 ND1 HIS A 315 8396 8404 7746 71 -349 -657 N
ATOM 2041 CD2 HIS A 315 44.792 16.866 22.534 1.00 58.58 C
ANISOU 2041 CD2 HIS A 315 7661 7556 7043 58 -347 -731 C
ATOM 2042 CE1 HIS A 315 44.312 15.124 23.780 1.00 61.38 C
ANISOU 2042 CE1 HIS A 315 8017 8021 7284 102 -338 -682 C
ATOM 2043 NE2 HIS A 315 44.140 16.428 23.663 1.00 57.86 N
ANISOU 2043 NE2 HIS A 315 7588 7525 6872 96 -337 -730 N
ATOM 2044 N PRO A 316 42.970 15.691 19.751 1.00 54.09 N
ANISOU 2044 N PRO A 316 7069 6953 6530 70 -251 -630 N
ATOM 2045 CA PRO A 316 42.695 14.426 20.444 1.00 49.90 C
ANISOU 2045 CA PRO A 316 6533 6493 5933 92 -245 -595 C
ATOM 2046 C PRO A 316 42.040 13.368 19.559 1.00 49.81 C
ANISOU 2046 C PRO A 316 6506 6496 5922 98 -212 -543 C
ATOM 2047 O PRO A 316 41.183 12.626 20.055 1.00 43.50 O
ANISOU 2047 O PRO A 316 5711 5746 5071 125 -185 -515 O
ATOM 2048 CB PRO A 316 41.659 14.856 21.482 1.00 50.05 C
ANISOU 2048 CB PRO A 316 6579 6540 5897 129 -223 -616 C
ATOM 2049 CG PRO A 316 40.881 16.004 20.761 1.00 55.51 C
ANISOU 2049 CG PRO A 316 7283 7174 6633 136 -197 -639 C
ATOM 2050 CD PRO A 316 41.716 16.442 19.563 1.00 55.28 C
ANISOU 2050 CD PRO A 316 7241 7082 6682 97 -214 -641 C
ATOM 2051 N LEU A 317 42.421 13.302 18.286 1.00 46.31 N
ANISOU 2051 N LEU A 317 6046 6013 5537 73 -212 -530 N
ATOM 2052 CA LEU A 317 41.786 12.373 17.353 1.00 52.93 C
ANISOU 2052 CA LEU A 317 6872 6861 6378 78 -183 -487 C
ATOM 2053 C LEU A 317 42.010 10.896 17.720 1.00 56.10 C
ANISOU 2053 C LEU A 317 7257 7313 6743 79 -183 -435 C
ATOM 2054 O LEU A 317 41.093 10.069 17.585 1.00 50.02 O
ANISOU 2054 O LEU A 317 6483 6567 5955 92 -148 -390 O
ATOM 2055 CB LEU A 317 42.227 12.654 15.910 1.00 49.89 C
ANISOU 2055 CB LEU A 317 6470 6414 6070 47 -177 -467 C
ATOM 2056 CG LEU A 317 41.835 14.033 15.369 1.00 50.01 C
ANISOU 2056 CG LEU A 317 6502 6371 6126 48 -167 -501 C
ATOM 2057 CD1 LEU A 317 42.389 14.257 13.968 1.00 50.02 C
ANISOU 2057 CD1 LEU A 317 6489 6317 6198 17 -160 -474 C
ATOM 2058 CD2 LEU A 317 40.325 14.205 15.385 1.00 48.32 C
ANISOU 2058 CD2 LEU A 317 6304 6170 5887 85 -131 -496 C
ATOM 2059 N ASP A 318 43.216 10.570 18.186 1.00 54.21 N
ANISOU 2059 N ASP A 318 7009 7091 6500 66 -223 -442 N
ATOM 2060 CA ASP A 318 43.544 9.182 18.521 1.00 55.52 C
ANISOU 2060 CA ASP A 318 7160 7298 6636 69 -227 -391 C
ATOM 2061 C ASP A 318 42.833 8.670 19.771 1.00 57.69 C
ANISOU 2061 C ASP A 318 7455 7637 6829 104 -217 -381 C
ATOM 2062 O ASP A 318 42.403 7.513 19.803 1.00 57.89 O
ANISOU 2062 O ASP A 318 7473 7687 6835 112 -192 -323 O
ATOM 2063 CB ASP A 318 45.057 8.957 18.627 1.00 54.54 C
ANISOU 2063 CB ASP A 318 7014 7174 6533 49 -274 -396 C
ATOM 2064 CG ASP A 318 45.742 8.935 17.266 1.00 55.22 C
ANISOU 2064 CG ASP A 318 7073 7209 6699 17 -268 -377 C
ATOM 2065 OD1 ASP A 318 45.606 7.924 16.534 1.00 48.51 O
ANISOU 2065 OD1 ASP A 318 6211 6355 5867 14 -243 -324 O
ATOM 2066 OD2 ASP A 318 46.420 9.929 16.933 1.00 55.18 O
ANISOU 2066 OD2 ASP A 318 7061 7167 6739 -7 -289 -416 O
ATOM 2067 N MET A 319 42.695 9.519 20.789 1.00 55.11 N
ANISOU 2067 N MET A 319 7147 7319 6471 118 -224 -418 N
ATOM 2068 CA MET A 319 42.058 9.075 22.027 1.00 60.53 C
ANISOU 2068 CA MET A 319 7851 8059 7087 149 -207 -399 C
ATOM 2069 C MET A 319 40.536 8.936 21.908 1.00 51.30 C
ANISOU 2069 C MET A 319 6689 6904 5900 170 -151 -376 C
ATOM 2070 O MET A 319 39.915 8.219 22.687 1.00 47.95 O
ANISOU 2070 O MET A 319 6270 6526 5424 191 -125 -340 O
ATOM 2071 CB MET A 319 42.458 9.949 23.229 1.00 70.90 C
ANISOU 2071 CB MET A 319 9185 9384 8371 158 -235 -446 C
ATOM 2072 CG MET A 319 41.937 11.376 23.221 1.00 74.17 C
ANISOU 2072 CG MET A 319 9615 9762 8804 161 -225 -502 C
ATOM 2073 SD MET A 319 42.193 12.187 24.822 1.00 91.07 S
ANISOU 2073 SD MET A 319 11783 11928 10889 180 -252 -553 S
ATOM 2074 CE MET A 319 41.213 11.140 25.901 1.00 86.92 C
ANISOU 2074 CE MET A 319 11270 11478 10278 220 -213 -504 C
ATOM 2075 N PHE A 320 39.947 9.601 20.914 1.00 49.65 N
ANISOU 2075 N PHE A 320 6476 6654 5736 164 -131 -394 N
ATOM 2076 CA PHE A 320 38.504 9.532 20.689 1.00 52.29 C
ANISOU 2076 CA PHE A 320 6807 6999 6061 183 -80 -375 C
ATOM 2077 C PHE A 320 38.109 8.700 19.466 1.00 55.65 C
ANISOU 2077 C PHE A 320 7210 7411 6525 167 -57 -328 C
ATOM 2078 O PHE A 320 36.925 8.612 19.130 1.00 52.90 O
ANISOU 2078 O PHE A 320 6851 7066 6183 177 -17 -308 O
ATOM 2079 CB PHE A 320 37.907 10.935 20.559 1.00 57.01 C
ANISOU 2079 CB PHE A 320 7417 7562 6683 195 -69 -423 C
ATOM 2080 CG PHE A 320 37.782 11.664 21.864 1.00 64.00 C
ANISOU 2080 CG PHE A 320 8325 8466 7526 218 -73 -458 C
ATOM 2081 CD1 PHE A 320 37.008 11.141 22.890 1.00 66.29 C
ANISOU 2081 CD1 PHE A 320 8620 8813 7756 245 -43 -434 C
ATOM 2082 CD2 PHE A 320 38.425 12.879 22.063 1.00 64.58 C
ANISOU 2082 CD2 PHE A 320 8415 8500 7621 210 -105 -516 C
ATOM 2083 CE1 PHE A 320 36.888 11.810 24.095 1.00 69.51 C
ANISOU 2083 CE1 PHE A 320 9050 9241 8121 268 -46 -470 C
ATOM 2084 CE2 PHE A 320 38.307 13.554 23.264 1.00 64.06 C
ANISOU 2084 CE2 PHE A 320 8372 8453 7514 232 -110 -553 C
ATOM 2085 CZ PHE A 320 37.538 13.020 24.281 1.00 67.23 C
ANISOU 2085 CZ PHE A 320 8780 8914 7851 262 -81 -531 C
ATOM 2086 N GLY A 321 39.095 8.098 18.804 1.00 50.74 N
ANISOU 2086 N GLY A 321 6574 6762 5943 137 -81 -304 N
ATOM 2087 CA GLY A 321 38.839 7.308 17.614 1.00 48.85 C
ANISOU 2087 CA GLY A 321 6312 6493 5755 114 -61 -256 C
ATOM 2088 C GLY A 321 37.966 6.084 17.846 1.00 49.94 C
ANISOU 2088 C GLY A 321 6439 6664 5873 119 -27 -198 C
ATOM 2089 O GLY A 321 37.190 5.697 16.973 1.00 41.38 O
ANISOU 2089 O GLY A 321 5338 5561 4823 109 -2 -171 O
ATOM 2090 N GLU A 322 38.084 5.472 19.022 1.00 58.57 N
ANISOU 2090 N GLU A 322 7541 7805 6908 135 -27 -178 N
ATOM 2091 CA GLU A 322 37.329 4.252 19.310 1.00 60.25 C
ANISOU 2091 CA GLU A 322 7744 8046 7104 136 7 -116 C
ATOM 2092 C GLU A 322 35.874 4.523 19.726 1.00 59.66 C
ANISOU 2092 C GLU A 322 7663 8003 7001 157 53 -112 C
ATOM 2093 O GLU A 322 35.074 3.591 19.845 1.00 64.27 O
ANISOU 2093 O GLU A 322 8231 8604 7582 153 89 -59 O
ATOM 2094 CB GLU A 322 38.044 3.400 20.367 1.00 59.90 C
ANISOU 2094 CB GLU A 322 7711 8039 7009 147 -8 -84 C
ATOM 2095 CG GLU A 322 38.321 1.960 19.929 1.00 65.58 C
ANISOU 2095 CG GLU A 322 8416 8739 7762 127 -4 -19 C
ATOM 2096 CD GLU A 322 39.813 1.677 19.762 1.00 73.10 C
ANISOU 2096 CD GLU A 322 9370 9673 8732 119 -51 -23 C
ATOM 2097 OE1 GLU A 322 40.574 1.904 20.731 1.00 72.29 O
ANISOU 2097 OE1 GLU A 322 9282 9605 8581 138 -82 -39 O
ATOM 2098 OE2 GLU A 322 40.226 1.236 18.662 1.00 71.01 O
ANISOU 2098 OE2 GLU A 322 9090 9360 8529 96 -58 -12 O
ATOM 2099 N TRP A 323 35.539 5.798 19.914 1.00 49.34 N
ANISOU 2099 N TRP A 323 6368 6700 5680 178 54 -168 N
ATOM 2100 CA TRP A 323 34.243 6.225 20.454 1.00 48.70 C
ANISOU 2100 CA TRP A 323 6284 6656 5565 208 97 -174 C
ATOM 2101 C TRP A 323 32.990 5.527 19.889 1.00 48.36 C
ANISOU 2101 C TRP A 323 6205 6614 5555 197 142 -125 C
ATOM 2102 O TRP A 323 32.229 4.893 20.633 1.00 39.10 O
ANISOU 2102 O TRP A 323 5021 5488 4346 208 181 -85 O
ATOM 2103 CB TRP A 323 34.090 7.735 20.288 1.00 54.06 C
ANISOU 2103 CB TRP A 323 6975 7314 6251 228 88 -244 C
ATOM 2104 CG TRP A 323 33.029 8.321 21.156 1.00 59.62 C
ANISOU 2104 CG TRP A 323 7681 8045 6925 260 123 -257 C
ATOM 2105 CD1 TRP A 323 31.711 8.494 20.842 1.00 60.93 C
ANISOU 2105 CD1 TRP A 323 7823 8221 7107 276 165 -247 C
ATOM 2106 CD2 TRP A 323 33.193 8.812 22.489 1.00 62.16 C
ANISOU 2106 CD2 TRP A 323 8029 8390 7200 282 117 -282 C
ATOM 2107 NE1 TRP A 323 31.045 9.063 21.899 1.00 61.96 N
ANISOU 2107 NE1 TRP A 323 7962 8378 7203 306 188 -264 N
ATOM 2108 CE2 TRP A 323 31.933 9.269 22.923 1.00 61.38 C
ANISOU 2108 CE2 TRP A 323 7921 8312 7088 311 160 -286 C
ATOM 2109 CE3 TRP A 323 34.285 8.907 23.361 1.00 60.75 C
ANISOU 2109 CE3 TRP A 323 7876 8217 6987 281 78 -302 C
ATOM 2110 CZ2 TRP A 323 31.734 9.815 24.187 1.00 55.56 C
ANISOU 2110 CZ2 TRP A 323 7205 7603 6303 339 167 -312 C
ATOM 2111 CZ3 TRP A 323 34.087 9.448 24.610 1.00 57.29 C
ANISOU 2111 CZ3 TRP A 323 7459 7806 6501 307 83 -328 C
ATOM 2112 CH2 TRP A 323 32.821 9.895 25.013 1.00 58.80 C
ANISOU 2112 CH2 TRP A 323 7645 8018 6677 336 129 -333 C
ATOM 2113 N ASN A 324 32.760 5.663 18.586 1.00 48.09 N
ANISOU 2113 N ASN A 324 6152 6533 5588 175 136 -127 N
ATOM 2114 CA ASN A 324 31.565 5.078 17.990 1.00 45.61 C
ANISOU 2114 CA ASN A 324 5801 6221 5309 163 170 -89 C
ATOM 2115 C ASN A 324 31.564 3.564 18.062 1.00 42.51 C
ANISOU 2115 C ASN A 324 5392 5833 4925 135 182 -24 C
ATOM 2116 O ASN A 324 30.507 2.956 18.252 1.00 39.33 O
ANISOU 2116 O ASN A 324 4961 5455 4526 131 220 15 O
ATOM 2117 CB ASN A 324 31.345 5.565 16.554 1.00 43.61 C
ANISOU 2117 CB ASN A 324 5533 5918 5119 150 155 -107 C
ATOM 2118 CG ASN A 324 30.520 6.829 16.500 1.00 43.22 C
ANISOU 2118 CG ASN A 324 5480 5873 5068 183 169 -148 C
ATOM 2119 OD1 ASN A 324 30.510 7.602 17.455 1.00 41.96 O
ANISOU 2119 OD1 ASN A 324 5340 5739 4863 216 177 -181 O
ATOM 2120 ND2 ASN A 324 29.812 7.043 15.389 1.00 42.19 N
ANISOU 2120 ND2 ASN A 324 5326 5720 4987 178 170 -146 N
ATOM 2121 N ARG A 325 32.752 2.974 17.925 1.00 28.15 N
ANISOU 2121 N ARG A 325 3592 3990 3114 116 149 -13 N
ATOM 2122 CA ARG A 325 32.916 1.528 18.026 1.00 31.79 C
ANISOU 2122 CA ARG A 325 4046 4448 3586 93 156 47 C
ATOM 2123 C ARG A 325 32.674 1.031 19.467 1.00 36.29 C
ANISOU 2123 C ARG A 325 4623 5073 4091 112 185 85 C
ATOM 2124 O ARG A 325 32.064 -0.022 19.674 1.00 40.86 O
ANISOU 2124 O ARG A 325 5184 5660 4679 97 217 144 O
ATOM 2125 CB ARG A 325 34.292 1.090 17.476 1.00 26.38 C
ANISOU 2125 CB ARG A 325 3375 3720 2926 76 114 46 C
ATOM 2126 CG ARG A 325 34.685 -0.342 17.803 1.00 31.85 C
ANISOU 2126 CG ARG A 325 4070 4409 3622 62 116 104 C
ATOM 2127 CD ARG A 325 35.650 -0.915 16.765 1.00 34.03 C
ANISOU 2127 CD ARG A 325 4348 4632 3951 40 84 105 C
ATOM 2128 NE ARG A 325 34.909 -1.453 15.629 1.00 47.50 N
ANISOU 2128 NE ARG A 325 6031 6300 5715 12 96 117 N
ATOM 2129 CZ ARG A 325 34.878 -2.738 15.287 1.00 48.46 C
ANISOU 2129 CZ ARG A 325 6147 6393 5874 -10 101 158 C
ATOM 2130 NH1 ARG A 325 35.574 -3.630 15.973 1.00 36.73 N
ANISOU 2130 NH1 ARG A 325 4675 4906 4373 -6 97 197 N
ATOM 2131 NH2 ARG A 325 34.166 -3.128 14.237 1.00 59.45 N
ANISOU 2131 NH2 ARG A 325 7518 7752 7317 -35 106 158 N
ATOM 2132 N ALA A 326 33.122 1.806 20.454 1.00 34.15 N
ANISOU 2132 N ALA A 326 4380 4840 3756 146 176 53 N
ATOM 2133 CA ALA A 326 32.931 1.454 21.865 1.00 33.63 C
ANISOU 2133 CA ALA A 326 4328 4835 3614 172 203 85 C
ATOM 2134 C ALA A 326 31.467 1.502 22.301 1.00 40.74 C
ANISOU 2134 C ALA A 326 5205 5779 4498 185 263 107 C
ATOM 2135 O ALA A 326 31.043 0.693 23.133 1.00 41.86 O
ANISOU 2135 O ALA A 326 5343 5949 4614 186 297 163 O
ATOM 2136 CB ALA A 326 33.778 2.339 22.769 1.00 26.56 C
ANISOU 2136 CB ALA A 326 3469 3971 2651 206 171 34 C
ATOM 2137 N TYR A 327 30.695 2.437 21.742 1.00 39.51 N
ANISOU 2137 N TYR A 327 5030 5615 4367 193 274 64 N
ATOM 2138 CA TYR A 327 29.301 2.609 22.162 1.00 42.58 C
ANISOU 2138 CA TYR A 327 5391 6041 4748 208 329 77 C
ATOM 2139 C TYR A 327 28.305 2.264 21.075 1.00 43.89 C
ANISOU 2139 C TYR A 327 5507 6185 4985 180 350 100 C
ATOM 2140 O TYR A 327 27.102 2.403 21.278 1.00 41.24 O
ANISOU 2140 O TYR A 327 5137 5883 4651 192 396 112 O
ATOM 2141 CB TYR A 327 29.043 4.042 22.642 1.00 49.71 C
ANISOU 2141 CB TYR A 327 6311 6952 5626 247 324 9 C
ATOM 2142 CG TYR A 327 30.019 4.507 23.693 1.00 52.77 C
ANISOU 2142 CG TYR A 327 6746 7347 5958 268 292 -24 C
ATOM 2143 CD1 TYR A 327 30.072 3.888 24.940 1.00 50.51 C
ANISOU 2143 CD1 TYR A 327 6474 7097 5620 278 307 13 C
ATOM 2144 CD2 TYR A 327 30.893 5.561 23.439 1.00 52.08 C
ANISOU 2144 CD2 TYR A 327 6685 7229 5872 277 244 -92 C
ATOM 2145 CE1 TYR A 327 30.967 4.304 25.902 1.00 57.02 C
ANISOU 2145 CE1 TYR A 327 7339 7933 6393 297 274 -19 C
ATOM 2146 CE2 TYR A 327 31.793 5.985 24.397 1.00 54.23 C
ANISOU 2146 CE2 TYR A 327 6995 7509 6100 291 211 -124 C
ATOM 2147 CZ TYR A 327 31.827 5.353 25.627 1.00 60.68 C
ANISOU 2147 CZ TYR A 327 7825 8367 6862 303 224 -89 C
ATOM 2148 OH TYR A 327 32.721 5.767 26.588 1.00 64.66 O
ANISOU 2148 OH TYR A 327 8364 8882 7320 318 188 -123 O
ATOM 2149 N GLY A 328 28.803 1.833 19.917 1.00 44.56 N
ANISOU 2149 N GLY A 328 5587 6210 5135 143 313 101 N
ATOM 2150 CA GLY A 328 27.937 1.473 18.806 1.00 41.61 C
ANISOU 2150 CA GLY A 328 5169 5807 4835 112 320 116 C
ATOM 2151 C GLY A 328 27.315 0.103 18.985 1.00 48.05 C
ANISOU 2151 C GLY A 328 5953 6629 5676 78 353 187 C
ATOM 2152 O GLY A 328 27.749 -0.667 19.851 1.00 46.32 O
ANISOU 2152 O GLY A 328 5752 6425 5421 76 367 231 O
ATOM 2153 N PRO A 329 26.301 -0.218 18.162 1.00 49.58 N
ANISOU 2153 N PRO A 329 6097 6808 5932 51 365 200 N
ATOM 2154 CA PRO A 329 25.814 0.632 17.067 1.00 49.97 C
ANISOU 2154 CA PRO A 329 6125 6838 6022 56 344 152 C
ATOM 2155 C PRO A 329 24.780 1.654 17.525 1.00 50.29 C
ANISOU 2155 C PRO A 329 6140 6929 6039 96 379 130 C
ATOM 2156 O PRO A 329 24.310 2.442 16.700 1.00 43.32 O
ANISOU 2156 O PRO A 329 5239 6035 5186 108 364 93 O
ATOM 2157 CB PRO A 329 25.113 -0.377 16.155 1.00 46.49 C
ANISOU 2157 CB PRO A 329 5639 6369 5655 8 342 183 C
ATOM 2158 CG PRO A 329 24.520 -1.361 17.122 1.00 43.72 C
ANISOU 2158 CG PRO A 329 5264 6050 5299 -9 392 248 C
ATOM 2159 CD PRO A 329 25.559 -1.493 18.230 1.00 46.50 C
ANISOU 2159 CD PRO A 329 5669 6417 5583 12 397 265 C
ATOM 2160 N ALA A 330 24.432 1.629 18.810 1.00 54.92 N
ANISOU 2160 N ALA A 330 6725 7571 6569 121 427 154 N
ATOM 2161 CA ALA A 330 23.240 2.319 19.307 1.00 63.13 C
ANISOU 2161 CA ALA A 330 7728 8665 7591 157 475 146 C
ATOM 2162 C ALA A 330 23.530 3.698 19.886 1.00 57.91 C
ANISOU 2162 C ALA A 330 7109 8021 6874 213 469 84 C
ATOM 2163 O ALA A 330 22.611 4.441 20.230 1.00 58.53 O
ANISOU 2163 O ALA A 330 7170 8120 6950 245 493 64 O
ATOM 2164 CB ALA A 330 22.531 1.451 20.355 1.00 68.12 C
ANISOU 2164 CB ALA A 330 8340 9332 8212 145 526 206 C
ATOM 2165 N GLY A 331 24.811 4.032 19.995 1.00 52.23 N
ANISOU 2165 N GLY A 331 6446 7281 6119 222 431 53 N
ATOM 2166 CA GLY A 331 25.213 5.245 20.676 1.00 41.95 C
ANISOU 2166 CA GLY A 331 5189 5978 4771 265 415 -6 C
ATOM 2167 C GLY A 331 25.205 6.479 19.800 1.00 35.17 C
ANISOU 2167 C GLY A 331 4335 5089 3939 288 389 -68 C
ATOM 2168 O GLY A 331 24.557 7.478 20.126 1.00 32.66 O
ANISOU 2168 O GLY A 331 4017 4777 3616 325 401 -102 O
ATOM 2169 N PHE A 332 25.928 6.419 18.687 1.00 30.45 N
ANISOU 2169 N PHE A 332 3747 4440 3384 260 344 -78 N
ATOM 2170 CA PHE A 332 26.252 7.636 17.946 1.00 30.39 C
ANISOU 2170 CA PHE A 332 3760 4387 3400 278 310 -134 C
ATOM 2171 C PHE A 332 26.233 7.463 16.434 1.00 31.81 C
ANISOU 2171 C PHE A 332 3920 4516 3650 247 278 -126 C
ATOM 2172 O PHE A 332 26.604 6.419 15.911 1.00 32.89 O
ANISOU 2172 O PHE A 332 4049 4634 3814 204 263 -91 O
ATOM 2173 CB PHE A 332 27.624 8.166 18.377 1.00 25.79 C
ANISOU 2173 CB PHE A 332 3234 3781 2782 284 273 -175 C
ATOM 2174 CG PHE A 332 27.700 8.525 19.820 1.00 31.96 C
ANISOU 2174 CG PHE A 332 4044 4601 3500 314 289 -194 C
ATOM 2175 CD1 PHE A 332 27.474 9.832 20.232 1.00 36.13 C
ANISOU 2175 CD1 PHE A 332 4593 5115 4021 349 285 -246 C
ATOM 2176 CD2 PHE A 332 27.986 7.556 20.776 1.00 32.95 C
ANISOU 2176 CD2 PHE A 332 4177 4761 3583 302 301 -153 C
ATOM 2177 CE1 PHE A 332 27.529 10.168 21.570 1.00 33.38 C
ANISOU 2177 CE1 PHE A 332 4270 4789 3622 370 293 -263 C
ATOM 2178 CE2 PHE A 332 28.032 7.877 22.113 1.00 34.56 C
ANISOU 2178 CE2 PHE A 332 4407 4990 3735 325 308 -167 C
ATOM 2179 CZ PHE A 332 27.811 9.189 22.514 1.00 38.40 C
ANISOU 2179 CZ PHE A 332 4912 5465 4212 359 304 -224 C
ATOM 2180 N LEU A 333 25.802 8.507 15.739 1.00 32.80 N
ANISOU 2180 N LEU A 333 4041 4620 3803 272 269 -159 N
ATOM 2181 CA LEU A 333 25.845 8.524 14.285 1.00 27.40 C
ANISOU 2181 CA LEU A 333 3346 3889 3175 251 236 -156 C
ATOM 2182 C LEU A 333 26.810 9.610 13.841 1.00 28.14 C
ANISOU 2182 C LEU A 333 3486 3931 3273 262 202 -199 C
ATOM 2183 O LEU A 333 26.596 10.793 14.125 1.00 25.70 O
ANISOU 2183 O LEU A 333 3194 3617 2954 304 207 -237 O
ATOM 2184 CB LEU A 333 24.457 8.780 13.693 1.00 28.08 C
ANISOU 2184 CB LEU A 333 3382 3992 3295 270 252 -149 C
ATOM 2185 CG LEU A 333 24.372 8.774 12.162 1.00 27.41 C
ANISOU 2185 CG LEU A 333 3285 3869 3262 253 216 -144 C
ATOM 2186 CD1 LEU A 333 24.513 7.364 11.619 1.00 22.67 C
ANISOU 2186 CD1 LEU A 333 2664 3263 2686 199 202 -106 C
ATOM 2187 CD2 LEU A 333 23.076 9.406 11.685 1.00 31.70 C
ANISOU 2187 CD2 LEU A 333 3785 4429 3831 288 225 -149 C
ATOM 2188 N GLN A 334 27.882 9.187 13.173 1.00 14.03 N
ANISOU 2188 N GLN A 334 1721 2106 1505 226 169 -191 N
ATOM 2189 CA GLN A 334 28.848 10.089 12.579 1.00 18.20 C
ANISOU 2189 CA GLN A 334 2287 2582 2048 227 138 -222 C
ATOM 2190 C GLN A 334 28.206 10.680 11.337 1.00 25.89 C
ANISOU 2190 C GLN A 334 3246 3528 3062 240 129 -222 C
ATOM 2191 O GLN A 334 27.340 10.053 10.726 1.00 30.79 O
ANISOU 2191 O GLN A 334 3830 4167 3703 233 133 -194 O
ATOM 2192 CB GLN A 334 30.123 9.334 12.191 1.00 21.69 C
ANISOU 2192 CB GLN A 334 2746 2997 2498 185 111 -207 C
ATOM 2193 CG GLN A 334 29.972 8.424 10.959 1.00 31.96 C
ANISOU 2193 CG GLN A 334 4025 4283 3836 155 100 -173 C
ATOM 2194 CD GLN A 334 29.061 7.207 11.180 1.00 36.23 C
ANISOU 2194 CD GLN A 334 4526 4861 4377 140 120 -136 C
ATOM 2195 OE1 GLN A 334 28.976 6.665 12.293 1.00 32.74 O
ANISOU 2195 OE1 GLN A 334 4080 4453 3906 139 141 -122 O
ATOM 2196 NE2 GLN A 334 28.381 6.770 10.107 1.00 25.30 N
ANISOU 2196 NE2 GLN A 334 3114 3470 3028 127 112 -120 N
ATOM 2197 N TYR A 335 28.613 11.892 10.976 1.00 23.36 N
ANISOU 2197 N TYR A 335 2956 3166 2754 260 115 -252 N
ATOM 2198 CA TYR A 335 28.055 12.572 9.817 1.00 24.98 C
ANISOU 2198 CA TYR A 335 3155 3344 2994 280 105 -249 C
ATOM 2199 C TYR A 335 29.067 13.565 9.274 1.00 23.03 C
ANISOU 2199 C TYR A 335 2950 3035 2764 279 84 -268 C
ATOM 2200 O TYR A 335 29.404 14.538 9.937 1.00 27.08 O
ANISOU 2200 O TYR A 335 3491 3526 3271 299 86 -304 O
ATOM 2201 CB TYR A 335 26.746 13.289 10.178 1.00 22.42 C
ANISOU 2201 CB TYR A 335 2807 3044 2667 330 129 -262 C
ATOM 2202 CG TYR A 335 25.965 13.781 8.969 1.00 23.09 C
ANISOU 2202 CG TYR A 335 2874 3113 2786 354 118 -249 C
ATOM 2203 CD1 TYR A 335 25.133 12.918 8.258 1.00 26.26 C
ANISOU 2203 CD1 TYR A 335 3230 3545 3202 341 113 -217 C
ATOM 2204 CD2 TYR A 335 26.066 15.101 8.537 1.00 18.33 C
ANISOU 2204 CD2 TYR A 335 2301 2462 2201 388 109 -269 C
ATOM 2205 CE1 TYR A 335 24.412 13.356 7.153 1.00 25.92 C
ANISOU 2205 CE1 TYR A 335 3169 3494 3185 366 97 -206 C
ATOM 2206 CE2 TYR A 335 25.365 15.550 7.429 1.00 18.34 C
ANISOU 2206 CE2 TYR A 335 2288 2451 2229 414 97 -252 C
ATOM 2207 CZ TYR A 335 24.530 14.674 6.743 1.00 26.79 C
ANISOU 2207 CZ TYR A 335 3311 3560 3307 405 89 -221 C
ATOM 2208 OH TYR A 335 23.818 15.108 5.648 1.00 23.56 O
ANISOU 2208 OH TYR A 335 2886 3146 2920 434 72 -205 O
ATOM 2209 N GLN A 336 29.537 13.308 8.061 1.00 18.99 N
ANISOU 2209 N GLN A 336 2443 2497 2277 256 65 -245 N
ATOM 2210 CA GLN A 336 30.556 14.131 7.430 1.00 21.42 C
ANISOU 2210 CA GLN A 336 2786 2746 2605 248 50 -252 C
ATOM 2211 C GLN A 336 30.068 14.710 6.103 1.00 20.44 C
ANISOU 2211 C GLN A 336 2664 2596 2506 269 43 -233 C
ATOM 2212 O GLN A 336 29.446 14.019 5.295 1.00 17.24 O
ANISOU 2212 O GLN A 336 2233 2215 2102 267 37 -206 O
ATOM 2213 CB GLN A 336 31.855 13.328 7.220 1.00 13.90 C
ANISOU 2213 CB GLN A 336 1844 1784 1654 202 37 -240 C
ATOM 2214 CG GLN A 336 32.945 14.151 6.555 1.00 15.88 C
ANISOU 2214 CG GLN A 336 2125 1978 1930 190 26 -243 C
ATOM 2215 CD GLN A 336 34.328 13.556 6.683 1.00 22.00 C
ANISOU 2215 CD GLN A 336 2908 2746 2707 150 16 -241 C
ATOM 2216 OE1 GLN A 336 34.528 12.493 7.285 1.00 22.69 O
ANISOU 2216 OE1 GLN A 336 2980 2868 2773 132 15 -237 O
ATOM 2217 NE2 GLN A 336 35.306 14.252 6.118 1.00 18.12 N
ANISOU 2217 NE2 GLN A 336 2435 2207 2242 136 10 -242 N
ATOM 2218 N PHE A 337 30.347 15.988 5.886 1.00 17.82 N
ANISOU 2218 N PHE A 337 2362 2214 2195 290 41 -246 N
ATOM 2219 CA PHE A 337 29.984 16.626 4.628 1.00 23.58 C
ANISOU 2219 CA PHE A 337 3099 2914 2945 313 34 -221 C
ATOM 2220 C PHE A 337 30.927 17.781 4.298 1.00 18.93 C
ANISOU 2220 C PHE A 337 2553 2256 2385 311 32 -226 C
ATOM 2221 O PHE A 337 31.617 18.310 5.172 1.00 17.15 O
ANISOU 2221 O PHE A 337 2348 2003 2167 300 35 -259 O
ATOM 2222 CB PHE A 337 28.521 17.100 4.665 1.00 21.75 C
ANISOU 2222 CB PHE A 337 2846 2705 2716 365 41 -223 C
ATOM 2223 CG PHE A 337 28.262 18.191 5.671 1.00 22.29 C
ANISOU 2223 CG PHE A 337 2930 2751 2789 402 55 -262 C
ATOM 2224 CD1 PHE A 337 28.385 19.535 5.314 1.00 23.55 C
ANISOU 2224 CD1 PHE A 337 3123 2847 2978 432 54 -268 C
ATOM 2225 CD2 PHE A 337 27.910 17.879 6.971 1.00 21.17 C
ANISOU 2225 CD2 PHE A 337 2772 2650 2623 408 71 -292 C
ATOM 2226 CE1 PHE A 337 28.154 20.535 6.240 1.00 24.04 C
ANISOU 2226 CE1 PHE A 337 3204 2884 3047 467 65 -310 C
ATOM 2227 CE2 PHE A 337 27.676 18.877 7.913 1.00 19.03 C
ANISOU 2227 CE2 PHE A 337 2519 2361 2351 445 84 -334 C
ATOM 2228 CZ PHE A 337 27.799 20.201 7.551 1.00 20.72 C
ANISOU 2228 CZ PHE A 337 2768 2509 2597 475 80 -347 C
ATOM 2229 N VAL A 338 30.971 18.150 3.024 1.00 19.79 N
ANISOU 2229 N VAL A 338 2674 2337 2509 319 27 -192 N
ATOM 2230 CA VAL A 338 31.759 19.291 2.577 1.00 16.61 C
ANISOU 2230 CA VAL A 338 2310 1864 2138 318 30 -185 C
ATOM 2231 C VAL A 338 30.868 20.176 1.720 1.00 23.66 C
ANISOU 2231 C VAL A 338 3212 2733 3043 369 30 -160 C
ATOM 2232 O VAL A 338 30.116 19.676 0.891 1.00 18.96 O
ANISOU 2232 O VAL A 338 2597 2175 2430 387 21 -131 O
ATOM 2233 CB VAL A 338 33.021 18.865 1.767 1.00 16.52 C
ANISOU 2233 CB VAL A 338 2310 1836 2132 273 29 -157 C
ATOM 2234 CG1 VAL A 338 32.654 17.955 0.610 1.00 9.51 C
ANISOU 2234 CG1 VAL A 338 1406 987 1219 275 23 -119 C
ATOM 2235 CG2 VAL A 338 33.788 20.096 1.261 1.00 16.37 C
ANISOU 2235 CG2 VAL A 338 2327 1741 2152 270 37 -143 C
ATOM 2236 N ILE A 339 30.935 21.483 1.957 1.00 22.94 N
ANISOU 2236 N ILE A 339 3152 2580 2986 393 36 -173 N
ATOM 2237 CA ILE A 339 30.196 22.481 1.191 1.00 21.83 C
ANISOU 2237 CA ILE A 339 3027 2404 2864 445 37 -146 C
ATOM 2238 C ILE A 339 31.209 23.306 0.391 1.00 22.08 C
ANISOU 2238 C ILE A 339 3099 2361 2928 428 44 -114 C
ATOM 2239 O ILE A 339 32.217 23.730 0.940 1.00 20.68 O
ANISOU 2239 O ILE A 339 2942 2135 2779 392 50 -137 O
ATOM 2240 CB ILE A 339 29.425 23.419 2.137 1.00 21.20 C
ANISOU 2240 CB ILE A 339 2953 2302 2801 493 43 -187 C
ATOM 2241 CG1 ILE A 339 28.486 22.621 3.050 1.00 15.28 C
ANISOU 2241 CG1 ILE A 339 2160 1628 2018 508 45 -218 C
ATOM 2242 CG2 ILE A 339 28.674 24.510 1.365 1.00 20.47 C
ANISOU 2242 CG2 ILE A 339 2879 2166 2733 554 43 -157 C
ATOM 2243 CD1 ILE A 339 27.504 21.754 2.326 1.00 13.47 C
ANISOU 2243 CD1 ILE A 339 1888 1465 1763 525 35 -184 C
ATOM 2244 N PRO A 340 30.956 23.513 -0.915 1.00 18.98 N
ANISOU 2244 N PRO A 340 2718 1962 2533 451 42 -59 N
ATOM 2245 CA PRO A 340 31.879 24.259 -1.783 1.00 22.59 C
ANISOU 2245 CA PRO A 340 3213 2352 3018 436 55 -16 C
ATOM 2246 C PRO A 340 32.234 25.613 -1.193 1.00 27.50 C
ANISOU 2246 C PRO A 340 3869 2883 3696 441 65 -36 C
ATOM 2247 O PRO A 340 31.355 26.274 -0.628 1.00 25.52 O
ANISOU 2247 O PRO A 340 3622 2617 3459 488 62 -64 O
ATOM 2248 CB PRO A 340 31.077 24.445 -3.081 1.00 18.86 C
ANISOU 2248 CB PRO A 340 2748 1893 2526 486 49 42 C
ATOM 2249 CG PRO A 340 30.138 23.293 -3.103 1.00 21.30 C
ANISOU 2249 CG PRO A 340 3013 2292 2787 499 29 30 C
ATOM 2250 CD PRO A 340 29.775 23.032 -1.655 1.00 22.19 C
ANISOU 2250 CD PRO A 340 3099 2427 2906 494 28 -32 C
ATOM 2251 N THR A 341 33.506 25.989 -1.316 1.00 25.83 N
ANISOU 2251 N THR A 341 3680 2616 3520 392 78 -26 N
ATOM 2252 CA THR A 341 34.060 27.222 -0.757 1.00 30.12 C
ANISOU 2252 CA THR A 341 4254 3065 4125 381 86 -50 C
ATOM 2253 C THR A 341 33.159 28.439 -0.926 1.00 32.65 C
ANISOU 2253 C THR A 341 4596 3333 4475 440 86 -39 C
ATOM 2254 O THR A 341 32.931 29.194 0.023 1.00 36.39 O
ANISOU 2254 O THR A 341 5070 3776 4981 447 79 -91 O
ATOM 2255 CB THR A 341 35.392 27.572 -1.450 1.00 34.50 C
ANISOU 2255 CB THR A 341 4827 3563 4718 329 105 -8 C
ATOM 2256 OG1 THR A 341 36.206 26.395 -1.571 1.00 30.58 O
ANISOU 2256 OG1 THR A 341 4301 3126 4191 279 105 -4 O
ATOM 2257 CG2 THR A 341 36.138 28.676 -0.684 1.00 31.52 C
ANISOU 2257 CG2 THR A 341 4466 3100 4409 296 103 -46 C
ATOM 2258 N GLU A 342 32.654 28.622 -2.144 1.00 29.58 N
ANISOU 2258 N GLU A 342 4215 2952 4073 475 89 27 N
ATOM 2259 CA GLU A 342 31.894 29.819 -2.496 1.00 31.19 C
ANISOU 2259 CA GLU A 342 4429 3115 4306 521 85 50 C
ATOM 2260 C GLU A 342 30.531 29.862 -1.811 1.00 33.87 C
ANISOU 2260 C GLU A 342 4746 3493 4631 578 72 9 C
ATOM 2261 O GLU A 342 29.882 30.905 -1.786 1.00 39.32 O
ANISOU 2261 O GLU A 342 5441 4146 5354 616 69 10 O
ATOM 2262 CB GLU A 342 31.727 29.928 -4.020 1.00 27.35 C
ANISOU 2262 CB GLU A 342 3955 2636 3799 543 90 134 C
ATOM 2263 N ALA A 343 30.104 28.728 -1.258 1.00 26.27 N
ANISOU 2263 N ALA A 343 3755 2606 3622 584 66 -25 N
ATOM 2264 CA ALA A 343 28.803 28.617 -0.596 1.00 23.79 C
ANISOU 2264 CA ALA A 343 3409 2342 3288 634 57 -61 C
ATOM 2265 C ALA A 343 28.933 28.723 0.922 1.00 26.44 C
ANISOU 2265 C ALA A 343 3737 2674 3636 617 62 -139 C
ATOM 2266 O ALA A 343 28.275 28.006 1.677 1.00 28.99 O
ANISOU 2266 O ALA A 343 4029 3064 3924 632 60 -176 O
ATOM 2267 CB ALA A 343 28.110 27.316 -0.995 1.00 20.74 C
ANISOU 2267 CB ALA A 343 2988 2048 2842 654 45 -46 C
ATOM 2268 N VAL A 344 29.782 29.643 1.356 1.00 30.19 N
ANISOU 2268 N VAL A 344 4239 3072 4161 585 68 -163 N
ATOM 2269 CA VAL A 344 30.088 29.815 2.767 1.00 31.06 C
ANISOU 2269 CA VAL A 344 4348 3174 4280 563 71 -237 C
ATOM 2270 C VAL A 344 28.854 30.197 3.597 1.00 33.30 C
ANISOU 2270 C VAL A 344 4612 3486 4555 616 78 -277 C
ATOM 2271 O VAL A 344 28.706 29.775 4.748 1.00 33.01 O
ANISOU 2271 O VAL A 344 4560 3493 4488 611 82 -331 O
ATOM 2272 CB VAL A 344 31.242 30.840 2.944 1.00 39.79 C
ANISOU 2272 CB VAL A 344 5483 4185 5450 517 74 -253 C
ATOM 2273 CG1 VAL A 344 30.884 32.179 2.308 1.00 33.43 C
ANISOU 2273 CG1 VAL A 344 4696 3304 4701 550 76 -221 C
ATOM 2274 CG2 VAL A 344 31.606 30.998 4.404 1.00 41.73 C
ANISOU 2274 CG2 VAL A 344 5730 4428 5697 492 78 -331 C
ATOM 2275 N ASP A 345 27.953 30.971 3.004 1.00 34.29 N
ANISOU 2275 N ASP A 345 4737 3589 4703 669 80 -246 N
ATOM 2276 CA ASP A 345 26.714 31.348 3.685 1.00 37.58 C
ANISOU 2276 CA ASP A 345 5133 4034 5114 724 88 -278 C
ATOM 2277 C ASP A 345 25.809 30.144 3.943 1.00 32.05 C
ANISOU 2277 C ASP A 345 4386 3438 4352 745 87 -281 C
ATOM 2278 O ASP A 345 25.274 29.978 5.041 1.00 33.81 O
ANISOU 2278 O ASP A 345 4589 3703 4553 759 99 -329 O
ATOM 2279 CB ASP A 345 25.966 32.408 2.880 1.00 50.46 C
ANISOU 2279 CB ASP A 345 6770 5619 6784 777 87 -238 C
ATOM 2280 CG ASP A 345 26.208 33.812 3.401 1.00 63.36 C
ANISOU 2280 CG ASP A 345 8433 7160 8480 781 97 -271 C
ATOM 2281 OD1 ASP A 345 27.275 34.061 4.010 1.00 61.58 O
ANISOU 2281 OD1 ASP A 345 8232 6888 8279 731 102 -309 O
ATOM 2282 OD2 ASP A 345 25.320 34.669 3.203 1.00 71.26 O
ANISOU 2282 OD2 ASP A 345 9431 8135 9509 836 100 -261 O
ATOM 2283 N GLU A 346 25.647 29.309 2.923 1.00 28.90 N
ANISOU 2283 N GLU A 346 3971 3083 3927 747 74 -229 N
ATOM 2284 CA GLU A 346 24.907 28.062 3.055 1.00 36.14 C
ANISOU 2284 CA GLU A 346 4841 4098 4793 758 70 -229 C
ATOM 2285 C GLU A 346 25.543 27.175 4.118 1.00 38.75 C
ANISOU 2285 C GLU A 346 5165 4465 5093 713 77 -276 C
ATOM 2286 O GLU A 346 24.846 26.470 4.857 1.00 35.07 O
ANISOU 2286 O GLU A 346 4661 4071 4594 724 85 -299 O
ATOM 2287 CB GLU A 346 24.867 27.323 1.721 1.00 33.46 C
ANISOU 2287 CB GLU A 346 4492 3789 4433 759 52 -169 C
ATOM 2288 CG GLU A 346 24.022 27.999 0.662 1.00 46.95 C
ANISOU 2288 CG GLU A 346 6195 5486 6156 810 41 -119 C
ATOM 2289 CD GLU A 346 24.794 29.027 -0.154 1.00 58.84 C
ANISOU 2289 CD GLU A 346 7752 6904 7700 801 40 -81 C
ATOM 2290 OE1 GLU A 346 24.559 29.096 -1.382 1.00 62.99 O
ANISOU 2290 OE1 GLU A 346 8281 7433 8218 822 27 -22 O
ATOM 2291 OE2 GLU A 346 25.626 29.764 0.425 1.00 54.30 O
ANISOU 2291 OE2 GLU A 346 7210 6258 7161 773 53 -109 O
ATOM 2292 N PHE A 347 26.870 27.219 4.193 1.00 34.59 N
ANISOU 2292 N PHE A 347 4674 3890 4578 661 73 -286 N
ATOM 2293 CA PHE A 347 27.593 26.454 5.190 1.00 27.43 C
ANISOU 2293 CA PHE A 347 3765 3014 3644 616 75 -328 C
ATOM 2294 C PHE A 347 27.273 26.939 6.615 1.00 28.83 C
ANISOU 2294 C PHE A 347 3940 3199 3816 625 89 -388 C
ATOM 2295 O PHE A 347 27.019 26.131 7.509 1.00 26.53 O
ANISOU 2295 O PHE A 347 3624 2975 3482 620 96 -415 O
ATOM 2296 CB PHE A 347 29.098 26.499 4.924 1.00 29.79 C
ANISOU 2296 CB PHE A 347 4100 3257 3964 558 66 -325 C
ATOM 2297 CG PHE A 347 29.917 25.912 6.037 1.00 31.58 C
ANISOU 2297 CG PHE A 347 4325 3507 4167 511 63 -373 C
ATOM 2298 CD1 PHE A 347 29.948 24.532 6.238 1.00 27.31 C
ANISOU 2298 CD1 PHE A 347 3757 3039 3579 494 58 -373 C
ATOM 2299 CD2 PHE A 347 30.641 26.733 6.894 1.00 26.84 C
ANISOU 2299 CD2 PHE A 347 3749 2857 3592 484 63 -419 C
ATOM 2300 CE1 PHE A 347 30.689 23.981 7.273 1.00 26.23 C
ANISOU 2300 CE1 PHE A 347 3618 2929 3419 453 53 -412 C
ATOM 2301 CE2 PHE A 347 31.382 26.190 7.931 1.00 30.60 C
ANISOU 2301 CE2 PHE A 347 4222 3363 4040 443 55 -461 C
ATOM 2302 CZ PHE A 347 31.406 24.813 8.122 1.00 28.28 C
ANISOU 2302 CZ PHE A 347 3902 3144 3698 429 50 -455 C
ATOM 2303 N LYS A 348 27.285 28.254 6.819 1.00 28.82 N
ANISOU 2303 N LYS A 348 3967 3129 3856 641 95 -408 N
ATOM 2304 CA LYS A 348 26.871 28.842 8.103 1.00 32.22 C
ANISOU 2304 CA LYS A 348 4399 3563 4280 660 111 -464 C
ATOM 2305 C LYS A 348 25.455 28.424 8.488 1.00 30.18 C
ANISOU 2305 C LYS A 348 4098 3382 3988 711 126 -465 C
ATOM 2306 O LYS A 348 25.200 28.025 9.623 1.00 32.90 O
ANISOU 2306 O LYS A 348 4429 3779 4294 711 139 -502 O
ATOM 2307 CB LYS A 348 27.018 30.374 8.083 1.00 34.74 C
ANISOU 2307 CB LYS A 348 4755 3788 4657 675 116 -480 C
ATOM 2308 CG LYS A 348 28.485 30.828 8.119 1.00 41.79 C
ANISOU 2308 CG LYS A 348 5687 4608 5584 615 107 -496 C
ATOM 2309 CD LYS A 348 28.736 32.159 7.417 1.00 44.99 C
ANISOU 2309 CD LYS A 348 6123 4910 6062 622 110 -477 C
ATOM 2310 CE LYS A 348 28.264 33.330 8.255 1.00 55.61 C
ANISOU 2310 CE LYS A 348 7488 6212 7431 655 126 -526 C
ATOM 2311 NZ LYS A 348 29.058 34.566 7.987 1.00 58.70 N
ANISOU 2311 NZ LYS A 348 7919 6492 7891 632 131 -529 N
ATOM 2312 N LYS A 349 24.542 28.481 7.529 1.00 25.98 N
ANISOU 2312 N LYS A 349 3542 2859 3469 752 124 -420 N
ATOM 2313 CA LYS A 349 23.157 28.099 7.784 1.00 30.84 C
ANISOU 2313 CA LYS A 349 4109 3549 4061 798 138 -415 C
ATOM 2314 C LYS A 349 23.007 26.646 8.247 1.00 31.97 C
ANISOU 2314 C LYS A 349 4212 3783 4151 775 143 -416 C
ATOM 2315 O LYS A 349 22.244 26.364 9.167 1.00 33.08 O
ANISOU 2315 O LYS A 349 4322 3981 4265 794 164 -437 O
ATOM 2316 CB LYS A 349 22.267 28.398 6.567 1.00 42.48 C
ANISOU 2316 CB LYS A 349 5561 5019 5560 844 128 -364 C
ATOM 2317 CG LYS A 349 22.065 29.908 6.317 1.00 59.67 C
ANISOU 2317 CG LYS A 349 7769 7115 7789 882 131 -365 C
ATOM 2318 CD LYS A 349 21.084 30.179 5.174 1.00 66.35 C
ANISOU 2318 CD LYS A 349 8590 7967 8653 931 119 -311 C
ATOM 2319 N ILE A 350 23.744 25.732 7.626 1.00 28.72 N
ANISOU 2319 N ILE A 350 3801 3384 3727 735 125 -390 N
ATOM 2320 CA ILE A 350 23.715 24.336 8.039 1.00 28.61 C
ANISOU 2320 CA ILE A 350 3752 3449 3669 708 129 -389 C
ATOM 2321 C ILE A 350 24.225 24.173 9.474 1.00 30.10 C
ANISOU 2321 C ILE A 350 3955 3655 3827 682 143 -437 C
ATOM 2322 O ILE A 350 23.641 23.436 10.272 1.00 33.23 O
ANISOU 2322 O ILE A 350 4317 4122 4187 685 162 -444 O
ATOM 2323 CB ILE A 350 24.536 23.463 7.096 1.00 37.23 C
ANISOU 2323 CB ILE A 350 4849 4540 4756 670 108 -357 C
ATOM 2324 CG1 ILE A 350 23.865 23.415 5.721 1.00 37.25 C
ANISOU 2324 CG1 ILE A 350 4830 4547 4775 701 92 -307 C
ATOM 2325 CG2 ILE A 350 24.723 22.057 7.681 1.00 36.83 C
ANISOU 2325 CG2 ILE A 350 4769 4560 4663 636 113 -363 C
ATOM 2326 CD1 ILE A 350 24.548 22.476 4.735 1.00 34.28 C
ANISOU 2326 CD1 ILE A 350 4453 4181 4389 655 72 -268 C
ATOM 2327 N ILE A 351 25.301 24.876 9.803 1.00 21.22 N
ANISOU 2327 N ILE A 351 2879 2467 2717 655 134 -467 N
ATOM 2328 CA ILE A 351 25.813 24.865 11.163 1.00 26.77 C
ANISOU 2328 CA ILE A 351 3599 3183 3390 632 142 -514 C
ATOM 2329 C ILE A 351 24.751 25.376 12.142 1.00 34.09 C
ANISOU 2329 C ILE A 351 4513 4138 4301 678 169 -543 C
ATOM 2330 O ILE A 351 24.523 24.768 13.196 1.00 32.52 O
ANISOU 2330 O ILE A 351 4299 4001 4056 675 185 -560 O
ATOM 2331 CB ILE A 351 27.098 25.702 11.301 1.00 24.90 C
ANISOU 2331 CB ILE A 351 3413 2868 3181 597 124 -544 C
ATOM 2332 CG1 ILE A 351 28.160 25.195 10.331 1.00 27.74 C
ANISOU 2332 CG1 ILE A 351 3782 3200 3557 552 101 -513 C
ATOM 2333 CG2 ILE A 351 27.623 25.624 12.727 1.00 23.71 C
ANISOU 2333 CG2 ILE A 351 3278 2740 2992 575 126 -593 C
ATOM 2334 CD1 ILE A 351 28.525 23.732 10.530 1.00 25.47 C
ANISOU 2334 CD1 ILE A 351 3472 2981 3226 518 96 -502 C
ATOM 2335 N GLY A 352 24.099 26.483 11.779 1.00 32.17 N
ANISOU 2335 N GLY A 352 4276 3849 4096 722 175 -544 N
ATOM 2336 CA GLY A 352 23.022 27.040 12.581 1.00 32.52 C
ANISOU 2336 CA GLY A 352 4307 3917 4133 772 203 -570 C
ATOM 2337 C GLY A 352 21.890 26.049 12.797 1.00 29.57 C
ANISOU 2337 C GLY A 352 3873 3636 3725 793 225 -545 C
ATOM 2338 O GLY A 352 21.431 25.859 13.923 1.00 34.05 O
ANISOU 2338 O GLY A 352 4429 4253 4256 805 250 -570 O
ATOM 2339 N VAL A 353 21.455 25.408 11.717 1.00 27.63 N
ANISOU 2339 N VAL A 353 3591 3416 3493 795 215 -496 N
ATOM 2340 CA VAL A 353 20.430 24.367 11.782 1.00 30.31 C
ANISOU 2340 CA VAL A 353 3867 3842 3808 806 232 -468 C
ATOM 2341 C VAL A 353 20.849 23.217 12.701 1.00 28.14 C
ANISOU 2341 C VAL A 353 3582 3626 3482 765 244 -475 C
ATOM 2342 O VAL A 353 20.040 22.695 13.476 1.00 28.02 O
ANISOU 2342 O VAL A 353 3529 3678 3440 776 274 -473 O
ATOM 2343 CB VAL A 353 20.113 23.823 10.374 1.00 34.25 C
ANISOU 2343 CB VAL A 353 4332 4352 4330 805 210 -417 C
ATOM 2344 CG1 VAL A 353 19.106 22.697 10.441 1.00 29.47 C
ANISOU 2344 CG1 VAL A 353 3656 3835 3707 807 226 -389 C
ATOM 2345 CG2 VAL A 353 19.590 24.939 9.505 1.00 40.20 C
ANISOU 2345 CG2 VAL A 353 5091 5053 5128 851 199 -403 C
ATOM 2346 N ILE A 354 22.119 22.833 12.634 1.00 30.66 N
ANISOU 2346 N ILE A 354 3936 3921 3791 717 223 -480 N
ATOM 2347 CA ILE A 354 22.603 21.747 13.480 1.00 30.03 C
ANISOU 2347 CA ILE A 354 3852 3895 3664 678 230 -482 C
ATOM 2348 C ILE A 354 22.520 22.130 14.948 1.00 29.03 C
ANISOU 2348 C ILE A 354 3743 3786 3500 690 253 -523 C
ATOM 2349 O ILE A 354 22.010 21.362 15.763 1.00 31.69 O
ANISOU 2349 O ILE A 354 4051 4192 3799 690 280 -514 O
ATOM 2350 CB ILE A 354 24.040 21.327 13.141 1.00 27.12 C
ANISOU 2350 CB ILE A 354 3517 3494 3292 626 200 -483 C
ATOM 2351 CG1 ILE A 354 24.061 20.479 11.868 1.00 27.66 C
ANISOU 2351 CG1 ILE A 354 3559 3573 3379 609 184 -438 C
ATOM 2352 CG2 ILE A 354 24.650 20.536 14.298 1.00 28.01 C
ANISOU 2352 CG2 ILE A 354 3638 3650 3355 592 206 -496 C
ATOM 2353 CD1 ILE A 354 25.460 20.132 11.370 1.00 17.90 C
ANISOU 2353 CD1 ILE A 354 2355 2299 2147 562 156 -437 C
ATOM 2354 N GLN A 355 23.010 23.318 15.286 1.00 26.94 N
ANISOU 2354 N GLN A 355 3527 3460 3250 700 244 -566 N
ATOM 2355 CA GLN A 355 22.953 23.779 16.675 1.00 34.80 C
ANISOU 2355 CA GLN A 355 4544 4470 4209 716 263 -610 C
ATOM 2356 C GLN A 355 21.516 23.854 17.221 1.00 35.71 C
ANISOU 2356 C GLN A 355 4621 4638 4311 766 304 -608 C
ATOM 2357 O GLN A 355 21.260 23.472 18.362 1.00 32.44 O
ANISOU 2357 O GLN A 355 4200 4278 3847 771 329 -620 O
ATOM 2358 CB GLN A 355 23.668 25.123 16.837 1.00 33.73 C
ANISOU 2358 CB GLN A 355 4464 4252 4099 719 245 -659 C
ATOM 2359 CG GLN A 355 23.973 25.479 18.288 1.00 33.56 C
ANISOU 2359 CG GLN A 355 4474 4243 4034 722 253 -712 C
ATOM 2360 CD GLN A 355 22.764 26.042 19.015 1.00 33.90 C
ANISOU 2360 CD GLN A 355 4505 4313 4063 780 290 -733 C
ATOM 2361 OE1 GLN A 355 21.899 26.656 18.395 1.00 30.93 O
ANISOU 2361 OE1 GLN A 355 4112 3914 3728 820 303 -724 O
ATOM 2362 NE2 GLN A 355 22.693 25.825 20.332 1.00 31.55 N
ANISOU 2362 NE2 GLN A 355 4216 4066 3707 787 309 -761 N
ATOM 2363 N ALA A 356 20.587 24.332 16.394 1.00 35.44 N
ANISOU 2363 N ALA A 356 4558 4588 4319 804 311 -589 N
ATOM 2364 CA ALA A 356 19.197 24.512 16.809 1.00 35.16 C
ANISOU 2364 CA ALA A 356 4481 4597 4280 855 349 -587 C
ATOM 2365 C ALA A 356 18.402 23.213 16.868 1.00 40.93 C
ANISOU 2365 C ALA A 356 5147 5415 4989 845 373 -542 C
ATOM 2366 O ALA A 356 17.284 23.200 17.383 1.00 43.05 O
ANISOU 2366 O ALA A 356 5377 5732 5250 880 409 -538 O
ATOM 2367 CB ALA A 356 18.493 25.504 15.891 1.00 26.09 C
ANISOU 2367 CB ALA A 356 3323 3402 3189 900 344 -581 C
ATOM 2368 N SER A 357 18.970 22.131 16.340 1.00 37.30 N
ANISOU 2368 N SER A 357 4675 4973 4523 798 354 -508 N
ATOM 2369 CA SER A 357 18.229 20.877 16.177 1.00 33.02 C
ANISOU 2369 CA SER A 357 4068 4505 3974 783 373 -460 C
ATOM 2370 C SER A 357 17.899 20.151 17.476 1.00 29.22 C
ANISOU 2370 C SER A 357 3570 4092 3442 776 413 -457 C
ATOM 2371 O SER A 357 16.924 19.403 17.544 1.00 36.81 O
ANISOU 2371 O SER A 357 4469 5112 4404 778 442 -422 O
ATOM 2372 CB SER A 357 18.971 19.919 15.232 1.00 32.94 C
ANISOU 2372 CB SER A 357 4052 4491 3974 735 342 -427 C
ATOM 2373 OG SER A 357 20.204 19.478 15.788 1.00 33.37 O
ANISOU 2373 OG SER A 357 4150 4537 3992 693 330 -441 O
ATOM 2374 N GLY A 358 18.705 20.355 18.507 1.00 24.32 N
ANISOU 2374 N GLY A 358 3001 3463 2777 767 414 -491 N
ATOM 2375 CA GLY A 358 18.556 19.550 19.712 1.00 15.35 C
ANISOU 2375 CA GLY A 358 1855 2392 1586 756 447 -481 C
ATOM 2376 C GLY A 358 19.470 18.335 19.700 1.00 32.87 C
ANISOU 2376 C GLY A 358 4080 4630 3781 700 431 -452 C
ATOM 2377 O GLY A 358 19.556 17.602 20.688 1.00 35.41 O
ANISOU 2377 O GLY A 358 4401 4999 4053 685 454 -439 O
ATOM 2378 N HIS A 359 20.149 18.115 18.572 1.00 27.30 N
ANISOU 2378 N HIS A 359 3379 3886 3109 671 393 -439 N
ATOM 2379 CA HIS A 359 21.114 17.023 18.452 1.00 26.72 C
ANISOU 2379 CA HIS A 359 3314 3821 3016 619 374 -415 C
ATOM 2380 C HIS A 359 22.523 17.565 18.656 1.00 29.23 C
ANISOU 2380 C HIS A 359 3698 4088 3322 601 336 -455 C
ATOM 2381 O HIS A 359 23.017 18.367 17.868 1.00 29.83 O
ANISOU 2381 O HIS A 359 3799 4100 3434 603 305 -477 O
ATOM 2382 CB HIS A 359 20.956 16.318 17.105 1.00 19.79 C
ANISOU 2382 CB HIS A 359 2395 2942 2182 597 359 -375 C
ATOM 2383 CG HIS A 359 19.564 15.821 16.861 1.00 24.99 C
ANISOU 2383 CG HIS A 359 2983 3651 2862 610 391 -338 C
ATOM 2384 ND1 HIS A 359 19.034 14.746 17.544 1.00 31.45 N
ANISOU 2384 ND1 HIS A 359 3761 4532 3658 590 427 -301 N
ATOM 2385 CD2 HIS A 359 18.582 16.267 16.041 1.00 22.23 C
ANISOU 2385 CD2 HIS A 359 2591 3297 2557 639 391 -330 C
ATOM 2386 CE1 HIS A 359 17.792 14.541 17.142 1.00 29.33 C
ANISOU 2386 CE1 HIS A 359 3427 4295 3423 603 448 -274 C
ATOM 2387 NE2 HIS A 359 17.493 15.452 16.231 1.00 28.75 N
ANISOU 2387 NE2 HIS A 359 3350 4184 3390 634 425 -292 N
ATOM 2388 N TYR A 360 23.165 17.129 19.730 1.00 28.73 N
ANISOU 2388 N TYR A 360 3661 4050 3207 583 338 -462 N
ATOM 2389 CA TYR A 360 24.336 17.832 20.235 1.00 29.35 C
ANISOU 2389 CA TYR A 360 3797 4086 3268 574 305 -509 C
ATOM 2390 C TYR A 360 25.611 17.003 20.117 1.00 28.76 C
ANISOU 2390 C TYR A 360 3740 4006 3180 525 272 -495 C
ATOM 2391 O TYR A 360 25.740 15.951 20.728 1.00 30.53 O
ANISOU 2391 O TYR A 360 3954 4280 3364 507 284 -465 O
ATOM 2392 CB TYR A 360 24.073 18.279 21.683 1.00 29.40 C
ANISOU 2392 CB TYR A 360 3825 4122 3223 603 327 -541 C
ATOM 2393 CG TYR A 360 22.855 19.196 21.813 1.00 29.05 C
ANISOU 2393 CG TYR A 360 3766 4079 3194 655 360 -561 C
ATOM 2394 CD1 TYR A 360 22.685 20.274 20.951 1.00 37.32 C
ANISOU 2394 CD1 TYR A 360 4820 5064 4296 676 346 -584 C
ATOM 2395 CD2 TYR A 360 21.871 18.968 22.778 1.00 30.47 C
ANISOU 2395 CD2 TYR A 360 3922 4320 3334 685 407 -552 C
ATOM 2396 CE1 TYR A 360 21.588 21.111 21.050 1.00 41.69 C
ANISOU 2396 CE1 TYR A 360 5359 5615 4865 726 374 -601 C
ATOM 2397 CE2 TYR A 360 20.758 19.810 22.892 1.00 28.77 C
ANISOU 2397 CE2 TYR A 360 3691 4106 3135 735 438 -571 C
ATOM 2398 CZ TYR A 360 20.630 20.878 22.022 1.00 36.40 C
ANISOU 2398 CZ TYR A 360 4665 5010 4157 756 420 -596 C
ATOM 2399 OH TYR A 360 19.546 21.723 22.094 1.00 39.28 O
ANISOU 2399 OH TYR A 360 5012 5372 4540 808 448 -613 O
ATOM 2400 N SER A 361 26.551 17.496 19.319 1.00 28.15 N
ANISOU 2400 N SER A 361 3689 3868 3141 505 233 -515 N
ATOM 2401 CA SER A 361 27.804 16.801 19.071 1.00 22.43 C
ANISOU 2401 CA SER A 361 2979 3132 2412 459 200 -504 C
ATOM 2402 C SER A 361 29.006 17.564 19.635 1.00 26.11 C
ANISOU 2402 C SER A 361 3492 3558 2871 444 163 -552 C
ATOM 2403 O SER A 361 29.189 18.743 19.347 1.00 26.34 O
ANISOU 2403 O SER A 361 3545 3529 2935 453 149 -589 O
ATOM 2404 CB SER A 361 27.980 16.577 17.562 1.00 18.80 C
ANISOU 2404 CB SER A 361 2503 2636 2004 440 184 -480 C
ATOM 2405 OG SER A 361 29.304 16.202 17.237 1.00 18.86 O
ANISOU 2405 OG SER A 361 2531 2619 2018 399 148 -481 O
ATOM 2406 N PHE A 362 29.819 16.865 20.428 1.00 25.96 N
ANISOU 2406 N PHE A 362 3484 3569 2810 421 148 -548 N
ATOM 2407 CA PHE A 362 31.068 17.387 20.978 1.00 26.85 C
ANISOU 2407 CA PHE A 362 3634 3653 2914 400 108 -589 C
ATOM 2408 C PHE A 362 32.269 17.094 20.086 1.00 35.83 C
ANISOU 2408 C PHE A 362 4773 4751 4089 356 70 -580 C
ATOM 2409 O PHE A 362 33.223 17.867 20.052 1.00 42.01 O
ANISOU 2409 O PHE A 362 5580 5484 4896 337 36 -617 O
ATOM 2410 CB PHE A 362 31.347 16.768 22.348 1.00 33.17 C
ANISOU 2410 CB PHE A 362 4443 4512 3646 402 108 -588 C
ATOM 2411 CG PHE A 362 30.648 17.453 23.475 1.00 54.56 C
ANISOU 2411 CG PHE A 362 7169 7246 6316 442 131 -622 C
ATOM 2412 CD1 PHE A 362 31.164 18.622 24.022 1.00 60.99 C
ANISOU 2412 CD1 PHE A 362 8019 8024 7130 448 106 -683 C
ATOM 2413 CD2 PHE A 362 29.471 16.931 23.998 1.00 62.79 C
ANISOU 2413 CD2 PHE A 362 8188 8347 7321 472 179 -592 C
ATOM 2414 CE1 PHE A 362 30.517 19.263 25.071 1.00 62.28 C
ANISOU 2414 CE1 PHE A 362 8199 8210 7253 488 128 -719 C
ATOM 2415 CE2 PHE A 362 28.817 17.565 25.048 1.00 61.37 C
ANISOU 2415 CE2 PHE A 362 8023 8191 7102 511 203 -624 C
ATOM 2416 CZ PHE A 362 29.343 18.731 25.584 1.00 61.34 C
ANISOU 2416 CZ PHE A 362 8059 8152 7095 521 177 -689 C
ATOM 2417 N LEU A 363 32.245 15.958 19.396 1.00 35.62 N
ANISOU 2417 N LEU A 363 4720 4746 4067 338 76 -532 N
ATOM 2418 CA LEU A 363 33.374 15.571 18.555 1.00 32.43 C
ANISOU 2418 CA LEU A 363 4316 4311 3695 298 43 -522 C
ATOM 2419 C LEU A 363 33.193 16.099 17.131 1.00 32.75 C
ANISOU 2419 C LEU A 363 4352 4296 3798 296 43 -519 C
ATOM 2420 O LEU A 363 32.583 15.440 16.280 1.00 29.08 O
ANISOU 2420 O LEU A 363 3861 3844 3344 299 61 -483 O
ATOM 2421 CB LEU A 363 33.547 14.055 18.557 1.00 33.51 C
ANISOU 2421 CB LEU A 363 4432 4498 3804 280 48 -474 C
ATOM 2422 CG LEU A 363 33.490 13.407 19.947 1.00 42.10 C
ANISOU 2422 CG LEU A 363 5523 5647 4826 290 57 -462 C
ATOM 2423 CD1 LEU A 363 33.376 11.877 19.859 1.00 37.30 C
ANISOU 2423 CD1 LEU A 363 4890 5085 4196 277 73 -404 C
ATOM 2424 CD2 LEU A 363 34.689 13.825 20.809 1.00 38.29 C
ANISOU 2424 CD2 LEU A 363 5068 5156 4325 277 16 -499 C
ATOM 2425 N ASN A 364 33.706 17.303 16.884 1.00 21.21 N
ANISOU 2425 N ASN A 364 2913 2770 2375 291 23 -555 N
ATOM 2426 CA ASN A 364 33.570 17.922 15.574 1.00 23.39 C
ANISOU 2426 CA ASN A 364 3189 2987 2709 292 23 -549 C
ATOM 2427 C ASN A 364 34.931 18.312 15.008 1.00 26.22 C
ANISOU 2427 C ASN A 364 3564 3287 3113 251 -11 -561 C
ATOM 2428 O ASN A 364 35.702 19.027 15.645 1.00 28.75 O
ANISOU 2428 O ASN A 364 3903 3581 3439 235 -33 -596 O
ATOM 2429 CB ASN A 364 32.662 19.147 15.637 1.00 22.46 C
ANISOU 2429 CB ASN A 364 3084 2839 2610 331 41 -573 C
ATOM 2430 CG ASN A 364 31.440 18.913 16.477 1.00 28.37 C
ANISOU 2430 CG ASN A 364 3818 3647 3314 370 74 -570 C
ATOM 2431 OD1 ASN A 364 30.578 18.112 16.120 1.00 30.40 O
ANISOU 2431 OD1 ASN A 364 4043 3947 3560 384 98 -534 O
ATOM 2432 ND2 ASN A 364 31.354 19.608 17.610 1.00 26.11 N
ANISOU 2432 ND2 ASN A 364 3552 3366 3002 387 77 -610 N
ATOM 2433 N VAL A 365 35.223 17.818 13.813 1.00 22.38 N
ANISOU 2433 N VAL A 365 3065 2782 2657 232 -15 -530 N
ATOM 2434 CA VAL A 365 36.460 18.153 13.138 1.00 26.26 C
ANISOU 2434 CA VAL A 365 3565 3217 3197 193 -41 -532 C
ATOM 2435 C VAL A 365 36.135 18.975 11.907 1.00 26.45 C
ANISOU 2435 C VAL A 365 3596 3179 3275 199 -29 -512 C
ATOM 2436 O VAL A 365 35.254 18.638 11.134 1.00 29.96 O
ANISOU 2436 O VAL A 365 4025 3637 3721 217 -8 -471 O
ATOM 2437 CB VAL A 365 37.236 16.901 12.736 1.00 26.21 C
ANISOU 2437 CB VAL A 365 3533 3239 3188 153 -49 -487 C
ATOM 2438 CG1 VAL A 365 38.666 17.267 12.358 1.00 26.02 C
ANISOU 2438 CG1 VAL A 365 3511 3165 3208 109 -75 -494 C
ATOM 2439 CG2 VAL A 365 37.242 15.932 13.880 1.00 29.85 C
ANISOU 2439 CG2 VAL A 365 3985 3767 3588 156 -53 -491 C
ATOM 2440 N PHE A 366 36.868 20.056 11.732 1.00 24.91 N
ANISOU 2440 N PHE A 366 3423 2915 3127 184 -44 -539 N
ATOM 2441 CA PHE A 366 36.610 20.984 10.661 1.00 23.64 C
ANISOU 2441 CA PHE A 366 3276 2687 3018 194 -33 -521 C
ATOM 2442 C PHE A 366 37.897 21.220 9.869 1.00 26.69 C
ANISOU 2442 C PHE A 366 3663 3020 3458 143 -45 -500 C
ATOM 2443 O PHE A 366 38.988 21.217 10.427 1.00 25.40 O
ANISOU 2443 O PHE A 366 3497 2849 3304 107 -69 -528 O
ATOM 2444 CB PHE A 366 36.104 22.276 11.289 1.00 24.25 C
ANISOU 2444 CB PHE A 366 3378 2729 3105 221 -27 -558 C
ATOM 2445 CG PHE A 366 36.114 23.462 10.373 1.00 26.08 C
ANISOU 2445 CG PHE A 366 3631 2877 3400 226 -20 -546 C
ATOM 2446 CD1 PHE A 366 37.239 24.262 10.261 1.00 26.15 C
ANISOU 2446 CD1 PHE A 366 3657 2822 3459 184 -34 -556 C
ATOM 2447 CD2 PHE A 366 34.980 23.812 9.669 1.00 32.79 C
ANISOU 2447 CD2 PHE A 366 4485 3715 4259 273 1 -521 C
ATOM 2448 CE1 PHE A 366 37.237 25.367 9.430 1.00 28.61 C
ANISOU 2448 CE1 PHE A 366 3990 3052 3827 187 -23 -538 C
ATOM 2449 CE2 PHE A 366 34.975 24.923 8.847 1.00 34.13 C
ANISOU 2449 CE2 PHE A 366 4676 3806 4484 281 8 -503 C
ATOM 2450 CZ PHE A 366 36.100 25.696 8.729 1.00 31.42 C
ANISOU 2450 CZ PHE A 366 4353 3395 4191 238 -1 -511 C
ATOM 2451 N LYS A 367 37.760 21.440 8.570 1.00 26.15 N
ANISOU 2451 N LYS A 367 3595 2918 3424 143 -29 -449 N
ATOM 2452 CA LYS A 367 38.905 21.731 7.726 1.00 25.36 C
ANISOU 2452 CA LYS A 367 3495 2767 3375 99 -31 -422 C
ATOM 2453 C LYS A 367 38.450 22.398 6.444 1.00 28.78 C
ANISOU 2453 C LYS A 367 3944 3151 3842 118 -9 -375 C
ATOM 2454 O LYS A 367 37.343 22.140 5.961 1.00 29.73 O
ANISOU 2454 O LYS A 367 4061 3300 3936 157 5 -348 O
ATOM 2455 CB LYS A 367 39.650 20.448 7.367 1.00 26.51 C
ANISOU 2455 CB LYS A 367 3609 2961 3502 64 -32 -387 C
ATOM 2456 CG LYS A 367 41.076 20.695 6.972 1.00 30.75 C
ANISOU 2456 CG LYS A 367 4139 3458 4089 13 -38 -377 C
ATOM 2457 CD LYS A 367 41.594 19.716 5.956 1.00 26.69 C
ANISOU 2457 CD LYS A 367 3600 2970 3570 -7 -24 -321 C
ATOM 2458 CE LYS A 367 42.738 20.354 5.183 1.00 27.13 C
ANISOU 2458 CE LYS A 367 3653 2969 3686 -46 -15 -298 C
ATOM 2459 NZ LYS A 367 43.425 21.413 6.007 1.00 20.98 N
ANISOU 2459 NZ LYS A 367 2882 2136 2954 -73 -36 -348 N
ATOM 2460 N LEU A 368 39.302 23.253 5.891 1.00 25.11 N
ANISOU 2460 N LEU A 368 3492 2615 3435 88 -6 -363 N
ATOM 2461 CA LEU A 368 39.062 23.780 4.559 1.00 25.76 C
ANISOU 2461 CA LEU A 368 3588 2653 3545 101 17 -305 C
ATOM 2462 C LEU A 368 39.848 22.942 3.564 1.00 26.65 C
ANISOU 2462 C LEU A 368 3679 2792 3655 67 29 -250 C
ATOM 2463 O LEU A 368 41.080 22.996 3.543 1.00 25.72 O
ANISOU 2463 O LEU A 368 3550 2651 3571 19 28 -249 O
ATOM 2464 CB LEU A 368 39.492 25.243 4.477 1.00 27.29 C
ANISOU 2464 CB LEU A 368 3813 2748 3808 91 19 -316 C
ATOM 2465 CG LEU A 368 39.474 25.912 3.097 1.00 26.97 C
ANISOU 2465 CG LEU A 368 3791 2651 3805 98 45 -248 C
ATOM 2466 CD1 LEU A 368 38.071 25.940 2.522 1.00 17.15 C
ANISOU 2466 CD1 LEU A 368 2560 1429 2528 163 56 -218 C
ATOM 2467 CD2 LEU A 368 40.059 27.320 3.178 1.00 20.11 C
ANISOU 2467 CD2 LEU A 368 2950 1683 3008 77 45 -259 C
ATOM 2468 N PHE A 369 39.139 22.148 2.764 1.00 17.94 N
ANISOU 2468 N PHE A 369 2567 1738 2510 93 41 -208 N
ATOM 2469 CA PHE A 369 39.771 21.341 1.718 1.00 16.92 C
ANISOU 2469 CA PHE A 369 2423 1636 2371 71 55 -157 C
ATOM 2470 C PHE A 369 40.362 22.227 0.629 1.00 26.62 C
ANISOU 2470 C PHE A 369 3670 2801 3644 58 78 -109 C
ATOM 2471 O PHE A 369 39.889 23.340 0.392 1.00 32.86 O
ANISOU 2471 O PHE A 369 4488 3534 4462 83 85 -100 O
ATOM 2472 CB PHE A 369 38.759 20.384 1.071 1.00 13.31 C
ANISOU 2472 CB PHE A 369 1956 1241 1859 105 57 -130 C
ATOM 2473 CG PHE A 369 38.437 19.163 1.899 1.00 22.45 C
ANISOU 2473 CG PHE A 369 3088 2467 2975 103 42 -159 C
ATOM 2474 CD1 PHE A 369 39.292 18.734 2.897 1.00 23.87 C
ANISOU 2474 CD1 PHE A 369 3252 2660 3157 69 29 -193 C
ATOM 2475 CD2 PHE A 369 37.278 18.430 1.657 1.00 21.05 C
ANISOU 2475 CD2 PHE A 369 2901 2342 2757 135 39 -149 C
ATOM 2476 CE1 PHE A 369 38.993 17.596 3.655 1.00 23.45 C
ANISOU 2476 CE1 PHE A 369 3178 2668 3064 70 17 -212 C
ATOM 2477 CE2 PHE A 369 36.978 17.303 2.395 1.00 21.39 C
ANISOU 2477 CE2 PHE A 369 2919 2442 2766 130 28 -169 C
ATOM 2478 CZ PHE A 369 37.837 16.881 3.402 1.00 24.19 C
ANISOU 2478 CZ PHE A 369 3262 2807 3121 99 20 -198 C
ATOM 2479 N GLY A 370 41.394 21.732 -0.044 1.00 27.70 N
ANISOU 2479 N GLY A 370 3791 2948 3788 24 94 -76 N
ATOM 2480 CA GLY A 370 41.937 22.425 -1.202 1.00 17.24 C
ANISOU 2480 CA GLY A 370 2481 1574 2495 14 124 -19 C
ATOM 2481 C GLY A 370 41.394 21.865 -2.509 1.00 20.90 C
ANISOU 2481 C GLY A 370 2953 2078 2911 47 142 37 C
ATOM 2482 O GLY A 370 40.340 21.225 -2.542 1.00 24.08 O
ANISOU 2482 O GLY A 370 3355 2531 3263 84 127 29 O
ATOM 2483 N PRO A 371 42.115 22.110 -3.609 1.00 22.69 N
ANISOU 2483 N PRO A 371 3186 2283 3151 34 174 94 N
ATOM 2484 CA PRO A 371 41.704 21.644 -4.940 1.00 21.30 C
ANISOU 2484 CA PRO A 371 3023 2145 2924 66 192 147 C
ATOM 2485 C PRO A 371 41.456 20.137 -4.980 1.00 22.06 C
ANISOU 2485 C PRO A 371 3097 2325 2961 74 177 128 C
ATOM 2486 O PRO A 371 42.148 19.386 -4.297 1.00 23.11 O
ANISOU 2486 O PRO A 371 3201 2482 3100 41 169 96 O
ATOM 2487 CB PRO A 371 42.905 22.018 -5.820 1.00 23.60 C
ANISOU 2487 CB PRO A 371 3315 2406 3245 36 234 201 C
ATOM 2488 CG PRO A 371 43.505 23.237 -5.113 1.00 20.96 C
ANISOU 2488 CG PRO A 371 2984 1989 2992 0 237 188 C
ATOM 2489 CD PRO A 371 43.354 22.914 -3.653 1.00 24.63 C
ANISOU 2489 CD PRO A 371 3427 2466 3464 -14 197 111 C
ATOM 2490 N ARG A 372 40.466 19.718 -5.764 1.00 19.69 N
ANISOU 2490 N ARG A 372 2810 2065 2607 117 170 148 N
ATOM 2491 CA ARG A 372 40.137 18.310 -5.922 1.00 21.43 C
ANISOU 2491 CA ARG A 372 3012 2356 2774 125 154 130 C
ATOM 2492 C ARG A 372 41.040 17.658 -6.960 1.00 26.32 C
ANISOU 2492 C ARG A 372 3631 3001 3371 114 182 164 C
ATOM 2493 O ARG A 372 41.814 18.344 -7.641 1.00 25.57 O
ANISOU 2493 O ARG A 372 3548 2872 3295 104 216 207 O
ATOM 2494 CB ARG A 372 38.670 18.144 -6.334 1.00 19.26 C
ANISOU 2494 CB ARG A 372 2749 2115 2456 174 131 132 C
ATOM 2495 CG ARG A 372 38.302 18.807 -7.667 1.00 23.86 C
ANISOU 2495 CG ARG A 372 3363 2687 3015 213 144 189 C
ATOM 2496 CD ARG A 372 37.019 18.217 -8.254 1.00 27.85 C
ANISOU 2496 CD ARG A 372 3869 3247 3465 257 115 188 C
ATOM 2497 NE ARG A 372 37.208 16.789 -8.508 1.00 35.36 N
ANISOU 2497 NE ARG A 372 4802 4255 4377 243 106 167 N
ATOM 2498 CZ ARG A 372 36.280 15.848 -8.366 1.00 29.48 C
ANISOU 2498 CZ ARG A 372 4038 3560 3602 255 73 136 C
ATOM 2499 NH1 ARG A 372 35.048 16.163 -7.982 1.00 21.37 N
ANISOU 2499 NH1 ARG A 372 3002 2540 2577 283 47 122 N
ATOM 2500 NH2 ARG A 372 36.596 14.580 -8.611 1.00 27.37 N
ANISOU 2500 NH2 ARG A 372 3759 3332 3307 238 68 118 N
ATOM 2501 N ASN A 373 40.942 16.333 -7.069 1.00 22.05 N
ANISOU 2501 N ASN A 373 3073 2515 2789 116 169 143 N
ATOM 2502 CA ASN A 373 41.684 15.582 -8.084 1.00 21.93 C
ANISOU 2502 CA ASN A 373 3059 2531 2743 114 193 167 C
ATOM 2503 C ASN A 373 40.738 15.056 -9.160 1.00 19.53 C
ANISOU 2503 C ASN A 373 2775 2270 2374 157 181 179 C
ATOM 2504 O ASN A 373 39.570 15.420 -9.187 1.00 20.06 O
ANISOU 2504 O ASN A 373 2855 2341 2427 186 155 178 O
ATOM 2505 CB ASN A 373 42.539 14.462 -7.463 1.00 17.88 C
ANISOU 2505 CB ASN A 373 2513 2041 2239 82 191 134 C
ATOM 2506 CG ASN A 373 41.697 13.353 -6.816 1.00 15.82 C
ANISOU 2506 CG ASN A 373 2238 1818 1953 89 153 90 C
ATOM 2507 OD1 ASN A 373 40.582 13.059 -7.240 1.00 13.76 O
ANISOU 2507 OD1 ASN A 373 1990 1583 1655 118 133 86 O
ATOM 2508 ND2 ASN A 373 42.243 12.736 -5.795 1.00 9.53 N
ANISOU 2508 ND2 ASN A 373 1415 1027 1180 61 144 59 N
ATOM 2509 N GLN A 374 41.228 14.190 -10.036 1.00 23.01 N
ANISOU 2509 N GLN A 374 3220 2747 2776 162 196 188 N
ATOM 2510 CA GLN A 374 40.446 13.815 -11.209 1.00 24.01 C
ANISOU 2510 CA GLN A 374 3371 2914 2837 204 184 201 C
ATOM 2511 C GLN A 374 39.593 12.544 -11.099 1.00 22.50 C
ANISOU 2511 C GLN A 374 3168 2769 2612 213 142 154 C
ATOM 2512 O GLN A 374 38.927 12.178 -12.065 1.00 27.89 O
ANISOU 2512 O GLN A 374 3870 3487 3241 245 125 157 O
ATOM 2513 CB GLN A 374 41.324 13.800 -12.475 1.00 29.11 C
ANISOU 2513 CB GLN A 374 4039 3574 3449 216 227 243 C
ATOM 2514 CG GLN A 374 42.569 12.949 -12.381 1.00 40.00 C
ANISOU 2514 CG GLN A 374 5396 4964 4839 188 255 230 C
ATOM 2515 CD GLN A 374 43.662 13.365 -13.375 1.00 42.30 C
ANISOU 2515 CD GLN A 374 5699 5252 5119 191 313 282 C
ATOM 2516 OE1 GLN A 374 43.518 13.205 -14.591 1.00 40.66 O
ANISOU 2516 OE1 GLN A 374 5522 5078 4848 227 328 307 O
ATOM 2517 NE2 GLN A 374 44.767 13.889 -12.849 1.00 30.74 N
ANISOU 2517 NE2 GLN A 374 4210 3752 3716 153 347 298 N
ATOM 2518 N ALA A 375 39.600 11.886 -9.938 1.00 22.22 N
ANISOU 2518 N ALA A 375 3103 2732 2608 184 124 112 N
ATOM 2519 CA ALA A 375 38.743 10.707 -9.709 1.00 18.69 C
ANISOU 2519 CA ALA A 375 2641 2319 2140 187 86 71 C
ATOM 2520 C ALA A 375 37.283 11.120 -9.642 1.00 20.36 C
ANISOU 2520 C ALA A 375 2853 2541 2343 212 51 67 C
ATOM 2521 O ALA A 375 36.910 11.919 -8.776 1.00 23.23 O
ANISOU 2521 O ALA A 375 3206 2880 2740 208 47 66 O
ATOM 2522 CB ALA A 375 39.133 9.991 -8.403 1.00 6.56 C
ANISOU 2522 CB ALA A 375 1074 777 643 151 80 37 C
ATOM 2523 N PRO A 376 36.453 10.579 -10.550 1.00 21.13 N
ANISOU 2523 N PRO A 376 2959 2676 2394 238 24 60 N
ATOM 2524 CA PRO A 376 35.034 10.937 -10.624 1.00 16.76 C
ANISOU 2524 CA PRO A 376 2399 2139 1830 266 -12 57 C
ATOM 2525 C PRO A 376 34.362 10.855 -9.268 1.00 14.80 C
ANISOU 2525 C PRO A 376 2116 1884 1623 247 -29 30 C
ATOM 2526 O PRO A 376 33.586 11.753 -8.956 1.00 15.78 O
ANISOU 2526 O PRO A 376 2235 1999 1761 268 -37 39 O
ATOM 2527 CB PRO A 376 34.447 9.865 -11.549 1.00 18.83 C
ANISOU 2527 CB PRO A 376 2664 2447 2044 280 -45 35 C
ATOM 2528 CG PRO A 376 35.559 9.481 -12.420 1.00 20.27 C
ANISOU 2528 CG PRO A 376 2874 2633 2195 281 -17 45 C
ATOM 2529 CD PRO A 376 36.817 9.593 -11.579 1.00 24.18 C
ANISOU 2529 CD PRO A 376 3360 3093 2735 246 24 51 C
ATOM 2530 N LEU A 377 34.654 9.821 -8.476 1.00 15.23 N
ANISOU 2530 N LEU A 377 2147 1942 1696 213 -31 -2 N
ATOM 2531 CA LEU A 377 33.950 9.633 -7.199 1.00 18.28 C
ANISOU 2531 CA LEU A 377 2501 2330 2115 197 -45 -25 C
ATOM 2532 C LEU A 377 34.717 10.072 -5.974 1.00 13.95 C
ANISOU 2532 C LEU A 377 1947 1751 1604 174 -20 -28 C
ATOM 2533 O LEU A 377 34.344 9.702 -4.861 1.00 16.48 O
ANISOU 2533 O LEU A 377 2242 2076 1942 158 -27 -48 O
ATOM 2534 CB LEU A 377 33.577 8.178 -6.957 1.00 16.48 C
ANISOU 2534 CB LEU A 377 2249 2127 1885 175 -66 -56 C
ATOM 2535 CG LEU A 377 32.309 7.544 -7.471 1.00 22.12 C
ANISOU 2535 CG LEU A 377 2945 2876 2583 186 -104 -72 C
ATOM 2536 CD1 LEU A 377 31.922 6.490 -6.443 1.00 21.20 C
ANISOU 2536 CD1 LEU A 377 2795 2766 2495 153 -113 -97 C
ATOM 2537 CD2 LEU A 377 31.234 8.569 -7.686 1.00 16.96 C
ANISOU 2537 CD2 LEU A 377 2285 2234 1925 221 -120 -58 C
ATOM 2538 N SER A 378 35.795 10.816 -6.165 1.00 16.72 N
ANISOU 2538 N SER A 378 2319 2071 1964 170 7 -7 N
ATOM 2539 CA SER A 378 36.532 11.356 -5.030 1.00 20.33 C
ANISOU 2539 CA SER A 378 2770 2497 2458 147 24 -13 C
ATOM 2540 C SER A 378 35.634 12.233 -4.131 1.00 15.93 C
ANISOU 2540 C SER A 378 2204 1928 1919 161 15 -24 C
ATOM 2541 O SER A 378 34.890 13.077 -4.619 1.00 19.97 O
ANISOU 2541 O SER A 378 2728 2434 2427 193 11 -8 O
ATOM 2542 CB SER A 378 37.742 12.155 -5.526 1.00 17.66 C
ANISOU 2542 CB SER A 378 2452 2124 2133 140 54 14 C
ATOM 2543 OG SER A 378 38.571 12.548 -4.444 1.00 17.04 O
ANISOU 2543 OG SER A 378 2364 2018 2093 112 65 2 O
ATOM 2544 N PHE A 379 35.694 12.022 -2.823 1.00 12.36 N
ANISOU 2544 N PHE A 379 1734 1476 1485 142 13 -49 N
ATOM 2545 CA PHE A 379 34.912 12.849 -1.893 1.00 13.01 C
ANISOU 2545 CA PHE A 379 1810 1550 1582 158 10 -64 C
ATOM 2546 C PHE A 379 35.333 14.337 -1.785 1.00 15.49 C
ANISOU 2546 C PHE A 379 2148 1814 1923 167 23 -57 C
ATOM 2547 O PHE A 379 34.485 15.214 -1.902 1.00 15.19 O
ANISOU 2547 O PHE A 379 2118 1764 1889 200 20 -53 O
ATOM 2548 CB PHE A 379 34.803 12.187 -0.504 1.00 12.98 C
ANISOU 2548 CB PHE A 379 1784 1567 1582 139 5 -93 C
ATOM 2549 CG PHE A 379 34.375 13.133 0.602 1.00 16.07 C
ANISOU 2549 CG PHE A 379 2174 1945 1986 154 9 -114 C
ATOM 2550 CD1 PHE A 379 33.064 13.620 0.662 1.00 17.96 C
ANISOU 2550 CD1 PHE A 379 2405 2197 2222 189 4 -117 C
ATOM 2551 CD2 PHE A 379 35.279 13.523 1.596 1.00 13.49 C
ANISOU 2551 CD2 PHE A 379 1855 1597 1675 134 14 -134 C
ATOM 2552 CE1 PHE A 379 32.666 14.500 1.683 1.00 18.21 C
ANISOU 2552 CE1 PHE A 379 2438 2216 2264 208 10 -141 C
ATOM 2553 CE2 PHE A 379 34.892 14.406 2.628 1.00 11.07 C
ANISOU 2553 CE2 PHE A 379 1553 1278 1376 150 16 -161 C
ATOM 2554 CZ PHE A 379 33.584 14.890 2.667 1.00 15.66 C
ANISOU 2554 CZ PHE A 379 2129 1870 1952 189 16 -165 C
ATOM 2555 N PRO A 380 36.629 14.625 -1.551 1.00 15.63 N
ANISOU 2555 N PRO A 380 2175 1800 1963 139 37 -58 N
ATOM 2556 CA PRO A 380 36.986 16.038 -1.330 1.00 17.49 C
ANISOU 2556 CA PRO A 380 2432 1982 2233 142 48 -56 C
ATOM 2557 C PRO A 380 36.768 16.962 -2.519 1.00 18.43 C
ANISOU 2557 C PRO A 380 2576 2070 2356 168 59 -17 C
ATOM 2558 O PRO A 380 37.052 16.618 -3.662 1.00 18.00 O
ANISOU 2558 O PRO A 380 2529 2027 2282 170 68 17 O
ATOM 2559 CB PRO A 380 38.481 15.970 -0.980 1.00 19.25 C
ANISOU 2559 CB PRO A 380 2650 2183 2481 99 58 -62 C
ATOM 2560 CG PRO A 380 38.635 14.577 -0.344 1.00 17.75 C
ANISOU 2560 CG PRO A 380 2434 2041 2269 81 46 -83 C
ATOM 2561 CD PRO A 380 37.754 13.723 -1.224 1.00 16.77 C
ANISOU 2561 CD PRO A 380 2306 1955 2109 102 41 -66 C
ATOM 2562 N ILE A 381 36.225 18.133 -2.224 1.00 20.47 N
ANISOU 2562 N ILE A 381 2850 2290 2637 193 59 -20 N
ATOM 2563 CA ILE A 381 36.194 19.248 -3.155 1.00 23.89 C
ANISOU 2563 CA ILE A 381 3314 2678 3087 216 72 20 C
ATOM 2564 C ILE A 381 36.618 20.456 -2.343 1.00 20.85 C
ANISOU 2564 C ILE A 381 2943 2226 2753 206 79 0 C
ATOM 2565 O ILE A 381 36.509 20.437 -1.123 1.00 21.85 O
ANISOU 2565 O ILE A 381 3059 2355 2889 198 68 -48 O
ATOM 2566 CB ILE A 381 34.796 19.469 -3.761 1.00 22.27 C
ANISOU 2566 CB ILE A 381 3113 2493 2856 271 59 37 C
ATOM 2567 CG1 ILE A 381 33.783 19.822 -2.672 1.00 20.82 C
ANISOU 2567 CG1 ILE A 381 2916 2312 2683 297 45 -2 C
ATOM 2568 CG2 ILE A 381 34.364 18.244 -4.565 1.00 12.39 C
ANISOU 2568 CG2 ILE A 381 1845 1308 1556 277 45 49 C
ATOM 2569 CD1 ILE A 381 32.389 20.135 -3.209 1.00 19.14 C
ANISOU 2569 CD1 ILE A 381 2701 2118 2453 354 31 15 C
ATOM 2570 N PRO A 382 37.150 21.491 -2.999 1.00 18.81 N
ANISOU 2570 N PRO A 382 2712 1906 2527 205 98 36 N
ATOM 2571 CA PRO A 382 37.578 22.638 -2.196 1.00 22.81 C
ANISOU 2571 CA PRO A 382 3234 2341 3091 191 102 11 C
ATOM 2572 C PRO A 382 36.384 23.217 -1.457 1.00 21.44 C
ANISOU 2572 C PRO A 382 3068 2159 2919 235 86 -23 C
ATOM 2573 O PRO A 382 35.328 23.402 -2.051 1.00 21.81 O
ANISOU 2573 O PRO A 382 3123 2219 2947 285 83 1 O
ATOM 2574 CB PRO A 382 38.125 23.630 -3.245 1.00 22.73 C
ANISOU 2574 CB PRO A 382 3254 2267 3116 189 128 69 C
ATOM 2575 CG PRO A 382 37.613 23.137 -4.567 1.00 19.92 C
ANISOU 2575 CG PRO A 382 2904 1956 2710 222 135 124 C
ATOM 2576 CD PRO A 382 37.465 21.655 -4.427 1.00 19.93 C
ANISOU 2576 CD PRO A 382 2874 2040 2660 213 119 100 C
ATOM 2577 N GLY A 383 36.534 23.468 -0.165 1.00 20.41 N
ANISOU 2577 N GLY A 383 2933 2013 2810 221 75 -81 N
ATOM 2578 CA GLY A 383 35.403 23.921 0.605 1.00 18.66 C
ANISOU 2578 CA GLY A 383 2716 1792 2584 267 65 -119 C
ATOM 2579 C GLY A 383 35.398 23.543 2.070 1.00 30.04 C
ANISOU 2579 C GLY A 383 4140 3262 4012 255 51 -186 C
ATOM 2580 O GLY A 383 36.384 23.027 2.626 1.00 25.28 O
ANISOU 2580 O GLY A 383 3525 2671 3410 208 45 -208 O
ATOM 2581 N TRP A 384 34.254 23.808 2.692 1.00 28.21 N
ANISOU 2581 N TRP A 384 3907 3046 3767 303 47 -215 N
ATOM 2582 CA TRP A 384 34.107 23.716 4.134 1.00 26.45 C
ANISOU 2582 CA TRP A 384 3677 2844 3530 304 38 -280 C
ATOM 2583 C TRP A 384 33.736 22.306 4.574 1.00 22.22 C
ANISOU 2583 C TRP A 384 3104 2399 2940 297 34 -285 C
ATOM 2584 O TRP A 384 32.628 21.843 4.345 1.00 23.90 O
ANISOU 2584 O TRP A 384 3295 2660 3125 332 38 -269 O
ATOM 2585 CB TRP A 384 33.083 24.753 4.587 1.00 24.86 C
ANISOU 2585 CB TRP A 384 3493 2611 3341 363 42 -309 C
ATOM 2586 CG TRP A 384 33.408 26.085 3.985 1.00 30.47 C
ANISOU 2586 CG TRP A 384 4242 3225 4110 372 47 -293 C
ATOM 2587 CD1 TRP A 384 32.799 26.674 2.920 1.00 25.85 C
ANISOU 2587 CD1 TRP A 384 3671 2608 3541 412 56 -242 C
ATOM 2588 CD2 TRP A 384 34.468 26.963 4.378 1.00 30.09 C
ANISOU 2588 CD2 TRP A 384 4222 3099 4113 334 44 -322 C
ATOM 2589 NE1 TRP A 384 33.397 27.876 2.641 1.00 28.58 N
ANISOU 2589 NE1 TRP A 384 4048 2863 3947 399 62 -233 N
ATOM 2590 CE2 TRP A 384 34.426 28.076 3.519 1.00 26.54 C
ANISOU 2590 CE2 TRP A 384 3794 2576 3715 347 55 -282 C
ATOM 2591 CE3 TRP A 384 35.441 26.921 5.384 1.00 32.79 C
ANISOU 2591 CE3 TRP A 384 4560 3437 4462 284 32 -373 C
ATOM 2592 CZ2 TRP A 384 35.318 29.139 3.631 1.00 31.80 C
ANISOU 2592 CZ2 TRP A 384 4476 3161 4447 310 58 -293 C
ATOM 2593 CZ3 TRP A 384 36.326 27.978 5.499 1.00 33.37 C
ANISOU 2593 CZ3 TRP A 384 4655 3434 4589 247 36 -384 C
ATOM 2594 CH2 TRP A 384 36.262 29.073 4.624 1.00 31.37 C
ANISOU 2594 CH2 TRP A 384 4427 3103 4389 259 54 -343 C
ATOM 2595 N ASN A 385 34.685 21.622 5.194 1.00 21.61 N
ANISOU 2595 N ASN A 385 3016 2343 2851 251 26 -304 N
ATOM 2596 CA ASN A 385 34.483 20.234 5.562 1.00 23.33 C
ANISOU 2596 CA ASN A 385 3202 2640 3023 239 23 -302 C
ATOM 2597 C ASN A 385 34.301 20.045 7.061 1.00 23.63 C
ANISOU 2597 C ASN A 385 3235 2712 3032 245 19 -353 C
ATOM 2598 O ASN A 385 35.078 20.559 7.869 1.00 18.43 O
ANISOU 2598 O ASN A 385 2594 2026 2385 228 8 -395 O
ATOM 2599 CB ASN A 385 35.656 19.375 5.078 1.00 24.82 C
ANISOU 2599 CB ASN A 385 3379 2837 3212 188 18 -276 C
ATOM 2600 CG ASN A 385 35.611 17.964 5.650 1.00 25.97 C
ANISOU 2600 CG ASN A 385 3497 3054 3317 173 14 -278 C
ATOM 2601 OD1 ASN A 385 36.209 17.689 6.684 1.00 36.57 O
ANISOU 2601 OD1 ASN A 385 4836 4411 4648 153 4 -309 O
ATOM 2602 ND2 ASN A 385 34.880 17.078 4.994 1.00 11.37 N
ANISOU 2602 ND2 ASN A 385 1628 1246 1446 183 18 -246 N
ATOM 2603 N ILE A 386 33.291 19.278 7.440 1.00 20.51 N
ANISOU 2603 N ILE A 386 2814 2380 2598 269 27 -351 N
ATOM 2604 CA ILE A 386 33.119 18.985 8.848 1.00 20.99 C
ANISOU 2604 CA ILE A 386 2870 2483 2623 276 28 -392 C
ATOM 2605 C ILE A 386 32.555 17.597 9.111 1.00 21.99 C
ANISOU 2605 C ILE A 386 2961 2685 2709 271 36 -368 C
ATOM 2606 O ILE A 386 31.623 17.141 8.443 1.00 22.81 O
ANISOU 2606 O ILE A 386 3040 2815 2810 287 46 -336 O
ATOM 2607 CB ILE A 386 32.274 20.072 9.585 1.00 26.71 C
ANISOU 2607 CB ILE A 386 3610 3192 3345 328 38 -436 C
ATOM 2608 CG1 ILE A 386 32.307 19.840 11.101 1.00 36.71 C
ANISOU 2608 CG1 ILE A 386 4879 4502 4568 334 39 -483 C
ATOM 2609 CG2 ILE A 386 30.849 20.065 9.104 1.00 24.32 C
ANISOU 2609 CG2 ILE A 386 3286 2916 3040 374 56 -411 C
ATOM 2610 CD1 ILE A 386 31.939 21.062 11.938 1.00 43.52 C
ANISOU 2610 CD1 ILE A 386 5764 5338 5434 363 45 -527 C
ATOM 2611 N CYS A 387 33.133 16.926 10.098 1.00 20.87 N
ANISOU 2611 N CYS A 387 2816 2577 2536 249 30 -385 N
ATOM 2612 CA CYS A 387 32.556 15.697 10.591 1.00 20.39 C
ANISOU 2612 CA CYS A 387 2726 2583 2437 247 42 -365 C
ATOM 2613 C CYS A 387 32.001 15.960 11.985 1.00 20.67 C
ANISOU 2613 C CYS A 387 2766 2655 2432 280 56 -403 C
ATOM 2614 O CYS A 387 32.686 16.514 12.835 1.00 20.29 O
ANISOU 2614 O CYS A 387 2743 2593 2371 279 44 -446 O
ATOM 2615 CB CYS A 387 33.585 14.556 10.598 1.00 21.72 C
ANISOU 2615 CB CYS A 387 2887 2768 2597 202 29 -343 C
ATOM 2616 SG CYS A 387 32.944 12.948 11.244 1.00 34.74 S
ANISOU 2616 SG CYS A 387 4504 4493 4205 196 45 -312 S
ATOM 2617 N VAL A 388 30.741 15.594 12.195 1.00 21.06 N
ANISOU 2617 N VAL A 388 2787 2751 2462 308 82 -389 N
ATOM 2618 CA VAL A 388 30.125 15.681 13.507 1.00 18.00 C
ANISOU 2618 CA VAL A 388 2400 2411 2030 342 104 -417 C
ATOM 2619 C VAL A 388 29.673 14.289 13.942 1.00 23.49 C
ANISOU 2619 C VAL A 388 3061 3173 2693 327 123 -378 C
ATOM 2620 O VAL A 388 29.645 13.350 13.134 1.00 20.31 O
ANISOU 2620 O VAL A 388 2633 2774 2310 296 118 -333 O
ATOM 2621 CB VAL A 388 28.905 16.639 13.509 1.00 31.15 C
ANISOU 2621 CB VAL A 388 4059 4074 3704 398 126 -437 C
ATOM 2622 CG1 VAL A 388 29.322 18.058 13.115 1.00 28.78 C
ANISOU 2622 CG1 VAL A 388 3795 3697 3442 411 109 -470 C
ATOM 2623 CG2 VAL A 388 27.832 16.120 12.579 1.00 24.22 C
ANISOU 2623 CG2 VAL A 388 3137 3218 2849 404 140 -390 C
ATOM 2624 N ASP A 389 29.309 14.158 15.214 1.00 24.77 N
ANISOU 2624 N ASP A 389 3223 3385 2804 350 145 -394 N
ATOM 2625 CA ASP A 389 28.926 12.862 15.764 1.00 23.98 C
ANISOU 2625 CA ASP A 389 3093 3346 2671 336 168 -353 C
ATOM 2626 C ASP A 389 27.722 12.985 16.702 1.00 25.15 C
ANISOU 2626 C ASP A 389 3222 3549 2784 378 211 -356 C
ATOM 2627 O ASP A 389 27.869 13.360 17.862 1.00 24.00 O
ANISOU 2627 O ASP A 389 3100 3415 2603 389 215 -377 O
ATOM 2628 CB ASP A 389 30.129 12.250 16.489 1.00 26.36 C
ANISOU 2628 CB ASP A 389 3419 3658 2938 308 147 -353 C
ATOM 2629 CG ASP A 389 29.984 10.753 16.730 1.00 28.70 C
ANISOU 2629 CG ASP A 389 3689 3998 3217 281 163 -297 C
ATOM 2630 OD1 ASP A 389 29.145 10.097 16.073 1.00 27.42 O
ANISOU 2630 OD1 ASP A 389 3489 3845 3083 270 181 -256 O
ATOM 2631 OD2 ASP A 389 30.742 10.234 17.580 1.00 33.13 O
ANISOU 2631 OD2 ASP A 389 4268 4583 3738 271 154 -293 O
ATOM 2632 N PHE A 390 26.534 12.674 16.188 1.00 26.56 N
ANISOU 2632 N PHE A 390 3354 3753 2984 390 238 -327 N
ATOM 2633 CA PHE A 390 25.295 12.804 16.957 1.00 31.89 C
ANISOU 2633 CA PHE A 390 4002 4473 3643 422 279 -320 C
ATOM 2634 C PHE A 390 25.025 11.603 17.851 1.00 35.47 C
ANISOU 2634 C PHE A 390 4433 4987 4058 404 310 -277 C
ATOM 2635 O PHE A 390 25.176 10.459 17.426 1.00 39.08 O
ANISOU 2635 O PHE A 390 4866 5461 4522 371 312 -236 O
ATOM 2636 CB PHE A 390 24.082 12.980 16.035 1.00 25.38 C
ANISOU 2636 CB PHE A 390 3128 3654 2862 444 294 -304 C
ATOM 2637 CG PHE A 390 24.204 14.122 15.082 1.00 26.86 C
ANISOU 2637 CG PHE A 390 3335 3783 3090 466 267 -335 C
ATOM 2638 CD1 PHE A 390 24.247 15.424 15.544 1.00 27.82 C
ANISOU 2638 CD1 PHE A 390 3492 3867 3210 497 262 -377 C
ATOM 2639 CD2 PHE A 390 24.259 13.899 13.719 1.00 31.30 C
ANISOU 2639 CD2 PHE A 390 3881 4312 3698 443 240 -311 C
ATOM 2640 CE1 PHE A 390 24.355 16.483 14.665 1.00 27.16 C
ANISOU 2640 CE1 PHE A 390 3428 3723 3168 517 239 -398 C
ATOM 2641 CE2 PHE A 390 24.363 14.953 12.836 1.00 30.14 C
ANISOU 2641 CE2 PHE A 390 3755 4110 3587 464 216 -330 C
ATOM 2642 CZ PHE A 390 24.407 16.246 13.311 1.00 28.84 C
ANISOU 2642 CZ PHE A 390 3625 3915 3416 509 220 -377 C
ATOM 2643 N PRO A 391 24.610 11.863 19.095 1.00 30.16 N
ANISOU 2643 N PRO A 391 3769 4344 3347 427 336 -285 N
ATOM 2644 CA PRO A 391 24.010 10.811 19.920 1.00 29.51 C
ANISOU 2644 CA PRO A 391 3658 4320 3236 417 377 -236 C
ATOM 2645 C PRO A 391 22.734 10.330 19.238 1.00 32.34 C
ANISOU 2645 C PRO A 391 3948 4703 3636 415 408 -198 C
ATOM 2646 O PRO A 391 21.968 11.156 18.742 1.00 38.53 O
ANISOU 2646 O PRO A 391 4713 5476 4452 444 411 -219 O
ATOM 2647 CB PRO A 391 23.655 11.542 21.215 1.00 21.86 C
ANISOU 2647 CB PRO A 391 2711 3372 2223 454 398 -264 C
ATOM 2648 CG PRO A 391 24.562 12.724 21.251 1.00 29.67 C
ANISOU 2648 CG PRO A 391 3754 4311 3208 468 358 -327 C
ATOM 2649 CD PRO A 391 24.762 13.132 19.821 1.00 25.57 C
ANISOU 2649 CD PRO A 391 3229 3741 2747 460 329 -338 C
ATOM 2650 N ILE A 392 22.504 9.025 19.195 1.00 28.88 N
ANISOU 2650 N ILE A 392 3474 4295 3204 379 427 -141 N
ATOM 2651 CA ILE A 392 21.292 8.530 18.568 1.00 36.18 C
ANISOU 2651 CA ILE A 392 4329 5243 4177 369 453 -105 C
ATOM 2652 C ILE A 392 20.087 8.824 19.458 1.00 37.26 C
ANISOU 2652 C ILE A 392 4437 5417 4303 398 499 -98 C
ATOM 2653 O ILE A 392 20.066 8.465 20.629 1.00 39.02 O
ANISOU 2653 O ILE A 392 4674 5670 4481 399 528 -81 O
ATOM 2654 CB ILE A 392 21.404 7.040 18.196 1.00 39.92 C
ANISOU 2654 CB ILE A 392 4769 5728 4671 314 458 -46 C
ATOM 2655 CG1 ILE A 392 22.441 6.879 17.086 1.00 37.62 C
ANISOU 2655 CG1 ILE A 392 4504 5380 4410 282 402 -57 C
ATOM 2656 CG2 ILE A 392 20.049 6.490 17.734 1.00 36.61 C
ANISOU 2656 CG2 ILE A 392 4270 5333 4306 298 484 -8 C
ATOM 2657 CD1 ILE A 392 22.687 5.456 16.690 1.00 43.47 C
ANISOU 2657 CD1 ILE A 392 5229 6105 5183 221 391 -6 C
ATOM 2658 N LYS A 393 19.107 9.521 18.888 1.00 40.66 N
ANISOU 2658 N LYS A 393 4829 5847 4773 426 504 -114 N
ATOM 2659 CA LYS A 393 17.945 10.004 19.617 1.00 43.70 C
ANISOU 2659 CA LYS A 393 5187 6265 5153 462 546 -117 C
ATOM 2660 C LYS A 393 16.742 10.023 18.698 1.00 44.03 C
ANISOU 2660 C LYS A 393 5155 6316 5257 465 552 -101 C
ATOM 2661 O LYS A 393 16.891 10.023 17.470 1.00 36.66 O
ANISOU 2661 O LYS A 393 4205 5356 4367 453 515 -104 O
ATOM 2662 CB LYS A 393 18.171 11.437 20.094 1.00 45.53 C
ANISOU 2662 CB LYS A 393 5470 6475 5355 514 537 -178 C
ATOM 2663 CG LYS A 393 18.956 11.586 21.369 1.00 53.45 C
ANISOU 2663 CG LYS A 393 6535 7485 6291 522 542 -198 C
ATOM 2664 CD LYS A 393 18.597 12.893 22.065 1.00 63.27 C
ANISOU 2664 CD LYS A 393 7804 8724 7511 577 554 -250 C
ATOM 2665 CE LYS A 393 18.295 14.022 21.073 1.00 66.51 C
ANISOU 2665 CE LYS A 393 8210 9090 7971 607 530 -286 C
ATOM 2666 NZ LYS A 393 16.833 14.211 20.809 1.00 65.73 N
ANISOU 2666 NZ LYS A 393 8046 9018 7910 634 564 -271 N
ATOM 2667 N ASP A 394 15.553 10.067 19.293 1.00 45.61 N
ANISOU 2667 N ASP A 394 5310 6555 5463 484 597 -87 N
ATOM 2668 CA ASP A 394 14.323 10.160 18.521 1.00 47.76 C
ANISOU 2668 CA ASP A 394 5509 6840 5797 491 601 -75 C
ATOM 2669 C ASP A 394 14.375 11.382 17.619 1.00 41.41 C
ANISOU 2669 C ASP A 394 4720 5997 5017 533 562 -120 C
ATOM 2670 O ASP A 394 14.748 12.473 18.052 1.00 42.36 O
ANISOU 2670 O ASP A 394 4895 6095 5106 576 558 -165 O
ATOM 2671 CB ASP A 394 13.093 10.203 19.435 1.00 57.07 C
ANISOU 2671 CB ASP A 394 6644 8066 6974 512 658 -61 C
ATOM 2672 CG ASP A 394 12.829 8.869 20.126 1.00 63.75 C
ANISOU 2672 CG ASP A 394 7459 8948 7814 464 698 -4 C
ATOM 2673 OD1 ASP A 394 13.234 7.810 19.593 1.00 61.93 O
ANISOU 2673 OD1 ASP A 394 7216 8706 7608 408 680 31 O
ATOM 2674 OD2 ASP A 394 12.212 8.879 21.209 1.00 69.80 O
ANISOU 2674 OD2 ASP A 394 8216 9753 8552 482 750 6 O
ATOM 2675 N GLY A 395 14.037 11.178 16.351 1.00 40.56 N
ANISOU 2675 N GLY A 395 4566 5879 4964 519 530 -108 N
ATOM 2676 CA GLY A 395 14.040 12.252 15.374 1.00 39.65 C
ANISOU 2676 CA GLY A 395 4463 5726 4875 558 490 -142 C
ATOM 2677 C GLY A 395 15.338 12.419 14.602 1.00 37.02 C
ANISOU 2677 C GLY A 395 4187 5344 4535 547 441 -161 C
ATOM 2678 O GLY A 395 15.392 13.206 13.658 1.00 41.20 O
ANISOU 2678 O GLY A 395 4727 5839 5089 574 406 -181 O
ATOM 2679 N LEU A 396 16.381 11.688 14.987 1.00 28.59 N
ANISOU 2679 N LEU A 396 3157 4273 3433 508 440 -153 N
ATOM 2680 CA LEU A 396 17.689 11.888 14.367 1.00 29.25 C
ANISOU 2680 CA LEU A 396 3297 4309 3506 498 398 -176 C
ATOM 2681 C LEU A 396 17.688 11.518 12.885 1.00 31.51 C
ANISOU 2681 C LEU A 396 3550 4583 3839 479 358 -162 C
ATOM 2682 O LEU A 396 18.190 12.277 12.054 1.00 32.19 O
ANISOU 2682 O LEU A 396 3677 4617 3939 494 317 -184 O
ATOM 2683 CB LEU A 396 18.794 11.126 15.106 1.00 24.84 C
ANISOU 2683 CB LEU A 396 2782 3752 2903 460 404 -168 C
ATOM 2684 CG LEU A 396 20.230 11.373 14.605 1.00 26.59 C
ANISOU 2684 CG LEU A 396 3068 3923 3114 448 362 -194 C
ATOM 2685 CD1 LEU A 396 20.614 12.847 14.730 1.00 23.76 C
ANISOU 2685 CD1 LEU A 396 2765 3519 2745 493 347 -246 C
ATOM 2686 CD2 LEU A 396 21.260 10.493 15.321 1.00 21.07 C
ANISOU 2686 CD2 LEU A 396 2404 3225 2375 405 363 -179 C
ATOM 2687 N GLY A 397 17.121 10.361 12.560 1.00 27.95 N
ANISOU 2687 N GLY A 397 3041 4160 3419 432 359 -121 N
ATOM 2688 CA GLY A 397 17.143 9.873 11.191 1.00 29.54 C
ANISOU 2688 CA GLY A 397 3226 4332 3666 394 306 -107 C
ATOM 2689 C GLY A 397 16.488 10.846 10.236 1.00 30.22 C
ANISOU 2689 C GLY A 397 3292 4409 3782 441 278 -123 C
ATOM 2690 O GLY A 397 16.997 11.136 9.160 1.00 31.48 O
ANISOU 2690 O GLY A 397 3485 4523 3954 437 230 -132 O
ATOM 2691 N LYS A 398 15.344 11.357 10.657 1.00 36.90 N
ANISOU 2691 N LYS A 398 4084 5300 4637 490 312 -126 N
ATOM 2692 CA LYS A 398 14.598 12.335 9.896 1.00 39.52 C
ANISOU 2692 CA LYS A 398 4398 5619 4998 539 287 -138 C
ATOM 2693 C LYS A 398 15.422 13.620 9.764 1.00 38.80 C
ANISOU 2693 C LYS A 398 4387 5471 4885 585 271 -173 C
ATOM 2694 O LYS A 398 15.494 14.228 8.683 1.00 34.85 O
ANISOU 2694 O LYS A 398 3899 4938 4404 610 230 -178 O
ATOM 2695 CB LYS A 398 13.279 12.608 10.618 1.00 44.06 C
ANISOU 2695 CB LYS A 398 4922 6230 5587 564 327 -130 C
ATOM 2696 CG LYS A 398 12.208 13.232 9.766 1.00 50.04 C
ANISOU 2696 CG LYS A 398 5633 6991 6387 602 301 -129 C
ATOM 2697 CD LYS A 398 11.286 14.090 10.621 1.00 57.37 C
ANISOU 2697 CD LYS A 398 6548 7935 7316 652 343 -140 C
ATOM 2698 CE LYS A 398 10.075 14.562 9.828 1.00 62.65 C
ANISOU 2698 CE LYS A 398 7157 8616 8032 686 320 -133 C
ATOM 2699 NZ LYS A 398 9.467 15.792 10.411 1.00 66.97 N
ANISOU 2699 NZ LYS A 398 7713 9155 8576 752 349 -154 N
ATOM 2700 N PHE A 399 16.059 14.027 10.862 1.00 29.47 N
ANISOU 2700 N PHE A 399 3260 4273 3662 594 301 -196 N
ATOM 2701 CA PHE A 399 16.902 15.217 10.829 1.00 19.70 C
ANISOU 2701 CA PHE A 399 2100 2974 2410 627 286 -232 C
ATOM 2702 C PHE A 399 18.089 15.124 9.866 1.00 27.96 C
ANISOU 2702 C PHE A 399 3193 3971 3459 601 242 -234 C
ATOM 2703 O PHE A 399 18.381 16.090 9.168 1.00 29.41 O
ANISOU 2703 O PHE A 399 3414 4103 3657 631 216 -247 O
ATOM 2704 CB PHE A 399 17.426 15.593 12.215 1.00 21.62 C
ANISOU 2704 CB PHE A 399 2396 3210 2611 631 318 -259 C
ATOM 2705 CG PHE A 399 18.357 16.785 12.194 1.00 25.38 C
ANISOU 2705 CG PHE A 399 2949 3616 3078 654 298 -299 C
ATOM 2706 CD1 PHE A 399 17.873 18.055 11.882 1.00 30.05 C
ANISOU 2706 CD1 PHE A 399 3552 4170 3695 703 291 -316 C
ATOM 2707 CD2 PHE A 399 19.707 16.639 12.459 1.00 23.99 C
ANISOU 2707 CD2 PHE A 399 2830 3408 2875 622 284 -316 C
ATOM 2708 CE1 PHE A 399 18.718 19.160 11.843 1.00 22.90 C
ANISOU 2708 CE1 PHE A 399 2716 3194 2792 718 273 -349 C
ATOM 2709 CE2 PHE A 399 20.564 17.739 12.419 1.00 21.07 C
ANISOU 2709 CE2 PHE A 399 2527 2970 2508 635 264 -351 C
ATOM 2710 CZ PHE A 399 20.064 19.000 12.113 1.00 23.02 C
ANISOU 2710 CZ PHE A 399 2785 3177 2783 681 259 -367 C
ATOM 2711 N VAL A 400 18.788 13.985 9.840 1.00 28.25 N
ANISOU 2711 N VAL A 400 3238 4010 3486 534 232 -213 N
ATOM 2712 CA VAL A 400 19.946 13.859 8.948 1.00 29.08 C
ANISOU 2712 CA VAL A 400 3395 4059 3596 495 189 -209 C
ATOM 2713 C VAL A 400 19.530 13.773 7.473 1.00 25.95 C
ANISOU 2713 C VAL A 400 2974 3652 3234 492 148 -188 C
ATOM 2714 O VAL A 400 20.286 14.175 6.574 1.00 21.78 O
ANISOU 2714 O VAL A 400 2492 3074 2711 487 115 -188 O
ATOM 2715 CB VAL A 400 20.915 12.705 9.341 1.00 35.10 C
ANISOU 2715 CB VAL A 400 4178 4821 4338 430 188 -197 C
ATOM 2716 CG1 VAL A 400 21.445 12.914 10.742 1.00 30.66 C
ANISOU 2716 CG1 VAL A 400 3648 4266 3734 438 221 -220 C
ATOM 2717 CG2 VAL A 400 20.234 11.365 9.232 1.00 40.32 C
ANISOU 2717 CG2 VAL A 400 4778 5527 5014 388 193 -162 C
ATOM 2718 N SER A 401 18.319 13.279 7.226 1.00 21.46 N
ANISOU 2718 N SER A 401 2333 3133 2687 496 149 -169 N
ATOM 2719 CA SER A 401 17.764 13.314 5.876 1.00 23.61 C
ANISOU 2719 CA SER A 401 2577 3404 2988 505 106 -154 C
ATOM 2720 C SER A 401 17.555 14.764 5.451 1.00 23.69 C
ANISOU 2720 C SER A 401 2611 3384 3005 574 97 -167 C
ATOM 2721 O SER A 401 17.721 15.118 4.287 1.00 31.13 O
ANISOU 2721 O SER A 401 3574 4298 3956 585 57 -157 O
ATOM 2722 CB SER A 401 16.459 12.526 5.798 1.00 31.65 C
ANISOU 2722 CB SER A 401 3505 4486 4034 495 108 -136 C
ATOM 2723 OG SER A 401 16.724 11.134 5.889 1.00 38.48 O
ANISOU 2723 OG SER A 401 4354 5364 4902 424 106 -120 O
ATOM 2724 N GLU A 402 17.216 15.609 6.408 1.00 26.91 N
ANISOU 2724 N GLU A 402 3021 3797 3407 625 134 -189 N
ATOM 2725 CA GLU A 402 17.091 17.028 6.127 1.00 27.24 C
ANISOU 2725 CA GLU A 402 3093 3799 3458 693 129 -203 C
ATOM 2726 C GLU A 402 18.464 17.641 5.807 1.00 26.80 C
ANISOU 2726 C GLU A 402 3125 3666 3391 680 112 -214 C
ATOM 2727 O GLU A 402 18.594 18.436 4.865 1.00 26.78 O
ANISOU 2727 O GLU A 402 3152 3619 3404 709 86 -204 O
ATOM 2728 CB GLU A 402 16.386 17.748 7.287 1.00 30.94 C
ANISOU 2728 CB GLU A 402 3553 4280 3924 733 173 -224 C
ATOM 2729 CG GLU A 402 16.225 19.254 7.099 1.00 50.53 C
ANISOU 2729 CG GLU A 402 6074 6705 6421 787 168 -238 C
ATOM 2730 CD GLU A 402 15.470 19.628 5.823 1.00 64.35 C
ANISOU 2730 CD GLU A 402 7796 8453 8202 820 131 -210 C
ATOM 2731 OE1 GLU A 402 14.676 18.800 5.315 1.00 70.56 O
ANISOU 2731 OE1 GLU A 402 8514 9294 9000 807 115 -186 O
ATOM 2732 OE2 GLU A 402 15.678 20.758 5.326 1.00 63.42 O
ANISOU 2732 OE2 GLU A 402 7724 8276 8098 856 116 -211 O
ATOM 2733 N LEU A 403 19.489 17.259 6.569 1.00 20.27 N
ANISOU 2733 N LEU A 403 2338 2824 2541 636 127 -229 N
ATOM 2734 CA LEU A 403 20.841 17.727 6.280 1.00 22.23 C
ANISOU 2734 CA LEU A 403 2659 3003 2784 614 111 -238 C
ATOM 2735 C LEU A 403 21.255 17.289 4.881 1.00 24.46 C
ANISOU 2735 C LEU A 403 2950 3268 3076 581 72 -204 C
ATOM 2736 O LEU A 403 21.800 18.091 4.121 1.00 24.03 O
ANISOU 2736 O LEU A 403 2941 3158 3032 595 54 -198 O
ATOM 2737 CB LEU A 403 21.852 17.233 7.315 1.00 22.37 C
ANISOU 2737 CB LEU A 403 2708 3018 2774 569 128 -258 C
ATOM 2738 CG LEU A 403 21.656 17.762 8.737 1.00 32.29 C
ANISOU 2738 CG LEU A 403 3972 4288 4010 602 165 -297 C
ATOM 2739 CD1 LEU A 403 22.708 17.183 9.677 1.00 31.26 C
ANISOU 2739 CD1 LEU A 403 3871 4160 3845 556 173 -313 C
ATOM 2740 CD2 LEU A 403 21.662 19.296 8.775 1.00 25.97 C
ANISOU 2740 CD2 LEU A 403 3212 3431 3225 660 166 -328 C
ATOM 2741 N ASP A 404 20.988 16.024 4.554 1.00 19.64 N
ANISOU 2741 N ASP A 404 2298 2702 2461 539 60 -184 N
ATOM 2742 CA ASP A 404 21.312 15.462 3.243 1.00 21.38 C
ANISOU 2742 CA ASP A 404 2523 2914 2684 509 22 -158 C
ATOM 2743 C ASP A 404 20.819 16.378 2.143 1.00 24.27 C
ANISOU 2743 C ASP A 404 2895 3262 3064 560 -3 -142 C
ATOM 2744 O ASP A 404 21.572 16.753 1.244 1.00 28.86 O
ANISOU 2744 O ASP A 404 3523 3800 3642 557 -22 -128 O
ATOM 2745 CB ASP A 404 20.626 14.109 3.063 1.00 25.37 C
ANISOU 2745 CB ASP A 404 2969 3477 3194 472 12 -144 C
ATOM 2746 CG ASP A 404 21.366 12.967 3.737 1.00 24.12 C
ANISOU 2746 CG ASP A 404 2817 3326 3023 411 26 -146 C
ATOM 2747 OD1 ASP A 404 22.320 13.202 4.504 1.00 24.24 O
ANISOU 2747 OD1 ASP A 404 2876 3313 3022 399 45 -161 O
ATOM 2748 OD2 ASP A 404 20.973 11.817 3.494 1.00 23.77 O
ANISOU 2748 OD2 ASP A 404 2732 3313 2985 374 14 -134 O
ATOM 2749 N ARG A 405 19.547 16.750 2.240 1.00 23.02 N
ANISOU 2749 N ARG A 405 2687 3139 2921 609 0 -142 N
ATOM 2750 CA ARG A 405 18.910 17.610 1.249 1.00 33.12 C
ANISOU 2750 CA ARG A 405 3963 4409 4214 667 -27 -124 C
ATOM 2751 C ARG A 405 19.640 18.953 1.113 1.00 30.83 C
ANISOU 2751 C ARG A 405 3743 4043 3928 703 -20 -126 C
ATOM 2752 O ARG A 405 19.872 19.430 0.001 1.00 24.29 O
ANISOU 2752 O ARG A 405 2945 3184 3099 720 -46 -99 O
ATOM 2753 CB ARG A 405 17.434 17.817 1.610 1.00 43.96 C
ANISOU 2753 CB ARG A 405 5264 5833 5605 719 -19 -128 C
ATOM 2754 CG ARG A 405 16.573 18.410 0.500 1.00 55.97 C
ANISOU 2754 CG ARG A 405 6762 7364 7139 777 -56 -105 C
ATOM 2755 CD ARG A 405 15.124 18.551 0.950 1.00 60.10 C
ANISOU 2755 CD ARG A 405 7212 7938 7686 811 -44 -108 C
ATOM 2756 N ARG A 406 20.023 19.540 2.244 1.00 24.64 N
ANISOU 2756 N ARG A 406 2986 3229 3146 711 15 -156 N
ATOM 2757 CA ARG A 406 20.708 20.833 2.243 1.00 28.33 C
ANISOU 2757 CA ARG A 406 3519 3618 3627 740 22 -164 C
ATOM 2758 C ARG A 406 22.107 20.743 1.670 1.00 28.30 C
ANISOU 2758 C ARG A 406 3572 3564 3616 689 11 -150 C
ATOM 2759 O ARG A 406 22.512 21.587 0.872 1.00 32.90 O
ANISOU 2759 O ARG A 406 4198 4091 4212 709 1 -128 O
ATOM 2760 CB ARG A 406 20.768 21.437 3.652 1.00 26.72 C
ANISOU 2760 CB ARG A 406 3330 3397 3427 760 58 -209 C
ATOM 2761 CG ARG A 406 19.395 21.718 4.227 1.00 32.90 C
ANISOU 2761 CG ARG A 406 4061 4223 4218 804 76 -219 C
ATOM 2762 CD ARG A 406 19.444 22.438 5.564 1.00 37.17 C
ANISOU 2762 CD ARG A 406 4624 4742 4758 813 110 -261 C
ATOM 2763 NE ARG A 406 18.181 22.247 6.271 1.00 49.09 N
ANISOU 2763 NE ARG A 406 6073 6314 6264 837 134 -268 N
ATOM 2764 CZ ARG A 406 17.487 23.219 6.855 1.00 56.74 C
ANISOU 2764 CZ ARG A 406 7042 7270 7248 879 155 -287 C
ATOM 2765 NH1 ARG A 406 17.938 24.468 6.827 1.00 57.71 N
ANISOU 2765 NH1 ARG A 406 7221 7315 7391 900 153 -302 N
ATOM 2766 NH2 ARG A 406 16.340 22.939 7.470 1.00 56.48 N
ANISOU 2766 NH2 ARG A 406 6950 7298 7212 899 179 -289 N
ATOM 2767 N VAL A 407 22.846 19.723 2.096 1.00 26.40 N
ANISOU 2767 N VAL A 407 3331 3342 3357 625 16 -160 N
ATOM 2768 CA VAL A 407 24.178 19.479 1.578 1.00 22.56 C
ANISOU 2768 CA VAL A 407 2888 2818 2864 574 8 -147 C
ATOM 2769 C VAL A 407 24.090 19.330 0.060 1.00 18.08 C
ANISOU 2769 C VAL A 407 2324 2253 2292 579 -20 -105 C
ATOM 2770 O VAL A 407 24.848 19.947 -0.689 1.00 16.30 O
ANISOU 2770 O VAL A 407 2145 1977 2072 579 -24 -82 O
ATOM 2771 CB VAL A 407 24.791 18.208 2.202 1.00 19.95 C
ANISOU 2771 CB VAL A 407 2545 2522 2514 511 14 -160 C
ATOM 2772 CG1 VAL A 407 26.004 17.749 1.408 1.00 13.07 C
ANISOU 2772 CG1 VAL A 407 1706 1626 1636 463 2 -140 C
ATOM 2773 CG2 VAL A 407 25.152 18.457 3.664 1.00 15.98 C
ANISOU 2773 CG2 VAL A 407 2053 2010 2008 505 40 -201 C
ATOM 2774 N LEU A 408 23.134 18.522 -0.372 1.00 17.64 N
ANISOU 2774 N LEU A 408 2218 2260 2225 584 -40 -94 N
ATOM 2775 CA LEU A 408 22.881 18.285 -1.779 1.00 18.95 C
ANISOU 2775 CA LEU A 408 2381 2442 2378 594 -73 -60 C
ATOM 2776 C LEU A 408 22.622 19.586 -2.554 1.00 22.60 C
ANISOU 2776 C LEU A 408 2873 2865 2850 655 -82 -32 C
ATOM 2777 O LEU A 408 23.364 19.929 -3.480 1.00 17.51 O
ANISOU 2777 O LEU A 408 2274 2183 2196 652 -88 -2 O
ATOM 2778 CB LEU A 408 21.702 17.321 -1.922 1.00 25.00 C
ANISOU 2778 CB LEU A 408 3079 3282 3139 594 -95 -62 C
ATOM 2779 CG LEU A 408 21.079 17.190 -3.308 1.00 38.51 C
ANISOU 2779 CG LEU A 408 4774 5021 4836 619 -138 -35 C
ATOM 2780 CD1 LEU A 408 22.150 16.797 -4.309 1.00 41.17 C
ANISOU 2780 CD1 LEU A 408 5159 5338 5145 585 -152 -17 C
ATOM 2781 CD2 LEU A 408 19.951 16.172 -3.285 1.00 41.32 C
ANISOU 2781 CD2 LEU A 408 5055 5448 5195 608 -161 -46 C
ATOM 2782 N GLU A 409 21.590 20.318 -2.153 1.00 23.73 N
ANISOU 2782 N GLU A 409 2990 3013 3013 713 -78 -39 N
ATOM 2783 CA GLU A 409 21.225 21.558 -2.829 1.00 23.30 C
ANISOU 2783 CA GLU A 409 2961 2920 2972 780 -87 -11 C
ATOM 2784 C GLU A 409 22.339 22.599 -2.837 1.00 27.02 C
ANISOU 2784 C GLU A 409 3504 3301 3459 778 -65 -1 C
ATOM 2785 O GLU A 409 22.448 23.399 -3.774 1.00 21.86 O
ANISOU 2785 O GLU A 409 2888 2608 2810 813 -75 39 O
ATOM 2786 CB GLU A 409 19.941 22.148 -2.225 1.00 25.28 C
ANISOU 2786 CB GLU A 409 3168 3192 3246 846 -82 -26 C
ATOM 2787 CG GLU A 409 18.697 21.262 -2.393 1.00 33.32 C
ANISOU 2787 CG GLU A 409 4106 4298 4257 855 -107 -27 C
ATOM 2788 CD GLU A 409 18.291 21.037 -3.851 1.00 48.25 C
ANISOU 2788 CD GLU A 409 5986 6218 6127 867 -154 12 C
ATOM 2789 OE1 GLU A 409 18.872 21.673 -4.772 1.00 54.38 O
ANISOU 2789 OE1 GLU A 409 6820 6949 6893 879 -164 46 O
ATOM 2790 OE2 GLU A 409 17.375 20.213 -4.072 1.00 47.21 O
ANISOU 2790 OE2 GLU A 409 5790 6158 5992 861 -180 8 O
ATOM 2791 N PHE A 410 23.176 22.589 -1.803 1.00 25.31 N
ANISOU 2791 N PHE A 410 3309 3054 3254 737 -38 -36 N
ATOM 2792 CA PHE A 410 24.222 23.606 -1.703 1.00 27.51 C
ANISOU 2792 CA PHE A 410 3650 3244 3558 730 -19 -34 C
ATOM 2793 C PHE A 410 25.466 23.171 -2.444 1.00 28.55 C
ANISOU 2793 C PHE A 410 3814 3358 3675 673 -20 -7 C
ATOM 2794 O PHE A 410 26.500 23.834 -2.376 1.00 28.62 O
ANISOU 2794 O PHE A 410 3869 3298 3707 651 -3 -4 O
ATOM 2795 CB PHE A 410 24.540 23.950 -0.245 1.00 26.66 C
ANISOU 2795 CB PHE A 410 3551 3109 3471 718 7 -89 C
ATOM 2796 CG PHE A 410 23.361 24.492 0.511 1.00 35.14 C
ANISOU 2796 CG PHE A 410 4596 4197 4557 778 16 -117 C
ATOM 2797 CD1 PHE A 410 22.337 25.156 -0.162 1.00 38.23 C
ANISOU 2797 CD1 PHE A 410 4971 4592 4961 828 4 -87 C
ATOM 2798 CD2 PHE A 410 23.255 24.323 1.889 1.00 40.10 C
ANISOU 2798 CD2 PHE A 410 5208 4846 5182 767 37 -170 C
ATOM 2799 CE1 PHE A 410 21.238 25.657 0.527 1.00 44.32 C
ANISOU 2799 CE1 PHE A 410 5709 5383 5747 867 15 -110 C
ATOM 2800 CE2 PHE A 410 22.153 24.823 2.589 1.00 44.75 C
ANISOU 2800 CE2 PHE A 410 5766 5457 5781 806 50 -192 C
ATOM 2801 CZ PHE A 410 21.146 25.489 1.907 1.00 47.16 C
ANISOU 2801 CZ PHE A 410 6053 5761 6103 856 40 -163 C
ATOM 2802 N GLY A 411 25.357 22.044 -3.148 1.00 24.33 N
ANISOU 2802 N GLY A 411 3254 2885 3106 649 -40 10 N
ATOM 2803 CA GLY A 411 26.435 21.566 -3.991 1.00 23.64 C
ANISOU 2803 CA GLY A 411 3194 2789 2998 604 -40 37 C
ATOM 2804 C GLY A 411 27.488 20.742 -3.267 1.00 25.48 C
ANISOU 2804 C GLY A 411 3427 3026 3230 536 -25 7 C
ATOM 2805 O GLY A 411 28.557 20.478 -3.818 1.00 22.44 O
ANISOU 2805 O GLY A 411 3067 2623 2836 498 -19 26 O
ATOM 2806 N GLY A 412 27.187 20.332 -2.037 1.00 20.49 N
ANISOU 2806 N GLY A 412 2765 2418 2603 523 -19 -37 N
ATOM 2807 CA GLY A 412 28.097 19.498 -1.279 1.00 20.92 C
ANISOU 2807 CA GLY A 412 2816 2482 2652 464 -9 -63 C
ATOM 2808 C GLY A 412 27.892 17.999 -1.459 1.00 21.68 C
ANISOU 2808 C GLY A 412 2875 2644 2719 432 -23 -65 C
ATOM 2809 O GLY A 412 27.090 17.560 -2.276 1.00 15.30 O
ANISOU 2809 O GLY A 412 2045 1875 1894 451 -44 -47 O
ATOM 2810 N ARG A 413 28.627 17.213 -0.683 1.00 19.19 N
ANISOU 2810 N ARG A 413 2554 2338 2399 384 -13 -87 N
ATOM 2811 CA ARG A 413 28.490 15.765 -0.702 1.00 20.22 C
ANISOU 2811 CA ARG A 413 2653 2521 2509 351 -24 -91 C
ATOM 2812 C ARG A 413 28.776 15.140 0.668 1.00 18.65 C
ANISOU 2812 C ARG A 413 2438 2338 2309 320 -10 -121 C
ATOM 2813 O ARG A 413 29.409 15.745 1.534 1.00 17.99 O
ANISOU 2813 O ARG A 413 2374 2223 2236 314 5 -141 O
ATOM 2814 CB ARG A 413 29.441 15.146 -1.740 1.00 14.10 C
ANISOU 2814 CB ARG A 413 1897 1740 1719 321 -30 -69 C
ATOM 2815 CG ARG A 413 30.925 15.446 -1.486 1.00 14.49 C
ANISOU 2815 CG ARG A 413 1980 1744 1781 289 -12 -70 C
ATOM 2816 CD ARG A 413 31.435 16.586 -2.400 1.00 16.79 C
ANISOU 2816 CD ARG A 413 2311 1986 2084 307 -4 -40 C
ATOM 2817 NE ARG A 413 31.074 16.317 -3.787 1.00 16.33 N
ANISOU 2817 NE ARG A 413 2257 1949 1999 326 -18 -8 N
ATOM 2818 CZ ARG A 413 31.756 15.503 -4.588 1.00 22.34 C
ANISOU 2818 CZ ARG A 413 3025 2725 2738 302 -19 5 C
ATOM 2819 NH1 ARG A 413 32.853 14.900 -4.144 1.00 19.44 N
ANISOU 2819 NH1 ARG A 413 2658 2351 2377 259 -5 -7 N
ATOM 2820 NH2 ARG A 413 31.337 15.281 -5.828 1.00 18.40 N
ANISOU 2820 NH2 ARG A 413 2533 2251 2208 325 -35 29 N
ATOM 2821 N LEU A 414 28.298 13.913 0.825 1.00 17.47 N
ANISOU 2821 N LEU A 414 2253 2237 2148 299 -17 -122 N
ATOM 2822 CA LEU A 414 28.719 12.999 1.872 1.00 17.72 C
ANISOU 2822 CA LEU A 414 2272 2286 2173 262 -6 -138 C
ATOM 2823 C LEU A 414 29.892 12.141 1.389 1.00 19.04 C
ANISOU 2823 C LEU A 414 2457 2444 2335 221 -12 -129 C
ATOM 2824 O LEU A 414 30.224 12.119 0.199 1.00 22.89 O
ANISOU 2824 O LEU A 414 2959 2918 2819 220 -23 -111 O
ATOM 2825 CB LEU A 414 27.561 12.070 2.214 1.00 17.64 C
ANISOU 2825 CB LEU A 414 2214 2330 2160 260 -8 -138 C
ATOM 2826 CG LEU A 414 26.276 12.790 2.592 1.00 21.59 C
ANISOU 2826 CG LEU A 414 2685 2851 2668 305 -1 -144 C
ATOM 2827 CD1 LEU A 414 25.131 11.807 2.736 1.00 22.83 C
ANISOU 2827 CD1 LEU A 414 2785 3061 2827 297 -4 -139 C
ATOM 2828 CD2 LEU A 414 26.489 13.562 3.873 1.00 24.44 C
ANISOU 2828 CD2 LEU A 414 3062 3200 3026 321 24 -169 C
ATOM 2829 N TYR A 415 30.468 11.397 2.323 1.00 20.37 N
ANISOU 2829 N TYR A 415 2620 2620 2498 190 -3 -139 N
ATOM 2830 CA TYR A 415 31.664 10.583 2.120 1.00 17.32 C
ANISOU 2830 CA TYR A 415 2248 2224 2110 153 -6 -133 C
ATOM 2831 C TYR A 415 31.290 9.119 2.363 1.00 17.32 C
ANISOU 2831 C TYR A 415 2219 2257 2104 129 -10 -129 C
ATOM 2832 O TYR A 415 30.766 8.778 3.435 1.00 22.28 O
ANISOU 2832 O TYR A 415 2826 2911 2729 126 0 -135 O
ATOM 2833 CB TYR A 415 32.674 11.027 3.172 1.00 16.45 C
ANISOU 2833 CB TYR A 415 2155 2093 2002 142 5 -150 C
ATOM 2834 CG TYR A 415 34.069 10.450 3.120 1.00 19.93 C
ANISOU 2834 CG TYR A 415 2608 2519 2445 109 3 -146 C
ATOM 2835 CD1 TYR A 415 34.551 9.789 1.996 1.00 15.41 C
ANISOU 2835 CD1 TYR A 415 2039 1941 1873 96 -2 -129 C
ATOM 2836 CD2 TYR A 415 34.908 10.569 4.227 1.00 14.09 C
ANISOU 2836 CD2 TYR A 415 1874 1774 1705 95 6 -163 C
ATOM 2837 CE1 TYR A 415 35.839 9.282 1.972 1.00 13.25 C
ANISOU 2837 CE1 TYR A 415 1773 1656 1604 71 0 -126 C
ATOM 2838 CE2 TYR A 415 36.185 10.071 4.215 1.00 13.07 C
ANISOU 2838 CE2 TYR A 415 1749 1634 1581 69 3 -159 C
ATOM 2839 CZ TYR A 415 36.655 9.431 3.090 1.00 18.78 C
ANISOU 2839 CZ TYR A 415 2474 2351 2310 57 2 -140 C
ATOM 2840 OH TYR A 415 37.945 8.944 3.101 1.00 19.29 O
ANISOU 2840 OH TYR A 415 2540 2407 2383 35 1 -136 O
ATOM 2841 N THR A 416 31.555 8.247 1.394 1.00 9.45 N
ANISOU 2841 N THR A 416 1223 1260 1106 112 -23 -119 N
ATOM 2842 CA THR A 416 31.230 6.825 1.559 1.00 14.04 C
ANISOU 2842 CA THR A 416 1781 1862 1690 86 -28 -116 C
ATOM 2843 C THR A 416 31.868 6.185 2.793 1.00 16.53 C
ANISOU 2843 C THR A 416 2095 2180 2005 64 -15 -116 C
ATOM 2844 O THR A 416 31.349 5.202 3.321 1.00 17.61 O
ANISOU 2844 O THR A 416 2209 2337 2146 47 -12 -109 O
ATOM 2845 CB THR A 416 31.648 5.966 0.343 1.00 13.94 C
ANISOU 2845 CB THR A 416 1778 1842 1676 72 -45 -113 C
ATOM 2846 OG1 THR A 416 33.037 6.182 0.048 1.00 19.67 O
ANISOU 2846 OG1 THR A 416 2536 2541 2398 67 -37 -110 O
ATOM 2847 CG2 THR A 416 30.793 6.276 -0.868 1.00 16.34 C
ANISOU 2847 CG2 THR A 416 2078 2156 1974 93 -65 -112 C
ATOM 2848 N ALA A 417 32.999 6.725 3.239 1.00 16.99 N
ANISOU 2848 N ALA A 417 2177 2219 2059 63 -8 -121 N
ATOM 2849 CA ALA A 417 33.704 6.166 4.398 1.00 15.85 C
ANISOU 2849 CA ALA A 417 2033 2079 1909 46 0 -121 C
ATOM 2850 C ALA A 417 32.974 6.469 5.692 1.00 15.63 C
ANISOU 2850 C ALA A 417 1992 2078 1868 57 13 -127 C
ATOM 2851 O ALA A 417 33.305 5.917 6.735 1.00 16.49 O
ANISOU 2851 O ALA A 417 2098 2201 1964 47 19 -123 O
ATOM 2852 CB ALA A 417 35.136 6.688 4.467 1.00 12.36 C
ANISOU 2852 CB ALA A 417 1615 1613 1470 41 -2 -128 C
ATOM 2853 N LYS A 418 31.967 7.336 5.610 1.00 18.28 N
ANISOU 2853 N LYS A 418 2319 2423 2204 83 17 -135 N
ATOM 2854 CA LYS A 418 31.253 7.807 6.790 1.00 20.69 C
ANISOU 2854 CA LYS A 418 2613 2754 2494 102 35 -145 C
ATOM 2855 C LYS A 418 29.755 7.552 6.720 1.00 25.71 C
ANISOU 2855 C LYS A 418 3212 3423 3136 113 44 -135 C
ATOM 2856 O LYS A 418 28.995 8.049 7.550 1.00 29.59 O
ANISOU 2856 O LYS A 418 3689 3938 3615 137 62 -143 O
ATOM 2857 CB LYS A 418 31.518 9.299 6.988 1.00 15.37 C
ANISOU 2857 CB LYS A 418 1964 2059 1818 129 36 -171 C
ATOM 2858 CG LYS A 418 32.939 9.596 7.439 1.00 21.86 C
ANISOU 2858 CG LYS A 418 2813 2856 2635 115 28 -185 C
ATOM 2859 CD LYS A 418 33.173 9.099 8.851 1.00 24.56 C
ANISOU 2859 CD LYS A 418 3154 3228 2950 110 35 -191 C
ATOM 2860 CE LYS A 418 34.446 9.676 9.451 1.00 32.30 C
ANISOU 2860 CE LYS A 418 4160 4189 3924 103 22 -215 C
ATOM 2861 NZ LYS A 418 34.276 11.067 9.952 1.00 29.74 N
ANISOU 2861 NZ LYS A 418 3853 3850 3595 130 24 -252 N
ATOM 2862 N ASP A 419 29.327 6.775 5.734 1.00 27.69 N
ANISOU 2862 N ASP A 419 3443 3673 3404 97 30 -121 N
ATOM 2863 CA ASP A 419 27.903 6.621 5.480 1.00 20.26 C
ANISOU 2863 CA ASP A 419 2461 2762 2476 107 31 -114 C
ATOM 2864 C ASP A 419 27.432 5.185 5.266 1.00 24.20 C
ANISOU 2864 C ASP A 419 2929 3273 2993 71 26 -96 C
ATOM 2865 O ASP A 419 28.035 4.434 4.501 1.00 30.42 O
ANISOU 2865 O ASP A 419 3730 4038 3789 47 7 -93 O
ATOM 2866 CB ASP A 419 27.496 7.439 4.256 1.00 20.02 C
ANISOU 2866 CB ASP A 419 2433 2719 2455 132 11 -121 C
ATOM 2867 CG ASP A 419 26.085 7.113 3.788 1.00 25.23 C
ANISOU 2867 CG ASP A 419 3044 3411 3132 137 2 -114 C
ATOM 2868 OD1 ASP A 419 25.113 7.542 4.451 1.00 20.39 O
ANISOU 2868 OD1 ASP A 419 2399 2827 2522 160 20 -115 O
ATOM 2869 OD2 ASP A 419 25.949 6.410 2.767 1.00 21.38 O
ANISOU 2869 OD2 ASP A 419 2548 2920 2656 119 -24 -110 O
ATOM 2870 N SER A 420 26.329 4.822 5.915 1.00 21.85 N
ANISOU 2870 N SER A 420 2587 3010 2703 69 44 -84 N
ATOM 2871 CA SER A 420 25.604 3.619 5.526 1.00 26.87 C
ANISOU 2871 CA SER A 420 3185 3657 3369 36 35 -69 C
ATOM 2872 C SER A 420 24.094 3.854 5.560 1.00 28.02 C
ANISOU 2872 C SER A 420 3273 3840 3532 49 43 -65 C
ATOM 2873 O SER A 420 23.313 2.902 5.622 1.00 27.39 O
ANISOU 2873 O SER A 420 3148 3776 3480 19 45 -49 O
ATOM 2874 CB SER A 420 26.003 2.406 6.379 1.00 26.11 C
ANISOU 2874 CB SER A 420 3089 3557 3275 0 53 -45 C
ATOM 2875 OG SER A 420 25.728 2.618 7.753 1.00 25.49 O
ANISOU 2875 OG SER A 420 3000 3509 3176 12 91 -32 O
ATOM 2876 N ARG A 421 23.687 5.120 5.495 1.00 22.82 N
ANISOU 2876 N ARG A 421 2614 3194 2863 94 45 -79 N
ATOM 2877 CA ARG A 421 22.275 5.465 5.667 1.00 20.03 C
ANISOU 2877 CA ARG A 421 2203 2882 2526 116 57 -76 C
ATOM 2878 C ARG A 421 21.597 6.227 4.522 1.00 20.06 C
ANISOU 2878 C ARG A 421 2190 2890 2542 148 25 -89 C
ATOM 2879 O ARG A 421 20.392 6.077 4.347 1.00 25.98 O
ANISOU 2879 O ARG A 421 2879 3674 3317 152 21 -84 O
ATOM 2880 CB ARG A 421 22.051 6.201 6.993 1.00 22.08 C
ANISOU 2880 CB ARG A 421 2461 3168 2762 150 101 -78 C
ATOM 2881 CG ARG A 421 23.002 7.359 7.220 1.00 30.35 C
ANISOU 2881 CG ARG A 421 3568 4187 3778 183 102 -101 C
ATOM 2882 CD ARG A 421 22.334 8.508 7.959 1.00 34.70 C
ANISOU 2882 CD ARG A 421 4108 4761 4316 237 131 -116 C
ATOM 2883 NE ARG A 421 21.199 9.058 7.214 1.00 37.22 N
ANISOU 2883 NE ARG A 421 4385 5097 4660 269 118 -118 N
ATOM 2884 CZ ARG A 421 21.291 9.956 6.236 1.00 30.44 C
ANISOU 2884 CZ ARG A 421 3547 4209 3808 299 89 -130 C
ATOM 2885 NH1 ARG A 421 22.476 10.429 5.852 1.00 26.09 N
ANISOU 2885 NH1 ARG A 421 3059 3610 3244 297 73 -141 N
ATOM 2886 NH2 ARG A 421 20.185 10.381 5.638 1.00 23.08 N
ANISOU 2886 NH2 ARG A 421 2573 3300 2898 332 78 -128 N
ATOM 2887 N THR A 422 22.346 7.028 3.757 1.00 18.77 N
ANISOU 2887 N THR A 422 2076 2694 2362 171 3 -102 N
ATOM 2888 CA THR A 422 21.758 7.835 2.667 1.00 22.39 C
ANISOU 2888 CA THR A 422 2527 3155 2826 209 -27 -108 C
ATOM 2889 C THR A 422 21.213 7.005 1.496 1.00 22.75 C
ANISOU 2889 C THR A 422 2542 3213 2891 186 -70 -107 C
ATOM 2890 O THR A 422 21.462 5.807 1.408 1.00 24.66 O
ANISOU 2890 O THR A 422 2779 3449 3143 138 -78 -105 O
ATOM 2891 CB THR A 422 22.725 8.944 2.151 1.00 21.58 C
ANISOU 2891 CB THR A 422 2487 3009 2701 239 -35 -116 C
ATOM 2892 OG1 THR A 422 21.962 10.042 1.638 1.00 22.46 O
ANISOU 2892 OG1 THR A 422 2588 3129 2818 292 -47 -117 O
ATOM 2893 CG2 THR A 422 23.644 8.422 1.055 1.00 12.30 C
ANISOU 2893 CG2 THR A 422 1350 1806 1518 213 -64 -114 C
ATOM 2894 N THR A 423 20.452 7.641 0.607 1.00 20.84 N
ANISOU 2894 N THR A 423 2279 2986 2652 222 -100 -110 N
ATOM 2895 CA THR A 423 19.804 6.924 -0.509 1.00 12.24 C
ANISOU 2895 CA THR A 423 1156 1916 1578 205 -147 -114 C
ATOM 2896 C THR A 423 20.585 7.027 -1.815 1.00 13.60 C
ANISOU 2896 C THR A 423 1382 2062 1722 211 -184 -120 C
ATOM 2897 O THR A 423 21.399 7.937 -2.004 1.00 20.21 O
ANISOU 2897 O THR A 423 2275 2870 2535 240 -174 -115 O
ATOM 2898 CB THR A 423 18.387 7.498 -0.799 1.00 25.37 C
ANISOU 2898 CB THR A 423 2755 3623 3259 245 -166 -112 C
ATOM 2899 OG1 THR A 423 18.500 8.881 -1.177 1.00 20.45 O
ANISOU 2899 OG1 THR A 423 2166 2988 2615 307 -169 -109 O
ATOM 2900 CG2 THR A 423 17.488 7.388 0.427 1.00 17.73 C
ANISOU 2900 CG2 THR A 423 1725 2691 2321 243 -126 -105 C
ATOM 2901 N ALA A 424 20.310 6.108 -2.729 1.00 18.44 N
ANISOU 2901 N ALA A 424 1979 2685 2341 184 -226 -131 N
ATOM 2902 CA ALA A 424 20.919 6.133 -4.058 1.00 15.26 C
ANISOU 2902 CA ALA A 424 1624 2267 1905 194 -263 -138 C
ATOM 2903 C ALA A 424 20.648 7.462 -4.766 1.00 20.64 C
ANISOU 2903 C ALA A 424 2321 2957 2563 257 -278 -127 C
ATOM 2904 O ALA A 424 21.530 8.031 -5.410 1.00 22.77 O
ANISOU 2904 O ALA A 424 2651 3200 2799 279 -278 -118 O
ATOM 2905 CB ALA A 424 20.412 4.983 -4.882 1.00 14.58 C
ANISOU 2905 CB ALA A 424 1509 2199 1830 161 -311 -159 C
ATOM 2906 N GLU A 425 19.428 7.960 -4.627 1.00 21.71 N
ANISOU 2906 N GLU A 425 2401 3128 2718 289 -289 -123 N
ATOM 2907 CA GLU A 425 19.050 9.219 -5.250 1.00 22.42 C
ANISOU 2907 CA GLU A 425 2501 3226 2790 354 -305 -108 C
ATOM 2908 C GLU A 425 19.873 10.386 -4.701 1.00 23.69 C
ANISOU 2908 C GLU A 425 2717 3343 2940 385 -260 -92 C
ATOM 2909 O GLU A 425 20.408 11.192 -5.457 1.00 22.10 O
ANISOU 2909 O GLU A 425 2567 3118 2711 419 -267 -77 O
ATOM 2910 CB GLU A 425 17.576 9.484 -5.015 1.00 25.79 C
ANISOU 2910 CB GLU A 425 2850 3700 3248 383 -320 -107 C
ATOM 2911 CG GLU A 425 17.091 10.809 -5.546 1.00 41.66 C
ANISOU 2911 CG GLU A 425 4866 5718 5246 458 -335 -90 C
ATOM 2912 CD GLU A 425 15.631 11.026 -5.224 1.00 53.17 C
ANISOU 2912 CD GLU A 425 6237 7225 6739 488 -346 -90 C
ATOM 2913 OE1 GLU A 425 15.324 12.008 -4.515 1.00 55.52 O
ANISOU 2913 OE1 GLU A 425 6528 7518 7051 534 -311 -80 O
ATOM 2914 OE2 GLU A 425 14.798 10.195 -5.658 1.00 52.68 O
ANISOU 2914 OE2 GLU A 425 6113 7207 6695 464 -388 -103 O
ATOM 2915 N THR A 426 19.984 10.459 -3.381 1.00 17.63 N
ANISOU 2915 N THR A 426 1939 2566 2193 372 -215 -96 N
ATOM 2916 CA THR A 426 20.763 11.509 -2.741 1.00 17.74 C
ANISOU 2916 CA THR A 426 2002 2538 2200 396 -175 -90 C
ATOM 2917 C THR A 426 22.243 11.438 -3.122 1.00 21.01 C
ANISOU 2917 C THR A 426 2486 2907 2591 371 -168 -86 C
ATOM 2918 O THR A 426 22.851 12.450 -3.473 1.00 24.45 O
ANISOU 2918 O THR A 426 2971 3306 3015 401 -160 -73 O
ATOM 2919 CB THR A 426 20.597 11.464 -1.206 1.00 19.86 C
ANISOU 2919 CB THR A 426 2246 2812 2488 385 -131 -100 C
ATOM 2920 OG1 THR A 426 19.244 11.778 -0.879 1.00 20.52 O
ANISOU 2920 OG1 THR A 426 2266 2936 2593 420 -130 -100 O
ATOM 2921 CG2 THR A 426 21.503 12.476 -0.529 1.00 16.27 C
ANISOU 2921 CG2 THR A 426 1846 2310 2025 403 -96 -103 C
ATOM 2922 N PHE A 427 22.817 10.243 -3.072 1.00 13.35 N
ANISOU 2922 N PHE A 427 1519 1937 1618 318 -169 -95 N
ATOM 2923 CA PHE A 427 24.229 10.096 -3.374 1.00 12.94 C
ANISOU 2923 CA PHE A 427 1524 1846 1546 295 -159 -93 C
ATOM 2924 C PHE A 427 24.517 10.417 -4.841 1.00 18.95 C
ANISOU 2924 C PHE A 427 2322 2601 2279 318 -186 -80 C
ATOM 2925 O PHE A 427 25.469 11.139 -5.142 1.00 20.30 O
ANISOU 2925 O PHE A 427 2543 2736 2436 329 -170 -65 O
ATOM 2926 CB PHE A 427 24.721 8.689 -3.025 1.00 15.65 C
ANISOU 2926 CB PHE A 427 1861 2191 1894 238 -156 -105 C
ATOM 2927 CG PHE A 427 26.194 8.478 -3.284 1.00 19.36 C
ANISOU 2927 CG PHE A 427 2383 2624 2347 216 -143 -103 C
ATOM 2928 CD1 PHE A 427 27.135 8.756 -2.289 1.00 17.64 C
ANISOU 2928 CD1 PHE A 427 2188 2379 2135 203 -109 -103 C
ATOM 2929 CD2 PHE A 427 26.642 7.999 -4.511 1.00 16.35 C
ANISOU 2929 CD2 PHE A 427 2027 2241 1943 211 -166 -104 C
ATOM 2930 CE1 PHE A 427 28.493 8.557 -2.518 1.00 16.29 C
ANISOU 2930 CE1 PHE A 427 2057 2178 1953 184 -98 -100 C
ATOM 2931 CE2 PHE A 427 28.000 7.801 -4.745 1.00 14.50 C
ANISOU 2931 CE2 PHE A 427 1837 1978 1696 194 -150 -101 C
ATOM 2932 CZ PHE A 427 28.926 8.084 -3.742 1.00 10.52 C
ANISOU 2932 CZ PHE A 427 1348 1445 1204 180 -116 -98 C
ATOM 2933 N HIS A 428 23.703 9.884 -5.752 1.00 16.62 N
ANISOU 2933 N HIS A 428 2000 2342 1973 324 -228 -84 N
ATOM 2934 CA HIS A 428 23.932 10.133 -7.172 1.00 19.78 C
ANISOU 2934 CA HIS A 428 2435 2744 2335 350 -257 -72 C
ATOM 2935 C HIS A 428 23.865 11.638 -7.422 1.00 20.71 C
ANISOU 2935 C HIS A 428 2580 2844 2447 406 -247 -43 C
ATOM 2936 O HIS A 428 24.683 12.196 -8.149 1.00 20.30 O
ANISOU 2936 O HIS A 428 2580 2765 2368 422 -239 -20 O
ATOM 2937 CB HIS A 428 22.917 9.392 -8.059 1.00 15.12 C
ANISOU 2937 CB HIS A 428 1808 2202 1735 352 -311 -87 C
ATOM 2938 CG HIS A 428 23.236 7.942 -8.287 1.00 17.93 C
ANISOU 2938 CG HIS A 428 2161 2564 2089 301 -327 -115 C
ATOM 2939 ND1 HIS A 428 23.307 7.385 -9.547 1.00 19.62 N
ANISOU 2939 ND1 HIS A 428 2394 2795 2266 303 -367 -128 N
ATOM 2940 CD2 HIS A 428 23.489 6.937 -7.413 1.00 11.68 C
ANISOU 2940 CD2 HIS A 428 1350 1761 1327 249 -308 -133 C
ATOM 2941 CE1 HIS A 428 23.583 6.095 -9.441 1.00 17.42 C
ANISOU 2941 CE1 HIS A 428 2109 2512 1998 254 -373 -157 C
ATOM 2942 NE2 HIS A 428 23.696 5.800 -8.159 1.00 20.72 N
ANISOU 2942 NE2 HIS A 428 2503 2911 2458 220 -338 -157 N
ATOM 2943 N ALA A 429 22.905 12.307 -6.799 1.00 12.07 N
ANISOU 2943 N ALA A 429 1448 1759 1377 437 -245 -41 N
ATOM 2944 CA ALA A 429 22.787 13.736 -7.035 1.00 18.09 C
ANISOU 2944 CA ALA A 429 2236 2497 2138 494 -237 -13 C
ATOM 2945 C ALA A 429 24.023 14.516 -6.520 1.00 19.83 C
ANISOU 2945 C ALA A 429 2512 2656 2367 486 -192 -2 C
ATOM 2946 O ALA A 429 24.436 15.496 -7.127 1.00 18.63 O
ANISOU 2946 O ALA A 429 2403 2470 2204 519 -185 27 O
ATOM 2947 CB ALA A 429 21.493 14.264 -6.452 1.00 15.36 C
ANISOU 2947 CB ALA A 429 1838 2176 1821 533 -243 -17 C
ATOM 2948 N MET A 430 24.627 14.041 -5.434 1.00 18.88 N
ANISOU 2948 N MET A 430 2388 2520 2264 442 -163 -25 N
ATOM 2949 CA MET A 430 25.829 14.651 -4.845 1.00 17.22 C
ANISOU 2949 CA MET A 430 2222 2255 2065 426 -125 -22 C
ATOM 2950 C MET A 430 27.109 14.431 -5.657 1.00 18.68 C
ANISOU 2950 C MET A 430 2453 2416 2228 401 -118 -6 C
ATOM 2951 O MET A 430 28.107 15.133 -5.469 1.00 17.86 O
ANISOU 2951 O MET A 430 2386 2264 2135 395 -91 5 O
ATOM 2952 CB MET A 430 26.051 14.113 -3.431 1.00 15.54 C
ANISOU 2952 CB MET A 430 1988 2044 1872 389 -101 -52 C
ATOM 2953 CG MET A 430 24.985 14.511 -2.413 1.00 12.22 C
ANISOU 2953 CG MET A 430 1529 1642 1473 415 -93 -67 C
ATOM 2954 SD MET A 430 25.252 13.704 -0.824 1.00 20.72 S
ANISOU 2954 SD MET A 430 2583 2732 2558 370 -65 -96 S
ATOM 2955 CE MET A 430 24.229 14.753 0.215 1.00 17.89 C
ANISOU 2955 CE MET A 430 2200 2379 2217 421 -45 -111 C
ATOM 2956 N TYR A 431 27.083 13.449 -6.548 1.00 18.71 N
ANISOU 2956 N TYR A 431 2452 2453 2204 387 -142 -6 N
ATOM 2957 CA TYR A 431 28.244 13.146 -7.375 1.00 17.95 C
ANISOU 2957 CA TYR A 431 2396 2341 2082 369 -134 7 C
ATOM 2958 C TYR A 431 27.907 13.251 -8.866 1.00 23.18 C
ANISOU 2958 C TYR A 431 3078 3028 2703 404 -161 31 C
ATOM 2959 O TYR A 431 27.600 12.247 -9.518 1.00 29.68 O
ANISOU 2959 O TYR A 431 3888 3890 3498 395 -191 15 O
ATOM 2960 CB TYR A 431 28.775 11.752 -7.038 1.00 16.93 C
ANISOU 2960 CB TYR A 431 2254 2227 1953 318 -133 -20 C
ATOM 2961 CG TYR A 431 29.507 11.695 -5.714 1.00 18.97 C
ANISOU 2961 CG TYR A 431 2509 2458 2242 284 -102 -34 C
ATOM 2962 CD1 TYR A 431 28.804 11.691 -4.511 1.00 13.28 C
ANISOU 2962 CD1 TYR A 431 1754 1746 1546 280 -98 -53 C
ATOM 2963 CD2 TYR A 431 30.907 11.644 -5.664 1.00 15.11 C
ANISOU 2963 CD2 TYR A 431 2049 1937 1754 257 -76 -29 C
ATOM 2964 CE1 TYR A 431 29.456 11.653 -3.299 1.00 14.43 C
ANISOU 2964 CE1 TYR A 431 1899 1872 1710 253 -73 -67 C
ATOM 2965 CE2 TYR A 431 31.578 11.599 -4.443 1.00 18.32 C
ANISOU 2965 CE2 TYR A 431 2451 2324 2186 228 -54 -44 C
ATOM 2966 CZ TYR A 431 30.843 11.606 -3.266 1.00 19.87 C
ANISOU 2966 CZ TYR A 431 2618 2532 2401 227 -55 -63 C
ATOM 2967 OH TYR A 431 31.479 11.563 -2.055 1.00 15.21 O
ANISOU 2967 OH TYR A 431 2026 1927 1828 203 -36 -78 O
ATOM 2968 N PRO A 432 27.955 14.473 -9.415 1.00 19.81 N
ANISOU 2968 N PRO A 432 2683 2576 2269 446 -153 69 N
ATOM 2969 CA PRO A 432 27.583 14.686 -10.824 1.00 13.25 C
ANISOU 2969 CA PRO A 432 1873 1770 1391 488 -180 98 C
ATOM 2970 C PRO A 432 28.394 13.846 -11.805 1.00 16.08 C
ANISOU 2970 C PRO A 432 2259 2147 1702 470 -180 99 C
ATOM 2971 O PRO A 432 27.982 13.701 -12.958 1.00 18.74 O
ANISOU 2971 O PRO A 432 2608 2520 1990 501 -211 110 O
ATOM 2972 CB PRO A 432 27.838 16.182 -11.045 1.00 10.77 C
ANISOU 2972 CB PRO A 432 1598 1409 1086 527 -155 145 C
ATOM 2973 CG PRO A 432 28.513 16.671 -9.796 1.00 19.45 C
ANISOU 2973 CG PRO A 432 2698 2453 2238 497 -116 133 C
ATOM 2974 CD PRO A 432 28.189 15.735 -8.698 1.00 18.09 C
ANISOU 2974 CD PRO A 432 2480 2305 2088 460 -123 84 C
ATOM 2975 N ARG A 433 29.511 13.286 -11.353 1.00 13.83 N
ANISOU 2975 N ARG A 433 1984 1841 1431 423 -148 84 N
ATOM 2976 CA ARG A 433 30.331 12.437 -12.218 1.00 18.89 C
ANISOU 2976 CA ARG A 433 2648 2497 2030 408 -144 81 C
ATOM 2977 C ARG A 433 30.057 10.942 -12.031 1.00 20.33 C
ANISOU 2977 C ARG A 433 2802 2714 2211 374 -171 31 C
ATOM 2978 O ARG A 433 30.736 10.108 -12.624 1.00 16.29 O
ANISOU 2978 O ARG A 433 2308 2212 1670 360 -168 18 O
ATOM 2979 CB ARG A 433 31.815 12.755 -12.058 1.00 10.21 C
ANISOU 2979 CB ARG A 433 1579 1355 945 383 -91 102 C
ATOM 2980 CG ARG A 433 32.162 14.155 -12.540 1.00 14.82 C
ANISOU 2980 CG ARG A 433 2200 1905 1528 414 -63 157 C
ATOM 2981 CD ARG A 433 33.631 14.481 -12.400 1.00 12.53 C
ANISOU 2981 CD ARG A 433 1930 1571 1258 384 -11 178 C
ATOM 2982 NE ARG A 433 34.452 13.641 -13.257 1.00 24.50 N
ANISOU 2982 NE ARG A 433 3464 3113 2732 375 3 179 N
ATOM 2983 CZ ARG A 433 35.771 13.521 -13.132 1.00 25.72 C
ANISOU 2983 CZ ARG A 433 3625 3245 2903 344 46 187 C
ATOM 2984 NH1 ARG A 433 36.407 14.200 -12.185 1.00 24.68 N
ANISOU 2984 NH1 ARG A 433 3484 3063 2830 315 73 194 N
ATOM 2985 NH2 ARG A 433 36.454 12.721 -13.947 1.00 18.87 N
ANISOU 2985 NH2 ARG A 433 2771 2405 1993 342 60 185 N
ATOM 2986 N VAL A 434 29.028 10.616 -11.250 1.00 15.05 N
ANISOU 2986 N VAL A 434 2087 2060 1573 365 -197 4 N
ATOM 2987 CA VAL A 434 28.698 9.218 -10.976 1.00 18.72 C
ANISOU 2987 CA VAL A 434 2518 2548 2045 329 -222 -40 C
ATOM 2988 C VAL A 434 28.370 8.370 -12.217 1.00 23.53 C
ANISOU 2988 C VAL A 434 3137 3197 2608 339 -264 -60 C
ATOM 2989 O VAL A 434 28.793 7.218 -12.295 1.00 27.39 O
ANISOU 2989 O VAL A 434 3626 3687 3093 307 -267 -91 O
ATOM 2990 CB VAL A 434 27.598 9.065 -9.898 1.00 18.36 C
ANISOU 2990 CB VAL A 434 2417 2513 2044 316 -237 -58 C
ATOM 2991 CG1 VAL A 434 26.229 9.483 -10.434 1.00 8.70 C
ANISOU 2991 CG1 VAL A 434 1168 1328 811 356 -280 -55 C
ATOM 2992 CG2 VAL A 434 27.564 7.636 -9.386 1.00 13.42 C
ANISOU 2992 CG2 VAL A 434 1763 1895 1440 268 -246 -95 C
ATOM 2993 N ASP A 435 27.651 8.921 -13.195 1.00 26.33 N
ANISOU 2993 N ASP A 435 3499 3581 2923 384 -296 -45 N
ATOM 2994 CA ASP A 435 27.352 8.143 -14.412 1.00 25.10 C
ANISOU 2994 CA ASP A 435 3355 3467 2714 397 -341 -69 C
ATOM 2995 C ASP A 435 28.609 7.873 -15.248 1.00 19.77 C
ANISOU 2995 C ASP A 435 2736 2785 1991 400 -313 -63 C
ATOM 2996 O ASP A 435 28.752 6.811 -15.844 1.00 24.24 O
ANISOU 2996 O ASP A 435 3312 3370 2528 388 -335 -101 O
ATOM 2997 CB ASP A 435 26.261 8.805 -15.266 1.00 23.42 C
ANISOU 2997 CB ASP A 435 3137 3296 2466 450 -389 -53 C
ATOM 2998 CG ASP A 435 24.882 8.805 -14.580 1.00 31.75 C
ANISOU 2998 CG ASP A 435 4125 4370 3567 447 -426 -70 C
ATOM 2999 OD1 ASP A 435 24.599 7.914 -13.756 1.00 30.35 O
ANISOU 2999 OD1 ASP A 435 3905 4190 3436 400 -430 -105 O
ATOM 3000 OD2 ASP A 435 24.066 9.696 -14.875 1.00 37.14 O
ANISOU 3000 OD2 ASP A 435 4796 5074 4241 494 -449 -44 O
ATOM 3001 N GLU A 436 29.515 8.839 -15.293 1.00 21.04 N
ANISOU 3001 N GLU A 436 2932 2917 2145 415 -263 -16 N
ATOM 3002 CA GLU A 436 30.823 8.637 -15.907 1.00 18.99 C
ANISOU 3002 CA GLU A 436 2718 2647 1851 413 -223 -5 C
ATOM 3003 C GLU A 436 31.525 7.478 -15.199 1.00 15.22 C
ANISOU 3003 C GLU A 436 2225 2149 1408 363 -207 -45 C
ATOM 3004 O GLU A 436 31.992 6.534 -15.835 1.00 17.55 O
ANISOU 3004 O GLU A 436 2539 2458 1670 359 -210 -73 O
ATOM 3005 CB GLU A 436 31.647 9.928 -15.795 1.00 16.32 C
ANISOU 3005 CB GLU A 436 2407 2272 1523 427 -168 54 C
ATOM 3006 CG GLU A 436 33.107 9.812 -16.168 1.00 24.44 C
ANISOU 3006 CG GLU A 436 3469 3283 2534 416 -115 72 C
ATOM 3007 CD GLU A 436 33.920 11.017 -15.709 1.00 27.05 C
ANISOU 3007 CD GLU A 436 3811 3565 2902 411 -61 123 C
ATOM 3008 OE1 GLU A 436 33.323 12.080 -15.448 1.00 26.72 O
ANISOU 3008 OE1 GLU A 436 3767 3506 2881 430 -66 153 O
ATOM 3009 OE2 GLU A 436 35.160 10.903 -15.602 1.00 29.15 O
ANISOU 3009 OE2 GLU A 436 4086 3809 3180 388 -14 133 O
ATOM 3010 N TRP A 437 31.576 7.553 -13.872 1.00 15.04 N
ANISOU 3010 N TRP A 437 2170 2095 1449 329 -189 -47 N
ATOM 3011 CA TRP A 437 32.210 6.510 -13.068 1.00 19.03 C
ANISOU 3011 CA TRP A 437 2659 2579 1991 284 -174 -78 C
ATOM 3012 C TRP A 437 31.573 5.128 -13.313 1.00 21.99 C
ANISOU 3012 C TRP A 437 3018 2977 2361 267 -218 -130 C
ATOM 3013 O TRP A 437 32.278 4.147 -13.577 1.00 21.08 O
ANISOU 3013 O TRP A 437 2918 2856 2237 252 -211 -155 O
ATOM 3014 CB TRP A 437 32.194 6.870 -11.577 1.00 13.44 C
ANISOU 3014 CB TRP A 437 1919 1841 1345 255 -154 -72 C
ATOM 3015 CG TRP A 437 32.868 5.829 -10.749 1.00 18.64 C
ANISOU 3015 CG TRP A 437 2565 2481 2038 214 -140 -96 C
ATOM 3016 CD1 TRP A 437 34.193 5.767 -10.431 1.00 17.64 C
ANISOU 3016 CD1 TRP A 437 2452 2328 1923 198 -99 -87 C
ATOM 3017 CD2 TRP A 437 32.261 4.671 -10.165 1.00 18.09 C
ANISOU 3017 CD2 TRP A 437 2463 2416 1994 184 -165 -132 C
ATOM 3018 NE1 TRP A 437 34.450 4.651 -9.678 1.00 13.19 N
ANISOU 3018 NE1 TRP A 437 1870 1754 1389 165 -100 -113 N
ATOM 3019 CE2 TRP A 437 33.282 3.956 -9.505 1.00 13.08 C
ANISOU 3019 CE2 TRP A 437 1830 1756 1385 154 -139 -139 C
ATOM 3020 CE3 TRP A 437 30.954 4.172 -10.134 1.00 7.31 C
ANISOU 3020 CE3 TRP A 437 1066 1074 639 178 -208 -155 C
ATOM 3021 CZ2 TRP A 437 33.040 2.774 -8.821 1.00 6.64 C
ANISOU 3021 CZ2 TRP A 437 989 933 600 122 -152 -165 C
ATOM 3022 CZ3 TRP A 437 30.717 2.998 -9.456 1.00 13.72 C
ANISOU 3022 CZ3 TRP A 437 1850 1878 1486 140 -219 -182 C
ATOM 3023 CH2 TRP A 437 31.754 2.315 -8.803 1.00 13.97 C
ANISOU 3023 CH2 TRP A 437 1889 1880 1539 113 -190 -185 C
ATOM 3024 N ILE A 438 30.249 5.062 -13.242 1.00 17.12 N
ANISOU 3024 N ILE A 438 2368 2383 1753 270 -264 -145 N
ATOM 3025 CA ILE A 438 29.530 3.820 -13.501 1.00 19.77 C
ANISOU 3025 CA ILE A 438 2682 2738 2091 250 -312 -194 C
ATOM 3026 C ILE A 438 29.878 3.247 -14.882 1.00 24.81 C
ANISOU 3026 C ILE A 438 3362 3399 2667 272 -332 -220 C
ATOM 3027 O ILE A 438 30.050 2.038 -15.039 1.00 24.42 O
ANISOU 3027 O ILE A 438 3316 3343 2621 248 -347 -263 O
ATOM 3028 CB ILE A 438 27.999 4.016 -13.350 1.00 18.31 C
ANISOU 3028 CB ILE A 438 2450 2582 1925 254 -360 -202 C
ATOM 3029 CG1 ILE A 438 27.621 4.112 -11.865 1.00 18.14 C
ANISOU 3029 CG1 ILE A 438 2381 2540 1970 223 -340 -193 C
ATOM 3030 CG2 ILE A 438 27.213 2.883 -14.047 1.00 10.57 C
ANISOU 3030 CG2 ILE A 438 1454 1629 934 242 -421 -254 C
ATOM 3031 CD1 ILE A 438 26.171 4.554 -11.624 1.00 15.39 C
ANISOU 3031 CD1 ILE A 438 1982 2222 1643 235 -375 -191 C
ATOM 3032 N SER A 439 30.019 4.121 -15.873 1.00 17.11 N
ANISOU 3032 N SER A 439 2423 2447 1632 319 -329 -191 N
ATOM 3033 CA SER A 439 30.391 3.695 -17.218 1.00 14.65 C
ANISOU 3033 CA SER A 439 2147 2153 1267 337 -331 -204 C
ATOM 3034 C SER A 439 31.739 2.990 -17.237 1.00 24.78 C
ANISOU 3034 C SER A 439 3458 3411 2545 323 -288 -216 C
ATOM 3035 O SER A 439 31.906 1.974 -17.909 1.00 24.20 O
ANISOU 3035 O SER A 439 3395 3340 2461 315 -298 -254 O
ATOM 3036 CB SER A 439 30.462 4.891 -18.162 1.00 21.39 C
ANISOU 3036 CB SER A 439 3031 3026 2069 386 -317 -154 C
ATOM 3037 OG SER A 439 29.384 4.862 -19.060 1.00 37.92 O
ANISOU 3037 OG SER A 439 5113 5155 4139 404 -366 -167 O
ATOM 3038 N VAL A 440 32.707 3.556 -16.520 1.00 21.40 N
ANISOU 3038 N VAL A 440 3042 2958 2132 321 -237 -183 N
ATOM 3039 CA VAL A 440 34.024 2.941 -16.413 1.00 20.75 C
ANISOU 3039 CA VAL A 440 2977 2851 2055 307 -192 -190 C
ATOM 3040 C VAL A 440 33.901 1.588 -15.722 1.00 22.24 C
ANISOU 3040 C VAL A 440 3141 3018 2293 266 -212 -241 C
ATOM 3041 O VAL A 440 34.492 0.604 -16.162 1.00 22.58 O
ANISOU 3041 O VAL A 440 3201 3053 2324 264 -206 -274 O
ATOM 3042 CB VAL A 440 35.021 3.854 -15.675 1.00 12.49 C
ANISOU 3042 CB VAL A 440 1928 1774 1044 298 -131 -139 C
ATOM 3043 CG1 VAL A 440 36.404 3.221 -15.632 1.00 9.13 C
ANISOU 3043 CG1 VAL A 440 1515 1329 625 287 -85 -146 C
ATOM 3044 CG2 VAL A 440 35.077 5.205 -16.366 1.00 13.66 C
ANISOU 3044 CG2 VAL A 440 2102 1936 1151 335 -111 -85 C
ATOM 3045 N ARG A 441 33.090 1.531 -14.670 1.00 22.64 N
ANISOU 3045 N ARG A 441 3147 3054 2400 234 -233 -244 N
ATOM 3046 CA ARG A 441 32.907 0.291 -13.933 1.00 19.32 C
ANISOU 3046 CA ARG A 441 2701 2608 2030 193 -249 -282 C
ATOM 3047 C ARG A 441 32.285 -0.806 -14.795 1.00 22.70 C
ANISOU 3047 C ARG A 441 3138 3051 2437 193 -301 -339 C
ATOM 3048 O ARG A 441 32.640 -1.983 -14.673 1.00 29.24 O
ANISOU 3048 O ARG A 441 3968 3851 3290 169 -301 -373 O
ATOM 3049 CB ARG A 441 32.074 0.523 -12.679 1.00 24.68 C
ANISOU 3049 CB ARG A 441 3331 3277 2768 162 -258 -268 C
ATOM 3050 CG ARG A 441 31.337 -0.709 -12.224 1.00 31.66 C
ANISOU 3050 CG ARG A 441 4185 4149 3696 124 -293 -307 C
ATOM 3051 CD ARG A 441 30.935 -0.636 -10.783 1.00 27.70 C
ANISOU 3051 CD ARG A 441 3640 3630 3255 91 -279 -286 C
ATOM 3052 NE ARG A 441 30.061 -1.752 -10.456 1.00 37.40 N
ANISOU 3052 NE ARG A 441 4834 4850 4525 54 -314 -317 N
ATOM 3053 CZ ARG A 441 30.467 -3.012 -10.300 1.00 37.46 C
ANISOU 3053 CZ ARG A 441 4849 4825 4561 26 -314 -344 C
ATOM 3054 NH1 ARG A 441 31.741 -3.332 -10.439 1.00 25.53 N
ANISOU 3054 NH1 ARG A 441 3375 3290 3036 36 -283 -344 N
ATOM 3055 NH2 ARG A 441 29.589 -3.956 -9.993 1.00 46.36 N
ANISOU 3055 NH2 ARG A 441 5943 5939 5732 -11 -345 -367 N
ATOM 3056 N ARG A 442 31.366 -0.413 -15.669 1.00 21.22 N
ANISOU 3056 N ARG A 442 2946 2898 2217 212 -336 -340 N
ATOM 3057 CA ARG A 442 30.758 -1.342 -16.619 1.00 29.39 C
ANISOU 3057 CA ARG A 442 3981 3943 3243 206 -376 -382 C
ATOM 3058 C ARG A 442 31.778 -1.896 -17.620 1.00 26.39 C
ANISOU 3058 C ARG A 442 3645 3560 2822 225 -350 -397 C
ATOM 3059 O ARG A 442 31.759 -3.081 -17.909 1.00 25.07 O
ANISOU 3059 O ARG A 442 3481 3375 2668 206 -367 -441 O
ATOM 3060 CB ARG A 442 29.588 -0.680 -17.367 1.00 33.61 C
ANISOU 3060 CB ARG A 442 4502 4520 3749 228 -418 -374 C
ATOM 3061 CG ARG A 442 28.466 -0.152 -16.463 1.00 35.00 C
ANISOU 3061 CG ARG A 442 4628 4706 3966 214 -445 -361 C
ATOM 3062 CD ARG A 442 27.352 -1.150 -16.276 1.00 30.89 C
ANISOU 3062 CD ARG A 442 4063 4183 3493 174 -494 -401 C
ATOM 3063 NE ARG A 442 26.258 -0.616 -15.471 1.00 28.05 N
ANISOU 3063 NE ARG A 442 3647 3838 3172 163 -516 -386 N
ATOM 3064 CZ ARG A 442 26.077 -0.905 -14.184 1.00 40.71 C
ANISOU 3064 CZ ARG A 442 5212 5421 4836 127 -509 -386 C
ATOM 3065 NH1 ARG A 442 26.926 -1.727 -13.562 1.00 36.87 N
ANISOU 3065 NH1 ARG A 442 4739 4892 4377 97 -481 -400 N
ATOM 3066 NH2 ARG A 442 25.052 -0.375 -13.520 1.00 36.08 N
ANISOU 3066 NH2 ARG A 442 4571 4855 4282 123 -526 -371 N
ATOM 3067 N LYS A 443 32.662 -1.049 -18.148 1.00 20.89 N
ANISOU 3067 N LYS A 443 2982 2878 2078 262 -309 -361 N
ATOM 3068 CA LYS A 443 33.704 -1.535 -19.047 1.00 24.02 C
ANISOU 3068 CA LYS A 443 3415 3274 2436 282 -277 -372 C
ATOM 3069 C LYS A 443 34.537 -2.614 -18.364 1.00 26.19 C
ANISOU 3069 C LYS A 443 3689 3507 2755 256 -254 -399 C
ATOM 3070 O LYS A 443 34.843 -3.640 -18.968 1.00 33.66 O
ANISOU 3070 O LYS A 443 4652 4444 3695 256 -257 -438 O
ATOM 3071 CB LYS A 443 34.631 -0.413 -19.529 1.00 31.10 C
ANISOU 3071 CB LYS A 443 4342 4189 3287 320 -225 -319 C
ATOM 3072 CG LYS A 443 34.051 0.514 -20.599 1.00 41.55 C
ANISOU 3072 CG LYS A 443 5679 5553 4553 356 -241 -292 C
ATOM 3073 CD LYS A 443 34.969 1.726 -20.832 1.00 53.00 C
ANISOU 3073 CD LYS A 443 7154 7011 5973 386 -183 -229 C
ATOM 3074 CE LYS A 443 34.248 2.862 -21.562 1.00 63.96 C
ANISOU 3074 CE LYS A 443 8551 8431 7319 420 -199 -189 C
ATOM 3075 NZ LYS A 443 34.500 4.208 -20.943 1.00 64.07 N
ANISOU 3075 NZ LYS A 443 8565 8432 7346 429 -165 -126 N
ATOM 3076 N VAL A 444 34.878 -2.392 -17.097 1.00 19.25 N
ANISOU 3076 N VAL A 444 2793 2602 1921 235 -233 -379 N
ATOM 3077 CA VAL A 444 35.866 -3.230 -16.435 1.00 18.82 C
ANISOU 3077 CA VAL A 444 2740 2508 1903 220 -202 -393 C
ATOM 3078 C VAL A 444 35.270 -4.450 -15.706 1.00 21.84 C
ANISOU 3078 C VAL A 444 3098 2854 2346 178 -237 -433 C
ATOM 3079 O VAL A 444 35.944 -5.455 -15.511 1.00 22.01 O
ANISOU 3079 O VAL A 444 3127 2841 2394 169 -222 -455 O
ATOM 3080 CB VAL A 444 36.746 -2.392 -15.482 1.00 19.14 C
ANISOU 3080 CB VAL A 444 2778 2538 1958 222 -155 -350 C
ATOM 3081 CG1 VAL A 444 36.024 -2.127 -14.172 1.00 21.39 C
ANISOU 3081 CG1 VAL A 444 3022 2805 2300 186 -172 -333 C
ATOM 3082 CG2 VAL A 444 38.068 -3.102 -15.228 1.00 23.01 C
ANISOU 3082 CG2 VAL A 444 3278 2999 2466 224 -113 -357 C
ATOM 3083 N ASP A 445 34.001 -4.366 -15.328 1.00 13.65 N
ANISOU 3083 N ASP A 445 2031 1823 1333 154 -281 -439 N
ATOM 3084 CA ASP A 445 33.351 -5.441 -14.601 1.00 15.36 C
ANISOU 3084 CA ASP A 445 2219 2004 1612 110 -311 -468 C
ATOM 3085 C ASP A 445 31.931 -5.680 -15.150 1.00 22.44 C
ANISOU 3085 C ASP A 445 3094 2922 2512 94 -366 -493 C
ATOM 3086 O ASP A 445 30.928 -5.440 -14.464 1.00 19.97 O
ANISOU 3086 O ASP A 445 2740 2614 2233 69 -393 -485 O
ATOM 3087 CB ASP A 445 33.327 -5.114 -13.105 1.00 10.62 C
ANISOU 3087 CB ASP A 445 1590 1384 1061 85 -299 -442 C
ATOM 3088 CG ASP A 445 32.739 -6.227 -12.273 1.00 18.91 C
ANISOU 3088 CG ASP A 445 2609 2394 2181 37 -321 -462 C
ATOM 3089 OD1 ASP A 445 32.645 -7.360 -12.799 1.00 18.33 O
ANISOU 3089 OD1 ASP A 445 2545 2297 2121 24 -338 -498 O
ATOM 3090 OD2 ASP A 445 32.375 -5.976 -11.095 1.00 16.63 O
ANISOU 3090 OD2 ASP A 445 2283 2098 1939 9 -308 -425 O
ATOM 3091 N PRO A 446 31.847 -6.160 -16.399 1.00 24.01 N
ANISOU 3091 N PRO A 446 3316 3133 2673 110 -384 -524 N
ATOM 3092 CA PRO A 446 30.543 -6.316 -17.055 1.00 23.70 C
ANISOU 3092 CA PRO A 446 3258 3119 2628 100 -439 -549 C
ATOM 3093 C PRO A 446 29.631 -7.312 -16.338 1.00 25.75 C
ANISOU 3093 C PRO A 446 3477 3345 2960 46 -473 -575 C
ATOM 3094 O PRO A 446 28.416 -7.175 -16.406 1.00 23.90 O
ANISOU 3094 O PRO A 446 3208 3133 2741 30 -514 -580 O
ATOM 3095 CB PRO A 446 30.909 -6.823 -18.464 1.00 21.15 C
ANISOU 3095 CB PRO A 446 2976 2808 2251 128 -445 -583 C
ATOM 3096 CG PRO A 446 32.275 -7.438 -18.316 1.00 26.18 C
ANISOU 3096 CG PRO A 446 3644 3410 2893 135 -398 -589 C
ATOM 3097 CD PRO A 446 32.964 -6.605 -17.258 1.00 27.53 C
ANISOU 3097 CD PRO A 446 3806 3574 3080 139 -354 -540 C
ATOM 3098 N LEU A 447 30.202 -8.289 -15.647 1.00 26.66 N
ANISOU 3098 N LEU A 447 3596 3408 3125 19 -453 -586 N
ATOM 3099 CA LEU A 447 29.385 -9.293 -14.975 1.00 24.76 C
ANISOU 3099 CA LEU A 447 3321 3130 2958 -34 -479 -604 C
ATOM 3100 C LEU A 447 29.090 -8.928 -13.532 1.00 29.16 C
ANISOU 3100 C LEU A 447 3835 3675 3569 -63 -466 -567 C
ATOM 3101 O LEU A 447 28.430 -9.691 -12.822 1.00 31.67 O
ANISOU 3101 O LEU A 447 4118 3962 3952 -111 -480 -571 O
ATOM 3102 CB LEU A 447 30.074 -10.653 -15.025 1.00 28.25 C
ANISOU 3102 CB LEU A 447 3790 3516 3428 -48 -467 -636 C
ATOM 3103 CG LEU A 447 30.328 -11.217 -16.426 1.00 36.79 C
ANISOU 3103 CG LEU A 447 4912 4604 4463 -23 -481 -682 C
ATOM 3104 CD1 LEU A 447 31.100 -12.520 -16.327 1.00 36.37 C
ANISOU 3104 CD1 LEU A 447 4885 4491 4443 -33 -463 -709 C
ATOM 3105 CD2 LEU A 447 29.005 -11.416 -17.170 1.00 30.73 C
ANISOU 3105 CD2 LEU A 447 4124 3861 3691 -41 -539 -714 C
ATOM 3106 N ARG A 448 29.584 -7.770 -13.101 1.00 22.17 N
ANISOU 3106 N ARG A 448 2954 2815 2657 -36 -438 -530 N
ATOM 3107 CA ARG A 448 29.423 -7.342 -11.711 1.00 26.07 C
ANISOU 3107 CA ARG A 448 3411 3301 3195 -58 -423 -496 C
ATOM 3108 C ARG A 448 30.002 -8.403 -10.773 1.00 25.55 C
ANISOU 3108 C ARG A 448 3346 3174 3188 -91 -401 -496 C
ATOM 3109 O ARG A 448 29.355 -8.847 -9.824 1.00 22.18 O
ANISOU 3109 O ARG A 448 2878 2725 2823 -134 -407 -485 O
ATOM 3110 CB ARG A 448 27.948 -7.066 -11.390 1.00 29.03 C
ANISOU 3110 CB ARG A 448 3728 3702 3601 -85 -458 -491 C
ATOM 3111 CG ARG A 448 27.268 -6.080 -12.347 1.00 35.54 C
ANISOU 3111 CG ARG A 448 4548 4584 4370 -50 -486 -490 C
ATOM 3112 CD ARG A 448 25.759 -6.131 -12.199 1.00 44.47 C
ANISOU 3112 CD ARG A 448 5619 5737 5541 -78 -526 -493 C
ATOM 3113 NE ARG A 448 25.118 -4.861 -12.531 1.00 57.21 N
ANISOU 3113 NE ARG A 448 7214 7406 7116 -42 -542 -473 N
ATOM 3114 CZ ARG A 448 23.881 -4.529 -12.155 1.00 57.88 C
ANISOU 3114 CZ ARG A 448 7239 7520 7235 -56 -566 -462 C
ATOM 3115 NH1 ARG A 448 23.152 -5.381 -11.434 1.00 55.73 N
ANISOU 3115 NH1 ARG A 448 6916 7226 7032 -110 -574 -469 N
ATOM 3116 NH2 ARG A 448 23.372 -3.347 -12.496 1.00 46.27 N
ANISOU 3116 NH2 ARG A 448 5756 6097 5728 -15 -578 -442 N
ATOM 3117 N VAL A 449 31.221 -8.832 -11.075 1.00 20.36 N
ANISOU 3117 N VAL A 449 2733 2491 2512 -69 -373 -505 N
ATOM 3118 CA VAL A 449 31.971 -9.695 -10.177 1.00 19.15 C
ANISOU 3118 CA VAL A 449 2587 2281 2409 -88 -348 -497 C
ATOM 3119 C VAL A 449 32.240 -8.957 -8.851 1.00 25.66 C
ANISOU 3119 C VAL A 449 3385 3113 3251 -94 -304 -431 C
ATOM 3120 O VAL A 449 32.283 -9.567 -7.778 1.00 19.44 O
ANISOU 3120 O VAL A 449 2580 2291 2516 -124 -287 -405 O
ATOM 3121 CB VAL A 449 33.298 -10.138 -10.828 1.00 24.06 C
ANISOU 3121 CB VAL A 449 3258 2884 3000 -52 -320 -513 C
ATOM 3122 CG1 VAL A 449 34.268 -10.683 -9.803 1.00 25.20 C
ANISOU 3122 CG1 VAL A 449 3407 2980 3187 -58 -285 -489 C
ATOM 3123 CG2 VAL A 449 33.037 -11.166 -11.921 1.00 24.55 C
ANISOU 3123 CG2 VAL A 449 3339 2932 3057 -54 -343 -558 C
ATOM 3124 N PHE A 450 32.405 -7.639 -8.926 1.00 17.45 N
ANISOU 3124 N PHE A 450 2345 2120 2166 -65 -286 -403 N
ATOM 3125 CA PHE A 450 32.603 -6.859 -7.716 1.00 12.42 C
ANISOU 3125 CA PHE A 450 1684 1492 1541 -69 -250 -349 C
ATOM 3126 C PHE A 450 31.338 -6.180 -7.220 1.00 17.45 C
ANISOU 3126 C PHE A 450 2278 2162 2192 -86 -264 -330 C
ATOM 3127 O PHE A 450 30.639 -5.520 -7.977 1.00 23.71 O
ANISOU 3127 O PHE A 450 3065 2990 2955 -70 -290 -343 O
ATOM 3128 CB PHE A 450 33.786 -5.916 -7.885 1.00 10.71 C
ANISOU 3128 CB PHE A 450 1494 1292 1282 -31 -214 -326 C
ATOM 3129 CG PHE A 450 35.036 -6.650 -8.243 1.00 16.00 C
ANISOU 3129 CG PHE A 450 2199 1933 1948 -15 -195 -342 C
ATOM 3130 CD1 PHE A 450 35.737 -7.346 -7.273 1.00 10.28 C
ANISOU 3130 CD1 PHE A 450 1471 1173 1263 -29 -172 -323 C
ATOM 3131 CD2 PHE A 450 35.466 -6.717 -9.562 1.00 14.32 C
ANISOU 3131 CD2 PHE A 450 2022 1730 1690 16 -201 -375 C
ATOM 3132 CE1 PHE A 450 36.868 -8.052 -7.602 1.00 20.32 C
ANISOU 3132 CE1 PHE A 450 2770 2417 2535 -9 -156 -337 C
ATOM 3133 CE2 PHE A 450 36.598 -7.425 -9.901 1.00 11.50 C
ANISOU 3133 CE2 PHE A 450 1693 1347 1329 35 -181 -392 C
ATOM 3134 CZ PHE A 450 37.302 -8.093 -8.927 1.00 18.73 C
ANISOU 3134 CZ PHE A 450 2602 2226 2290 23 -158 -373 C
ATOM 3135 N ALA A 451 31.035 -6.393 -5.944 1.00 20.37 N
ANISOU 3135 N ALA A 451 2616 2519 2605 -115 -246 -298 N
ATOM 3136 CA ALA A 451 29.793 -5.897 -5.356 1.00 18.77 C
ANISOU 3136 CA ALA A 451 2365 2345 2420 -131 -253 -280 C
ATOM 3137 C ALA A 451 29.912 -5.789 -3.843 1.00 15.80 C
ANISOU 3137 C ALA A 451 1969 1965 2070 -146 -214 -235 C
ATOM 3138 O ALA A 451 30.653 -6.539 -3.215 1.00 18.70 O
ANISOU 3138 O ALA A 451 2350 2298 2458 -158 -194 -221 O
ATOM 3139 CB ALA A 451 28.648 -6.805 -5.719 1.00 18.66 C
ANISOU 3139 CB ALA A 451 2321 2323 2445 -167 -293 -309 C
ATOM 3140 N SER A 452 29.177 -4.851 -3.265 1.00 14.66 N
ANISOU 3140 N SER A 452 1793 1857 1922 -141 -205 -212 N
ATOM 3141 CA SER A 452 29.207 -4.621 -1.828 1.00 13.38 C
ANISOU 3141 CA SER A 452 1612 1699 1772 -149 -168 -172 C
ATOM 3142 C SER A 452 27.818 -4.189 -1.406 1.00 16.57 C
ANISOU 3142 C SER A 452 1965 2139 2192 -158 -171 -162 C
ATOM 3143 O SER A 452 26.993 -3.851 -2.252 1.00 18.12 O
ANISOU 3143 O SER A 452 2142 2358 2384 -151 -202 -183 O
ATOM 3144 CB SER A 452 30.195 -3.512 -1.495 1.00 11.55 C
ANISOU 3144 CB SER A 452 1407 1479 1501 -115 -142 -157 C
ATOM 3145 OG SER A 452 29.792 -2.288 -2.101 1.00 15.14 O
ANISOU 3145 OG SER A 452 1860 1965 1927 -85 -151 -164 O
ATOM 3146 N ASP A 453 27.555 -4.200 -0.106 1.00 15.09 N
ANISOU 3146 N ASP A 453 1753 1960 2022 -171 -139 -128 N
ATOM 3147 CA ASP A 453 26.284 -3.695 0.398 1.00 17.42 C
ANISOU 3147 CA ASP A 453 1996 2294 2329 -173 -132 -114 C
ATOM 3148 C ASP A 453 26.064 -2.257 -0.059 1.00 15.41 C
ANISOU 3148 C ASP A 453 1743 2074 2038 -130 -139 -125 C
ATOM 3149 O ASP A 453 24.965 -1.884 -0.474 1.00 17.22 O
ANISOU 3149 O ASP A 453 1935 2333 2276 -124 -159 -134 O
ATOM 3150 CB ASP A 453 26.239 -3.770 1.926 1.00 12.69 C
ANISOU 3150 CB ASP A 453 1382 1704 1738 -182 -88 -74 C
ATOM 3151 CG ASP A 453 26.040 -5.172 2.430 1.00 16.72 C
ANISOU 3151 CG ASP A 453 1875 2185 2293 -228 -79 -54 C
ATOM 3152 OD1 ASP A 453 26.019 -6.113 1.604 1.00 15.76 O
ANISOU 3152 OD1 ASP A 453 1758 2029 2201 -254 -109 -76 O
ATOM 3153 OD2 ASP A 453 25.919 -5.328 3.661 1.00 21.83 O
ANISOU 3153 OD2 ASP A 453 2508 2842 2944 -236 -42 -16 O
ATOM 3154 N MET A 454 27.128 -1.463 0.034 1.00 9.46 N
ANISOU 3154 N MET A 454 1032 1314 1247 -100 -123 -122 N
ATOM 3155 CA MET A 454 27.123 -0.072 -0.394 1.00 14.37 C
ANISOU 3155 CA MET A 454 1667 1957 1837 -58 -126 -128 C
ATOM 3156 C MET A 454 26.707 0.059 -1.873 1.00 17.05 C
ANISOU 3156 C MET A 454 2009 2303 2167 -45 -167 -153 C
ATOM 3157 O MET A 454 25.816 0.851 -2.195 1.00 16.51 O
ANISOU 3157 O MET A 454 1916 2265 2093 -22 -181 -155 O
ATOM 3158 CB MET A 454 28.509 0.545 -0.139 1.00 11.22 C
ANISOU 3158 CB MET A 454 1315 1538 1410 -39 -105 -122 C
ATOM 3159 CG MET A 454 28.617 2.070 -0.333 1.00 18.05 C
ANISOU 3159 CG MET A 454 2195 2414 2248 1 -99 -122 C
ATOM 3160 SD MET A 454 28.786 2.582 -2.056 1.00 43.15 S
ANISOU 3160 SD MET A 454 5403 5591 5403 27 -129 -137 S
ATOM 3161 CE MET A 454 30.513 2.276 -2.356 1.00 24.13 C
ANISOU 3161 CE MET A 454 3043 3148 2979 22 -116 -138 C
ATOM 3162 N ALA A 455 27.343 -0.712 -2.760 1.00 11.68 N
ANISOU 3162 N ALA A 455 1358 1599 1482 -56 -188 -172 N
ATOM 3163 CA ALA A 455 27.035 -0.635 -4.185 1.00 13.85 C
ANISOU 3163 CA ALA A 455 1642 1884 1736 -40 -228 -198 C
ATOM 3164 C ALA A 455 25.539 -0.869 -4.466 1.00 19.55 C
ANISOU 3164 C ALA A 455 2310 2635 2482 -52 -263 -211 C
ATOM 3165 O ALA A 455 24.952 -0.193 -5.315 1.00 22.19 O
ANISOU 3165 O ALA A 455 2639 2998 2796 -23 -292 -220 O
ATOM 3166 CB ALA A 455 27.892 -1.613 -4.986 1.00 9.44 C
ANISOU 3166 CB ALA A 455 1122 1296 1169 -51 -241 -222 C
ATOM 3167 N ARG A 456 24.932 -1.810 -3.739 1.00 15.88 N
ANISOU 3167 N ARG A 456 1805 2164 2065 -94 -259 -207 N
ATOM 3168 CA ARG A 456 23.512 -2.126 -3.914 1.00 21.91 C
ANISOU 3168 CA ARG A 456 2507 2954 2863 -113 -290 -218 C
ATOM 3169 C ARG A 456 22.625 -1.021 -3.356 1.00 19.25 C
ANISOU 3169 C ARG A 456 2128 2660 2526 -86 -276 -196 C
ATOM 3170 O ARG A 456 21.662 -0.607 -4.001 1.00 22.67 O
ANISOU 3170 O ARG A 456 2526 3127 2961 -69 -310 -208 O
ATOM 3171 CB ARG A 456 23.149 -3.507 -3.329 1.00 16.45 C
ANISOU 3171 CB ARG A 456 1783 2237 2229 -171 -288 -217 C
ATOM 3172 CG ARG A 456 23.658 -4.682 -4.205 1.00 29.34 C
ANISOU 3172 CG ARG A 456 3449 3829 3871 -197 -321 -253 C
ATOM 3173 CD ARG A 456 23.298 -6.084 -3.655 1.00 22.98 C
ANISOU 3173 CD ARG A 456 2615 2987 3131 -257 -319 -250 C
ATOM 3174 NE ARG A 456 24.026 -6.338 -2.426 1.00 31.81 N
ANISOU 3174 NE ARG A 456 3749 4080 4259 -266 -265 -210 N
ATOM 3175 CZ ARG A 456 25.160 -7.028 -2.342 1.00 28.23 C
ANISOU 3175 CZ ARG A 456 3345 3580 3802 -271 -252 -210 C
ATOM 3176 NH1 ARG A 456 25.689 -7.593 -3.415 1.00 21.16 N
ANISOU 3176 NH1 ARG A 456 2487 2655 2898 -269 -285 -251 N
ATOM 3177 NH2 ARG A 456 25.753 -7.164 -1.166 1.00 28.34 N
ANISOU 3177 NH2 ARG A 456 3368 3579 3820 -275 -206 -169 N
ATOM 3178 N ARG A 457 22.975 -0.510 -2.183 1.00 16.13 N
ANISOU 3178 N ARG A 457 1737 2263 2127 -77 -226 -166 N
ATOM 3179 CA ARG A 457 22.189 0.545 -1.547 1.00 21.37 C
ANISOU 3179 CA ARG A 457 2365 2965 2791 -47 -206 -149 C
ATOM 3180 C ARG A 457 22.204 1.831 -2.384 1.00 25.80 C
ANISOU 3180 C ARG A 457 2948 3540 3313 8 -225 -156 C
ATOM 3181 O ARG A 457 21.170 2.463 -2.596 1.00 23.42 O
ANISOU 3181 O ARG A 457 2605 3274 3018 34 -240 -155 O
ATOM 3182 CB ARG A 457 22.697 0.800 -0.119 1.00 16.77 C
ANISOU 3182 CB ARG A 457 1793 2376 2204 -45 -150 -122 C
ATOM 3183 CG ARG A 457 21.964 1.880 0.652 1.00 12.66 C
ANISOU 3183 CG ARG A 457 1240 1890 1678 -10 -123 -108 C
ATOM 3184 CD ARG A 457 22.498 2.032 2.110 1.00 16.42 C
ANISOU 3184 CD ARG A 457 1732 2364 2143 -10 -70 -87 C
ATOM 3185 NE ARG A 457 23.954 2.196 2.185 1.00 20.09 N
ANISOU 3185 NE ARG A 457 2262 2793 2578 -5 -62 -90 N
ATOM 3186 CZ ARG A 457 24.590 3.367 2.116 1.00 22.41 C
ANISOU 3186 CZ ARG A 457 2595 3078 2841 33 -57 -96 C
ATOM 3187 NH1 ARG A 457 23.902 4.487 1.963 1.00 18.30 N
ANISOU 3187 NH1 ARG A 457 2060 2578 2315 73 -58 -101 N
ATOM 3188 NH2 ARG A 457 25.919 3.422 2.191 1.00 15.78 N
ANISOU 3188 NH2 ARG A 457 1806 2207 1981 30 -50 -98 N
ATOM 3189 N LEU A 458 23.378 2.192 -2.886 1.00 21.46 N
ANISOU 3189 N LEU A 458 2462 2965 2727 26 -223 -159 N
ATOM 3190 CA LEU A 458 23.535 3.441 -3.614 1.00 16.61 C
ANISOU 3190 CA LEU A 458 1877 2357 2077 77 -232 -157 C
ATOM 3191 C LEU A 458 23.465 3.250 -5.121 1.00 16.52 C
ANISOU 3191 C LEU A 458 1883 2353 2042 88 -281 -176 C
ATOM 3192 O LEU A 458 23.697 4.192 -5.871 1.00 22.64 O
ANISOU 3192 O LEU A 458 2689 3131 2783 130 -289 -169 O
ATOM 3193 CB LEU A 458 24.860 4.100 -3.233 1.00 16.43 C
ANISOU 3193 CB LEU A 458 1910 2302 2030 91 -197 -144 C
ATOM 3194 CG LEU A 458 24.964 4.406 -1.738 1.00 15.94 C
ANISOU 3194 CG LEU A 458 1838 2238 1982 86 -153 -130 C
ATOM 3195 CD1 LEU A 458 26.265 5.121 -1.417 1.00 9.77 C
ANISOU 3195 CD1 LEU A 458 1108 1425 1179 99 -126 -124 C
ATOM 3196 CD2 LEU A 458 23.750 5.233 -1.300 1.00 10.86 C
ANISOU 3196 CD2 LEU A 458 1150 1627 1350 117 -148 -124 C
ATOM 3197 N GLU A 459 23.168 2.029 -5.557 1.00 16.38 N
ANISOU 3197 N GLU A 459 1847 2336 2042 51 -312 -199 N
ATOM 3198 CA GLU A 459 22.948 1.746 -6.972 1.00 20.94 C
ANISOU 3198 CA GLU A 459 2436 2927 2595 61 -365 -226 C
ATOM 3199 C GLU A 459 24.148 2.131 -7.815 1.00 23.60 C
ANISOU 3199 C GLU A 459 2844 3245 2879 88 -359 -225 C
ATOM 3200 O GLU A 459 24.016 2.804 -8.839 1.00 29.07 O
ANISOU 3200 O GLU A 459 3556 3958 3531 129 -385 -225 O
ATOM 3201 CB GLU A 459 21.698 2.459 -7.478 1.00 16.42 C
ANISOU 3201 CB GLU A 459 1820 2399 2019 94 -402 -225 C
ATOM 3202 CG GLU A 459 20.412 1.781 -7.040 1.00 21.37 C
ANISOU 3202 CG GLU A 459 2368 3051 2700 60 -423 -236 C
ATOM 3203 CD GLU A 459 19.179 2.599 -7.361 1.00 28.36 C
ANISOU 3203 CD GLU A 459 3201 3985 3588 99 -454 -231 C
ATOM 3204 OE1 GLU A 459 19.217 3.395 -8.333 1.00 31.12 O
ANISOU 3204 OE1 GLU A 459 3581 4352 3893 148 -482 -230 O
ATOM 3205 OE2 GLU A 459 18.182 2.457 -6.623 1.00 32.24 O
ANISOU 3205 OE2 GLU A 459 3622 4499 4127 82 -448 -225 O
ATOM 3206 N LEU A 460 25.318 1.720 -7.345 1.00 13.69 N
ANISOU 3206 N LEU A 460 1624 1953 1625 68 -323 -221 N
ATOM 3207 CA LEU A 460 26.561 1.856 -8.080 1.00 25.77 C
ANISOU 3207 CA LEU A 460 3216 3463 3113 86 -311 -221 C
ATOM 3208 C LEU A 460 26.888 0.522 -8.730 1.00 31.48 C
ANISOU 3208 C LEU A 460 3955 4172 3834 60 -335 -256 C
ATOM 3209 O LEU A 460 27.747 0.448 -9.610 1.00 27.97 O
ANISOU 3209 O LEU A 460 3558 3720 3350 77 -334 -266 O
ATOM 3210 CB LEU A 460 27.703 2.238 -7.127 1.00 16.14 C
ANISOU 3210 CB LEU A 460 2020 2212 1899 82 -258 -196 C
ATOM 3211 CG LEU A 460 27.541 3.561 -6.392 1.00 20.73 C
ANISOU 3211 CG LEU A 460 2594 2798 2484 106 -232 -167 C
ATOM 3212 CD1 LEU A 460 28.787 3.846 -5.544 1.00 16.73 C
ANISOU 3212 CD1 LEU A 460 2115 2261 1983 98 -187 -151 C
ATOM 3213 CD2 LEU A 460 27.287 4.670 -7.416 1.00 9.34 C
ANISOU 3213 CD2 LEU A 460 1171 1373 1006 154 -248 -156 C
ATOM 3214 N LEU A 461 26.216 -0.531 -8.263 1.00 36.31 N
ANISOU 3214 N LEU A 461 4527 4777 4492 18 -352 -275 N
ATOM 3215 CA LEU A 461 26.476 -1.904 -8.713 1.00 37.24 C
ANISOU 3215 CA LEU A 461 4657 4870 4621 -13 -374 -312 C
ATOM 3216 C LEU A 461 26.312 -2.014 -10.217 1.00 33.59 C
ANISOU 3216 C LEU A 461 4221 4429 4113 11 -421 -348 C
ATOM 3217 O LEU A 461 27.028 -2.778 -10.851 1.00 31.14 O
ANISOU 3217 O LEU A 461 3949 4097 3784 8 -427 -377 O
ATOM 3218 CB LEU A 461 25.534 -2.891 -8.012 1.00 32.53 C
ANISOU 3218 CB LEU A 461 4007 4264 4089 -63 -388 -322 C
ATOM 3219 CG LEU A 461 25.552 -4.337 -8.498 1.00 37.36 C
ANISOU 3219 CG LEU A 461 4625 4845 4725 -100 -420 -364 C
ATOM 3220 CD1 LEU A 461 26.753 -5.032 -7.943 1.00 28.79 C
ANISOU 3220 CD1 LEU A 461 3576 3710 3652 -114 -380 -356 C
ATOM 3221 CD2 LEU A 461 24.265 -5.115 -8.164 1.00 42.42 C
ANISOU 3221 CD2 LEU A 461 5202 5486 5428 -147 -451 -378 C
ATOM 3222 OXT LEU A 461 25.481 -1.328 -10.824 1.00 37.25 O
ANISOU 3222 OXT LEU A 461 4668 4933 4553 38 -455 -349 O
TER 3223 LEU A 461
HETATM 3224 PA FAD A 900 37.992 -0.850 4.941 1.00 10.46 P
ANISOU 3224 PA FAD A 900 1360 1341 1273 -44 -17 -51 P
HETATM 3225 O1A FAD A 900 37.181 -0.053 5.918 1.00 13.94 O
ANISOU 3225 O1A FAD A 900 1792 1810 1695 -40 -10 -50 O
HETATM 3226 O2A FAD A 900 38.287 -2.299 5.183 1.00 14.17 O
ANISOU 3226 O2A FAD A 900 1830 1793 1759 -53 -18 -32 O
HETATM 3227 O5B FAD A 900 37.333 -0.726 3.477 1.00 12.03 O
ANISOU 3227 O5B FAD A 900 1562 1530 1480 -44 -22 -68 O
HETATM 3228 C5B FAD A 900 37.028 0.577 2.960 1.00 14.06 C
ANISOU 3228 C5B FAD A 900 1822 1795 1724 -32 -22 -83 C
HETATM 3229 C4B FAD A 900 36.864 0.553 1.439 1.00 16.49 C
ANISOU 3229 C4B FAD A 900 2140 2092 2034 -26 -29 -96 C
HETATM 3230 O4B FAD A 900 38.130 0.253 0.807 1.00 14.27 O
ANISOU 3230 O4B FAD A 900 1874 1794 1756 -22 -25 -98 O
HETATM 3231 C3B FAD A 900 35.893 -0.525 0.979 1.00 17.27 C
ANISOU 3231 C3B FAD A 900 2229 2188 2145 -39 -41 -99 C
HETATM 3232 O3B FAD A 900 35.137 -0.061 -0.150 1.00 11.38 O
ANISOU 3232 O3B FAD A 900 1484 1449 1389 -29 -54 -114 O
HETATM 3233 C2B FAD A 900 36.824 -1.647 0.552 1.00 15.69 C
ANISOU 3233 C2B FAD A 900 2043 1963 1956 -43 -43 -102 C
HETATM 3234 O2B FAD A 900 36.191 -2.483 -0.403 1.00 13.39 O
ANISOU 3234 O2B FAD A 900 1754 1661 1674 -50 -59 -119 O
HETATM 3235 C1B FAD A 900 37.978 -0.871 -0.052 1.00 11.44 C
ANISOU 3235 C1B FAD A 900 1521 1421 1404 -25 -34 -107 C
HETATM 3236 N9A FAD A 900 39.243 -1.630 -0.078 1.00 13.84 N
ANISOU 3236 N9A FAD A 900 1833 1707 1718 -23 -27 -105 N
HETATM 3237 C8A FAD A 900 39.983 -1.963 0.990 1.00 11.12 C
ANISOU 3237 C8A FAD A 900 1481 1359 1384 -26 -22 -89 C
HETATM 3238 N7A FAD A 900 41.058 -2.664 0.579 1.00 12.24 N
ANISOU 3238 N7A FAD A 900 1630 1485 1537 -17 -17 -91 N
HETATM 3239 C5A FAD A 900 40.985 -2.759 -0.768 1.00 17.62 C
ANISOU 3239 C5A FAD A 900 2326 2159 2211 -8 -16 -110 C
HETATM 3240 C6A FAD A 900 41.794 -3.344 -1.734 1.00 11.66 C
ANISOU 3240 C6A FAD A 900 1583 1390 1456 8 -8 -122 C
HETATM 3241 N6A FAD A 900 42.914 -3.984 -1.358 1.00 13.86 N
ANISOU 3241 N6A FAD A 900 1857 1656 1752 17 0 -114 N
HETATM 3242 N1A FAD A 900 41.447 -3.275 -3.038 1.00 14.31 N
ANISOU 3242 N1A FAD A 900 1937 1728 1773 19 -9 -143 N
HETATM 3243 C2A FAD A 900 40.326 -2.637 -3.406 1.00 11.84 C
ANISOU 3243 C2A FAD A 900 1626 1430 1443 14 -21 -148 C
HETATM 3244 N3A FAD A 900 39.531 -2.054 -2.497 1.00 14.16 N
ANISOU 3244 N3A FAD A 900 1904 1736 1741 -1 -29 -136 N
HETATM 3245 C4A FAD A 900 39.836 -2.104 -1.176 1.00 14.87 C
ANISOU 3245 C4A FAD A 900 1978 1824 1847 -12 -24 -117 C
HETATM 3246 N1 FAD A 900 39.133 9.054 6.424 1.00 12.49 N
ANISOU 3246 N1 FAD A 900 1670 1570 1505 17 -17 -181 N
HETATM 3247 C2 FAD A 900 39.669 10.168 5.880 1.00 12.60 C
ANISOU 3247 C2 FAD A 900 1696 1549 1544 14 -16 -189 C
HETATM 3248 O2 FAD A 900 39.563 10.369 4.543 1.00 13.27 O
ANISOU 3248 O2 FAD A 900 1786 1612 1643 17 -5 -169 O
HETATM 3249 N3 FAD A 900 40.295 11.092 6.632 1.00 16.13 N
ANISOU 3249 N3 FAD A 900 2150 1979 2002 8 -26 -217 N
HETATM 3250 C4 FAD A 900 40.400 10.896 7.953 1.00 16.34 C
ANISOU 3250 C4 FAD A 900 2173 2031 2005 9 -40 -238 C
HETATM 3251 O4 FAD A 900 41.045 11.799 8.705 1.00 19.10 O
ANISOU 3251 O4 FAD A 900 2530 2365 2363 3 -56 -272 O
HETATM 3252 C4X FAD A 900 39.830 9.684 8.572 1.00 15.99 C
ANISOU 3252 C4X FAD A 900 2119 2032 1927 17 -38 -224 C
HETATM 3253 N5 FAD A 900 39.925 9.471 9.900 1.00 19.14 N
ANISOU 3253 N5 FAD A 900 2517 2461 2295 21 -49 -240 N
HETATM 3254 C5X FAD A 900 39.403 8.359 10.472 1.00 15.96 C
ANISOU 3254 C5X FAD A 900 2106 2096 1861 27 -43 -219 C
HETATM 3255 C6 FAD A 900 39.521 8.144 11.846 1.00 18.39 C
ANISOU 3255 C6 FAD A 900 2417 2439 2130 36 -53 -231 C
HETATM 3256 C7 FAD A 900 38.979 7.010 12.449 1.00 18.58 C
ANISOU 3256 C7 FAD A 900 2434 2501 2124 42 -42 -201 C
HETATM 3257 C7M FAD A 900 39.115 6.807 13.939 1.00 13.23 C
ANISOU 3257 C7M FAD A 900 1763 1866 1397 55 -50 -208 C
HETATM 3258 C8 FAD A 900 38.277 5.999 11.613 1.00 19.81 C
ANISOU 3258 C8 FAD A 900 2576 2654 2297 34 -23 -163 C
HETATM 3259 C8M FAD A 900 37.696 4.760 12.256 1.00 9.95 C
ANISOU 3259 C8M FAD A 900 1317 1437 1025 35 -9 -128 C
HETATM 3260 C9 FAD A 900 38.165 6.210 10.232 1.00 22.38 C
ANISOU 3260 C9 FAD A 900 2898 2946 2660 26 -19 -160 C
HETATM 3261 C9A FAD A 900 38.705 7.353 9.630 1.00 10.69 C
ANISOU 3261 C9A FAD A 900 1427 1433 1201 25 -27 -184 C
HETATM 3262 N10 FAD A 900 38.611 7.603 8.244 1.00 13.60 N
ANISOU 3262 N10 FAD A 900 1796 1772 1601 20 -21 -176 N
HETATM 3263 C10 FAD A 900 39.188 8.789 7.739 1.00 15.58 C
ANISOU 3263 C10 FAD A 900 2057 1987 1873 18 -25 -194 C
HETATM 3264 C1' FAD A 900 37.970 6.670 7.303 1.00 16.33 C
ANISOU 3264 C1' FAD A 900 2132 2119 1953 17 -12 -150 C
HETATM 3265 C2' FAD A 900 39.017 5.673 6.763 1.00 13.14 C
ANISOU 3265 C2' FAD A 900 1725 1705 1564 0 -18 -133 C
HETATM 3266 O2' FAD A 900 40.292 6.292 6.546 1.00 13.74 O
ANISOU 3266 O2' FAD A 900 1804 1759 1656 -8 -25 -143 O
HETATM 3267 C3' FAD A 900 38.613 5.059 5.430 1.00 11.96 C
ANISOU 3267 C3' FAD A 900 1573 1544 1427 -2 -13 -118 C
HETATM 3268 O3' FAD A 900 37.331 4.477 5.594 1.00 16.52 O
ANISOU 3268 O3' FAD A 900 2141 2141 1996 1 -8 -110 O
HETATM 3269 C4' FAD A 900 39.621 4.021 4.925 1.00 12.63 C
ANISOU 3269 C4' FAD A 900 1655 1618 1524 -14 -15 -106 C
HETATM 3270 O4' FAD A 900 39.193 3.537 3.633 1.00 14.33 O
ANISOU 3270 O4' FAD A 900 1875 1824 1747 -13 -12 -100 O
HETATM 3271 C5' FAD A 900 39.749 2.843 5.897 1.00 16.82 C
ANISOU 3271 C5' FAD A 900 2178 2164 2048 -19 -20 -92 C
HETATM 3272 O5' FAD A 900 40.710 1.889 5.410 1.00 17.22 O
ANISOU 3272 O5' FAD A 900 2228 2201 2115 -24 -22 -82 O
HETATM 3273 P FAD A 900 40.549 0.306 5.641 1.00 12.63 P
ANISOU 3273 P FAD A 900 1643 1618 1538 -28 -23 -61 P
HETATM 3274 O1P FAD A 900 41.803 -0.365 5.148 1.00 14.63 O
ANISOU 3274 O1P FAD A 900 1896 1853 1809 -26 -26 -57 O
HETATM 3275 O2P FAD A 900 40.146 0.093 7.072 1.00 12.98 O
ANISOU 3275 O2P FAD A 900 1683 1685 1563 -28 -25 -47 O
HETATM 3276 O3P FAD A 900 39.362 -0.047 4.609 1.00 13.24 O
ANISOU 3276 O3P FAD A 900 1722 1685 1622 -33 -19 -64 O
HETATM 3277 O38 0T5 A 901 36.204 15.472 9.439 1.00 57.03 O
ANISOU 3277 O38 0T5 A 901 7393 7137 7141 140 -9 -349 O
HETATM 3278 N8 0T5 A 901 37.332 15.052 8.758 1.00 61.73 N
ANISOU 3278 N8 0T5 A 901 7983 7714 7759 103 -18 -327 N
HETATM 3279 O10 0T5 A 901 37.360 15.066 7.369 1.00 69.45 O
ANISOU 3279 O10 0T5 A 901 8958 8666 8763 97 -10 -290 O
HETATM 3280 C2 0T5 A 901 38.440 14.598 9.468 1.00 61.51 C
ANISOU 3280 C2 0T5 A 901 7949 7698 7723 76 -37 -340 C
HETATM 3281 C1 0T5 A 901 39.702 15.139 9.227 1.00 63.13 C
ANISOU 3281 C1 0T5 A 901 8159 7862 7965 46 -51 -350 C
HETATM 3282 C6 0T5 A 901 40.805 14.676 9.939 1.00 64.72 C
ANISOU 3282 C6 0T5 A 901 8348 8080 8160 21 -74 -364 C
HETATM 3283 C7 0T5 A 901 42.162 15.279 9.659 1.00 69.90 C
ANISOU 3283 C7 0T5 A 901 9001 8694 8865 -14 -90 -374 C
HETATM 3284 F28 0T5 A 901 42.072 15.963 8.529 1.00 73.29 F
ANISOU 3284 F28 0T5 A 901 9438 9075 9334 -18 -71 -353 F
HETATM 3285 F27 0T5 A 901 42.526 16.099 10.636 1.00 72.52 F
ANISOU 3285 F27 0T5 A 901 9344 9012 9200 -18 -114 -426 F
HETATM 3286 F29 0T5 A 901 43.074 14.321 9.525 1.00 56.85 F
ANISOU 3286 F29 0T5 A 901 7323 7063 7213 -37 -97 -352 F
HETATM 3287 C5 0T5 A 901 40.626 13.670 10.895 1.00 58.20 C
ANISOU 3287 C5 0T5 A 901 7515 7313 7288 29 -80 -365 C
HETATM 3288 C3 0T5 A 901 38.260 13.595 10.408 1.00 54.66 C
ANISOU 3288 C3 0T5 A 901 7071 6886 6812 79 -39 -340 C
HETATM 3289 C4 0T5 A 901 39.354 13.129 11.125 1.00 55.96 C
ANISOU 3289 C4 0T5 A 901 7230 7067 6967 57 -61 -350 C
HETATM 3290 C14 0T5 A 901 39.127 12.035 12.131 1.00 51.53 C
ANISOU 3290 C14 0T5 A 901 6659 6564 6355 65 -62 -342 C
HETATM 3291 O15 0T5 A 901 40.008 11.729 12.914 1.00 47.82 O
ANISOU 3291 O15 0T5 A 901 6188 6113 5868 54 -84 -354 O
HETATM 3292 N13 0T5 A 901 37.950 11.410 12.125 1.00 51.78 N
ANISOU 3292 N13 0T5 A 901 6682 6627 6363 84 -38 -317 N
HETATM 3293 C12 0T5 A 901 37.598 10.413 13.127 1.00 47.18 C
ANISOU 3293 C12 0T5 A 901 6093 6100 5734 92 -32 -302 C
HETATM 3294 C13 0T5 A 901 36.316 9.665 12.737 1.00 42.20 C
ANISOU 3294 C13 0T5 A 901 5444 5491 5098 102 -3 -266 C
HETATM 3295 C20 0T5 A 901 37.454 11.052 14.458 1.00 46.91 C
ANISOU 3295 C20 0T5 A 901 6075 6090 5656 116 -37 -344 C
HETATM 3296 C25 0T5 A 901 36.569 12.115 14.633 1.00 42.46 C
ANISOU 3296 C25 0T5 A 901 5525 5519 5089 145 -22 -376 C
HETATM 3297 C24 0T5 A 901 36.450 12.703 15.888 1.00 48.45 C
ANISOU 3297 C24 0T5 A 901 6303 6303 5803 171 -26 -421 C
HETATM 3298 C23 0T5 A 901 37.207 12.238 16.965 1.00 47.28 C
ANISOU 3298 C23 0T5 A 901 6162 6191 5610 167 -47 -431 C
HETATM 3299 C22 0T5 A 901 38.091 11.172 16.789 1.00 46.41 C
ANISOU 3299 C22 0T5 A 901 6038 6091 5506 138 -64 -394 C
HETATM 3300 C21 0T5 A 901 38.215 10.581 15.532 1.00 45.93 C
ANISOU 3300 C21 0T5 A 901 5957 6001 5494 113 -57 -351 C
HETATM 3301 O HOH A1001 28.781 -8.815 4.523 1.00 11.60 O
HETATM 3302 O HOH A1002 33.945 8.333 16.366 1.00 34.31 O
HETATM 3303 O HOH A1003 31.989 -1.005 -1.807 1.00 8.47 O
HETATM 3304 O HOH A1004 37.007 -5.613 -12.765 1.00 27.46 O
HETATM 3305 O HOH A1005 45.375 15.209 2.744 1.00 16.86 O
HETATM 3306 O HOH A1006 36.552 7.529 -8.552 1.00 14.51 O
HETATM 3307 O HOH A1007 38.393 11.339 1.053 1.00 15.07 O
HETATM 3308 O HOH A1008 29.905 3.018 2.240 1.00 23.15 O
HETATM 3309 O HOH A1009 43.556 -3.509 1.518 1.00 11.34 O
HETATM 3310 O HOH A1010 43.107 -12.724 1.616 1.00 23.17 O
HETATM 3311 O HOH A1011 25.321 19.895 17.679 1.00 22.22 O
HETATM 3312 O HOH A1012 44.637 14.535 -10.255 1.00 19.87 O
HETATM 3313 O HOH A1013 37.287 -5.058 -4.095 1.00 12.92 O
HETATM 3314 O HOH A1014 36.851 9.641 -1.881 1.00 13.38 O
HETATM 3315 O HOH A1015 37.146 11.654 7.464 1.00 28.42 O
HETATM 3316 O HOH A1016 57.114 7.549 7.304 1.00 32.12 O
HETATM 3317 O HOH A1017 25.651 18.353 -4.503 1.00 18.30 O
HETATM 3318 O HOH A1018 27.836 -1.455 7.935 1.00 17.25 O
HETATM 3319 O HOH A1019 27.882 0.423 8.342 1.00 29.10 O
HETATM 3320 O HOH A1020 30.053 2.283 11.702 1.00 21.06 O
HETATM 3321 O HOH A1021 22.540 8.901 -11.708 1.00 27.68 O
HETATM 3322 O HOH A1022 41.401 15.378 -3.231 1.00 11.54 O
HETATM 3323 O HOH A1023 32.880 -8.842 -15.057 1.00 20.44 O
HETATM 3324 O HOH A1024 57.355 -6.488 4.687 1.00 18.64 O
HETATM 3325 O HOH A1025 34.495 -1.067 7.194 1.00 15.37 O
HETATM 3326 O HOH A1026 29.789 13.771 19.643 1.00 28.37 O
HETATM 3327 O HOH A1027 55.903 11.243 15.143 1.00 30.55 O
HETATM 3328 O HOH A1028 48.161 9.787 -8.964 1.00 14.01 O
HETATM 3329 O HOH A1029 42.910 25.465 4.133 1.00 27.78 O
HETATM 3330 O HOH A1030 39.388 21.997 -7.546 1.00 21.36 O
HETATM 3331 O HOH A1031 33.047 12.997 14.526 1.00 31.35 O
HETATM 3332 O HOH A1032 25.684 5.739 8.480 1.00 28.02 O
HETATM 3333 O HOH A1033 34.549 -2.513 10.845 1.00 15.85 O
HETATM 3334 O HOH A1034 44.461 20.059 -2.468 1.00 24.64 O
HETATM 3335 O HOH A1035 23.015 -6.113 0.398 1.00 30.60 O
HETATM 3336 O HOH A1036 22.904 -0.618 -9.241 1.00 27.35 O
HETATM 3337 O HOH A1037 50.270 -8.101 -3.967 1.00 20.86 O
HETATM 3338 O HOH A1038 27.831 10.531 7.003 1.00 15.68 O
HETATM 3339 O HOH A1039 33.819 13.593 -7.157 1.00 11.04 O
HETATM 3340 O HOH A1040 59.808 -2.667 -6.269 1.00 15.86 O
HETATM 3341 O HOH A1041 43.185 16.640 -4.730 1.00 16.62 O
HETATM 3342 O HOH A1042 41.425 2.986 -18.792 1.00 28.69 O
HETATM 3343 O HOH A1043 62.224 3.775 -7.473 1.00 31.74 O
HETATM 3344 O HOH A1044 31.432 -19.364 10.303 1.00 18.15 O
HETATM 3345 O HOH A1045 32.287 -1.856 5.663 1.00 13.51 O
HETATM 3346 O HOH A1046 25.886 11.966 -13.191 1.00 26.28 O
HETATM 3347 O HOH A1047 26.069 17.556 -7.263 1.00 22.88 O
HETATM 3348 O HOH A1048 39.229 15.094 -4.739 1.00 15.53 O
HETATM 3349 O HOH A1049 38.495 -1.219 -6.888 1.00 13.10 O
HETATM 3350 O HOH A1050 29.701 11.433 5.189 1.00 19.07 O
HETATM 3351 O HOH A1051 31.049 13.525 -8.844 1.00 15.84 O
HETATM 3352 O HOH A1052 41.739 23.992 9.645 1.00 21.43 O
HETATM 3353 O HOH A1053 24.915 -3.970 5.508 1.00 15.77 O
HETATM 3354 O HOH A1054 50.788 13.335 5.896 1.00 21.77 O
HETATM 3355 O HOH A1055 60.527 1.471 -4.417 1.00 14.32 O
HETATM 3356 O HOH A1056 32.714 9.382 -1.079 1.00 16.06 O
HETATM 3357 O HOH A1057 46.367 19.708 -4.438 1.00 34.92 O
HETATM 3358 O HOH A1058 30.435 21.234 20.160 1.00 25.54 O
HETATM 3359 O HOH A1059 23.592 -1.786 4.445 1.00 18.24 O
HETATM 3360 O HOH A1060 29.976 -19.622 12.214 1.00 19.97 O
HETATM 3361 O HOH A1061 41.532 18.722 15.236 1.00 29.79 O
HETATM 3362 O HOH A1062 24.505 12.836 -10.604 1.00 25.96 O
HETATM 3363 O HOH A1063 41.394 2.913 14.544 1.00 26.58 O
HETATM 3364 O HOH A1064 38.605 2.145 -18.728 1.00 27.92 O
HETATM 3365 O HOH A1065 38.520 1.026 -5.400 1.00 13.86 O
HETATM 3366 O HOH A1066 38.595 -1.871 -19.281 1.00 26.65 O
HETATM 3367 O HOH A1067 62.542 0.079 7.032 1.00 22.69 O
HETATM 3368 O HOH A1068 23.993 15.454 -9.833 1.00 26.75 O
HETATM 3369 O HOH A1069 25.345 9.625 6.259 1.00 21.79 O
HETATM 3370 O HOH A1070 34.547 7.852 -2.952 1.00 18.54 O
HETATM 3371 O HOH A1071 55.339 20.011 5.936 1.00 28.30 O
HETATM 3372 O HOH A1072 54.145 12.788 -2.998 1.00 23.71 O
HETATM 3373 O HOH A1073 60.657 2.205 -6.632 1.00 23.32 O
HETATM 3374 O HOH A1074 27.790 3.558 16.348 1.00 32.93 O
HETATM 3375 O HOH A1075 52.156 -0.968 -8.429 1.00 31.65 O
HETATM 3376 O HOH A1076 44.522 18.029 14.895 1.00 28.03 O
HETATM 3377 O HOH A1077 47.573 -4.601 7.959 1.00 34.56 O
HETATM 3378 O HOH A1078 32.985 -6.589 11.336 1.00 24.45 O
HETATM 3379 O HOH A1079 28.977 18.088 -5.174 1.00 19.19 O
HETATM 3380 O HOH A1080 28.660 11.594 -15.192 1.00 30.51 O
HETATM 3381 O HOH A1081 22.407 -3.071 0.330 1.00 24.31 O
HETATM 3382 O HOH A1082 41.859 23.827 7.254 1.00 22.89 O
HETATM 3383 O HOH A1083 38.010 8.062 -14.284 1.00 20.98 O
HETATM 3384 O HOH A1084 25.451 8.449 8.399 1.00 27.85 O
HETATM 3385 O HOH A1085 19.575 11.268 -8.235 1.00 28.90 O
HETATM 3386 O HOH A1086 21.838 -4.591 8.279 1.00 30.17 O
HETATM 3387 O HOH A1087 25.010 -8.204 -6.283 1.00 27.87 O
HETATM 3388 O HOH A1088 30.483 -16.475 -1.955 1.00 27.83 O
HETATM 3389 O HOH A1089 21.384 13.579 19.255 1.00 36.76 O
HETATM 3390 O HOH A1090 32.267 -3.589 6.537 1.00 34.87 O
HETATM 3391 O HOH A1091 36.403 8.597 -16.190 1.00 30.57 O
HETATM 3392 O HOH A1092 16.055 10.310 -1.423 1.00 30.61 O
HETATM 3393 O HOH A1093 53.713 16.018 4.441 1.00 33.81 O
HETATM 3394 O HOH A1094 30.856 18.221 -7.344 1.00 17.47 O
HETATM 3395 O HOH A1095 50.928 -3.130 12.071 1.00 39.08 O
HETATM 3396 O HOH A1096 21.621 15.385 21.497 1.00 31.36 O
HETATM 3397 O HOH A1097 55.221 1.579 -12.397 1.00 37.86 O
HETATM 3398 O HOH A1098 51.943 18.730 2.777 1.00 27.60 O
HETATM 3399 O HOH A1099 60.925 3.558 12.375 1.00 34.31 O
HETATM 3400 O HOH A1100 25.562 -15.872 -11.521 1.00 42.16 O
HETATM 3401 O HOH A1101 19.162 23.544 20.687 1.00 46.63 O
HETATM 3402 O HOH A1102 50.661 -5.624 8.722 1.00 28.05 O
HETATM 3403 O HOH A1103 21.424 27.504 15.960 1.00 35.01 O
HETATM 3404 O HOH A1104 17.144 6.307 -3.729 1.00 31.69 O
HETATM 3405 O HOH A1105 29.824 -14.569 -4.072 1.00 30.56 O
HETATM 3406 O HOH A1106 22.802 -0.502 12.577 1.00 36.37 O
HETATM 3407 O HOH A1107 23.609 -11.214 5.353 1.00 32.64 O
HETATM 3408 O HOH A1108 27.357 19.909 -8.691 1.00 27.87 O
HETATM 3409 O HOH A1109 34.276 23.570 -4.371 1.00 30.24 O
HETATM 3410 O HOH A1110 32.835 -21.946 10.092 1.00 38.80 O
HETATM 3411 O HOH A1111 23.115 2.364 8.882 1.00 31.38 O
HETATM 3412 O HOH A1112 48.245 31.148 13.082 1.00 45.47 O
HETATM 3413 O HOH A1113 27.861 4.564 18.273 1.00 35.35 O
HETATM 3414 O HOH A1114 37.649 -7.499 -16.517 1.00 38.42 O
HETATM 3415 O HOH A1115 53.178 -10.413 -1.623 1.00 38.19 O
HETATM 3416 O HOH A1116 13.688 15.304 13.412 1.00 36.20 O
HETATM 3417 O HOH A1117 28.004 31.953 15.925 1.00 44.49 O
HETATM 3418 O HOH A1118 52.679 15.294 1.952 1.00 29.98 O
HETATM 3419 O HOH A1119 51.479 -14.284 -2.387 1.00 37.48 O
HETATM 3420 O HOH A1120 57.316 -1.678 9.613 1.00 30.82 O
HETATM 3421 O HOH A1121 54.850 14.948 -1.505 1.00 34.06 O
HETATM 3422 O HOH A1122 29.020 4.842 13.412 1.00 39.39 O
HETATM 3423 O HOH A1123 41.764 8.120 16.042 1.00 34.14 O
HETATM 3424 O HOH A1124 13.874 17.249 11.741 1.00 33.68 O
HETATM 3425 O HOH A1125 48.581 12.298 -10.094 1.00 32.25 O
HETATM 3426 O HOH A1126 44.587 34.079 17.664 1.00 36.45 O
HETATM 3427 O HOH A1127 20.845 -1.965 -6.464 1.00 31.91 O
HETATM 3428 O HOH A1128 35.632 8.479 -19.058 1.00 32.69 O
HETATM 3429 O HOH A1129 28.039 32.498 0.332 1.00 41.00 O
HETATM 3430 O HOH A1130 45.881 12.199 18.702 1.00 35.59 O
HETATM 3431 O HOH A1131 36.349 22.231 -8.241 1.00 32.90 O
HETATM 3432 O HOH A1132 34.709 -6.629 18.176 1.00 42.79 O
HETATM 3433 O HOH A1133 38.723 -11.579 8.394 1.00 35.71 O
HETATM 3434 O HOH A1134 16.826 13.786 1.814 1.00 34.38 O
HETATM 3435 O HOH A1135 42.821 21.035 16.849 1.00 39.14 O
HETATM 3436 O HOH A1136 21.999 0.333 5.637 1.00 27.14 O
HETATM 3437 O HOH A1137 33.824 -3.478 -21.938 1.00 41.47 O
HETATM 3438 O HOH A1138 58.443 13.781 -3.211 1.00 34.97 O
HETATM 3439 O HOH A1139 34.434 21.144 -6.913 1.00 34.45 O
HETATM 3440 O HOH A1140 32.127 -20.981 6.983 1.00 31.84 O
HETATM 3441 O HOH A1141 46.631 -9.677 9.576 1.00 38.94 O
HETATM 3442 O HOH A1142 68.162 10.348 -1.306 1.00 31.92 O
HETATM 3443 O HOH A1143 14.991 9.511 22.530 1.00 45.21 O
HETATM 3444 O HOH A1144 33.180 7.025 -18.793 1.00 37.62 O
HETATM 3445 O HOH A1145 68.080 21.701 10.277 1.00 47.52 O
HETATM 3446 O HOH A1146 59.797 -1.660 9.655 1.00 38.20 O
HETATM 3447 O HOH A1147 53.457 -1.474 -7.074 1.00 40.80 O
HETATM 3448 O HOH A1148 16.335 19.910 -6.321 1.00 29.63 O
HETATM 3449 O HOH A1149 47.284 -5.596 9.666 1.00 40.60 O
HETATM 3450 O HOH A1150 16.023 8.143 14.641 1.00 39.20 O
HETATM 3451 O HOH A1151 20.537 -2.615 -1.009 1.00 32.16 O
HETATM 3452 O HOH A1152 33.741 19.189 -7.978 1.00 36.51 O
HETATM 3453 O HOH A1153 30.809 -21.458 5.157 1.00 41.20 O
HETATM 3454 O HOH A1154 61.319 18.030 7.858 1.00 39.67 O
HETATM 3455 O HOH A1155 42.772 1.439 16.717 1.00 40.30 O
HETATM 3456 O HOH A1156 17.926 8.989 7.611 1.00 31.43 O
HETATM 3457 O HOH A1157 53.830 -1.012 12.924 1.00 40.04 O
HETATM 3458 O HOH A1158 31.935 -19.200 4.027 1.00 48.20 O
HETATM 3459 O HOH A1159 59.565 23.590 9.341 1.00 36.88 O
HETATM 3460 O HOH A1160 46.772 14.357 -8.913 1.00 37.73 O
HETATM 3461 O HOH A1161 39.527 10.849 -15.107 1.00 45.26 O
HETATM 3462 O HOH A1162 17.996 7.941 4.074 1.00 44.14 O
HETATM 3463 O HOH A1163 62.768 6.216 12.302 1.00 45.82 O
HETATM 3464 O HOH A1164 26.665 -9.259 -8.174 1.00 38.54 O
HETATM 3465 O HOH A1165 22.658 2.013 -11.523 1.00 46.52 O
HETATM 3466 O HOH A1166 16.113 5.699 -5.772 1.00 37.02 O
HETATM 3467 O HOH A1167 46.748 28.201 13.852 1.00 35.86 O
HETATM 3468 O HOH A1168 55.648 -2.861 11.454 1.00 40.60 O
HETATM 3469 O HOH A1169 13.942 9.539 12.958 1.00 39.28 O
HETATM 3470 O HOH A1170 42.550 -4.536 13.924 1.00 40.06 O
HETATM 3471 O HOH A1171 16.083 16.429 19.777 1.00 44.45 O
HETATM 3472 O HOH A1172 18.167 3.809 -2.050 1.00 40.26 O
HETATM 3473 O HOH A1173 59.116 1.585 -8.423 1.00 39.14 O
HETATM 3474 O HOH A1174 43.454 31.171 5.183 1.00 51.17 O
HETATM 3475 O HOH A1175 51.530 8.134 -14.835 1.00 43.35 O
HETATM 3476 O HOH A1176 23.393 4.160 9.973 1.00 44.29 O
HETATM 3477 O HOH A1177 62.211 0.190 10.494 1.00 45.09 O
HETATM 3478 O HOH A1178 59.523 -4.283 10.911 1.00 34.84 O
HETATM 3479 O HOH A1179 44.278 -3.134 14.271 1.00 42.50 O
HETATM 3480 O HOH A1180 45.420 34.247 10.842 1.00 40.78 O
HETATM 3481 O HOH A1181 44.697 18.653 -7.350 1.00 40.76 O
HETATM 3482 O HOH A1182 36.752 20.677 -10.918 1.00 37.18 O
HETATM 3483 O HOH A1183 59.811 -6.970 3.401 1.00 40.08 O
HETATM 3484 O HOH A1184 41.448 20.849 -9.313 1.00 36.09 O
HETATM 3485 O HOH A1185 15.065 7.940 -2.240 1.00 44.33 O
HETATM 3486 O HOH A1186 39.237 37.022 6.029 1.00 43.99 O
HETATM 3487 O HOH A1187 46.739 -1.744 -17.930 1.00 49.03 O
HETATM 3488 O HOH A1188 56.691 -4.285 7.622 1.00 36.09 O
HETATM 3489 O HOH A1189 41.740 10.767 -16.044 1.00 49.50 O
HETATM 3490 O HOH A1190 63.404 12.232 -7.884 1.00 44.99 O
HETATM 3491 O HOH A1191 62.542 4.953 15.484 1.00 40.96 O
HETATM 3492 O HOH A1192 53.341 26.163 3.682 1.00 48.87 O
HETATM 3493 O HOH A1193 33.618 35.507 8.358 1.00 47.41 O
HETATM 3494 O HOH A1194 31.283 -6.579 14.048 1.00 43.68 O
CONECT 3224 3225 3226 3227 3276
CONECT 3225 3224
CONECT 3226 3224
CONECT 3227 3224 3228
CONECT 3228 3227 3229
CONECT 3229 3228 3230 3231
CONECT 3230 3229 3235
CONECT 3231 3229 3232 3233
CONECT 3232 3231
CONECT 3233 3231 3234 3235
CONECT 3234 3233
CONECT 3235 3230 3233 3236
CONECT 3236 3235 3237 3245
CONECT 3237 3236 3238
CONECT 3238 3237 3239
CONECT 3239 3238 3240 3245
CONECT 3240 3239 3241 3242
CONECT 3241 3240
CONECT 3242 3240 3243
CONECT 3243 3242 3244
CONECT 3244 3243 3245
CONECT 3245 3236 3239 3244
CONECT 3246 3247 3263
CONECT 3247 3246 3248 3249
CONECT 3248 3247
CONECT 3249 3247 3250
CONECT 3250 3249 3251 3252
CONECT 3251 3250
CONECT 3252 3250 3253 3263
CONECT 3253 3252 3254
CONECT 3254 3253 3255 3261
CONECT 3255 3254 3256
CONECT 3256 3255 3257 3258
CONECT 3257 3256
CONECT 3258 3256 3259 3260
CONECT 3259 3258
CONECT 3260 3258 3261
CONECT 3261 3254 3260 3262
CONECT 3262 3261 3263 3264
CONECT 3263 3246 3252 3262
CONECT 3264 3262 3265
CONECT 3265 3264 3266 3267
CONECT 3266 3265
CONECT 3267 3265 3268 3269
CONECT 3268 3267
CONECT 3269 3267 3270 3271
CONECT 3270 3269
CONECT 3271 3269 3272
CONECT 3272 3271 3273
CONECT 3273 3272 3274 3275 3276
CONECT 3274 3273
CONECT 3275 3273
CONECT 3276 3224 3273
CONECT 3277 3278
CONECT 3278 3277 3279 3280
CONECT 3279 3278
CONECT 3280 3278 3281 3288
CONECT 3281 3280 3282
CONECT 3282 3281 3283 3287
CONECT 3283 3282 3284 3285 3286
CONECT 3284 3283
CONECT 3285 3283
CONECT 3286 3283
CONECT 3287 3282 3289
CONECT 3288 3280 3289
CONECT 3289 3287 3288 3290
CONECT 3290 3289 3291 3292
CONECT 3291 3290
CONECT 3292 3290 3293
CONECT 3293 3292 3294 3295
CONECT 3294 3293
CONECT 3295 3293 3296 3300
CONECT 3296 3295 3297
CONECT 3297 3296 3298
CONECT 3298 3297 3299
CONECT 3299 3298 3300
CONECT 3300 3295 3299
MASTER 355 0 2 18 19 0 12 6 3493 1 77 37
END
A second structure was input as follows:
HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 31-MAR-14 4P8L
TITLE CRYSTAL STRUCTURE OF M. TUBERCULOSIS DPRE1 IN COMPLEX WITH THE NON-
TITLE 2 COVALENT INHIBITOR TY36C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE DECAPRENYLPHOSPHORYL-BETA-D-RIBOSE OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DPRE1;
COMPND 5 EC: 1.-.-.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: DPRE1, RV3790, MT3898;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS DPRE1, INHIBITOR, COMPLEX, NON-COVALENT, OXIDOREDUCTASE-
KEYWDS 2 OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.NERES,F.POJER,S.T.COLE
REVDAT 3 22-NOV-17 4P8L 1 SOURCE REMARK
REVDAT 2 01-APR-15 4P8L 1 JRNL
REVDAT 1 10-DEC-14 4P8L 0
JRNL AUTH J.NERES,R.C.HARTKOORN,L.R.CHIARELLI,R.GADUPUDI,M.R.PASCA,
JRNL AUTH 2 G.MORI,A.VENTURELLI,S.SAVINA,V.MAKAROV,G.S.KOLLY,E.MOLTENI,
JRNL AUTH 3 C.BINDA,N.DHAR,S.FERRARI,P.BRODIN,V.DELORME,V.LANDRY,
JRNL AUTH 4 A.L.DE JESUS LOPES RIBEIRO,D.FARINA,P.SAXENA,F.POJER,
JRNL AUTH 5 A.CARTA,R.LUCIANI,A.PORTA,G.ZANONI,E.DE ROSSI,M.P.COSTI,
JRNL AUTH 6 G.RICCARDI,S.T.COLE
JRNL TITL 2-CARBOXYQUINOXALINES KILL MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 2 THROUGH NONCOVALENT INHIBITION OF DPRE1.
JRNL REF ACS CHEM.BIOL. V. 10 705 2015
JRNL REFN ESSN 1554-8937
JRNL PMID 25427196
JRNL DOI 10.1021/CB5007163
REMARK 2
REMARK 2 RESOLUTION. 2.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 61205
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3264
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.02
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4291
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.3130
REMARK 3 BIN FREE R VALUE SET COUNT : 224
REMARK 3 BIN FREE R VALUE : 0.3490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6730
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 163
REMARK 3 SOLVENT ATOMS : 276
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.187
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.161
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.356
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7066 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9625 ; 1.221 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 872 ; 5.767 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 298 ;32.599 ;22.685
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1086 ;15.146 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;16.175 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1054 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5405 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4P8L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000200932.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : BARTELS MONOCHROMATOR WITH DUAL
REMARK 200 CHANNEL CUT CRYSTALS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123579
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 49.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.6900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.650
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: RMEAS 0.055 (OVERALL), 0.453 (OUTER SHELL)
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 36% POLYPROPYLENEGLYCOL 400, 100 MM
REMARK 280 IMIDAZOLE, PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 41.57450
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 SER A 3
REMARK 465 VAL A 4
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 SER B 3
REMARK 465 VAL B 4
REMARK 465 GLY B 5
REMARK 465 ALA B 6
REMARK 465 GLN B 271
REMARK 465 LEU B 272
REMARK 465 LEU B 273
REMARK 465 THR B 274
REMARK 465 LEU B 275
REMARK 465 PRO B 276
REMARK 465 ASP B 277
REMARK 465 VAL B 278
REMARK 465 PHE B 279
REMARK 465 PRO B 280
REMARK 465 ASN B 281
REMARK 465 GLY B 282
REMARK 465 LEU B 283
REMARK 465 ALA B 284
REMARK 465 ASN B 285
REMARK 465 LYS B 286
REMARK 465 TYR B 287
REMARK 465 THR B 288
REMARK 465 PHE B 289
REMARK 465 GLY B 290
REMARK 465 PRO B 291
REMARK 465 ILE B 292
REMARK 465 LEU B 317
REMARK 465 ASP B 318
REMARK 465 MET B 319
REMARK 465 PHE B 320
REMARK 465 GLY B 321
REMARK 465 GLU B 322
REMARK 465 TRP B 323
REMARK 465 ASN B 324
REMARK 465 ARG B 325
REMARK 465 ALA B 326
REMARK 465 TYR B 327
REMARK 465 GLY B 328
REMARK 465 PRO B 329
REMARK 465 ALA B 330
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 20 61.62 38.77
REMARK 500 ASN A 66 79.09 -153.07
REMARK 500 LEU A 240 123.46 -38.53
REMARK 500 TYR A 327 -14.23 73.15
REMARK 500 GLU B 263 59.06 -141.48
REMARK 500 ALA B 343 45.00 -90.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 36C A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 36C B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4P8C RELATED DB: PDB
REMARK 900 RELATED ID: 4P8H RELATED DB: PDB
REMARK 900 RELATED ID: 4P8K RELATED DB: PDB
REMARK 900 RELATED ID: 4P8M RELATED DB: PDB
REMARK 900 RELATED ID: 4P8N RELATED DB: PDB
REMARK 900 RELATED ID: 4P8P RELATED DB: PDB
REMARK 900 RELATED ID: 4P8T RELATED DB: PDB
REMARK 900 RELATED ID: 4P8Y RELATED DB: PDB
DBREF 4P8L A 1 461 UNP P72056 DPRE1_MYCTU 1 461
DBREF 4P8L B 1 461 UNP P72056 DPRE1_MYCTU 1 461
SEQADV 4P8L GLY A -18 UNP P72056 EXPRESSION TAG
SEQADV 4P8L SER A -17 UNP P72056 EXPRESSION TAG
SEQADV 4P8L SER A -16 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS A -15 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS A -14 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS A -13 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS A -12 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS A -11 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS A -10 UNP P72056 EXPRESSION TAG
SEQADV 4P8L SER A -9 UNP P72056 EXPRESSION TAG
SEQADV 4P8L SER A -8 UNP P72056 EXPRESSION TAG
SEQADV 4P8L GLY A -7 UNP P72056 EXPRESSION TAG
SEQADV 4P8L LEU A -6 UNP P72056 EXPRESSION TAG
SEQADV 4P8L VAL A -5 UNP P72056 EXPRESSION TAG
SEQADV 4P8L PRO A -4 UNP P72056 EXPRESSION TAG
SEQADV 4P8L ARG A -3 UNP P72056 EXPRESSION TAG
SEQADV 4P8L GLY A -2 UNP P72056 EXPRESSION TAG
SEQADV 4P8L SER A -1 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS A 0 UNP P72056 EXPRESSION TAG
SEQADV 4P8L GLY B -18 UNP P72056 EXPRESSION TAG
SEQADV 4P8L SER B -17 UNP P72056 EXPRESSION TAG
SEQADV 4P8L SER B -16 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS B -15 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS B -14 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS B -13 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS B -12 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS B -11 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS B -10 UNP P72056 EXPRESSION TAG
SEQADV 4P8L SER B -9 UNP P72056 EXPRESSION TAG
SEQADV 4P8L SER B -8 UNP P72056 EXPRESSION TAG
SEQADV 4P8L GLY B -7 UNP P72056 EXPRESSION TAG
SEQADV 4P8L LEU B -6 UNP P72056 EXPRESSION TAG
SEQADV 4P8L VAL B -5 UNP P72056 EXPRESSION TAG
SEQADV 4P8L PRO B -4 UNP P72056 EXPRESSION TAG
SEQADV 4P8L ARG B -3 UNP P72056 EXPRESSION TAG
SEQADV 4P8L GLY B -2 UNP P72056 EXPRESSION TAG
SEQADV 4P8L SER B -1 UNP P72056 EXPRESSION TAG
SEQADV 4P8L HIS B 0 UNP P72056 EXPRESSION TAG
SEQRES 1 A 480 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 480 VAL PRO ARG GLY SER HIS MET LEU SER VAL GLY ALA THR
SEQRES 3 A 480 THR THR ALA THR ARG LEU THR GLY TRP GLY ARG THR ALA
SEQRES 4 A 480 PRO SER VAL ALA ASN VAL LEU ARG THR PRO ASP ALA GLU
SEQRES 5 A 480 MET ILE VAL LYS ALA VAL ALA ARG VAL ALA GLU SER GLY
SEQRES 6 A 480 GLY GLY ARG GLY ALA ILE ALA ARG GLY LEU GLY ARG SER
SEQRES 7 A 480 TYR GLY ASP ASN ALA GLN ASN GLY GLY GLY LEU VAL ILE
SEQRES 8 A 480 ASP MET THR PRO LEU ASN THR ILE HIS SER ILE ASP ALA
SEQRES 9 A 480 ASP THR LYS LEU VAL ASP ILE ASP ALA GLY VAL ASN LEU
SEQRES 10 A 480 ASP GLN LEU MET LYS ALA ALA LEU PRO PHE GLY LEU TRP
SEQRES 11 A 480 VAL PRO VAL LEU PRO GLY THR ARG GLN VAL THR VAL GLY
SEQRES 12 A 480 GLY ALA ILE ALA CYS ASP ILE HIS GLY LYS ASN HIS HIS
SEQRES 13 A 480 SER ALA GLY SER PHE GLY ASN HIS VAL ARG SER MET ASP
SEQRES 14 A 480 LEU LEU THR ALA ASP GLY GLU ILE ARG HIS LEU THR PRO
SEQRES 15 A 480 THR GLY GLU ASP ALA GLU LEU PHE TRP ALA THR VAL GLY
SEQRES 16 A 480 GLY ASN GLY LEU THR GLY ILE ILE MET ARG ALA THR ILE
SEQRES 17 A 480 GLU MET THR PRO THR SER THR ALA TYR PHE ILE ALA ASP
SEQRES 18 A 480 GLY ASP VAL THR ALA SER LEU ASP GLU THR ILE ALA LEU
SEQRES 19 A 480 HIS SER ASP GLY SER GLU ALA ARG TYR THR TYR SER SER
SEQRES 20 A 480 ALA TRP PHE ASP ALA ILE SER ALA PRO PRO LYS LEU GLY
SEQRES 21 A 480 ARG ALA ALA VAL SER ARG GLY ARG LEU ALA THR VAL GLU
SEQRES 22 A 480 GLN LEU PRO ALA LYS LEU ARG SER GLU PRO LEU LYS PHE
SEQRES 23 A 480 ASP ALA PRO GLN LEU LEU THR LEU PRO ASP VAL PHE PRO
SEQRES 24 A 480 ASN GLY LEU ALA ASN LYS TYR THR PHE GLY PRO ILE GLY
SEQRES 25 A 480 GLU LEU TRP TYR ARG LYS SER GLY THR TYR ARG GLY LYS
SEQRES 26 A 480 VAL GLN ASN LEU THR GLN PHE TYR HIS PRO LEU ASP MET
SEQRES 27 A 480 PHE GLY GLU TRP ASN ARG ALA TYR GLY PRO ALA GLY PHE
SEQRES 28 A 480 LEU GLN TYR GLN PHE VAL ILE PRO THR GLU ALA VAL ASP
SEQRES 29 A 480 GLU PHE LYS LYS ILE ILE GLY VAL ILE GLN ALA SER GLY
SEQRES 30 A 480 HIS TYR SER PHE LEU ASN VAL PHE LYS LEU PHE GLY PRO
SEQRES 31 A 480 ARG ASN GLN ALA PRO LEU SER PHE PRO ILE PRO GLY TRP
SEQRES 32 A 480 ASN ILE CYS VAL ASP PHE PRO ILE LYS ASP GLY LEU GLY
SEQRES 33 A 480 LYS PHE VAL SER GLU LEU ASP ARG ARG VAL LEU GLU PHE
SEQRES 34 A 480 GLY GLY ARG LEU TYR THR ALA LYS ASP SER ARG THR THR
SEQRES 35 A 480 ALA GLU THR PHE HIS ALA MET TYR PRO ARG VAL ASP GLU
SEQRES 36 A 480 TRP ILE SER VAL ARG ARG LYS VAL ASP PRO LEU ARG VAL
SEQRES 37 A 480 PHE ALA SER ASP MET ALA ARG ARG LEU GLU LEU LEU
SEQRES 1 B 480 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 B 480 VAL PRO ARG GLY SER HIS MET LEU SER VAL GLY ALA THR
SEQRES 3 B 480 THR THR ALA THR ARG LEU THR GLY TRP GLY ARG THR ALA
SEQRES 4 B 480 PRO SER VAL ALA ASN VAL LEU ARG THR PRO ASP ALA GLU
SEQRES 5 B 480 MET ILE VAL LYS ALA VAL ALA ARG VAL ALA GLU SER GLY
SEQRES 6 B 480 GLY GLY ARG GLY ALA ILE ALA ARG GLY LEU GLY ARG SER
SEQRES 7 B 480 TYR GLY ASP ASN ALA GLN ASN GLY GLY GLY LEU VAL ILE
SEQRES 8 B 480 ASP MET THR PRO LEU ASN THR ILE HIS SER ILE ASP ALA
SEQRES 9 B 480 ASP THR LYS LEU VAL ASP ILE ASP ALA GLY VAL ASN LEU
SEQRES 10 B 480 ASP GLN LEU MET LYS ALA ALA LEU PRO PHE GLY LEU TRP
SEQRES 11 B 480 VAL PRO VAL LEU PRO GLY THR ARG GLN VAL THR VAL GLY
SEQRES 12 B 480 GLY ALA ILE ALA CYS ASP ILE HIS GLY LYS ASN HIS HIS
SEQRES 13 B 480 SER ALA GLY SER PHE GLY ASN HIS VAL ARG SER MET ASP
SEQRES 14 B 480 LEU LEU THR ALA ASP GLY GLU ILE ARG HIS LEU THR PRO
SEQRES 15 B 480 THR GLY GLU ASP ALA GLU LEU PHE TRP ALA THR VAL GLY
SEQRES 16 B 480 GLY ASN GLY LEU THR GLY ILE ILE MET ARG ALA THR ILE
SEQRES 17 B 480 GLU MET THR PRO THR SER THR ALA TYR PHE ILE ALA ASP
SEQRES 18 B 480 GLY ASP VAL THR ALA SER LEU ASP GLU THR ILE ALA LEU
SEQRES 19 B 480 HIS SER ASP GLY SER GLU ALA ARG TYR THR TYR SER SER
SEQRES 20 B 480 ALA TRP PHE ASP ALA ILE SER ALA PRO PRO LYS LEU GLY
SEQRES 21 B 480 ARG ALA ALA VAL SER ARG GLY ARG LEU ALA THR VAL GLU
SEQRES 22 B 480 GLN LEU PRO ALA LYS LEU ARG SER GLU PRO LEU LYS PHE
SEQRES 23 B 480 ASP ALA PRO GLN LEU LEU THR LEU PRO ASP VAL PHE PRO
SEQRES 24 B 480 ASN GLY LEU ALA ASN LYS TYR THR PHE GLY PRO ILE GLY
SEQRES 25 B 480 GLU LEU TRP TYR ARG LYS SER GLY THR TYR ARG GLY LYS
SEQRES 26 B 480 VAL GLN ASN LEU THR GLN PHE TYR HIS PRO LEU ASP MET
SEQRES 27 B 480 PHE GLY GLU TRP ASN ARG ALA TYR GLY PRO ALA GLY PHE
SEQRES 28 B 480 LEU GLN TYR GLN PHE VAL ILE PRO THR GLU ALA VAL ASP
SEQRES 29 B 480 GLU PHE LYS LYS ILE ILE GLY VAL ILE GLN ALA SER GLY
SEQRES 30 B 480 HIS TYR SER PHE LEU ASN VAL PHE LYS LEU PHE GLY PRO
SEQRES 31 B 480 ARG ASN GLN ALA PRO LEU SER PHE PRO ILE PRO GLY TRP
SEQRES 32 B 480 ASN ILE CYS VAL ASP PHE PRO ILE LYS ASP GLY LEU GLY
SEQRES 33 B 480 LYS PHE VAL SER GLU LEU ASP ARG ARG VAL LEU GLU PHE
SEQRES 34 B 480 GLY GLY ARG LEU TYR THR ALA LYS ASP SER ARG THR THR
SEQRES 35 B 480 ALA GLU THR PHE HIS ALA MET TYR PRO ARG VAL ASP GLU
SEQRES 36 B 480 TRP ILE SER VAL ARG ARG LYS VAL ASP PRO LEU ARG VAL
SEQRES 37 B 480 PHE ALA SER ASP MET ALA ARG ARG LEU GLU LEU LEU
HET FAD A 501 53
HET 36C A 502 26
HET IMD A 503 5
HET FAD B 501 53
HET 36C B 502 26
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM 36C 3-[(4-FLUOROBENZYL)AMINO]-6-(TRIFLUOROMETHYL)
HETNAM 2 36C QUINOXALINE-2-CARBOXYLIC ACID
HETNAM IMD IMIDAZOLE
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 36C 2(C17 H11 F4 N3 O2)
FORMUL 5 IMD C3 H5 N2 1+
FORMUL 8 HOH *276(H2 O)
HELIX 1 AA1 ASP A 31 GLY A 46 1 16
HELIX 2 AA2 ASN A 97 LEU A 106 1 10
HELIX 3 AA3 THR A 122 CYS A 129 1 8
HELIX 4 AA4 ASN A 135 GLY A 140 1 6
HELIX 5 AA5 SER A 141 ASN A 144 5 4
HELIX 6 AA6 ASP A 167 VAL A 175 1 9
HELIX 7 AA7 SER A 208 ASP A 218 1 11
HELIX 8 AA8 GLY A 219 TYR A 224 5 6
HELIX 9 AA9 THR A 252 LEU A 256 5 5
HELIX 10 AB1 PRO A 257 SER A 262 1 6
HELIX 11 AB2 THR A 274 PHE A 279 1 6
HELIX 12 AB3 GLY A 290 GLY A 301 1 12
HELIX 13 AB4 ASN A 309 HIS A 315 1 7
HELIX 14 AB5 PRO A 316 ASN A 324 5 9
HELIX 15 AB6 ALA A 343 SER A 357 1 15
HELIX 16 AB7 GLY A 395 PHE A 410 1 16
HELIX 17 AB8 THR A 423 TYR A 431 1 9
HELIX 18 AB9 ARG A 433 ASP A 445 1 13
HELIX 19 AC1 SER A 452 LEU A 458 1 7
HELIX 20 AC2 ASP B 31 GLY B 46 1 16
HELIX 21 AC3 ASN B 97 LEU B 106 1 10
HELIX 22 AC4 THR B 122 CYS B 129 1 8
HELIX 23 AC5 ASN B 135 GLY B 140 1 6
HELIX 24 AC6 SER B 141 ASN B 144 5 4
HELIX 25 AC7 ASP B 167 VAL B 175 1 9
HELIX 26 AC8 SER B 208 ASP B 218 1 11
HELIX 27 AC9 GLY B 219 TYR B 224 5 6
HELIX 28 AD1 THR B 252 LEU B 256 5 5
HELIX 29 AD2 PRO B 257 SER B 262 1 6
HELIX 30 AD3 GLU B 294 GLY B 301 1 8
HELIX 31 AD4 ASN B 309 TYR B 314 1 6
HELIX 32 AD5 ALA B 343 SER B 357 1 15
HELIX 33 AD6 GLY B 395 PHE B 410 1 16
HELIX 34 AD7 THR B 423 TYR B 431 1 9
HELIX 35 AD8 ARG B 433 ASP B 445 1 13
HELIX 36 AD9 SER B 452 LEU B 458 1 7
SHEET 1 AA1 4 THR A 7 LEU A 13 0
SHEET 2 AA1 4 SER A 22 ARG A 28 -1 O VAL A 26 N THR A 9
SHEET 3 AA1 4 LEU A 70 ASP A 73 1 O VAL A 71 N LEU A 27
SHEET 4 AA1 4 ALA A 51 ARG A 54 1 N ILE A 52 O ILE A 72
SHEET 1 AA210 ILE A 158 LEU A 161 0
SHEET 2 AA210 VAL A 146 LEU A 152 -1 N MET A 149 O LEU A 161
SHEET 3 AA210 ILE A 183 GLU A 190 -1 O ILE A 183 N LEU A 152
SHEET 4 AA210 LEU A 89 ASP A 93 -1 N ILE A 92 O ALA A 187
SHEET 5 AA210 ILE A 80 ASP A 84 -1 N SER A 82 O ASP A 91
SHEET 6 AA210 ILE B 80 ASP B 84 -1 O ILE B 83 N ILE A 83
SHEET 7 AA210 LEU B 89 ASP B 93 -1 O ASP B 91 N SER B 82
SHEET 8 AA210 ILE B 183 GLU B 190 -1 O ALA B 187 N ILE B 92
SHEET 9 AA210 VAL B 146 LEU B 152 -1 N LEU B 152 O ILE B 183
SHEET 10 AA210 ILE B 158 LEU B 161 -1 O LEU B 161 N MET B 149
SHEET 1 AA3 2 LEU A 110 TRP A 111 0
SHEET 2 AA3 2 THR A 192 PRO A 193 -1 O THR A 192 N TRP A 111
SHEET 1 AA4 8 TYR A 303 GLN A 308 0
SHEET 2 AA4 8 PHE A 199 VAL A 205 -1 N PHE A 199 O GLN A 308
SHEET 3 AA4 8 ALA A 243 LEU A 250 -1 O ARG A 247 N ASP A 202
SHEET 4 AA4 8 TYR A 226 PHE A 231 -1 N SER A 228 O SER A 246
SHEET 5 AA4 8 VAL A 365 PHE A 369 -1 O PHE A 366 N ALA A 229
SHEET 6 AA4 8 GLY A 383 PRO A 391 -1 O ASN A 385 N LYS A 367
SHEET 7 AA4 8 PHE A 332 PRO A 340 -1 N LEU A 333 O PHE A 390
SHEET 8 AA4 8 ARG A 413 LEU A 414 -1 O ARG A 413 N VAL A 338
SHEET 1 AA5 4 THR B 9 LEU B 13 0
SHEET 2 AA5 4 SER B 22 LEU B 27 -1 O ALA B 24 N THR B 11
SHEET 3 AA5 4 LEU B 70 ASP B 73 1 O VAL B 71 N ASN B 25
SHEET 4 AA5 4 ALA B 51 ARG B 54 1 N ARG B 54 O ILE B 72
SHEET 1 AA6 2 LEU B 110 TRP B 111 0
SHEET 2 AA6 2 THR B 192 PRO B 193 -1 O THR B 192 N TRP B 111
SHEET 1 AA7 4 TYR B 226 PHE B 231 0
SHEET 2 AA7 4 ALA B 243 LEU B 250 -1 O SER B 246 N SER B 228
SHEET 3 AA7 4 PHE B 199 VAL B 205 -1 N ASP B 204 O VAL B 245
SHEET 4 AA7 4 TYR B 303 GLN B 308 -1 O LYS B 306 N ALA B 201
SHEET 1 AA8 4 VAL B 365 PHE B 369 0
SHEET 2 AA8 4 GLY B 383 PRO B 391 -1 O ASN B 385 N LYS B 367
SHEET 3 AA8 4 PHE B 332 PRO B 340 -1 N ILE B 339 O TRP B 384
SHEET 4 AA8 4 ARG B 413 LEU B 414 -1 O ARG B 413 N VAL B 338
CISPEP 1 SER A 45 GLY A 46 0 -15.72
CISPEP 2 PRO A 237 PRO A 238 0 7.89
CISPEP 3 GLY B 48 ARG B 49 0 11.20
CISPEP 4 PRO B 237 PRO B 238 0 4.60
CISPEP 5 HIS B 315 PRO B 316 0 -4.50
SITE 1 AC1 33 TRP A 16 ILE A 52 ALA A 53 GLY A 55
SITE 2 AC1 33 LEU A 56 GLY A 57 ARG A 58 SER A 59
SITE 3 AC1 33 TYR A 60 ASN A 63 ALA A 64 MET A 74
SITE 4 AC1 33 ALA A 94 PRO A 116 GLY A 117 THR A 118
SITE 5 AC1 33 VAL A 121 THR A 122 GLY A 124 GLY A 125
SITE 6 AC1 33 ALA A 128 CYS A 129 ILE A 131 HIS A 132
SITE 7 AC1 33 ASN A 178 GLY A 179 GLY A 182 ILE A 184
SITE 8 AC1 33 TYR A 415 ALA A 417 36C A 502 HOH A 658
SITE 9 AC1 33 HOH A 660
SITE 1 AC2 14 TYR A 60 HIS A 132 GLY A 133 LYS A 134
SITE 2 AC2 14 LEU A 317 ASN A 324 ARG A 325 GLN A 336
SITE 3 AC2 14 VAL A 365 LYS A 367 ASN A 385 CYS A 387
SITE 4 AC2 14 LYS A 418 FAD A 501
SITE 1 AC3 4 SER A 82 ASP A 84 SER B 82 ASP B 84
SITE 1 AC4 33 TRP B 16 ILE B 52 ALA B 53 GLY B 55
SITE 2 AC4 33 LEU B 56 GLY B 57 ARG B 58 SER B 59
SITE 3 AC4 33 TYR B 60 ASN B 63 ALA B 64 MET B 74
SITE 4 AC4 33 ALA B 94 PRO B 116 GLY B 117 THR B 118
SITE 5 AC4 33 VAL B 121 THR B 122 GLY B 124 GLY B 125
SITE 6 AC4 33 ALA B 128 CYS B 129 ILE B 131 HIS B 132
SITE 7 AC4 33 ASN B 178 GLY B 179 GLY B 182 ILE B 184
SITE 8 AC4 33 TYR B 415 ALA B 417 36C B 502 HOH B 623
SITE 9 AC4 33 HOH B 650
SITE 1 AC5 11 TYR B 60 HIS B 132 GLY B 133 LYS B 134
SITE 2 AC5 11 TRP B 230 ASN B 364 VAL B 365 LYS B 367
SITE 3 AC5 11 CYS B 387 LYS B 418 FAD B 501
CRYST1 76.946 83.149 80.524 90.00 102.79 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012996 0.000000 0.002950 0.00000
SCALE2 0.000000 0.012027 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012735 0.00000
ATOM 1 N GLY A 5 8.283 -3.889 1.680 1.00 59.83 N
ATOM 2 CA GLY A 5 8.844 -3.507 0.351 1.00 61.35 C
ATOM 3 C GLY A 5 7.777 -3.287 -0.705 1.00 61.52 C
ATOM 4 O GLY A 5 7.197 -4.246 -1.220 1.00 62.70 O
ATOM 5 N ALA A 6 7.533 -2.020 -1.035 1.00 60.10 N
ATOM 6 CA ALA A 6 6.507 -1.631 -2.010 1.00 60.00 C
ATOM 7 C ALA A 6 6.805 -2.114 -3.429 1.00 60.18 C
ATOM 8 O ALA A 6 7.940 -2.010 -3.906 1.00 59.11 O
ATOM 9 CB ALA A 6 6.317 -0.120 -2.008 1.00 58.46 C
ATOM 10 N THR A 7 5.774 -2.641 -4.088 1.00 59.10 N
ATOM 11 CA THR A 7 5.841 -3.027 -5.501 1.00 57.90 C
ATOM 12 C THR A 7 4.584 -2.562 -6.248 1.00 59.24 C
ATOM 13 O THR A 7 3.473 -2.614 -5.704 1.00 54.64 O
ATOM 14 CB THR A 7 5.994 -4.558 -5.692 1.00 57.62 C
ATOM 15 OG1 THR A 7 4.858 -5.237 -5.142 1.00 56.63 O
ATOM 16 CG2 THR A 7 7.276 -5.087 -5.035 1.00 55.40 C
ATOM 17 N THR A 8 4.781 -2.092 -7.481 1.00 59.06 N
ATOM 18 CA THR A 8 3.692 -1.762 -8.406 1.00 60.01 C
ATOM 19 C THR A 8 3.844 -2.612 -9.663 1.00 60.90 C
ATOM 20 O THR A 8 4.817 -2.462 -10.409 1.00 60.51 O
ATOM 21 CB THR A 8 3.666 -0.263 -8.792 1.00 61.63 C
ATOM 22 OG1 THR A 8 4.998 0.192 -9.074 1.00 64.23 O
ATOM 23 CG2 THR A 8 3.069 0.584 -7.671 1.00 59.28 C
ATOM 24 N THR A 9 2.880 -3.503 -9.885 1.00 59.67 N
ATOM 25 CA THR A 9 2.965 -4.515 -10.938 1.00 60.74 C
ATOM 26 C THR A 9 1.677 -4.570 -11.757 1.00 60.00 C
ATOM 27 O THR A 9 0.581 -4.567 -11.195 1.00 62.60 O
ATOM 28 CB THR A 9 3.203 -5.918 -10.334 1.00 60.74 C
ATOM 29 OG1 THR A 9 4.150 -5.831 -9.263 1.00 63.50 O
ATOM 30 CG2 THR A 9 3.715 -6.898 -11.385 1.00 61.53 C
ATOM 31 N ALA A 10 1.813 -4.622 -13.081 1.00 57.47 N
ATOM 32 CA ALA A 10 0.674 -4.864 -13.961 1.00 54.96 C
ATOM 33 C ALA A 10 0.204 -6.300 -13.749 1.00 54.59 C
ATOM 34 O ALA A 10 0.993 -7.241 -13.868 1.00 54.16 O
ATOM 35 CB ALA A 10 1.055 -4.630 -15.412 1.00 53.71 C
ATOM 36 N THR A 11 -1.074 -6.466 -13.411 1.00 50.60 N
ATOM 37 CA THR A 11 -1.597 -7.788 -13.067 1.00 49.70 C
ATOM 38 C THR A 11 -2.992 -8.014 -13.641 1.00 49.75 C
ATOM 39 O THR A 11 -3.862 -7.140 -13.566 1.00 49.48 O
ATOM 40 CB THR A 11 -1.618 -8.006 -11.534 1.00 49.00 C
ATOM 41 OG1 THR A 11 -0.403 -7.508 -10.960 1.00 45.92 O
ATOM 42 CG2 THR A 11 -1.782 -9.485 -11.179 1.00 47.88 C
ATOM 43 N ARG A 12 -3.184 -9.194 -14.220 1.00 51.09 N
ATOM 44 CA ARG A 12 -4.475 -9.623 -14.728 1.00 51.31 C
ATOM 45 C ARG A 12 -5.305 -10.121 -13.550 1.00 49.60 C
ATOM 46 O ARG A 12 -4.947 -11.107 -12.897 1.00 49.19 O
ATOM 47 CB ARG A 12 -4.286 -10.738 -15.759 1.00 53.35 C
ATOM 48 CG ARG A 12 -5.573 -11.313 -16.328 1.00 55.37 C
ATOM 49 CD ARG A 12 -5.318 -12.723 -16.833 1.00 58.15 C
ATOM 50 NE ARG A 12 -6.180 -13.089 -17.953 1.00 59.70 N
ATOM 51 CZ ARG A 12 -7.202 -13.936 -17.880 1.00 60.96 C
ATOM 52 NH1 ARG A 12 -7.517 -14.516 -16.727 1.00 64.43 N
ATOM 53 NH2 ARG A 12 -7.915 -14.201 -18.968 1.00 61.81 N
ATOM 54 N LEU A 13 -6.410 -9.435 -13.277 1.00 46.44 N
ATOM 55 CA LEU A 13 -7.220 -9.764 -12.111 1.00 45.13 C
ATOM 56 C LEU A 13 -8.604 -10.254 -12.482 1.00 43.85 C
ATOM 57 O LEU A 13 -9.221 -9.757 -13.429 1.00 44.74 O
ATOM 58 CB LEU A 13 -7.333 -8.558 -11.181 1.00 43.79 C
ATOM 59 CG LEU A 13 -6.026 -7.918 -10.713 1.00 43.78 C
ATOM 60 CD1 LEU A 13 -6.308 -6.515 -10.209 1.00 41.65 C
ATOM 61 CD2 LEU A 13 -5.337 -8.772 -9.651 1.00 40.87 C
ATOM 62 N THR A 14 -9.065 -11.249 -11.730 1.00 43.95 N
ATOM 63 CA THR A 14 -10.457 -11.690 -11.738 1.00 44.40 C
ATOM 64 C THR A 14 -10.918 -11.796 -10.283 1.00 42.70 C
ATOM 65 O THR A 14 -10.093 -11.886 -9.375 1.00 42.66 O
ATOM 66 CB THR A 14 -10.650 -13.078 -12.413 1.00 44.89 C
ATOM 67 OG1 THR A 14 -10.230 -14.128 -11.525 1.00 43.10 O
ATOM 68 CG2 THR A 14 -9.897 -13.183 -13.748 1.00 45.52 C
ATOM 69 N GLY A 15 -12.230 -11.788 -10.062 1.00 42.58 N
ATOM 70 CA GLY A 15 -12.785 -12.170 -8.763 1.00 40.56 C
ATOM 71 C GLY A 15 -12.719 -13.682 -8.613 1.00 41.21 C
ATOM 72 O GLY A 15 -12.184 -14.383 -9.480 1.00 39.93 O
ATOM 73 N TRP A 16 -13.282 -14.191 -7.521 1.00 41.61 N
ATOM 74 CA TRP A 16 -13.297 -15.625 -7.240 1.00 40.68 C
ATOM 75 C TRP A 16 -13.899 -16.446 -8.356 1.00 42.91 C
ATOM 76 O TRP A 16 -13.531 -17.605 -8.538 1.00 42.76 O
ATOM 77 CB TRP A 16 -14.029 -15.889 -5.931 1.00 40.48 C
ATOM 78 CG TRP A 16 -13.586 -17.147 -5.228 1.00 40.19 C
ATOM 79 CD1 TRP A 16 -14.336 -18.294 -4.982 1.00 37.39 C
ATOM 80 CD2 TRP A 16 -12.255 -17.430 -4.657 1.00 40.80 C
ATOM 81 NE1 TRP A 16 -13.590 -19.230 -4.310 1.00 40.44 N
ATOM 82 CE2 TRP A 16 -12.334 -18.781 -4.088 1.00 41.05 C
ATOM 83 CE3 TRP A 16 -11.055 -16.728 -4.570 1.00 42.84 C
ATOM 84 CZ2 TRP A 16 -11.249 -19.381 -3.461 1.00 43.50 C
ATOM 85 CZ3 TRP A 16 -9.964 -17.342 -3.935 1.00 44.75 C
ATOM 86 CH2 TRP A 16 -10.061 -18.640 -3.395 1.00 44.86 C
ATOM 87 N GLY A 17 -14.813 -15.845 -9.121 1.00 45.14 N
ATOM 88 CA GLY A 17 -15.496 -16.513 -10.234 1.00 46.48 C
ATOM 89 C GLY A 17 -14.655 -16.785 -11.476 1.00 49.34 C
ATOM 90 O GLY A 17 -15.093 -17.504 -12.375 1.00 46.92 O
ATOM 91 N ARG A 18 -13.451 -16.212 -11.520 1.00 51.48 N
ATOM 92 CA ARG A 18 -12.515 -16.348 -12.654 1.00 54.94 C
ATOM 93 C ARG A 18 -13.080 -15.842 -13.996 1.00 54.47 C
ATOM 94 O ARG A 18 -12.728 -16.358 -15.057 1.00 55.43 O
ATOM 95 CB ARG A 18 -11.976 -17.790 -12.797 1.00 58.94 C
ATOM 96 CG ARG A 18 -11.687 -18.541 -11.500 1.00 62.55 C
ATOM 97 CD ARG A 18 -10.587 -17.904 -10.665 1.00 66.22 C
ATOM 98 NE ARG A 18 -10.485 -18.553 -9.358 1.00 70.57 N
ATOM 99 CZ ARG A 18 -9.884 -18.031 -8.291 1.00 70.61 C
ATOM 100 NH1 ARG A 18 -9.316 -16.829 -8.349 1.00 68.03 N
ATOM 101 NH2 ARG A 18 -9.858 -18.717 -7.155 1.00 70.13 N
ATOM 102 N THR A 19 -13.949 -14.833 -13.942 1.00 54.31 N
ATOM 103 CA THR A 19 -14.525 -14.233 -15.152 1.00 53.90 C
ATOM 104 C THR A 19 -14.144 -12.758 -15.274 1.00 50.57 C
ATOM 105 O THR A 19 -13.546 -12.191 -14.361 1.00 47.92 O
ATOM 106 CB THR A 19 -16.064 -14.383 -15.215 1.00 55.03 C
ATOM 107 OG1 THR A 19 -16.651 -13.884 -14.005 1.00 58.47 O
ATOM 108 CG2 THR A 19 -16.464 -15.841 -15.412 1.00 55.70 C
ATOM 109 N ALA A 20 -14.488 -12.158 -16.414 1.00 49.44 N
ATOM 110 CA ALA A 20 -14.189 -10.752 -16.725 1.00 50.21 C
ATOM 111 C ALA A 20 -12.805 -10.266 -16.249 1.00 49.22 C
ATOM 112 O ALA A 20 -12.720 -9.357 -15.419 1.00 46.27 O
ATOM 113 CB ALA A 20 -15.301 -9.846 -16.199 1.00 50.28 C
ATOM 114 N PRO A 21 -11.714 -10.878 -16.763 1.00 49.42 N
ATOM 115 CA PRO A 21 -10.374 -10.395 -16.395 1.00 48.44 C
ATOM 116 C PRO A 21 -10.088 -8.989 -16.923 1.00 48.78 C
ATOM 117 O PRO A 21 -10.568 -8.617 -17.995 1.00 51.28 O
ATOM 118 CB PRO A 21 -9.435 -11.411 -17.056 1.00 49.80 C
ATOM 119 CG PRO A 21 -10.239 -12.033 -18.149 1.00 49.43 C
ATOM 120 CD PRO A 21 -11.650 -12.063 -17.640 1.00 49.55 C
ATOM 121 N SER A 22 -9.329 -8.210 -16.161 1.00 47.09 N
ATOM 122 CA SER A 22 -8.867 -6.899 -16.613 1.00 45.70 C
ATOM 123 C SER A 22 -7.524 -6.577 -15.967 1.00 44.77 C
ATOM 124 O SER A 22 -7.241 -7.016 -14.849 1.00 45.69 O
ATOM 125 CB SER A 22 -9.901 -5.806 -16.315 1.00 44.10 C
ATOM 126 OG SER A 22 -10.029 -5.584 -14.923 1.00 41.85 O
ATOM 127 N VAL A 23 -6.699 -5.817 -16.680 1.00 44.55 N
ATOM 128 CA VAL A 23 -5.325 -5.567 -16.253 1.00 43.22 C
ATOM 129 C VAL A 23 -5.246 -4.237 -15.511 1.00 43.03 C
ATOM 130 O VAL A 23 -5.735 -3.215 -15.996 1.00 43.16 O
ATOM 131 CB VAL A 23 -4.325 -5.592 -17.442 1.00 42.41 C
ATOM 132 CG1 VAL A 23 -2.890 -5.466 -16.944 1.00 40.89 C
ATOM 133 CG2 VAL A 23 -4.478 -6.872 -18.252 1.00 40.46 C
ATOM 134 N ALA A 24 -4.639 -4.271 -14.329 1.00 43.57 N
ATOM 135 CA ALA A 24 -4.464 -3.084 -13.504 1.00 44.28 C
ATOM 136 C ALA A 24 -3.066 -3.044 -12.902 1.00 44.07 C
ATOM 137 O ALA A 24 -2.422 -4.084 -12.738 1.00 46.12 O
ATOM 138 CB ALA A 24 -5.506 -3.063 -12.396 1.00 42.58 C
ATOM 139 N ASN A 25 -2.599 -1.840 -12.579 1.00 44.52 N
ATOM 140 CA ASN A 25 -1.395 -1.684 -11.769 1.00 46.48 C
ATOM 141 C ASN A 25 -1.713 -2.013 -10.312 1.00 45.76 C
ATOM 142 O ASN A 25 -2.414 -1.248 -9.643 1.00 46.69 O
ATOM 143 CB ASN A 25 -0.841 -0.260 -11.880 1.00 48.87 C
ATOM 144 CG ASN A 25 0.064 -0.076 -13.083 1.00 55.34 C
ATOM 145 OD1 ASN A 25 1.190 -0.586 -13.114 1.00 58.21 O
ATOM 146 ND2 ASN A 25 -0.416 0.666 -14.077 1.00 53.51 N
ATOM 147 N VAL A 26 -1.207 -3.147 -9.830 1.00 43.27 N
ATOM 148 CA VAL A 26 -1.426 -3.562 -8.444 1.00 40.79 C
ATOM 149 C VAL A 26 -0.324 -3.049 -7.521 1.00 41.91 C
ATOM 150 O VAL A 26 0.823 -3.501 -7.597 1.00 44.31 O
ATOM 151 CB VAL A 26 -1.559 -5.096 -8.310 1.00 39.85 C
ATOM 152 CG1 VAL A 26 -1.577 -5.520 -6.844 1.00 38.32 C
ATOM 153 CG2 VAL A 26 -2.819 -5.590 -9.004 1.00 39.37 C
ATOM 154 N LEU A 27 -0.670 -2.088 -6.668 1.00 39.75 N
ATOM 155 CA LEU A 27 0.226 -1.661 -5.597 1.00 41.74 C
ATOM 156 C LEU A 27 0.127 -2.611 -4.406 1.00 42.98 C
ATOM 157 O LEU A 27 -0.969 -3.005 -3.989 1.00 43.02 O
ATOM 158 CB LEU A 27 -0.058 -0.214 -5.161 1.00 42.54 C
ATOM 159 CG LEU A 27 0.622 0.307 -3.880 1.00 43.86 C
ATOM 160 CD1 LEU A 27 2.145 0.287 -3.979 1.00 42.51 C
ATOM 161 CD2 LEU A 27 0.128 1.704 -3.530 1.00 42.14 C
ATOM 162 N ARG A 28 1.281 -2.976 -3.860 1.00 42.31 N
ATOM 163 CA ARG A 28 1.340 -3.855 -2.707 1.00 41.79 C
ATOM 164 C ARG A 28 2.429 -3.407 -1.741 1.00 43.19 C
ATOM 165 O ARG A 28 3.615 -3.675 -1.951 1.00 43.74 O
ATOM 166 CB ARG A 28 1.559 -5.292 -3.159 1.00 43.04 C
ATOM 167 CG ARG A 28 1.661 -6.293 -2.031 1.00 45.43 C
ATOM 168 CD ARG A 28 1.702 -7.705 -2.578 1.00 48.42 C
ATOM 169 NE ARG A 28 2.214 -8.626 -1.572 1.00 52.77 N
ATOM 170 CZ ARG A 28 1.461 -9.395 -0.793 1.00 54.38 C
ATOM 171 NH1 ARG A 28 0.135 -9.380 -0.901 1.00 53.42 N
ATOM 172 NH2 ARG A 28 2.043 -10.189 0.094 1.00 55.12 N
ATOM 173 N THR A 29 2.012 -2.722 -0.681 1.00 41.71 N
ATOM 174 CA THR A 29 2.939 -2.171 0.308 1.00 43.03 C
ATOM 175 C THR A 29 2.414 -2.362 1.729 1.00 42.79 C
ATOM 176 O THR A 29 1.213 -2.233 1.957 1.00 40.34 O
ATOM 177 CB THR A 29 3.219 -0.670 0.047 1.00 42.31 C
ATOM 178 OG1 THR A 29 3.943 -0.109 1.149 1.00 44.67 O
ATOM 179 CG2 THR A 29 1.924 0.121 -0.156 1.00 41.58 C
ATOM 180 N PRO A 30 3.309 -2.676 2.690 1.00 44.45 N
ATOM 181 CA PRO A 30 2.857 -2.716 4.084 1.00 43.63 C
ATOM 182 C PRO A 30 2.824 -1.332 4.721 1.00 44.74 C
ATOM 183 O PRO A 30 2.436 -1.191 5.882 1.00 44.22 O
ATOM 184 CB PRO A 30 3.901 -3.604 4.767 1.00 45.92 C
ATOM 185 CG PRO A 30 5.143 -3.427 3.949 1.00 44.65 C
ATOM 186 CD PRO A 30 4.706 -3.133 2.541 1.00 44.51 C
ATOM 187 N ASP A 31 3.207 -0.318 3.951 1.00 43.45 N
ATOM 188 CA ASP A 31 3.353 1.033 4.466 1.00 44.51 C
ATOM 189 C ASP A 31 2.110 1.894 4.176 1.00 43.89 C
ATOM 190 O ASP A 31 1.823 2.228 3.025 1.00 43.06 O
ATOM 191 CB ASP A 31 4.634 1.654 3.886 1.00 46.23 C
ATOM 192 CG ASP A 31 4.951 3.025 4.462 1.00 49.61 C
ATOM 193 OD1 ASP A 31 4.166 3.561 5.279 1.00 49.23 O
ATOM 194 OD2 ASP A 31 6.006 3.573 4.087 1.00 52.90 O
ATOM 195 N ALA A 32 1.383 2.247 5.233 1.00 44.01 N
ATOM 196 CA ALA A 32 0.191 3.097 5.128 1.00 45.20 C
ATOM 197 C ALA A 32 0.469 4.434 4.440 1.00 47.27 C
ATOM 198 O ALA A 32 -0.356 4.920 3.653 1.00 45.31 O
ATOM 199 CB ALA A 32 -0.417 3.332 6.503 1.00 45.08 C
ATOM 200 N GLU A 33 1.629 5.018 4.749 1.00 47.82 N
ATOM 201 CA GLU A 33 2.063 6.294 4.182 1.00 48.74 C
ATOM 202 C GLU A 33 2.154 6.246 2.655 1.00 46.37 C
ATOM 203 O GLU A 33 1.791 7.207 1.971 1.00 44.77 O
ATOM 204 CB GLU A 33 3.415 6.698 4.782 1.00 53.92 C
ATOM 205 CG GLU A 33 3.714 8.186 4.725 1.00 61.56 C
ATOM 206 CD GLU A 33 2.844 9.005 5.665 1.00 66.33 C
ATOM 207 OE1 GLU A 33 3.027 8.896 6.900 1.00 69.36 O
ATOM 208 OE2 GLU A 33 1.985 9.768 5.167 1.00 68.85 O
ATOM 209 N MET A 34 2.638 5.120 2.136 1.00 44.28 N
ATOM 210 CA MET A 34 2.734 4.891 0.696 1.00 44.68 C
ATOM 211 C MET A 34 1.349 4.816 0.043 1.00 43.83 C
ATOM 212 O MET A 34 1.114 5.412 -1.014 1.00 42.32 O
ATOM 213 CB MET A 34 3.525 3.610 0.421 1.00 45.76 C
ATOM 214 CG MET A 34 3.696 3.255 -1.047 1.00 50.33 C
ATOM 215 SD MET A 34 4.863 4.329 -1.913 1.00 59.66 S
ATOM 216 CE MET A 34 3.758 5.494 -2.697 1.00 53.45 C
ATOM 217 N ILE A 35 0.430 4.093 0.678 1.00 41.53 N
ATOM 218 CA ILE A 35 -0.944 4.026 0.187 1.00 40.71 C
ATOM 219 C ILE A 35 -1.522 5.440 0.054 1.00 39.71 C
ATOM 220 O ILE A 35 -2.061 5.787 -0.995 1.00 39.94 O
ATOM 221 CB ILE A 35 -1.825 3.111 1.071 1.00 40.31 C
ATOM 222 CG1 ILE A 35 -1.309 1.675 1.000 1.00 39.13 C
ATOM 223 CG2 ILE A 35 -3.295 3.189 0.654 1.00 40.72 C
ATOM 224 CD1 ILE A 35 -1.884 0.761 2.063 1.00 42.06 C
ATOM 225 N VAL A 36 -1.368 6.257 1.099 1.00 40.94 N
ATOM 226 CA VAL A 36 -1.821 7.658 1.085 1.00 40.27 C
ATOM 227 C VAL A 36 -1.243 8.424 -0.110 1.00 42.18 C
ATOM 228 O VAL A 36 -1.973 9.149 -0.805 1.00 40.55 O
ATOM 229 CB VAL A 36 -1.480 8.391 2.405 1.00 40.19 C
ATOM 230 CG1 VAL A 36 -1.721 9.895 2.281 1.00 39.31 C
ATOM 231 CG2 VAL A 36 -2.292 7.818 3.558 1.00 39.83 C
ATOM 232 N LYS A 37 0.059 8.243 -0.347 1.00 43.28 N
ATOM 233 CA LYS A 37 0.754 8.915 -1.449 1.00 44.44 C
ATOM 234 C LYS A 37 0.191 8.569 -2.821 1.00 43.05 C
ATOM 235 O LYS A 37 -0.006 9.460 -3.653 1.00 43.10 O
ATOM 236 CB LYS A 37 2.253 8.628 -1.405 1.00 46.93 C
ATOM 237 CG LYS A 37 3.028 9.668 -0.628 1.00 51.83 C
ATOM 238 CD LYS A 37 4.296 9.094 -0.015 1.00 54.90 C
ATOM 239 CE LYS A 37 4.602 9.809 1.291 1.00 56.07 C
ATOM 240 NZ LYS A 37 3.340 9.990 2.071 1.00 57.56 N
ATOM 241 N ALA A 38 -0.064 7.277 -3.047 1.00 41.33 N
ATOM 242 CA ALA A 38 -0.653 6.801 -4.301 1.00 39.95 C
ATOM 243 C ALA A 38 -2.030 7.419 -4.560 1.00 39.16 C
ATOM 244 O ALA A 38 -2.330 7.843 -5.678 1.00 39.44 O
ATOM 245 CB ALA A 38 -0.729 5.281 -4.311 1.00 39.18 C
ATOM 246 N VAL A 39 -2.858 7.476 -3.519 1.00 38.28 N
ATOM 247 CA VAL A 39 -4.183 8.084 -3.626 1.00 37.68 C
ATOM 248 C VAL A 39 -4.063 9.589 -3.896 1.00 38.37 C
ATOM 249 O VAL A 39 -4.848 10.146 -4.667 1.00 36.61 O
ATOM 250 CB VAL A 39 -5.047 7.802 -2.376 1.00 36.99 C
ATOM 251 CG1 VAL A 39 -6.383 8.534 -2.455 1.00 35.46 C
ATOM 252 CG2 VAL A 39 -5.266 6.301 -2.220 1.00 36.95 C
ATOM 253 N ALA A 40 -3.067 10.228 -3.280 1.00 39.23 N
ATOM 254 CA ALA A 40 -2.788 11.648 -3.514 1.00 40.60 C
ATOM 255 C ALA A 40 -2.323 11.895 -4.952 1.00 41.58 C
ATOM 256 O ALA A 40 -2.674 12.910 -5.555 1.00 43.40 O
ATOM 257 CB ALA A 40 -1.763 12.164 -2.514 1.00 41.32 C
ATOM 258 N ARG A 41 -1.556 10.946 -5.487 1.00 42.41 N
ATOM 259 CA ARG A 41 -1.082 10.969 -6.865 1.00 45.71 C
ATOM 260 C ARG A 41 -2.233 10.850 -7.875 1.00 45.80 C
ATOM 261 O ARG A 41 -2.371 11.691 -8.771 1.00 44.37 O
ATOM 262 CB ARG A 41 -0.063 9.845 -7.080 1.00 49.71 C
ATOM 263 CG ARG A 41 0.871 10.059 -8.258 1.00 55.91 C
ATOM 264 CD ARG A 41 2.130 10.808 -7.843 1.00 62.46 C
ATOM 265 NE ARG A 41 2.882 11.287 -9.005 1.00 69.74 N
ATOM 266 CZ ARG A 41 3.670 10.527 -9.768 1.00 74.32 C
ATOM 267 NH1 ARG A 41 3.827 9.227 -9.511 1.00 77.09 N
ATOM 268 NH2 ARG A 41 4.303 11.070 -10.802 1.00 77.71 N
ATOM 269 N VAL A 42 -3.054 9.807 -7.725 1.00 44.06 N
ATOM 270 CA VAL A 42 -4.271 9.641 -8.531 1.00 42.53 C
ATOM 271 C VAL A 42 -5.152 10.897 -8.466 1.00 43.33 C
ATOM 272 O VAL A 42 -5.656 11.359 -9.491 1.00 45.41 O
ATOM 273 CB VAL A 42 -5.077 8.379 -8.111 1.00 42.36 C
ATOM 274 CG1 VAL A 42 -6.417 8.308 -8.841 1.00 41.61 C
ATOM 275 CG2 VAL A 42 -4.274 7.112 -8.376 1.00 41.30 C
ATOM 276 N ALA A 43 -5.304 11.463 -7.272 1.00 42.88 N
ATOM 277 CA ALA A 43 -6.166 12.631 -7.071 1.00 46.65 C
ATOM 278 C ALA A 43 -5.595 13.932 -7.649 1.00 51.47 C
ATOM 279 O ALA A 43 -6.344 14.878 -7.910 1.00 51.42 O
ATOM 280 CB ALA A 43 -6.479 12.807 -5.599 1.00 45.15 C
ATOM 281 N GLU A 44 -4.277 14.010 -7.748 1.00 54.69 N
ATOM 282 CA GLU A 44 -3.584 15.144 -8.335 1.00 57.74 C
ATOM 283 C GLU A 44 -3.719 15.201 -9.834 1.00 59.47 C
ATOM 284 O GLU A 44 -3.710 16.247 -10.443 1.00 58.59 O
ATOM 285 CB GLU A 44 -2.150 15.226 -7.852 1.00 57.66 C
ATOM 286 CG GLU A 44 -2.055 16.164 -6.679 1.00 60.20 C
ATOM 287 CD GLU A 44 -0.863 15.937 -5.780 1.00 62.67 C
ATOM 288 OE1 GLU A 44 -0.173 14.923 -5.875 1.00 61.28 O
ATOM 289 OE2 GLU A 44 -0.618 16.809 -4.950 1.00 64.51 O
ATOM 290 N SER A 45 -3.829 14.021 -10.402 1.00 62.12 N
ATOM 291 CA SER A 45 -3.920 13.827 -11.816 1.00 63.41 C
ATOM 292 C SER A 45 -5.153 14.465 -12.478 1.00 65.61 C
ATOM 293 O SER A 45 -5.015 14.994 -13.546 1.00 68.97 O
ATOM 294 CB SER A 45 -3.696 12.370 -12.174 1.00 62.26 C
ATOM 295 OG SER A 45 -4.898 11.718 -12.413 1.00 64.21 O
ATOM 296 N GLY A 46 -6.327 14.485 -11.863 1.00 64.99 N
ATOM 297 CA GLY A 46 -6.673 13.676 -10.725 1.00 68.16 C
ATOM 298 C GLY A 46 -7.925 12.872 -11.013 1.00 69.81 C
ATOM 299 O GLY A 46 -8.993 13.408 -11.231 1.00 71.39 O
ATOM 300 N GLY A 47 -7.760 11.562 -10.975 1.00 70.36 N
ATOM 301 CA GLY A 47 -8.776 10.594 -11.328 1.00 66.37 C
ATOM 302 C GLY A 47 -8.187 9.633 -12.340 1.00 65.51 C
ATOM 303 O GLY A 47 -7.744 8.559 -11.972 1.00 62.57 O
ATOM 304 N GLY A 48 -8.114 10.041 -13.609 1.00 63.52 N
ATOM 305 CA GLY A 48 -7.703 9.117 -14.658 1.00 58.07 C
ATOM 306 C GLY A 48 -8.663 7.956 -14.674 1.00 54.16 C
ATOM 307 O GLY A 48 -9.830 8.186 -14.764 1.00 54.17 O
ATOM 308 N ARG A 49 -8.164 6.733 -14.599 1.00 50.53 N
ATOM 309 CA ARG A 49 -8.982 5.552 -14.386 1.00 47.54 C
ATOM 310 C ARG A 49 -9.164 5.196 -12.922 1.00 44.88 C
ATOM 311 O ARG A 49 -9.730 4.175 -12.619 1.00 44.12 O
ATOM 312 CB ARG A 49 -8.388 4.350 -15.076 1.00 48.11 C
ATOM 313 CG ARG A 49 -8.637 4.283 -16.561 1.00 50.53 C
ATOM 314 CD ARG A 49 -10.095 4.106 -16.880 1.00 51.02 C
ATOM 315 NE ARG A 49 -10.436 2.705 -16.938 1.00 51.84 N
ATOM 316 CZ ARG A 49 -11.405 2.235 -17.678 1.00 51.01 C
ATOM 317 NH1 ARG A 49 -12.111 3.073 -18.390 1.00 51.51 N
ATOM 318 NH2 ARG A 49 -11.663 0.953 -17.694 1.00 49.12 N
ATOM 319 N GLY A 50 -8.608 6.004 -12.034 1.00 41.02 N
ATOM 320 CA GLY A 50 -8.795 5.883 -10.577 1.00 37.32 C
ATOM 321 C GLY A 50 -8.154 4.696 -9.874 1.00 34.51 C
ATOM 322 O GLY A 50 -7.267 4.032 -10.421 1.00 32.99 O
ATOM 323 N ALA A 51 -8.628 4.424 -8.656 1.00 32.74 N
ATOM 324 CA ALA A 51 -8.072 3.376 -7.790 1.00 31.65 C
ATOM 325 C ALA A 51 -9.160 2.631 -7.001 1.00 31.04 C
ATOM 326 O ALA A 51 -10.209 3.202 -6.693 1.00 30.83 O
ATOM 327 CB ALA A 51 -7.056 3.978 -6.827 1.00 30.24 C
ATOM 328 N ILE A 52 -8.903 1.366 -6.669 1.00 30.91 N
ATOM 329 CA ILE A 52 -9.806 0.597 -5.793 1.00 30.12 C
ATOM 330 C ILE A 52 -9.005 -0.291 -4.836 1.00 30.58 C
ATOM 331 O ILE A 52 -7.961 -0.837 -5.220 1.00 31.38 O
ATOM 332 CB ILE A 52 -10.851 -0.234 -6.601 1.00 28.82 C
ATOM 333 CG1 ILE A 52 -12.050 -0.625 -5.728 1.00 28.87 C
ATOM 334 CG2 ILE A 52 -10.238 -1.470 -7.240 1.00 28.40 C
ATOM 335 CD1 ILE A 52 -13.045 0.500 -5.545 1.00 28.44 C
ATOM 336 N ALA A 53 -9.466 -0.420 -3.590 1.00 27.06 N
ATOM 337 CA ALA A 53 -8.884 -1.421 -2.696 1.00 27.20 C
ATOM 338 C ALA A 53 -9.208 -2.853 -3.130 1.00 26.89 C
ATOM 339 O ALA A 53 -10.240 -3.115 -3.755 1.00 27.42 O
ATOM 340 CB ALA A 53 -9.311 -1.188 -1.254 1.00 26.10 C
ATOM 341 N ARG A 54 -8.300 -3.766 -2.810 1.00 26.99 N
ATOM 342 CA ARG A 54 -8.537 -5.200 -2.945 1.00 27.75 C
ATOM 343 C ARG A 54 -8.153 -5.894 -1.648 1.00 26.39 C
ATOM 344 O ARG A 54 -7.130 -5.573 -1.041 1.00 26.08 O
ATOM 345 CB ARG A 54 -7.730 -5.770 -4.107 1.00 28.33 C
ATOM 346 CG ARG A 54 -7.901 -7.259 -4.350 1.00 29.80 C
ATOM 347 CD ARG A 54 -7.092 -7.651 -5.580 1.00 30.92 C
ATOM 348 NE ARG A 54 -7.317 -9.036 -5.969 1.00 32.75 N
ATOM 349 CZ ARG A 54 -8.253 -9.442 -6.827 1.00 32.67 C
ATOM 350 NH1 ARG A 54 -9.081 -8.569 -7.396 1.00 34.48 N
ATOM 351 NH2 ARG A 54 -8.364 -10.731 -7.116 1.00 31.33 N
ATOM 352 N GLY A 55 -8.993 -6.833 -1.221 1.00 27.46 N
ATOM 353 CA GLY A 55 -8.725 -7.644 -0.034 1.00 27.76 C
ATOM 354 C GLY A 55 -8.193 -9.006 -0.450 1.00 28.31 C
ATOM 355 O GLY A 55 -7.204 -9.091 -1.166 1.00 27.27 O
ATOM 356 N LEU A 56 -8.859 -10.075 -0.029 1.00 27.59 N
ATOM 357 CA LEU A 56 -8.400 -11.420 -0.374 1.00 27.55 C
ATOM 358 C LEU A 56 -8.967 -11.955 -1.694 1.00 28.07 C
ATOM 359 O LEU A 56 -8.738 -13.111 -2.047 1.00 28.26 O
ATOM 360 CB LEU A 56 -8.634 -12.394 0.791 1.00 26.79 C
ATOM 361 CG LEU A 56 -7.540 -12.296 1.869 1.00 27.36 C
ATOM 362 CD1 LEU A 56 -8.015 -12.894 3.185 1.00 25.70 C
ATOM 363 CD2 LEU A 56 -6.226 -12.945 1.434 1.00 25.21 C
ATOM 364 N GLY A 57 -9.711 -11.112 -2.412 1.00 28.58 N
ATOM 365 CA GLY A 57 -10.279 -11.485 -3.706 1.00 29.51 C
ATOM 366 C GLY A 57 -11.375 -12.541 -3.652 1.00 29.78 C
ATOM 367 O GLY A 57 -11.638 -13.213 -4.648 1.00 30.99 O
ATOM 368 N ARG A 58 -12.022 -12.696 -2.497 1.00 29.74 N
ATOM 369 CA ARG A 58 -13.093 -13.696 -2.356 1.00 28.85 C
ATOM 370 C ARG A 58 -14.438 -13.317 -2.981 1.00 27.87 C
ATOM 371 O ARG A 58 -15.295 -14.182 -3.146 1.00 28.87 O
ATOM 372 CB ARG A 58 -13.270 -14.146 -0.892 1.00 27.49 C
ATOM 373 CG ARG A 58 -12.558 -15.450 -0.560 1.00 29.31 C
ATOM 374 CD ARG A 58 -11.064 -15.369 -0.856 1.00 32.19 C
ATOM 375 NE ARG A 58 -10.358 -16.592 -0.474 1.00 33.76 N
ATOM 376 CZ ARG A 58 -9.037 -16.756 -0.535 1.00 34.78 C
ATOM 377 NH1 ARG A 58 -8.246 -15.773 -0.962 1.00 33.73 N
ATOM 378 NH2 ARG A 58 -8.506 -17.907 -0.152 1.00 36.57 N
ATOM 379 N SER A 59 -14.644 -12.045 -3.313 1.00 27.39 N
ATOM 380 CA SER A 59 -15.853 -11.680 -4.068 1.00 28.18 C
ATOM 381 C SER A 59 -15.782 -12.312 -5.455 1.00 28.69 C
ATOM 382 O SER A 59 -14.718 -12.321 -6.087 1.00 27.35 O
ATOM 383 CB SER A 59 -16.046 -10.165 -4.187 1.00 26.54 C
ATOM 384 OG SER A 59 -16.024 -9.559 -2.910 1.00 27.64 O
ATOM 385 N TYR A 60 -16.912 -12.835 -5.913 1.00 27.66 N
ATOM 386 CA TYR A 60 -16.949 -13.599 -7.155 1.00 29.08 C
ATOM 387 C TYR A 60 -16.845 -12.734 -8.399 1.00 29.41 C
ATOM 388 O TYR A 60 -16.390 -13.205 -9.431 1.00 29.16 O
ATOM 389 CB TYR A 60 -18.220 -14.448 -7.245 1.00 28.27 C
ATOM 390 CG TYR A 60 -18.277 -15.599 -6.277 1.00 30.28 C
ATOM 391 CD1 TYR A 60 -18.087 -16.924 -6.710 1.00 31.25 C
ATOM 392 CD2 TYR A 60 -18.530 -15.377 -4.919 1.00 30.01 C
ATOM 393 CE1 TYR A 60 -18.153 -17.986 -5.811 1.00 31.65 C
ATOM 394 CE2 TYR A 60 -18.593 -16.423 -4.022 1.00 31.31 C
ATOM 395 CZ TYR A 60 -18.411 -17.722 -4.463 1.00 32.01 C
ATOM 396 OH TYR A 60 -18.475 -18.733 -3.534 1.00 31.69 O
ATOM 397 N GLY A 61 -17.274 -11.479 -8.303 1.00 28.57 N
ATOM 398 CA GLY A 61 -17.362 -10.621 -9.474 1.00 30.02 C
ATOM 399 C GLY A 61 -16.228 -9.628 -9.576 1.00 29.98 C
ATOM 400 O GLY A 61 -15.094 -9.930 -9.227 1.00 30.37 O
ATOM 401 N ASP A 62 -16.562 -8.419 -10.003 1.00 30.03 N
ATOM 402 CA ASP A 62 -15.571 -7.442 -10.454 1.00 30.00 C
ATOM 403 C ASP A 62 -15.454 -6.200 -9.563 1.00 29.28 C
ATOM 404 O ASP A 62 -15.034 -5.137 -10.033 1.00 28.64 O
ATOM 405 CB ASP A 62 -15.912 -7.021 -11.895 1.00 29.19 C
ATOM 406 CG ASP A 62 -17.357 -6.540 -12.042 1.00 30.34 C
ATOM 407 OD1 ASP A 62 -18.119 -6.594 -11.048 1.00 28.78 O
ATOM 408 OD2 ASP A 62 -17.738 -6.111 -13.153 1.00 29.58 O
ATOM 409 N ASN A 63 -15.809 -6.316 -8.285 1.00 27.79 N
ATOM 410 CA ASN A 63 -15.749 -5.136 -7.413 1.00 27.84 C
ATOM 411 C ASN A 63 -14.358 -4.747 -6.909 1.00 27.76 C
ATOM 412 O ASN A 63 -14.175 -3.617 -6.441 1.00 27.49 O
ATOM 413 CB ASN A 63 -16.741 -5.229 -6.241 1.00 27.51 C
ATOM 414 CG ASN A 63 -16.550 -6.479 -5.402 1.00 28.16 C
ATOM 415 OD1 ASN A 63 -15.679 -7.317 -5.682 1.00 31.15 O
ATOM 416 ND2 ASN A 63 -17.374 -6.623 -4.370 1.00 26.07 N
ATOM 417 N ALA A 64 -13.396 -5.673 -7.007 1.00 28.55 N
ATOM 418 CA ALA A 64 -12.017 -5.460 -6.526 1.00 28.37 C
ATOM 419 C ALA A 64 -10.998 -5.443 -7.665 1.00 30.66 C
ATOM 420 O ALA A 64 -9.810 -5.787 -7.486 1.00 27.19 O
ATOM 421 CB ALA A 64 -11.635 -6.512 -5.488 1.00 28.02 C
ATOM 422 N GLN A 65 -11.466 -5.035 -8.836 1.00 30.86 N
ATOM 423 CA GLN A 65 -10.569 -4.816 -9.958 1.00 33.91 C
ATOM 424 C GLN A 65 -10.868 -3.501 -10.657 1.00 32.67 C
ATOM 425 O GLN A 65 -11.950 -2.931 -10.509 1.00 29.71 O
ATOM 426 CB GLN A 65 -10.601 -5.995 -10.923 1.00 34.29 C
ATOM 427 CG GLN A 65 -11.951 -6.257 -11.542 1.00 36.66 C
ATOM 428 CD GLN A 65 -11.992 -7.608 -12.207 1.00 38.46 C
ATOM 429 OE1 GLN A 65 -12.196 -8.627 -11.549 1.00 39.72 O
ATOM 430 NE2 GLN A 65 -11.791 -7.627 -13.520 1.00 39.43 N
ATOM 431 N ASN A 66 -9.892 -3.021 -11.414 1.00 31.55 N
ATOM 432 CA ASN A 66 -9.990 -1.712 -12.016 1.00 33.38 C
ATOM 433 C ASN A 66 -9.150 -1.658 -13.293 1.00 34.33 C
ATOM 434 O ASN A 66 -8.034 -1.131 -13.285 1.00 34.06 O
ATOM 435 CB ASN A 66 -9.544 -0.645 -11.013 1.00 32.81 C
ATOM 436 CG ASN A 66 -9.794 0.767 -11.506 1.00 34.94 C
ATOM 437 OD1 ASN A 66 -10.612 0.990 -12.402 1.00 38.15 O
ATOM 438 ND2 ASN A 66 -9.102 1.735 -10.909 1.00 32.95 N
ATOM 439 N GLY A 67 -9.708 -2.215 -14.371 1.00 33.88 N
ATOM 440 CA GLY A 67 -9.026 -2.330 -15.665 1.00 34.35 C
ATOM 441 C GLY A 67 -8.463 -1.015 -16.139 1.00 34.62 C
ATOM 442 O GLY A 67 -9.184 -0.021 -16.242 1.00 34.92 O
ATOM 443 N GLY A 68 -7.158 -1.007 -16.392 1.00 35.42 N
ATOM 444 CA GLY A 68 -6.454 0.191 -16.830 1.00 36.49 C
ATOM 445 C GLY A 68 -6.210 1.231 -15.758 1.00 37.44 C
ATOM 446 O GLY A 68 -5.921 2.386 -16.070 1.00 39.05 O
ATOM 447 N GLY A 69 -6.329 0.833 -14.493 1.00 37.90 N
ATOM 448 CA GLY A 69 -6.119 1.754 -13.382 1.00 37.08 C
ATOM 449 C GLY A 69 -5.341 1.127 -12.246 1.00 36.85 C
ATOM 450 O GLY A 69 -4.649 0.129 -12.437 1.00 36.40 O
ATOM 451 N LEU A 70 -5.470 1.708 -11.054 1.00 36.76 N
ATOM 452 CA LEU A 70 -4.734 1.234 -9.883 1.00 36.07 C
ATOM 453 C LEU A 70 -5.587 0.322 -8.988 1.00 36.58 C
ATOM 454 O LEU A 70 -6.762 0.610 -8.708 1.00 33.84 O
ATOM 455 CB LEU A 70 -4.175 2.422 -9.091 1.00 36.13 C
ATOM 456 CG LEU A 70 -3.311 2.182 -7.846 1.00 37.45 C
ATOM 457 CD1 LEU A 70 -1.900 1.743 -8.211 1.00 38.42 C
ATOM 458 CD2 LEU A 70 -3.260 3.434 -6.986 1.00 37.83 C
ATOM 459 N VAL A 71 -4.995 -0.800 -8.585 1.00 35.28 N
ATOM 460 CA VAL A 71 -5.560 -1.649 -7.538 1.00 34.58 C
ATOM 461 C VAL A 71 -4.591 -1.632 -6.363 1.00 35.03 C
ATOM 462 O VAL A 71 -3.385 -1.859 -6.538 1.00 35.26 O
ATOM 463 CB VAL A 71 -5.784 -3.101 -8.022 1.00 33.81 C
ATOM 464 CG1 VAL A 71 -6.124 -4.022 -6.860 1.00 32.25 C
ATOM 465 CG2 VAL A 71 -6.890 -3.150 -9.066 1.00 33.12 C
ATOM 466 N ILE A 72 -5.102 -1.355 -5.169 1.00 32.53 N
ATOM 467 CA ILE A 72 -4.258 -1.393 -3.980 1.00 32.71 C
ATOM 468 C ILE A 72 -4.537 -2.638 -3.142 1.00 33.74 C
ATOM 469 O ILE A 72 -5.601 -2.763 -2.514 1.00 31.88 O
ATOM 470 CB ILE A 72 -4.363 -0.100 -3.147 1.00 32.83 C
ATOM 471 CG1 ILE A 72 -3.895 1.097 -3.981 1.00 33.21 C
ATOM 472 CG2 ILE A 72 -3.531 -0.208 -1.869 1.00 33.09 C
ATOM 473 CD1 ILE A 72 -4.339 2.443 -3.452 1.00 34.17 C
ATOM 474 N ASP A 73 -3.571 -3.560 -3.153 1.00 32.76 N
ATOM 475 CA ASP A 73 -3.654 -4.795 -2.383 1.00 33.40 C
ATOM 476 C ASP A 73 -3.451 -4.505 -0.890 1.00 33.45 C
ATOM 477 O ASP A 73 -2.359 -4.121 -0.463 1.00 30.87 O
ATOM 478 CB ASP A 73 -2.640 -5.822 -2.909 1.00 34.92 C
ATOM 479 CG ASP A 73 -2.551 -7.074 -2.043 1.00 36.99 C
ATOM 480 OD1 ASP A 73 -3.336 -7.241 -1.088 1.00 34.33 O
ATOM 481 OD2 ASP A 73 -1.671 -7.911 -2.321 1.00 40.06 O
ATOM 482 N MET A 74 -4.517 -4.697 -0.107 1.00 31.96 N
ATOM 483 CA MET A 74 -4.527 -4.289 1.295 1.00 31.27 C
ATOM 484 C MET A 74 -4.026 -5.358 2.260 1.00 30.54 C
ATOM 485 O MET A 74 -3.862 -5.082 3.454 1.00 30.72 O
ATOM 486 CB MET A 74 -5.941 -3.846 1.725 1.00 30.63 C
ATOM 487 CG MET A 74 -6.437 -2.558 1.087 1.00 30.42 C
ATOM 488 SD MET A 74 -5.353 -1.136 1.322 1.00 31.14 S
ATOM 489 CE MET A 74 -5.468 -0.821 3.083 1.00 28.58 C
ATOM 490 N THR A 75 -3.799 -6.569 1.754 1.00 29.45 N
ATOM 491 CA THR A 75 -3.388 -7.702 2.601 1.00 30.44 C
ATOM 492 C THR A 75 -2.106 -7.516 3.452 1.00 31.39 C
ATOM 493 O THR A 75 -2.001 -8.127 4.518 1.00 30.30 O
ATOM 494 CB THR A 75 -3.294 -9.035 1.817 1.00 31.33 C
ATOM 495 OG1 THR A 75 -2.410 -8.873 0.706 1.00 31.58 O
ATOM 496 CG2 THR A 75 -4.668 -9.487 1.308 1.00 30.93 C
ATOM 497 N PRO A 76 -1.134 -6.689 2.996 1.00 32.11 N
ATOM 498 CA PRO A 76 0.040 -6.451 3.858 1.00 33.00 C
ATOM 499 C PRO A 76 -0.229 -5.567 5.082 1.00 34.28 C
ATOM 500 O PRO A 76 0.564 -5.593 6.023 1.00 36.37 O
ATOM 501 CB PRO A 76 1.052 -5.753 2.924 1.00 32.64 C
ATOM 502 CG PRO A 76 0.548 -5.985 1.543 1.00 32.28 C
ATOM 503 CD PRO A 76 -0.940 -6.102 1.655 1.00 31.93 C
ATOM 504 N LEU A 77 -1.310 -4.783 5.076 1.00 32.90 N
ATOM 505 CA LEU A 77 -1.687 -4.016 6.272 1.00 33.03 C
ATOM 506 C LEU A 77 -2.520 -4.917 7.158 1.00 31.09 C
ATOM 507 O LEU A 77 -3.737 -4.874 7.097 1.00 30.56 O
ATOM 508 CB LEU A 77 -2.510 -2.780 5.907 1.00 34.89 C
ATOM 509 CG LEU A 77 -1.811 -1.444 5.717 1.00 38.31 C
ATOM 510 CD1 LEU A 77 -1.040 -1.453 4.408 1.00 41.40 C
ATOM 511 CD2 LEU A 77 -2.853 -0.340 5.721 1.00 37.00 C
ATOM 512 N ASN A 78 -1.861 -5.733 7.969 1.00 30.04 N
ATOM 513 CA ASN A 78 -2.526 -6.814 8.668 1.00 29.71 C
ATOM 514 C ASN A 78 -2.143 -6.879 10.147 1.00 28.99 C
ATOM 515 O ASN A 78 -2.114 -7.953 10.749 1.00 27.73 O
ATOM 516 CB ASN A 78 -2.226 -8.148 7.972 1.00 30.28 C
ATOM 517 CG ASN A 78 -0.786 -8.604 8.173 1.00 31.08 C
ATOM 518 OD1 ASN A 78 0.092 -7.804 8.495 1.00 29.66 O
ATOM 519 ND2 ASN A 78 -0.544 -9.898 7.994 1.00 31.07 N
ATOM 520 N THR A 79 -1.859 -5.719 10.720 1.00 27.98 N
ATOM 521 CA THR A 79 -1.505 -5.623 12.122 1.00 28.90 C
ATOM 522 C THR A 79 -2.759 -5.617 12.966 1.00 28.27 C
ATOM 523 O THR A 79 -3.694 -4.861 12.702 1.00 28.87 O
ATOM 524 CB THR A 79 -0.712 -4.335 12.411 1.00 28.49 C
ATOM 525 OG1 THR A 79 0.452 -4.312 11.587 1.00 30.51 O
ATOM 526 CG2 THR A 79 -0.288 -4.253 13.876 1.00 28.88 C
ATOM 527 N ILE A 80 -2.774 -6.487 13.963 1.00 27.88 N
ATOM 528 CA ILE A 80 -3.736 -6.396 15.037 1.00 27.06 C
ATOM 529 C ILE A 80 -3.120 -5.480 16.099 1.00 25.96 C
ATOM 530 O ILE A 80 -2.168 -5.862 16.772 1.00 24.98 O
ATOM 531 CB ILE A 80 -4.064 -7.789 15.616 1.00 27.22 C
ATOM 532 CG1 ILE A 80 -4.752 -8.662 14.557 1.00 26.80 C
ATOM 533 CG2 ILE A 80 -4.944 -7.671 16.856 1.00 27.02 C
ATOM 534 CD1 ILE A 80 -4.778 -10.139 14.913 1.00 26.80 C
ATOM 535 N HIS A 81 -3.665 -4.269 16.240 1.00 26.29 N
ATOM 536 CA HIS A 81 -3.124 -3.305 17.199 1.00 26.40 C
ATOM 537 C HIS A 81 -3.451 -3.641 18.623 1.00 26.26 C
ATOM 538 O HIS A 81 -2.577 -3.601 19.497 1.00 25.09 O
ATOM 539 CB HIS A 81 -3.583 -1.898 16.848 1.00 27.51 C
ATOM 540 CG HIS A 81 -3.076 -1.430 15.515 1.00 28.53 C
ATOM 541 ND1 HIS A 81 -3.797 -1.561 14.376 1.00 29.75 N
ATOM 542 CD2 HIS A 81 -1.863 -0.856 15.154 1.00 27.24 C
ATOM 543 CE1 HIS A 81 -3.084 -1.065 13.346 1.00 29.10 C
ATOM 544 NE2 HIS A 81 -1.899 -0.640 13.823 1.00 28.63 N
ATOM 545 N SER A 82 -4.712 -3.977 18.887 1.00 25.75 N
ATOM 546 CA SER A 82 -5.085 -4.371 20.235 1.00 24.08 C
ATOM 547 C SER A 82 -6.376 -5.148 20.281 1.00 24.36 C
ATOM 548 O SER A 82 -7.216 -5.059 19.376 1.00 24.45 O
ATOM 549 CB SER A 82 -5.182 -3.147 21.167 1.00 25.35 C
ATOM 550 OG SER A 82 -6.332 -2.362 20.874 1.00 24.16 O
ATOM 551 N ILE A 83 -6.521 -5.907 21.365 1.00 23.43 N
ATOM 552 CA ILE A 83 -7.750 -6.590 21.694 1.00 23.13 C
ATOM 553 C ILE A 83 -7.971 -6.334 23.187 1.00 23.98 C
ATOM 554 O ILE A 83 -7.035 -6.415 23.988 1.00 24.37 O
ATOM 555 CB ILE A 83 -7.666 -8.108 21.394 1.00 22.89 C
ATOM 556 CG1 ILE A 83 -7.474 -8.357 19.883 1.00 21.94 C
ATOM 557 CG2 ILE A 83 -8.900 -8.836 21.924 1.00 21.74 C
ATOM 558 CD1 ILE A 83 -7.571 -9.809 19.435 1.00 21.98 C
ATOM 559 N ASP A 84 -9.198 -6.018 23.569 1.00 25.43 N
ATOM 560 CA ASP A 84 -9.490 -5.737 24.977 1.00 25.99 C
ATOM 561 C ASP A 84 -10.706 -6.551 25.384 1.00 26.66 C
ATOM 562 O ASP A 84 -11.756 -6.388 24.792 1.00 26.99 O
ATOM 563 CB ASP A 84 -9.739 -4.234 25.151 1.00 26.80 C
ATOM 564 CG ASP A 84 -9.808 -3.805 26.609 1.00 27.69 C
ATOM 565 OD1 ASP A 84 -10.623 -4.373 27.370 1.00 26.12 O
ATOM 566 OD2 ASP A 84 -9.042 -2.889 26.980 1.00 28.63 O
ATOM 567 N ALA A 85 -10.556 -7.422 26.382 1.00 27.58 N
ATOM 568 CA ALA A 85 -11.640 -8.304 26.837 1.00 30.01 C
ATOM 569 C ALA A 85 -12.717 -7.552 27.615 1.00 30.83 C
ATOM 570 O ALA A 85 -13.876 -7.962 27.618 1.00 32.47 O
ATOM 571 CB ALA A 85 -11.097 -9.445 27.690 1.00 28.77 C
ATOM 572 N ASP A 86 -12.317 -6.465 28.273 1.00 31.07 N
ATOM 573 CA ASP A 86 -13.218 -5.680 29.107 1.00 33.26 C
ATOM 574 C ASP A 86 -14.151 -4.804 28.278 1.00 31.58 C
ATOM 575 O ASP A 86 -15.345 -4.774 28.527 1.00 30.41 O
ATOM 576 CB ASP A 86 -12.431 -4.818 30.109 1.00 34.65 C
ATOM 577 CG ASP A 86 -11.514 -5.644 30.995 1.00 36.51 C
ATOM 578 OD1 ASP A 86 -11.960 -6.686 31.521 1.00 37.35 O
ATOM 579 OD2 ASP A 86 -10.343 -5.242 31.166 1.00 36.38 O
ATOM 580 N THR A 87 -13.598 -4.086 27.305 1.00 30.01 N
ATOM 581 CA THR A 87 -14.409 -3.288 26.390 1.00 29.15 C
ATOM 582 C THR A 87 -14.943 -4.126 25.211 1.00 28.35 C
ATOM 583 O THR A 87 -15.827 -3.674 24.486 1.00 28.25 O
ATOM 584 CB THR A 87 -13.609 -2.100 25.834 1.00 29.84 C
ATOM 585 OG1 THR A 87 -12.605 -2.594 24.940 1.00 26.88 O
ATOM 586 CG2 THR A 87 -12.949 -1.312 26.971 1.00 29.79 C
ATOM 587 N LYS A 88 -14.395 -5.331 25.025 1.00 26.52 N
ATOM 588 CA LYS A 88 -14.740 -6.220 23.899 1.00 27.42 C
ATOM 589 C LYS A 88 -14.370 -5.674 22.518 1.00 26.49 C
ATOM 590 O LYS A 88 -14.850 -6.182 21.496 1.00 25.81 O
ATOM 591 CB LYS A 88 -16.219 -6.640 23.926 1.00 29.05 C
ATOM 592 CG LYS A 88 -16.635 -7.332 25.217 1.00 32.03 C
ATOM 593 CD LYS A 88 -18.136 -7.507 25.279 1.00 35.11 C
ATOM 594 CE LYS A 88 -18.825 -6.263 25.814 1.00 38.13 C
ATOM 595 NZ LYS A 88 -20.298 -6.472 25.810 1.00 41.03 N
ATOM 596 N LEU A 89 -13.508 -4.656 22.493 1.00 26.10 N
ATOM 597 CA LEU A 89 -13.108 -4.013 21.241 1.00 25.42 C
ATOM 598 C LEU A 89 -11.821 -4.594 20.685 1.00 25.00 C
ATOM 599 O LEU A 89 -10.906 -4.915 21.441 1.00 25.03 O
ATOM 600 CB LEU A 89 -12.932 -2.502 21.429 1.00 25.84 C
ATOM 601 CG LEU A 89 -14.130 -1.701 21.962 1.00 26.51 C
ATOM 602 CD1 LEU A 89 -13.762 -0.226 22.044 1.00 26.95 C
ATOM 603 CD2 LEU A 89 -15.368 -1.913 21.099 1.00 26.93 C
ATOM 604 N VAL A 90 -11.761 -4.720 19.360 1.00 23.72 N
ATOM 605 CA VAL A 90 -10.502 -5.014 18.674 1.00 23.90 C
ATOM 606 C VAL A 90 -10.160 -3.855 17.734 1.00 23.80 C
ATOM 607 O VAL A 90 -11.043 -3.335 17.050 1.00 25.01 O
ATOM 608 CB VAL A 90 -10.557 -6.353 17.891 1.00 24.12 C
ATOM 609 CG1 VAL A 90 -10.822 -7.520 18.827 1.00 23.47 C
ATOM 610 CG2 VAL A 90 -11.621 -6.320 16.798 1.00 23.94 C
ATOM 611 N ASP A 91 -8.889 -3.461 17.700 1.00 24.32 N
ATOM 612 CA ASP A 91 -8.404 -2.390 16.825 1.00 25.71 C
ATOM 613 C ASP A 91 -7.440 -2.995 15.814 1.00 26.49 C
ATOM 614 O ASP A 91 -6.338 -3.392 16.174 1.00 26.79 O
ATOM 615 CB ASP A 91 -7.697 -1.311 17.664 1.00 25.58 C
ATOM 616 CG ASP A 91 -7.098 -0.185 16.822 1.00 25.95 C
ATOM 617 OD1 ASP A 91 -7.421 -0.052 15.623 1.00 26.11 O
ATOM 618 OD2 ASP A 91 -6.289 0.585 17.377 1.00 27.40 O
ATOM 619 N ILE A 92 -7.859 -3.087 14.553 1.00 27.03 N
ATOM 620 CA ILE A 92 -7.079 -3.828 13.553 1.00 27.08 C
ATOM 621 C ILE A 92 -7.021 -3.120 12.206 1.00 27.79 C
ATOM 622 O ILE A 92 -7.971 -2.423 11.825 1.00 27.64 O
ATOM 623 CB ILE A 92 -7.571 -5.302 13.346 1.00 27.43 C
ATOM 624 CG1 ILE A 92 -8.829 -5.393 12.443 1.00 28.64 C
ATOM 625 CG2 ILE A 92 -7.693 -6.068 14.667 1.00 26.08 C
ATOM 626 CD1 ILE A 92 -10.131 -4.862 13.026 1.00 27.17 C
ATOM 627 N ASP A 93 -5.897 -3.301 11.506 1.00 27.31 N
ATOM 628 CA ASP A 93 -5.733 -2.857 10.118 1.00 27.89 C
ATOM 629 C ASP A 93 -6.753 -3.566 9.245 1.00 25.87 C
ATOM 630 O ASP A 93 -7.141 -4.694 9.541 1.00 25.66 O
ATOM 631 CB ASP A 93 -4.336 -3.225 9.584 1.00 27.63 C
ATOM 632 CG ASP A 93 -3.233 -2.388 10.172 1.00 30.01 C
ATOM 633 OD1 ASP A 93 -3.521 -1.334 10.775 1.00 29.10 O
ATOM 634 OD2 ASP A 93 -2.049 -2.787 10.019 1.00 32.75 O
ATOM 635 N ALA A 94 -7.155 -2.912 8.158 1.00 25.74 N
ATOM 636 CA ALA A 94 -8.187 -3.446 7.260 1.00 25.19 C
ATOM 637 C ALA A 94 -7.770 -4.731 6.529 1.00 24.83 C
ATOM 638 O ALA A 94 -8.626 -5.496 6.076 1.00 23.24 O
ATOM 639 CB ALA A 94 -8.615 -2.385 6.263 1.00 26.06 C
ATOM 640 N GLY A 95 -6.466 -4.976 6.421 1.00 24.84 N
ATOM 641 CA GLY A 95 -5.971 -6.192 5.767 1.00 25.26 C
ATOM 642 C GLY A 95 -5.970 -7.452 6.619 1.00 25.69 C
ATOM 643 O GLY A 95 -5.716 -8.555 6.119 1.00 25.86 O
ATOM 644 N VAL A 96 -6.210 -7.293 7.915 1.00 25.06 N
ATOM 645 CA VAL A 96 -6.395 -8.430 8.807 1.00 24.90 C
ATOM 646 C VAL A 96 -7.557 -9.287 8.275 1.00 25.90 C
ATOM 647 O VAL A 96 -8.599 -8.761 7.874 1.00 25.90 O
ATOM 648 CB VAL A 96 -6.675 -7.950 10.254 1.00 25.19 C
ATOM 649 CG1 VAL A 96 -7.159 -9.084 11.147 1.00 23.60 C
ATOM 650 CG2 VAL A 96 -5.434 -7.298 10.856 1.00 24.68 C
ATOM 651 N ASN A 97 -7.381 -10.604 8.244 1.00 25.35 N
ATOM 652 CA ASN A 97 -8.468 -11.467 7.812 1.00 24.11 C
ATOM 653 C ASN A 97 -9.177 -12.093 9.011 1.00 23.84 C
ATOM 654 O ASN A 97 -8.646 -12.101 10.111 1.00 22.68 O
ATOM 655 CB ASN A 97 -7.975 -12.536 6.839 1.00 25.17 C
ATOM 656 CG ASN A 97 -7.187 -13.637 7.525 1.00 25.78 C
ATOM 657 OD1 ASN A 97 -7.735 -14.419 8.300 1.00 27.48 O
ATOM 658 ND2 ASN A 97 -5.903 -13.722 7.217 1.00 24.94 N
ATOM 659 N LEU A 98 -10.362 -12.646 8.775 1.00 24.72 N
ATOM 660 CA LEU A 98 -11.249 -13.079 9.860 1.00 25.57 C
ATOM 661 C LEU A 98 -10.815 -14.371 10.557 1.00 26.12 C
ATOM 662 O LEU A 98 -11.184 -14.613 11.708 1.00 25.10 O
ATOM 663 CB LEU A 98 -12.694 -13.161 9.358 1.00 24.13 C
ATOM 664 CG LEU A 98 -13.353 -11.831 8.954 1.00 23.36 C
ATOM 665 CD1 LEU A 98 -14.798 -12.082 8.543 1.00 23.19 C
ATOM 666 CD2 LEU A 98 -13.280 -10.777 10.056 1.00 23.47 C
ATOM 667 N ASP A 99 -10.030 -15.191 9.859 1.00 26.49 N
ATOM 668 CA ASP A 99 -9.410 -16.369 10.455 1.00 26.85 C
ATOM 669 C ASP A 99 -8.332 -15.952 11.459 1.00 25.76 C
ATOM 670 O ASP A 99 -8.336 -16.401 12.603 1.00 24.69 O
ATOM 671 CB ASP A 99 -8.799 -17.256 9.362 1.00 30.73 C
ATOM 672 CG ASP A 99 -8.339 -18.610 9.890 1.00 34.56 C
ATOM 673 OD1 ASP A 99 -9.146 -19.313 10.543 1.00 35.00 O
ATOM 674 OD2 ASP A 99 -7.165 -18.970 9.642 1.00 37.72 O
ATOM 675 N GLN A 100 -7.408 -15.100 11.010 1.00 25.42 N
ATOM 676 CA GLN A 100 -6.408 -14.470 11.871 1.00 25.92 C
ATOM 677 C GLN A 100 -7.050 -13.819 13.112 1.00 25.80 C
ATOM 678 O GLN A 100 -6.617 -14.051 14.251 1.00 26.17 O
ATOM 679 CB GLN A 100 -5.637 -13.429 11.055 1.00 26.25 C
ATOM 680 CG GLN A 100 -4.608 -12.599 11.813 1.00 26.13 C
ATOM 681 CD GLN A 100 -4.134 -11.405 10.992 1.00 26.17 C
ATOM 682 OE1 GLN A 100 -4.617 -11.168 9.874 1.00 26.56 O
ATOM 683 NE2 GLN A 100 -3.187 -10.652 11.535 1.00 25.46 N
ATOM 684 N LEU A 101 -8.100 -13.033 12.881 1.00 25.11 N
ATOM 685 CA LEU A 101 -8.814 -12.344 13.964 1.00 23.98 C
ATOM 686 C LEU A 101 -9.477 -13.323 14.936 1.00 24.69 C
ATOM 687 O LEU A 101 -9.320 -13.196 16.152 1.00 25.25 O
ATOM 688 CB LEU A 101 -9.836 -11.359 13.395 1.00 21.91 C
ATOM 689 CG LEU A 101 -10.562 -10.406 14.359 1.00 21.79 C
ATOM 690 CD1 LEU A 101 -9.608 -9.750 15.346 1.00 19.92 C
ATOM 691 CD2 LEU A 101 -11.322 -9.345 13.568 1.00 22.46 C
ATOM 692 N MET A 102 -10.195 -14.310 14.405 1.00 26.30 N
ATOM 693 CA MET A 102 -10.806 -15.341 15.248 1.00 27.22 C
ATOM 694 C MET A 102 -9.801 -16.002 16.190 1.00 26.73 C
ATOM 695 O MET A 102 -10.058 -16.118 17.391 1.00 25.23 O
ATOM 696 CB MET A 102 -11.509 -16.417 14.408 1.00 29.92 C
ATOM 697 CG MET A 102 -11.944 -17.631 15.236 1.00 32.49 C
ATOM 698 SD MET A 102 -12.622 -18.991 14.265 1.00 40.30 S
ATOM 699 CE MET A 102 -14.244 -18.349 13.889 1.00 38.49 C
ATOM 700 N LYS A 103 -8.664 -16.419 15.634 1.00 27.39 N
ATOM 701 CA LYS A 103 -7.589 -17.069 16.389 1.00 28.66 C
ATOM 702 C LYS A 103 -6.957 -16.165 17.444 1.00 27.13 C
ATOM 703 O LYS A 103 -6.679 -16.616 18.556 1.00 28.53 O
ATOM 704 CB LYS A 103 -6.508 -17.606 15.447 1.00 29.91 C
ATOM 705 CG LYS A 103 -7.005 -18.691 14.505 1.00 35.35 C
ATOM 706 CD LYS A 103 -5.894 -19.211 13.596 1.00 38.92 C
ATOM 707 CE LYS A 103 -6.420 -20.191 12.550 1.00 42.06 C
ATOM 708 NZ LYS A 103 -7.246 -21.291 13.131 1.00 45.02 N
ATOM 709 N ALA A 104 -6.735 -14.899 17.101 1.00 26.09 N
ATOM 710 CA ALA A 104 -6.189 -13.923 18.047 1.00 25.30 C
ATOM 711 C ALA A 104 -7.168 -13.574 19.169 1.00 25.14 C
ATOM 712 O ALA A 104 -6.749 -13.359 20.303 1.00 26.61 O
ATOM 713 CB ALA A 104 -5.757 -12.655 17.320 1.00 25.36 C
ATOM 714 N ALA A 105 -8.463 -13.536 18.861 1.00 24.63 N
ATOM 715 CA ALA A 105 -9.487 -13.104 19.843 1.00 24.83 C
ATOM 716 C ALA A 105 -9.975 -14.180 20.837 1.00 25.28 C
ATOM 717 O ALA A 105 -10.402 -13.860 21.958 1.00 26.79 O
ATOM 718 CB ALA A 105 -10.665 -12.471 19.124 1.00 24.50 C
ATOM 719 N LEU A 106 -9.927 -15.442 20.425 1.00 25.47 N
ATOM 720 CA LEU A 106 -10.389 -16.559 21.261 1.00 26.85 C
ATOM 721 C LEU A 106 -9.793 -16.603 22.681 1.00 27.66 C
ATOM 722 O LEU A 106 -10.540 -16.783 23.646 1.00 28.41 O
ATOM 723 CB LEU A 106 -10.224 -17.921 20.544 1.00 26.77 C
ATOM 724 CG LEU A 106 -11.402 -18.406 19.685 1.00 28.14 C
ATOM 725 CD1 LEU A 106 -11.079 -19.741 19.027 1.00 29.12 C
ATOM 726 CD2 LEU A 106 -12.684 -18.533 20.507 1.00 25.64 C
ATOM 727 N PRO A 107 -8.467 -16.411 22.828 1.00 28.11 N
ATOM 728 CA PRO A 107 -7.936 -16.395 24.203 1.00 28.83 C
ATOM 729 C PRO A 107 -8.518 -15.318 25.128 1.00 29.05 C
ATOM 730 O PRO A 107 -8.312 -15.396 26.337 1.00 31.16 O
ATOM 731 CB PRO A 107 -6.446 -16.146 23.993 1.00 28.70 C
ATOM 732 CG PRO A 107 -6.170 -16.731 22.646 1.00 29.74 C
ATOM 733 CD PRO A 107 -7.378 -16.392 21.831 1.00 28.99 C
ATOM 734 N PHE A 108 -9.199 -14.316 24.574 1.00 28.10 N
ATOM 735 CA PHE A 108 -9.812 -13.244 25.376 1.00 27.69 C
ATOM 736 C PHE A 108 -11.280 -13.545 25.675 1.00 27.87 C
ATOM 737 O PHE A 108 -11.988 -12.712 26.260 1.00 27.13 O
ATOM 738 CB PHE A 108 -9.734 -11.894 24.654 1.00 26.69 C
ATOM 739 CG PHE A 108 -8.334 -11.458 24.304 1.00 25.91 C
ATOM 740 CD1 PHE A 108 -7.691 -10.468 25.052 1.00 26.30 C
ATOM 741 CD2 PHE A 108 -7.657 -12.029 23.228 1.00 25.66 C
ATOM 742 CE1 PHE A 108 -6.407 -10.051 24.729 1.00 25.50 C
ATOM 743 CE2 PHE A 108 -6.377 -11.614 22.896 1.00 24.07 C
ATOM 744 CZ PHE A 108 -5.750 -10.629 23.654 1.00 24.76 C
ATOM 745 N GLY A 109 -11.745 -14.708 25.230 1.00 27.60 N
ATOM 746 CA GLY A 109 -13.174 -15.030 25.290 1.00 28.44 C
ATOM 747 C GLY A 109 -13.978 -14.120 24.375 1.00 27.88 C
ATOM 748 O GLY A 109 -15.078 -13.690 24.718 1.00 26.31 O
ATOM 749 N LEU A 110 -13.419 -13.813 23.207 1.00 27.21 N
ATOM 750 CA LEU A 110 -14.110 -12.958 22.228 1.00 26.31 C
ATOM 751 C LEU A 110 -14.369 -13.693 20.918 1.00 26.60 C
ATOM 752 O LEU A 110 -13.497 -14.425 20.426 1.00 26.96 O
ATOM 753 CB LEU A 110 -13.322 -11.672 21.968 1.00 25.31 C
ATOM 754 CG LEU A 110 -13.148 -10.717 23.152 1.00 26.91 C
ATOM 755 CD1 LEU A 110 -12.407 -9.470 22.684 1.00 27.89 C
ATOM 756 CD2 LEU A 110 -14.485 -10.333 23.772 1.00 25.31 C
ATOM 757 N TRP A 111 -15.558 -13.467 20.357 1.00 24.65 N
ATOM 758 CA TRP A 111 -16.018 -14.127 19.147 1.00 24.68 C
ATOM 759 C TRP A 111 -16.282 -13.115 18.054 1.00 24.48 C
ATOM 760 O TRP A 111 -17.000 -12.130 18.286 1.00 24.35 O
ATOM 761 CB TRP A 111 -17.283 -14.948 19.470 1.00 24.01 C
ATOM 762 CG TRP A 111 -17.655 -15.921 18.377 1.00 24.01 C
ATOM 763 CD1 TRP A 111 -18.656 -15.784 17.426 1.00 22.86 C
ATOM 764 CD2 TRP A 111 -17.005 -17.208 18.063 1.00 23.77 C
ATOM 765 NE1 TRP A 111 -18.675 -16.860 16.581 1.00 23.69 N
ATOM 766 CE2 TRP A 111 -17.714 -17.749 16.901 1.00 23.55 C
ATOM 767 CE3 TRP A 111 -15.952 -17.940 18.615 1.00 24.45 C
ATOM 768 CZ2 TRP A 111 -17.369 -18.974 16.323 1.00 23.79 C
ATOM 769 CZ3 TRP A 111 -15.614 -19.172 18.028 1.00 23.70 C
ATOM 770 CH2 TRP A 111 -16.314 -19.677 16.913 1.00 23.38 C
ATOM 771 N VAL A 112 -15.689 -13.329 16.867 1.00 23.88 N
ATOM 772 CA VAL A 112 -15.977 -12.506 15.666 1.00 24.73 C
ATOM 773 C VAL A 112 -17.498 -12.455 15.477 1.00 25.35 C
ATOM 774 O VAL A 112 -18.136 -13.502 15.349 1.00 26.08 O
ATOM 775 CB VAL A 112 -15.285 -13.062 14.386 1.00 24.32 C
ATOM 776 CG1 VAL A 112 -15.689 -12.272 13.144 1.00 24.69 C
ATOM 777 CG2 VAL A 112 -13.764 -13.040 14.528 1.00 24.34 C
ATOM 778 N PRO A 113 -18.093 -11.247 15.508 1.00 24.97 N
ATOM 779 CA PRO A 113 -19.573 -11.173 15.576 1.00 24.64 C
ATOM 780 C PRO A 113 -20.317 -11.624 14.309 1.00 23.81 C
ATOM 781 O PRO A 113 -21.449 -12.101 14.394 1.00 23.22 O
ATOM 782 CB PRO A 113 -19.837 -9.689 15.889 1.00 24.92 C
ATOM 783 CG PRO A 113 -18.620 -8.981 15.352 1.00 25.46 C
ATOM 784 CD PRO A 113 -17.477 -9.916 15.652 1.00 25.18 C
ATOM 785 N VAL A 114 -19.693 -11.493 13.141 1.00 23.28 N
ATOM 786 CA VAL A 114 -20.301 -11.968 11.896 1.00 22.35 C
ATOM 787 C VAL A 114 -19.258 -12.746 11.087 1.00 24.59 C
ATOM 788 O VAL A 114 -18.226 -12.182 10.693 1.00 22.57 O
ATOM 789 CB VAL A 114 -20.893 -10.795 11.074 1.00 22.61 C
ATOM 790 CG1 VAL A 114 -21.435 -11.270 9.737 1.00 21.92 C
ATOM 791 CG2 VAL A 114 -21.998 -10.073 11.856 1.00 21.96 C
ATOM 792 N LEU A 115 -19.519 -14.040 10.871 1.00 24.78 N
ATOM 793 CA LEU A 115 -18.646 -14.894 10.060 1.00 26.01 C
ATOM 794 C LEU A 115 -19.353 -15.384 8.796 1.00 26.30 C
ATOM 795 O LEU A 115 -20.459 -15.922 8.865 1.00 28.18 O
ATOM 796 CB LEU A 115 -18.138 -16.097 10.865 1.00 26.21 C
ATOM 797 CG LEU A 115 -17.210 -15.818 12.047 1.00 28.04 C
ATOM 798 CD1 LEU A 115 -17.295 -16.968 13.040 1.00 27.74 C
ATOM 799 CD2 LEU A 115 -15.775 -15.584 11.591 1.00 28.22 C
ATOM 800 N PRO A 116 -18.721 -15.190 7.635 1.00 25.80 N
ATOM 801 CA PRO A 116 -19.234 -15.699 6.371 1.00 25.65 C
ATOM 802 C PRO A 116 -18.837 -17.168 6.208 1.00 27.28 C
ATOM 803 O PRO A 116 -18.155 -17.718 7.074 1.00 28.52 O
ATOM 804 CB PRO A 116 -18.500 -14.837 5.341 1.00 25.13 C
ATOM 805 CG PRO A 116 -17.171 -14.581 5.978 1.00 24.98 C
ATOM 806 CD PRO A 116 -17.446 -14.465 7.459 1.00 26.07 C
ATOM 807 N GLY A 117 -19.237 -17.782 5.099 1.00 28.76 N
ATOM 808 CA GLY A 117 -18.985 -19.209 4.848 1.00 31.94 C
ATOM 809 C GLY A 117 -17.546 -19.586 4.521 1.00 33.29 C
ATOM 810 O GLY A 117 -17.247 -20.754 4.314 1.00 36.70 O
ATOM 811 N THR A 118 -16.660 -18.600 4.469 1.00 34.09 N
ATOM 812 CA THR A 118 -15.217 -18.837 4.359 1.00 35.38 C
ATOM 813 C THR A 118 -14.473 -17.861 5.264 1.00 36.39 C
ATOM 814 O THR A 118 -14.888 -16.710 5.407 1.00 37.86 O
ATOM 815 CB THR A 118 -14.707 -18.691 2.913 1.00 36.40 C
ATOM 816 OG1 THR A 118 -13.292 -18.941 2.889 1.00 38.96 O
ATOM 817 CG2 THR A 118 -14.973 -17.284 2.366 1.00 33.89 C
ATOM 818 N ARG A 119 -13.375 -18.299 5.872 1.00 37.64 N
ATOM 819 CA ARG A 119 -12.635 -17.414 6.788 1.00 39.09 C
ATOM 820 C ARG A 119 -11.572 -16.538 6.133 1.00 37.55 C
ATOM 821 O ARG A 119 -11.004 -15.653 6.787 1.00 35.69 O
ATOM 822 CB ARG A 119 -12.050 -18.198 7.960 1.00 43.79 C
ATOM 823 CG ARG A 119 -12.786 -17.959 9.274 1.00 48.80 C
ATOM 824 CD ARG A 119 -13.209 -19.259 9.951 1.00 53.04 C
ATOM 825 NE ARG A 119 -12.102 -20.090 10.448 1.00 56.20 N
ATOM 826 CZ ARG A 119 -11.539 -21.103 9.781 1.00 57.52 C
ATOM 827 NH1 ARG A 119 -11.937 -21.417 8.551 1.00 58.99 N
ATOM 828 NH2 ARG A 119 -10.555 -21.798 10.341 1.00 54.42 N
ATOM 829 N GLN A 120 -11.318 -16.759 4.846 1.00 33.45 N
ATOM 830 CA GLN A 120 -10.329 -15.957 4.133 1.00 33.48 C
ATOM 831 C GLN A 120 -10.940 -14.685 3.546 1.00 30.61 C
ATOM 832 O GLN A 120 -10.997 -14.516 2.329 1.00 30.67 O
ATOM 833 CB GLN A 120 -9.617 -16.783 3.045 1.00 35.54 C
ATOM 834 CG GLN A 120 -8.837 -17.990 3.557 1.00 36.99 C
ATOM 835 CD GLN A 120 -7.789 -17.633 4.598 1.00 41.19 C
ATOM 836 OE1 GLN A 120 -6.983 -16.712 4.412 1.00 43.57 O
ATOM 837 NE2 GLN A 120 -7.795 -18.362 5.704 1.00 42.03 N
ATOM 838 N VAL A 121 -11.424 -13.791 4.403 1.00 30.10 N
ATOM 839 CA VAL A 121 -11.839 -12.459 3.920 1.00 28.18 C
ATOM 840 C VAL A 121 -11.253 -11.391 4.828 1.00 26.64 C
ATOM 841 O VAL A 121 -11.089 -11.623 6.035 1.00 25.51 O
ATOM 842 CB VAL A 121 -13.375 -12.285 3.727 1.00 28.61 C
ATOM 843 CG1 VAL A 121 -14.039 -13.527 3.140 1.00 26.92 C
ATOM 844 CG2 VAL A 121 -14.071 -11.845 5.008 1.00 30.44 C
ATOM 845 N THR A 122 -10.898 -10.244 4.243 1.00 25.41 N
ATOM 846 CA THR A 122 -10.318 -9.150 5.017 1.00 23.61 C
ATOM 847 C THR A 122 -11.412 -8.410 5.782 1.00 23.58 C
ATOM 848 O THR A 122 -12.601 -8.519 5.460 1.00 23.70 O
ATOM 849 CB THR A 122 -9.530 -8.147 4.150 1.00 23.74 C
ATOM 850 OG1 THR A 122 -10.388 -7.595 3.147 1.00 23.60 O
ATOM 851 CG2 THR A 122 -8.305 -8.841 3.492 1.00 23.29 C
ATOM 852 N VAL A 123 -10.990 -7.671 6.801 1.00 23.23 N
ATOM 853 CA VAL A 123 -11.869 -6.782 7.540 1.00 22.12 C
ATOM 854 C VAL A 123 -12.394 -5.716 6.595 1.00 21.25 C
ATOM 855 O VAL A 123 -13.574 -5.401 6.604 1.00 19.70 O
ATOM 856 CB VAL A 123 -11.133 -6.176 8.751 1.00 22.89 C
ATOM 857 CG1 VAL A 123 -11.774 -4.869 9.217 1.00 22.12 C
ATOM 858 CG2 VAL A 123 -11.065 -7.207 9.881 1.00 22.84 C
ATOM 859 N GLY A 124 -11.529 -5.168 5.743 1.00 19.81 N
ATOM 860 CA GLY A 124 -12.010 -4.203 4.751 1.00 19.60 C
ATOM 861 C GLY A 124 -13.044 -4.780 3.783 1.00 19.89 C
ATOM 862 O GLY A 124 -14.010 -4.104 3.394 1.00 20.34 O
ATOM 863 N GLY A 125 -12.849 -6.034 3.377 1.00 19.50 N
ATOM 864 CA GLY A 125 -13.787 -6.672 2.443 1.00 19.50 C
ATOM 865 C GLY A 125 -15.094 -6.986 3.173 1.00 20.09 C
ATOM 866 O GLY A 125 -16.185 -6.903 2.599 1.00 19.55 O
ATOM 867 N ALA A 126 -14.963 -7.330 4.448 1.00 19.41 N
ATOM 868 CA ALA A 126 -16.118 -7.610 5.299 1.00 19.81 C
ATOM 869 C ALA A 126 -16.972 -6.348 5.462 1.00 19.38 C
ATOM 870 O ALA A 126 -18.192 -6.406 5.356 1.00 20.67 O
ATOM 871 CB ALA A 126 -15.653 -8.150 6.637 1.00 18.97 C
ATOM 872 N ILE A 127 -16.328 -5.199 5.643 1.00 19.95 N
ATOM 873 CA ILE A 127 -17.055 -3.922 5.775 1.00 20.02 C
ATOM 874 C ILE A 127 -17.644 -3.474 4.438 1.00 20.06 C
ATOM 875 O ILE A 127 -18.820 -3.109 4.348 1.00 18.62 O
ATOM 876 CB ILE A 127 -16.171 -2.797 6.382 1.00 19.24 C
ATOM 877 CG1 ILE A 127 -15.686 -3.192 7.780 1.00 18.75 C
ATOM 878 CG2 ILE A 127 -16.917 -1.456 6.389 1.00 19.46 C
ATOM 879 CD1 ILE A 127 -14.605 -2.295 8.364 1.00 18.32 C
ATOM 880 N ALA A 128 -16.826 -3.535 3.395 1.00 21.04 N
ATOM 881 CA ALA A 128 -17.209 -3.005 2.089 1.00 21.12 C
ATOM 882 C ALA A 128 -18.363 -3.749 1.469 1.00 21.05 C
ATOM 883 O ALA A 128 -19.068 -3.185 0.627 1.00 21.47 O
ATOM 884 CB ALA A 128 -16.021 -2.997 1.135 1.00 21.70 C
ATOM 885 N CYS A 129 -18.550 -5.014 1.851 1.00 19.97 N
ATOM 886 CA CYS A 129 -19.657 -5.783 1.305 1.00 20.48 C
ATOM 887 C CYS A 129 -20.756 -5.970 2.341 1.00 19.53 C
ATOM 888 O CYS A 129 -21.761 -6.592 2.033 1.00 19.40 O
ATOM 889 CB CYS A 129 -19.203 -7.136 0.740 1.00 21.56 C
ATOM 890 SG CYS A 129 -18.315 -7.001 -0.844 1.00 24.96 S
ATOM 891 N ASP A 130 -20.530 -5.419 3.540 1.00 19.21 N
ATOM 892 CA ASP A 130 -21.429 -5.513 4.698 1.00 20.35 C
ATOM 893 C ASP A 130 -21.878 -6.987 4.835 1.00 20.26 C
ATOM 894 O ASP A 130 -23.065 -7.312 4.782 1.00 20.52 O
ATOM 895 CB ASP A 130 -22.597 -4.516 4.571 1.00 19.49 C
ATOM 896 CG ASP A 130 -23.476 -4.445 5.842 1.00 19.95 C
ATOM 897 OD1 ASP A 130 -23.042 -4.897 6.922 1.00 19.22 O
ATOM 898 OD2 ASP A 130 -24.611 -3.929 5.751 1.00 21.27 O
ATOM 899 N ILE A 131 -20.888 -7.867 4.968 1.00 20.56 N
ATOM 900 CA ILE A 131 -21.106 -9.301 4.809 1.00 21.08 C
ATOM 901 C ILE A 131 -22.046 -9.833 5.886 1.00 20.96 C
ATOM 902 O ILE A 131 -22.175 -9.245 6.950 1.00 20.63 O
ATOM 903 CB ILE A 131 -19.795 -10.112 4.854 1.00 20.81 C
ATOM 904 CG1 ILE A 131 -19.173 -10.033 6.253 1.00 21.21 C
ATOM 905 CG2 ILE A 131 -18.833 -9.654 3.755 1.00 19.79 C
ATOM 906 CD1 ILE A 131 -18.070 -11.037 6.479 1.00 21.79 C
ATOM 907 N HIS A 132 -22.658 -10.974 5.610 1.00 21.15 N
ATOM 908 CA HIS A 132 -23.607 -11.565 6.551 1.00 20.79 C
ATOM 909 C HIS A 132 -23.212 -12.983 6.841 1.00 20.34 C
ATOM 910 O HIS A 132 -22.337 -13.552 6.179 1.00 19.57 O
ATOM 911 CB HIS A 132 -25.014 -11.496 5.975 1.00 20.99 C
ATOM 912 CG HIS A 132 -25.122 -12.079 4.594 1.00 21.89 C
ATOM 913 ND1 HIS A 132 -25.280 -13.406 4.373 1.00 23.72 N
ATOM 914 CD2 HIS A 132 -25.053 -11.478 3.347 1.00 21.36 C
ATOM 915 CE1 HIS A 132 -25.327 -13.633 3.050 1.00 22.76 C
ATOM 916 NE2 HIS A 132 -25.183 -12.453 2.422 1.00 24.36 N
ATOM 917 N GLY A 133 -23.852 -13.580 7.831 1.00 19.33 N
ATOM 918 CA GLY A 133 -23.566 -14.953 8.185 1.00 20.46 C
ATOM 919 C GLY A 133 -24.789 -15.679 8.701 1.00 22.29 C
ATOM 920 O GLY A 133 -25.915 -15.151 8.678 1.00 19.95 O
ATOM 921 N LYS A 134 -24.527 -16.884 9.187 1.00 22.97 N
ATOM 922 CA LYS A 134 -25.522 -17.796 9.738 1.00 25.72 C
ATOM 923 C LYS A 134 -26.314 -17.178 10.905 1.00 24.49 C
ATOM 924 O LYS A 134 -27.419 -17.608 11.202 1.00 26.02 O
ATOM 925 CB LYS A 134 -24.808 -19.076 10.188 1.00 27.01 C
ATOM 926 CG LYS A 134 -25.723 -20.240 10.514 1.00 30.46 C
ATOM 927 CD LYS A 134 -24.937 -21.534 10.710 1.00 32.44 C
ATOM 928 CE LYS A 134 -25.890 -22.715 10.848 1.00 30.39 C
ATOM 929 NZ LYS A 134 -25.117 -23.974 10.977 1.00 35.02 N
ATOM 930 N ASN A 135 -25.729 -16.187 11.570 1.00 23.80 N
ATOM 931 CA ASN A 135 -26.429 -15.466 12.633 1.00 23.19 C
ATOM 932 C ASN A 135 -27.056 -14.134 12.215 1.00 22.97 C
ATOM 933 O ASN A 135 -27.344 -13.317 13.089 1.00 23.35 O
ATOM 934 CB ASN A 135 -25.499 -15.235 13.835 1.00 22.14 C
ATOM 935 CG ASN A 135 -24.329 -14.317 13.499 1.00 20.75 C
ATOM 936 OD1 ASN A 135 -24.067 -14.050 12.334 1.00 21.59 O
ATOM 937 ND2 ASN A 135 -23.629 -13.842 14.507 1.00 18.75 N
ATOM 938 N HIS A 136 -27.298 -13.905 10.917 1.00 21.29 N
ATOM 939 CA HIS A 136 -27.839 -12.597 10.517 1.00 21.75 C
ATOM 940 C HIS A 136 -29.108 -12.234 11.234 1.00 22.43 C
ATOM 941 O HIS A 136 -29.289 -11.078 11.600 1.00 22.72 O
ATOM 942 CB HIS A 136 -28.071 -12.435 9.024 1.00 20.11 C
ATOM 943 CG HIS A 136 -28.601 -11.061 8.662 1.00 20.74 C
ATOM 944 ND1 HIS A 136 -29.924 -10.785 8.585 1.00 19.82 N
ATOM 945 CD2 HIS A 136 -27.930 -9.854 8.418 1.00 20.12 C
ATOM 946 CE1 HIS A 136 -30.091 -9.487 8.290 1.00 21.03 C
ATOM 947 NE2 HIS A 136 -28.867 -8.911 8.198 1.00 19.62 N
ATOM 948 N HIS A 137 -30.005 -13.201 11.425 1.00 22.57 N
ATOM 949 CA HIS A 137 -31.323 -12.891 11.994 1.00 24.66 C
ATOM 950 C HIS A 137 -31.266 -12.471 13.441 1.00 25.54 C
ATOM 951 O HIS A 137 -32.249 -11.930 13.964 1.00 27.27 O
ATOM 952 CB HIS A 137 -32.265 -14.082 11.851 1.00 23.81 C
ATOM 953 CG HIS A 137 -31.830 -15.276 12.661 1.00 25.64 C
ATOM 954 ND1 HIS A 137 -30.765 -16.038 12.313 1.00 25.65 N
ATOM 955 CD2 HIS A 137 -32.318 -15.802 13.854 1.00 25.84 C
ATOM 956 CE1 HIS A 137 -30.578 -17.000 13.240 1.00 26.14 C
ATOM 957 NE2 HIS A 137 -31.535 -16.867 14.177 1.00 27.98 N
ATOM 958 N SER A 138 -30.150 -12.751 14.114 1.00 24.92 N
ATOM 959 CA SER A 138 -29.972 -12.363 15.511 1.00 26.67 C
ATOM 960 C SER A 138 -28.917 -11.286 15.705 1.00 26.91 C
ATOM 961 O SER A 138 -28.947 -10.588 16.717 1.00 26.05 O
ATOM 962 CB SER A 138 -29.641 -13.575 16.403 1.00 27.39 C
ATOM 963 OG SER A 138 -28.327 -14.071 16.169 1.00 27.57 O
ATOM 964 N ALA A 139 -27.978 -11.149 14.761 1.00 25.66 N
ATOM 965 CA ALA A 139 -26.876 -10.190 14.964 1.00 24.51 C
ATOM 966 C ALA A 139 -26.673 -9.120 13.885 1.00 23.02 C
ATOM 967 O ALA A 139 -25.825 -8.238 14.052 1.00 21.76 O
ATOM 968 CB ALA A 139 -25.572 -10.926 15.247 1.00 25.89 C
ATOM 969 N GLY A 140 -27.457 -9.199 12.809 1.00 22.51 N
ATOM 970 CA GLY A 140 -27.351 -8.291 11.662 1.00 22.23 C
ATOM 971 C GLY A 140 -26.119 -8.636 10.851 1.00 22.01 C
ATOM 972 O GLY A 140 -25.608 -9.748 10.955 1.00 21.27 O
ATOM 973 N SER A 141 -25.659 -7.694 10.035 1.00 21.70 N
ATOM 974 CA SER A 141 -24.464 -7.908 9.214 1.00 23.05 C
ATOM 975 C SER A 141 -23.225 -7.266 9.840 1.00 23.16 C
ATOM 976 O SER A 141 -23.304 -6.648 10.904 1.00 21.88 O
ATOM 977 CB SER A 141 -24.693 -7.397 7.788 1.00 22.15 C
ATOM 978 OG SER A 141 -25.139 -6.049 7.802 1.00 22.06 O
ATOM 979 N PHE A 142 -22.080 -7.418 9.174 1.00 21.99 N
ATOM 980 CA PHE A 142 -20.812 -6.974 9.727 1.00 22.54 C
ATOM 981 C PHE A 142 -20.840 -5.496 10.143 1.00 22.87 C
ATOM 982 O PHE A 142 -20.319 -5.122 11.204 1.00 21.10 O
ATOM 983 CB PHE A 142 -19.681 -7.231 8.713 1.00 21.47 C
ATOM 984 CG PHE A 142 -18.326 -7.339 9.339 1.00 22.46 C
ATOM 985 CD1 PHE A 142 -17.908 -8.534 9.919 1.00 21.97 C
ATOM 986 CD2 PHE A 142 -17.452 -6.251 9.342 1.00 22.59 C
ATOM 987 CE1 PHE A 142 -16.663 -8.638 10.513 1.00 22.21 C
ATOM 988 CE2 PHE A 142 -16.204 -6.349 9.945 1.00 22.80 C
ATOM 989 CZ PHE A 142 -15.807 -7.542 10.526 1.00 22.48 C
ATOM 990 N GLY A 143 -21.467 -4.670 9.309 1.00 24.16 N
ATOM 991 CA GLY A 143 -21.524 -3.227 9.530 1.00 24.44 C
ATOM 992 C GLY A 143 -22.080 -2.844 10.888 1.00 24.61 C
ATOM 993 O GLY A 143 -21.634 -1.859 11.480 1.00 23.24 O
ATOM 994 N ASN A 144 -23.027 -3.648 11.383 1.00 24.59 N
ATOM 995 CA ASN A 144 -23.679 -3.430 12.677 1.00 24.58 C
ATOM 996 C ASN A 144 -22.700 -3.425 13.832 1.00 24.14 C
ATOM 997 O ASN A 144 -23.005 -2.907 14.892 1.00 23.42 O
ATOM 998 CB ASN A 144 -24.729 -4.515 12.956 1.00 23.75 C
ATOM 999 CG ASN A 144 -25.872 -4.514 11.955 1.00 24.55 C
ATOM 1000 OD1 ASN A 144 -25.669 -4.498 10.741 1.00 24.57 O
ATOM 1001 ND2 ASN A 144 -27.086 -4.587 12.465 1.00 24.27 N
ATOM 1002 N HIS A 145 -21.522 -4.003 13.620 1.00 22.54 N
ATOM 1003 CA HIS A 145 -20.584 -4.228 14.712 1.00 21.87 C
ATOM 1004 C HIS A 145 -19.352 -3.388 14.640 1.00 21.61 C
ATOM 1005 O HIS A 145 -18.489 -3.490 15.507 1.00 21.41 O
ATOM 1006 CB HIS A 145 -20.220 -5.711 14.793 1.00 22.38 C
ATOM 1007 CG HIS A 145 -21.412 -6.597 14.954 1.00 23.13 C
ATOM 1008 ND1 HIS A 145 -21.948 -6.881 16.163 1.00 23.53 N
ATOM 1009 CD2 HIS A 145 -22.210 -7.224 14.011 1.00 23.13 C
ATOM 1010 CE1 HIS A 145 -23.020 -7.670 15.990 1.00 24.23 C
ATOM 1011 NE2 HIS A 145 -23.177 -7.877 14.675 1.00 23.53 N
ATOM 1012 N VAL A 146 -19.246 -2.557 13.601 1.00 22.22 N
ATOM 1013 CA VAL A 146 -18.125 -1.632 13.474 1.00 22.38 C
ATOM 1014 C VAL A 146 -18.367 -0.397 14.358 1.00 23.27 C
ATOM 1015 O VAL A 146 -19.355 0.313 14.171 1.00 23.47 O
ATOM 1016 CB VAL A 146 -17.923 -1.214 12.010 1.00 22.31 C
ATOM 1017 CG1 VAL A 146 -16.818 -0.170 11.892 1.00 22.25 C
ATOM 1018 CG2 VAL A 146 -17.613 -2.439 11.141 1.00 22.76 C
ATOM 1019 N ARG A 147 -17.483 -0.151 15.318 1.00 23.03 N
ATOM 1020 CA ARG A 147 -17.643 1.016 16.195 1.00 25.09 C
ATOM 1021 C ARG A 147 -16.921 2.255 15.649 1.00 25.44 C
ATOM 1022 O ARG A 147 -17.330 3.374 15.916 1.00 23.96 O
ATOM 1023 CB ARG A 147 -17.241 0.704 17.649 1.00 25.53 C
ATOM 1024 CG ARG A 147 -18.067 -0.415 18.289 1.00 27.52 C
ATOM 1025 CD ARG A 147 -19.526 -0.011 18.544 1.00 28.64 C
ATOM 1026 NE ARG A 147 -20.376 -1.189 18.746 1.00 28.61 N
ATOM 1027 CZ ARG A 147 -21.236 -1.685 17.849 1.00 30.26 C
ATOM 1028 NH1 ARG A 147 -21.408 -1.106 16.663 1.00 27.85 N
ATOM 1029 NH2 ARG A 147 -21.941 -2.777 18.144 1.00 29.73 N
ATOM 1030 N SER A 148 -15.863 2.045 14.864 1.00 25.36 N
ATOM 1031 CA SER A 148 -15.227 3.133 14.136 1.00 27.16 C
ATOM 1032 C SER A 148 -14.422 2.568 12.972 1.00 26.87 C
ATOM 1033 O SER A 148 -14.108 1.375 12.958 1.00 25.86 O
ATOM 1034 CB SER A 148 -14.331 3.991 15.055 1.00 28.12 C
ATOM 1035 OG SER A 148 -13.059 3.404 15.258 1.00 30.65 O
ATOM 1036 N MET A 149 -14.115 3.423 12.000 1.00 26.35 N
ATOM 1037 CA MET A 149 -13.152 3.078 10.966 1.00 28.23 C
ATOM 1038 C MET A 149 -12.475 4.333 10.421 1.00 28.74 C
ATOM 1039 O MET A 149 -13.054 5.424 10.429 1.00 31.30 O
ATOM 1040 CB MET A 149 -13.791 2.223 9.848 1.00 29.19 C
ATOM 1041 CG MET A 149 -14.928 2.882 9.085 1.00 30.74 C
ATOM 1042 SD MET A 149 -15.712 1.784 7.876 1.00 33.95 S
ATOM 1043 CE MET A 149 -17.293 2.602 7.731 1.00 32.88 C
ATOM 1044 N ASP A 150 -11.239 4.161 9.980 1.00 28.49 N
ATOM 1045 CA ASP A 150 -10.443 5.226 9.396 1.00 29.14 C
ATOM 1046 C ASP A 150 -10.449 5.080 7.893 1.00 28.43 C
ATOM 1047 O ASP A 150 -9.922 4.105 7.348 1.00 30.27 O
ATOM 1048 CB ASP A 150 -9.020 5.178 9.937 1.00 30.55 C
ATOM 1049 CG ASP A 150 -8.972 5.366 11.443 1.00 33.73 C
ATOM 1050 OD1 ASP A 150 -9.811 6.121 11.985 1.00 36.10 O
ATOM 1051 OD2 ASP A 150 -8.103 4.755 12.089 1.00 35.60 O
ATOM 1052 N LEU A 151 -11.067 6.051 7.233 1.00 27.34 N
ATOM 1053 CA LEU A 151 -11.228 6.031 5.793 1.00 27.38 C
ATOM 1054 C LEU A 151 -10.310 7.040 5.104 1.00 28.00 C
ATOM 1055 O LEU A 151 -10.377 8.231 5.373 1.00 28.03 O
ATOM 1056 CB LEU A 151 -12.679 6.330 5.426 1.00 26.18 C
ATOM 1057 CG LEU A 151 -13.058 6.250 3.946 1.00 25.31 C
ATOM 1058 CD1 LEU A 151 -13.080 4.799 3.474 1.00 25.40 C
ATOM 1059 CD2 LEU A 151 -14.401 6.916 3.690 1.00 25.18 C
ATOM 1060 N LEU A 152 -9.469 6.547 4.201 1.00 29.30 N
ATOM 1061 CA LEU A 152 -8.656 7.406 3.350 1.00 31.13 C
ATOM 1062 C LEU A 152 -9.500 7.881 2.161 1.00 32.25 C
ATOM 1063 O LEU A 152 -9.853 7.090 1.276 1.00 33.47 O
ATOM 1064 CB LEU A 152 -7.403 6.648 2.876 1.00 30.24 C
ATOM 1065 CG LEU A 152 -6.522 7.309 1.802 1.00 31.35 C
ATOM 1066 CD1 LEU A 152 -5.957 8.650 2.271 1.00 31.03 C
ATOM 1067 CD2 LEU A 152 -5.402 6.358 1.381 1.00 30.04 C
ATOM 1068 N THR A 153 -9.835 9.169 2.153 1.00 33.10 N
ATOM 1069 CA THR A 153 -10.704 9.730 1.115 1.00 33.89 C
ATOM 1070 C THR A 153 -9.915 10.312 -0.068 1.00 35.51 C
ATOM 1071 O THR A 153 -8.673 10.356 -0.038 1.00 34.23 O
ATOM 1072 CB THR A 153 -11.756 10.711 1.695 1.00 35.02 C
ATOM 1073 OG1 THR A 153 -11.121 11.674 2.548 1.00 35.32 O
ATOM 1074 CG2 THR A 153 -12.776 9.944 2.521 1.00 34.05 C
ATOM 1075 N ALA A 154 -10.638 10.706 -1.118 1.00 35.35 N
ATOM 1076 CA ALA A 154 -10.040 11.192 -2.369 1.00 39.15 C
ATOM 1077 C ALA A 154 -9.173 12.439 -2.168 1.00 40.75 C
ATOM 1078 O ALA A 154 -8.176 12.620 -2.863 1.00 43.64 O
ATOM 1079 CB ALA A 154 -11.122 11.455 -3.410 1.00 37.22 C
ATOM 1080 N ASP A 155 -9.555 13.279 -1.207 1.00 42.70 N
ATOM 1081 CA ASP A 155 -8.792 14.481 -0.834 1.00 44.21 C
ATOM 1082 C ASP A 155 -7.459 14.178 -0.117 1.00 45.36 C
ATOM 1083 O ASP A 155 -6.740 15.097 0.285 1.00 44.65 O
ATOM 1084 CB ASP A 155 -9.663 15.416 0.019 1.00 44.03 C
ATOM 1085 CG ASP A 155 -10.072 14.799 1.356 1.00 45.51 C
ATOM 1086 OD1 ASP A 155 -9.669 13.659 1.664 1.00 48.33 O
ATOM 1087 OD2 ASP A 155 -10.803 15.458 2.118 1.00 46.93 O
ATOM 1088 N GLY A 156 -7.145 12.894 0.047 1.00 45.68 N
ATOM 1089 CA GLY A 156 -5.906 12.464 0.706 1.00 46.05 C
ATOM 1090 C GLY A 156 -5.925 12.492 2.226 1.00 45.18 C
ATOM 1091 O GLY A 156 -4.923 12.166 2.860 1.00 48.73 O
ATOM 1092 N GLU A 157 -7.052 12.883 2.815 1.00 44.93 N
ATOM 1093 CA GLU A 157 -7.208 12.890 4.272 1.00 46.34 C
ATOM 1094 C GLU A 157 -7.635 11.518 4.792 1.00 44.12 C
ATOM 1095 O GLU A 157 -8.187 10.709 4.041 1.00 43.24 O
ATOM 1096 CB GLU A 157 -8.252 13.927 4.707 1.00 50.81 C
ATOM 1097 CG GLU A 157 -8.055 15.333 4.152 1.00 57.32 C
ATOM 1098 CD GLU A 157 -6.948 16.104 4.849 1.00 62.85 C
ATOM 1099 OE1 GLU A 157 -7.275 17.017 5.640 1.00 67.23 O
ATOM 1100 OE2 GLU A 157 -5.758 15.799 4.610 1.00 62.83 O
ATOM 1101 N ILE A 158 -7.384 11.271 6.077 1.00 41.27 N
ATOM 1102 CA ILE A 158 -7.921 10.095 6.759 1.00 41.03 C
ATOM 1103 C ILE A 158 -8.986 10.508 7.772 1.00 41.50 C
ATOM 1104 O ILE A 158 -8.693 11.157 8.774 1.00 43.01 O
ATOM 1105 CB ILE A 158 -6.814 9.233 7.407 1.00 42.77 C
ATOM 1106 CG1 ILE A 158 -5.864 8.706 6.314 1.00 41.11 C
ATOM 1107 CG2 ILE A 158 -7.427 8.095 8.228 1.00 41.93 C
ATOM 1108 CD1 ILE A 158 -4.747 7.808 6.802 1.00 42.31 C
ATOM 1109 N ARG A 159 -10.229 10.131 7.490 1.00 40.35 N
ATOM 1110 CA ARG A 159 -11.362 10.522 8.321 1.00 39.87 C
ATOM 1111 C ARG A 159 -11.761 9.412 9.272 1.00 38.96 C
ATOM 1112 O ARG A 159 -11.921 8.252 8.866 1.00 39.64 O
ATOM 1113 CB ARG A 159 -12.536 10.952 7.444 1.00 40.65 C
ATOM 1114 CG ARG A 159 -12.248 12.263 6.729 1.00 41.97 C
ATOM 1115 CD ARG A 159 -13.063 12.428 5.467 1.00 43.20 C
ATOM 1116 NE ARG A 159 -14.432 12.840 5.763 1.00 44.60 N
ATOM 1117 CZ ARG A 159 -15.211 13.495 4.906 1.00 43.31 C
ATOM 1118 NH1 ARG A 159 -14.751 13.824 3.700 1.00 41.32 N
ATOM 1119 NH2 ARG A 159 -16.446 13.824 5.259 1.00 41.59 N
ATOM 1120 N HIS A 160 -11.881 9.775 10.544 1.00 37.56 N
ATOM 1121 CA HIS A 160 -12.336 8.866 11.581 1.00 37.79 C
ATOM 1122 C HIS A 160 -13.844 8.851 11.571 1.00 37.51 C
ATOM 1123 O HIS A 160 -14.492 9.847 11.902 1.00 38.77 O
ATOM 1124 CB HIS A 160 -11.780 9.303 12.930 1.00 38.43 C
ATOM 1125 CG HIS A 160 -11.958 8.281 14.029 1.00 39.06 C
ATOM 1126 ND1 HIS A 160 -11.209 7.168 14.109 1.00 40.02 N
ATOM 1127 CD2 HIS A 160 -12.825 8.252 15.121 1.00 39.50 C
ATOM 1128 CE1 HIS A 160 -11.575 6.457 15.190 1.00 40.11 C
ATOM 1129 NE2 HIS A 160 -12.566 7.123 15.810 1.00 40.68 N
ATOM 1130 N LEU A 161 -14.420 7.729 11.150 1.00 34.14 N
ATOM 1131 CA LEU A 161 -15.869 7.624 10.993 1.00 31.60 C
ATOM 1132 C LEU A 161 -16.439 6.753 12.090 1.00 30.31 C
ATOM 1133 O LEU A 161 -15.824 5.756 12.474 1.00 28.28 O
ATOM 1134 CB LEU A 161 -16.235 7.022 9.631 1.00 31.92 C
ATOM 1135 CG LEU A 161 -15.579 7.524 8.339 1.00 32.82 C
ATOM 1136 CD1 LEU A 161 -16.075 6.673 7.181 1.00 32.85 C
ATOM 1137 CD2 LEU A 161 -15.853 8.999 8.074 1.00 32.50 C
ATOM 1138 N THR A 162 -17.615 7.136 12.586 1.00 28.52 N
ATOM 1139 CA THR A 162 -18.327 6.389 13.618 1.00 29.27 C
ATOM 1140 C THR A 162 -19.794 6.271 13.198 1.00 28.60 C
ATOM 1141 O THR A 162 -20.288 7.135 12.470 1.00 27.96 O
ATOM 1142 CB THR A 162 -18.254 7.100 14.988 1.00 30.74 C
ATOM 1143 OG1 THR A 162 -18.855 8.392 14.877 1.00 33.97 O
ATOM 1144 CG2 THR A 162 -16.804 7.255 15.466 1.00 31.22 C
ATOM 1145 N PRO A 163 -20.499 5.203 13.639 1.00 28.12 N
ATOM 1146 CA PRO A 163 -21.851 4.968 13.118 1.00 28.84 C
ATOM 1147 C PRO A 163 -22.862 6.070 13.465 1.00 30.34 C
ATOM 1148 O PRO A 163 -23.830 6.258 12.723 1.00 28.54 O
ATOM 1149 CB PRO A 163 -22.268 3.642 13.774 1.00 27.15 C
ATOM 1150 CG PRO A 163 -21.409 3.519 14.980 1.00 27.17 C
ATOM 1151 CD PRO A 163 -20.100 4.160 14.598 1.00 27.64 C
ATOM 1152 N THR A 164 -22.643 6.780 14.573 1.00 32.55 N
ATOM 1153 CA THR A 164 -23.613 7.802 15.024 1.00 35.86 C
ATOM 1154 C THR A 164 -22.974 9.157 15.227 1.00 37.70 C
ATOM 1155 O THR A 164 -23.628 10.082 15.698 1.00 41.08 O
ATOM 1156 CB THR A 164 -24.318 7.430 16.346 1.00 34.17 C
ATOM 1157 OG1 THR A 164 -23.373 7.480 17.416 1.00 35.76 O
ATOM 1158 CG2 THR A 164 -24.941 6.051 16.281 1.00 35.30 C
ATOM 1159 N GLY A 165 -21.699 9.275 14.869 1.00 39.44 N
ATOM 1160 CA GLY A 165 -21.003 10.549 14.948 1.00 42.69 C
ATOM 1161 C GLY A 165 -21.418 11.536 13.872 1.00 45.98 C
ATOM 1162 O GLY A 165 -22.466 11.390 13.228 1.00 45.67 O
ATOM 1163 N GLU A 166 -20.574 12.542 13.679 1.00 47.22 N
ATOM 1164 CA GLU A 166 -20.849 13.628 12.758 1.00 49.11 C
ATOM 1165 C GLU A 166 -20.727 13.144 11.316 1.00 46.35 C
ATOM 1166 O GLU A 166 -21.368 13.680 10.422 1.00 45.90 O
ATOM 1167 CB GLU A 166 -19.860 14.762 13.018 1.00 52.44 C
ATOM 1168 CG GLU A 166 -20.478 16.146 12.997 1.00 55.86 C
ATOM 1169 CD GLU A 166 -19.686 17.147 13.819 1.00 58.23 C
ATOM 1170 OE1 GLU A 166 -18.438 17.052 13.857 1.00 57.47 O
ATOM 1171 OE2 GLU A 166 -20.319 18.031 14.434 1.00 59.39 O
ATOM 1172 N ASP A 167 -19.899 12.124 11.112 1.00 45.48 N
ATOM 1173 CA ASP A 167 -19.660 11.530 9.798 1.00 43.37 C
ATOM 1174 C ASP A 167 -20.449 10.226 9.587 1.00 41.05 C
ATOM 1175 O ASP A 167 -19.992 9.337 8.862 1.00 41.63 O
ATOM 1176 CB ASP A 167 -18.160 11.248 9.630 1.00 45.72 C
ATOM 1177 CG ASP A 167 -17.438 12.312 8.817 1.00 48.96 C
ATOM 1178 OD1 ASP A 167 -17.913 12.673 7.716 1.00 49.46 O
ATOM 1179 OD2 ASP A 167 -16.364 12.761 9.270 1.00 52.30 O
ATOM 1180 N ALA A 168 -21.623 10.117 10.209 1.00 35.14 N
ATOM 1181 CA ALA A 168 -22.437 8.898 10.132 1.00 34.52 C
ATOM 1182 C ALA A 168 -22.905 8.564 8.716 1.00 33.01 C
ATOM 1183 O ALA A 168 -22.965 7.392 8.333 1.00 31.21 O
ATOM 1184 CB ALA A 168 -23.630 8.985 11.080 1.00 33.26 C
ATOM 1185 N GLU A 169 -23.237 9.600 7.944 1.00 32.23 N
ATOM 1186 CA GLU A 169 -23.666 9.440 6.561 1.00 30.79 C
ATOM 1187 C GLU A 169 -22.587 8.749 5.724 1.00 28.33 C
ATOM 1188 O GLU A 169 -22.872 7.805 4.980 1.00 26.88 O
ATOM 1189 CB GLU A 169 -24.020 10.804 5.957 1.00 33.21 C
ATOM 1190 CG GLU A 169 -24.537 10.737 4.532 1.00 33.74 C
ATOM 1191 CD GLU A 169 -24.844 12.117 3.954 1.00 37.13 C
ATOM 1192 OE1 GLU A 169 -23.904 12.835 3.546 1.00 39.67 O
ATOM 1193 OE2 GLU A 169 -26.032 12.476 3.886 1.00 35.52 O
ATOM 1194 N LEU A 170 -21.354 9.231 5.854 1.00 26.80 N
ATOM 1195 CA LEU A 170 -20.206 8.638 5.167 1.00 26.17 C
ATOM 1196 C LEU A 170 -19.864 7.241 5.712 1.00 25.31 C
ATOM 1197 O LEU A 170 -19.427 6.355 4.959 1.00 23.81 O
ATOM 1198 CB LEU A 170 -18.981 9.564 5.256 1.00 25.53 C
ATOM 1199 CG LEU A 170 -17.733 9.070 4.505 1.00 25.78 C
ATOM 1200 CD1 LEU A 170 -18.074 8.746 3.055 1.00 25.06 C
ATOM 1201 CD2 LEU A 170 -16.607 10.092 4.596 1.00 26.25 C
ATOM 1202 N PHE A 171 -20.042 7.064 7.018 1.00 24.23 N
ATOM 1203 CA PHE A 171 -19.853 5.764 7.651 1.00 25.42 C
ATOM 1204 C PHE A 171 -20.761 4.725 6.993 1.00 24.82 C
ATOM 1205 O PHE A 171 -20.304 3.666 6.561 1.00 24.74 O
ATOM 1206 CB PHE A 171 -20.147 5.831 9.158 1.00 24.87 C
ATOM 1207 CG PHE A 171 -19.954 4.521 9.872 1.00 24.23 C
ATOM 1208 CD1 PHE A 171 -18.804 4.281 10.599 1.00 23.81 C
ATOM 1209 CD2 PHE A 171 -20.936 3.528 9.818 1.00 24.50 C
ATOM 1210 CE1 PHE A 171 -18.617 3.073 11.253 1.00 24.09 C
ATOM 1211 CE2 PHE A 171 -20.754 2.318 10.470 1.00 24.09 C
ATOM 1212 CZ PHE A 171 -19.597 2.090 11.185 1.00 23.90 C
ATOM 1213 N TRP A 172 -22.050 5.038 6.934 1.00 24.64 N
ATOM 1214 CA TRP A 172 -23.047 4.100 6.432 1.00 25.14 C
ATOM 1215 C TRP A 172 -23.077 3.951 4.934 1.00 25.23 C
ATOM 1216 O TRP A 172 -23.681 3.010 4.424 1.00 25.42 O
ATOM 1217 CB TRP A 172 -24.422 4.422 7.015 1.00 25.06 C
ATOM 1218 CG TRP A 172 -24.459 4.055 8.471 1.00 24.61 C
ATOM 1219 CD1 TRP A 172 -24.442 4.918 9.567 1.00 24.11 C
ATOM 1220 CD2 TRP A 172 -24.485 2.697 9.046 1.00 24.72 C
ATOM 1221 NE1 TRP A 172 -24.478 4.216 10.738 1.00 24.50 N
ATOM 1222 CE2 TRP A 172 -24.498 2.873 10.501 1.00 25.02 C
ATOM 1223 CE3 TRP A 172 -24.525 1.406 8.520 1.00 24.31 C
ATOM 1224 CZ2 TRP A 172 -24.536 1.785 11.379 1.00 24.60 C
ATOM 1225 CZ3 TRP A 172 -24.574 0.316 9.413 1.00 24.88 C
ATOM 1226 CH2 TRP A 172 -24.572 0.504 10.805 1.00 25.14 C
ATOM 1227 N ALA A 173 -22.395 4.855 4.226 1.00 23.92 N
ATOM 1228 CA ALA A 173 -22.201 4.732 2.782 1.00 23.11 C
ATOM 1229 C ALA A 173 -20.970 3.878 2.463 1.00 23.03 C
ATOM 1230 O ALA A 173 -20.887 3.302 1.386 1.00 23.08 O
ATOM 1231 CB ALA A 173 -22.074 6.108 2.132 1.00 22.70 C
ATOM 1232 N THR A 174 -20.040 3.807 3.407 1.00 22.23 N
ATOM 1233 CA THR A 174 -18.816 3.006 3.277 1.00 23.35 C
ATOM 1234 C THR A 174 -19.162 1.536 3.573 1.00 23.20 C
ATOM 1235 O THR A 174 -18.716 0.613 2.875 1.00 22.62 O
ATOM 1236 CB THR A 174 -17.711 3.536 4.222 1.00 23.39 C
ATOM 1237 OG1 THR A 174 -17.406 4.895 3.872 1.00 23.65 O
ATOM 1238 CG2 THR A 174 -16.419 2.679 4.149 1.00 22.66 C
ATOM 1239 N VAL A 175 -19.999 1.336 4.586 1.00 22.12 N
ATOM 1240 CA VAL A 175 -20.595 0.034 4.839 1.00 22.45 C
ATOM 1241 C VAL A 175 -21.352 -0.366 3.584 1.00 20.99 C
ATOM 1242 O VAL A 175 -22.206 0.373 3.095 1.00 21.91 O
ATOM 1243 CB VAL A 175 -21.549 0.079 6.057 1.00 22.50 C
ATOM 1244 CG1 VAL A 175 -22.360 -1.206 6.154 1.00 22.48 C
ATOM 1245 CG2 VAL A 175 -20.756 0.296 7.338 1.00 22.55 C
ATOM 1246 N GLY A 176 -21.009 -1.521 3.035 1.00 21.65 N
ATOM 1247 CA GLY A 176 -21.644 -1.984 1.806 1.00 22.45 C
ATOM 1248 C GLY A 176 -21.292 -1.187 0.557 1.00 22.25 C
ATOM 1249 O GLY A 176 -21.917 -1.379 -0.479 1.00 21.99 O
ATOM 1250 N GLY A 177 -20.284 -0.310 0.643 1.00 23.50 N
ATOM 1251 CA GLY A 177 -19.927 0.593 -0.477 1.00 22.89 C
ATOM 1252 C GLY A 177 -18.969 0.058 -1.539 1.00 25.23 C
ATOM 1253 O GLY A 177 -18.625 0.771 -2.492 1.00 24.62 O
ATOM 1254 N ASN A 178 -18.536 -1.189 -1.388 1.00 24.13 N
ATOM 1255 CA ASN A 178 -17.647 -1.820 -2.357 1.00 24.98 C
ATOM 1256 C ASN A 178 -16.438 -0.945 -2.678 1.00 24.94 C
ATOM 1257 O ASN A 178 -16.076 -0.787 -3.843 1.00 23.79 O
ATOM 1258 CB ASN A 178 -18.390 -2.195 -3.661 1.00 25.15 C
ATOM 1259 CG ASN A 178 -19.467 -3.249 -3.441 1.00 25.86 C
ATOM 1260 OD1 ASN A 178 -19.218 -4.441 -3.590 1.00 26.50 O
ATOM 1261 ND2 ASN A 178 -20.666 -2.808 -3.091 1.00 25.45 N
ATOM 1262 N GLY A 179 -15.850 -0.355 -1.641 1.00 25.50 N
ATOM 1263 CA GLY A 179 -14.609 0.421 -1.776 1.00 26.59 C
ATOM 1264 C GLY A 179 -14.733 1.773 -2.452 1.00 27.56 C
ATOM 1265 O GLY A 179 -13.721 2.420 -2.723 1.00 28.35 O
ATOM 1266 N LEU A 180 -15.963 2.220 -2.708 1.00 25.96 N
ATOM 1267 CA LEU A 180 -16.171 3.404 -3.546 1.00 27.01 C
ATOM 1268 C LEU A 180 -16.325 4.740 -2.812 1.00 27.22 C
ATOM 1269 O LEU A 180 -16.667 5.755 -3.434 1.00 29.04 O
ATOM 1270 CB LEU A 180 -17.307 3.171 -4.549 1.00 26.59 C
ATOM 1271 CG LEU A 180 -16.999 2.086 -5.589 1.00 26.97 C
ATOM 1272 CD1 LEU A 180 -18.285 1.560 -6.219 1.00 25.87 C
ATOM 1273 CD2 LEU A 180 -16.030 2.610 -6.644 1.00 28.92 C
ATOM 1274 N THR A 181 -16.044 4.743 -1.513 1.00 25.39 N
ATOM 1275 CA THR A 181 -15.984 5.978 -0.735 1.00 26.44 C
ATOM 1276 C THR A 181 -14.552 6.244 -0.285 1.00 26.85 C
ATOM 1277 O THR A 181 -14.265 7.278 0.312 1.00 27.82 O
ATOM 1278 CB THR A 181 -16.898 5.933 0.503 1.00 25.46 C
ATOM 1279 OG1 THR A 181 -16.429 4.919 1.403 1.00 24.90 O
ATOM 1280 CG2 THR A 181 -18.312 5.627 0.083 1.00 26.30 C
ATOM 1281 N GLY A 182 -13.662 5.305 -0.592 1.00 27.54 N
ATOM 1282 CA GLY A 182 -12.261 5.419 -0.231 1.00 27.84 C
ATOM 1283 C GLY A 182 -11.652 4.122 0.272 1.00 27.87 C
ATOM 1284 O GLY A 182 -12.197 3.030 0.079 1.00 26.56 O
ATOM 1285 N ILE A 183 -10.505 4.245 0.923 1.00 29.08 N
ATOM 1286 CA ILE A 183 -9.796 3.074 1.394 1.00 29.84 C
ATOM 1287 C ILE A 183 -9.905 3.005 2.904 1.00 29.54 C
ATOM 1288 O ILE A 183 -9.441 3.905 3.605 1.00 28.44 O
ATOM 1289 CB ILE A 183 -8.320 3.081 0.940 1.00 31.29 C
ATOM 1290 CG1 ILE A 183 -8.258 3.140 -0.594 1.00 32.69 C
ATOM 1291 CG2 ILE A 183 -7.584 1.864 1.493 1.00 32.07 C
ATOM 1292 CD1 ILE A 183 -6.910 2.814 -1.198 1.00 33.48 C
ATOM 1293 N ILE A 184 -10.548 1.942 3.392 1.00 28.13 N
ATOM 1294 CA ILE A 184 -10.614 1.674 4.815 1.00 27.02 C
ATOM 1295 C ILE A 184 -9.225 1.236 5.250 1.00 27.06 C
ATOM 1296 O ILE A 184 -8.698 0.242 4.750 1.00 27.19 O
ATOM 1297 CB ILE A 184 -11.651 0.579 5.157 1.00 26.24 C
ATOM 1298 CG1 ILE A 184 -13.031 0.940 4.585 1.00 25.44 C
ATOM 1299 CG2 ILE A 184 -11.685 0.347 6.660 1.00 26.09 C
ATOM 1300 CD1 ILE A 184 -14.030 -0.208 4.545 1.00 23.82 C
ATOM 1301 N MET A 185 -8.623 1.990 6.160 1.00 26.54 N
ATOM 1302 CA MET A 185 -7.262 1.700 6.593 1.00 26.29 C
ATOM 1303 C MET A 185 -7.258 0.857 7.854 1.00 24.92 C
ATOM 1304 O MET A 185 -6.370 0.037 8.057 1.00 22.27 O
ATOM 1305 CB MET A 185 -6.474 3.001 6.854 1.00 28.38 C
ATOM 1306 CG MET A 185 -6.358 3.958 5.658 1.00 31.40 C
ATOM 1307 SD MET A 185 -5.468 3.299 4.223 1.00 34.97 S
ATOM 1308 CE MET A 185 -3.794 3.132 4.846 1.00 36.08 C
ATOM 1309 N ARG A 186 -8.266 1.067 8.704 1.00 24.93 N
ATOM 1310 CA ARG A 186 -8.208 0.609 10.080 1.00 24.15 C
ATOM 1311 C ARG A 186 -9.621 0.710 10.647 1.00 24.22 C
ATOM 1312 O ARG A 186 -10.389 1.602 10.270 1.00 23.27 O
ATOM 1313 CB ARG A 186 -7.274 1.534 10.865 1.00 24.61 C
ATOM 1314 CG ARG A 186 -6.799 1.014 12.207 1.00 25.07 C
ATOM 1315 CD ARG A 186 -5.663 1.875 12.743 1.00 24.77 C
ATOM 1316 NE ARG A 186 -5.436 1.629 14.165 1.00 25.69 N
ATOM 1317 CZ ARG A 186 -4.345 1.992 14.833 1.00 26.49 C
ATOM 1318 NH1 ARG A 186 -3.363 2.619 14.206 1.00 25.52 N
ATOM 1319 NH2 ARG A 186 -4.231 1.720 16.137 1.00 26.99 N
ATOM 1320 N ALA A 187 -9.956 -0.197 11.548 1.00 23.66 N
ATOM 1321 CA ALA A 187 -11.291 -0.199 12.149 1.00 24.31 C
ATOM 1322 C ALA A 187 -11.235 -0.759 13.547 1.00 25.18 C
ATOM 1323 O ALA A 187 -10.290 -1.477 13.899 1.00 24.42 O
ATOM 1324 CB ALA A 187 -12.263 -1.008 11.300 1.00 23.14 C
ATOM 1325 N THR A 188 -12.261 -0.408 14.329 1.00 25.14 N
ATOM 1326 CA THR A 188 -12.494 -0.944 15.654 1.00 25.26 C
ATOM 1327 C THR A 188 -13.828 -1.695 15.585 1.00 24.89 C
ATOM 1328 O THR A 188 -14.826 -1.149 15.097 1.00 25.28 O
ATOM 1329 CB THR A 188 -12.532 0.197 16.707 1.00 27.58 C
ATOM 1330 OG1 THR A 188 -11.225 0.776 16.825 1.00 29.00 O
ATOM 1331 CG2 THR A 188 -12.950 -0.312 18.080 1.00 27.93 C
ATOM 1332 N ILE A 189 -13.829 -2.949 16.033 1.00 24.04 N
ATOM 1333 CA ILE A 189 -15.000 -3.819 15.967 1.00 24.15 C
ATOM 1334 C ILE A 189 -15.343 -4.242 17.381 1.00 24.43 C
ATOM 1335 O ILE A 189 -14.447 -4.576 18.154 1.00 24.29 O
ATOM 1336 CB ILE A 189 -14.686 -5.126 15.179 1.00 24.68 C
ATOM 1337 CG1 ILE A 189 -13.903 -4.854 13.880 1.00 25.02 C
ATOM 1338 CG2 ILE A 189 -15.940 -5.952 14.925 1.00 24.22 C
ATOM 1339 CD1 ILE A 189 -14.656 -4.122 12.800 1.00 24.68 C
ATOM 1340 N GLU A 190 -16.634 -4.242 17.719 1.00 24.58 N
ATOM 1341 CA GLU A 190 -17.071 -4.795 18.981 1.00 24.29 C
ATOM 1342 C GLU A 190 -17.339 -6.280 18.781 1.00 23.36 C
ATOM 1343 O GLU A 190 -18.118 -6.669 17.901 1.00 22.71 O
ATOM 1344 CB GLU A 190 -18.341 -4.099 19.489 1.00 25.38 C
ATOM 1345 CG GLU A 190 -18.901 -4.762 20.732 1.00 27.55 C
ATOM 1346 CD GLU A 190 -20.010 -3.966 21.411 1.00 29.22 C
ATOM 1347 OE1 GLU A 190 -20.469 -2.937 20.872 1.00 31.33 O
ATOM 1348 OE2 GLU A 190 -20.423 -4.388 22.501 1.00 31.27 O
ATOM 1349 N MET A 191 -16.705 -7.097 19.613 1.00 23.37 N
ATOM 1350 CA MET A 191 -16.774 -8.539 19.475 1.00 24.14 C
ATOM 1351 C MET A 191 -17.909 -9.061 20.338 1.00 24.57 C
ATOM 1352 O MET A 191 -18.482 -8.324 21.140 1.00 25.22 O
ATOM 1353 CB MET A 191 -15.435 -9.182 19.882 1.00 24.44 C
ATOM 1354 CG MET A 191 -14.238 -8.681 19.082 1.00 23.91 C
ATOM 1355 SD MET A 191 -14.189 -9.278 17.377 1.00 25.76 S
ATOM 1356 CE MET A 191 -13.402 -10.862 17.642 1.00 24.05 C
ATOM 1357 N THR A 192 -18.234 -10.332 20.158 1.00 24.26 N
ATOM 1358 CA THR A 192 -19.246 -10.998 20.955 1.00 23.94 C
ATOM 1359 C THR A 192 -18.546 -11.822 22.036 1.00 25.21 C
ATOM 1360 O THR A 192 -17.630 -12.598 21.725 1.00 25.23 O
ATOM 1361 CB THR A 192 -20.108 -11.885 20.038 1.00 23.63 C
ATOM 1362 OG1 THR A 192 -20.752 -11.049 19.066 1.00 23.88 O
ATOM 1363 CG2 THR A 192 -21.155 -12.688 20.823 1.00 21.98 C
ATOM 1364 N PRO A 193 -18.944 -11.649 23.314 1.00 25.88 N
ATOM 1365 CA PRO A 193 -18.272 -12.451 24.347 1.00 27.58 C
ATOM 1366 C PRO A 193 -18.667 -13.913 24.233 1.00 28.16 C
ATOM 1367 O PRO A 193 -19.774 -14.217 23.792 1.00 29.10 O
ATOM 1368 CB PRO A 193 -18.779 -11.865 25.676 1.00 26.04 C
ATOM 1369 CG PRO A 193 -19.644 -10.708 25.326 1.00 26.56 C
ATOM 1370 CD PRO A 193 -20.001 -10.781 23.871 1.00 26.06 C
ATOM 1371 N THR A 194 -17.749 -14.804 24.594 1.00 27.90 N
ATOM 1372 CA THR A 194 -18.005 -16.240 24.557 1.00 28.49 C
ATOM 1373 C THR A 194 -17.134 -16.928 25.607 1.00 29.50 C
ATOM 1374 O THR A 194 -16.023 -16.462 25.899 1.00 29.67 O
ATOM 1375 CB THR A 194 -17.752 -16.848 23.150 1.00 28.28 C
ATOM 1376 OG1 THR A 194 -18.194 -18.214 23.121 1.00 28.54 O
ATOM 1377 CG2 THR A 194 -16.268 -16.802 22.777 1.00 26.03 C
ATOM 1378 N SER A 195 -17.640 -18.021 26.177 1.00 28.70 N
ATOM 1379 CA SER A 195 -16.845 -18.812 27.116 1.00 29.58 C
ATOM 1380 C SER A 195 -16.214 -20.031 26.438 1.00 29.45 C
ATOM 1381 O SER A 195 -15.362 -20.692 27.027 1.00 30.46 O
ATOM 1382 CB SER A 195 -17.649 -19.206 28.365 1.00 30.00 C
ATOM 1383 OG SER A 195 -18.875 -19.837 28.034 1.00 31.54 O
ATOM 1384 N THR A 196 -16.611 -20.314 25.196 1.00 27.95 N
ATOM 1385 CA THR A 196 -16.087 -21.490 24.476 1.00 28.50 C
ATOM 1386 C THR A 196 -15.990 -21.269 22.969 1.00 26.51 C
ATOM 1387 O THR A 196 -16.602 -20.355 22.427 1.00 25.30 O
ATOM 1388 CB THR A 196 -16.963 -22.753 24.697 1.00 28.79 C
ATOM 1389 OG1 THR A 196 -18.037 -22.768 23.753 1.00 27.62 O
ATOM 1390 CG2 THR A 196 -17.545 -22.798 26.095 1.00 30.16 C
ATOM 1391 N ALA A 197 -15.252 -22.143 22.295 1.00 27.91 N
ATOM 1392 CA ALA A 197 -15.171 -22.119 20.829 1.00 28.44 C
ATOM 1393 C ALA A 197 -16.115 -23.139 20.169 1.00 28.98 C
ATOM 1394 O ALA A 197 -15.898 -23.551 19.031 1.00 31.71 O
ATOM 1395 CB ALA A 197 -13.727 -22.325 20.377 1.00 29.17 C
ATOM 1396 N TYR A 198 -17.178 -23.518 20.878 1.00 29.05 N
ATOM 1397 CA TYR A 198 -18.096 -24.563 20.420 1.00 28.97 C
ATOM 1398 C TYR A 198 -19.550 -24.102 20.314 1.00 29.09 C
ATOM 1399 O TYR A 198 -19.954 -23.131 20.962 1.00 27.17 O
ATOM 1400 CB TYR A 198 -18.039 -25.756 21.378 1.00 29.47 C
ATOM 1401 CG TYR A 198 -16.701 -26.436 21.418 1.00 32.22 C
ATOM 1402 CD1 TYR A 198 -16.423 -27.511 20.576 1.00 32.90 C
ATOM 1403 CD2 TYR A 198 -15.703 -26.001 22.291 1.00 32.26 C
ATOM 1404 CE1 TYR A 198 -15.192 -28.138 20.606 1.00 34.74 C
ATOM 1405 CE2 TYR A 198 -14.468 -26.622 22.333 1.00 33.71 C
ATOM 1406 CZ TYR A 198 -14.219 -27.690 21.494 1.00 36.16 C
ATOM 1407 OH TYR A 198 -12.992 -28.311 21.539 1.00 38.54 O
ATOM 1408 N PHE A 199 -20.324 -24.827 19.503 1.00 27.54 N
ATOM 1409 CA PHE A 199 -21.764 -24.623 19.371 1.00 27.26 C
ATOM 1410 C PHE A 199 -22.535 -25.815 19.950 1.00 28.41 C
ATOM 1411 O PHE A 199 -22.055 -26.955 19.911 1.00 27.48 O
ATOM 1412 CB PHE A 199 -22.160 -24.433 17.890 1.00 25.85 C
ATOM 1413 CG PHE A 199 -21.516 -23.233 17.224 1.00 26.93 C
ATOM 1414 CD1 PHE A 199 -22.186 -22.018 17.150 1.00 26.58 C
ATOM 1415 CD2 PHE A 199 -20.245 -23.325 16.656 1.00 28.03 C
ATOM 1416 CE1 PHE A 199 -21.602 -20.915 16.536 1.00 28.01 C
ATOM 1417 CE2 PHE A 199 -19.652 -22.222 16.042 1.00 28.33 C
ATOM 1418 CZ PHE A 199 -20.330 -21.013 15.990 1.00 28.11 C
ATOM 1419 N ILE A 200 -23.716 -25.531 20.494 1.00 28.59 N
ATOM 1420 CA ILE A 200 -24.743 -26.546 20.758 1.00 31.01 C
ATOM 1421 C ILE A 200 -25.766 -26.441 19.623 1.00 28.78 C
ATOM 1422 O ILE A 200 -26.349 -25.381 19.429 1.00 28.54 O
ATOM 1423 CB ILE A 200 -25.491 -26.301 22.096 1.00 32.95 C
ATOM 1424 CG1 ILE A 200 -24.519 -26.053 23.259 1.00 35.16 C
ATOM 1425 CG2 ILE A 200 -26.465 -27.441 22.396 1.00 32.61 C
ATOM 1426 CD1 ILE A 200 -23.622 -27.228 23.613 1.00 36.38 C
ATOM 1427 N ALA A 201 -25.998 -27.542 18.913 1.00 27.55 N
ATOM 1428 CA ALA A 201 -26.780 -27.549 17.667 1.00 28.29 C
ATOM 1429 C ALA A 201 -27.990 -28.509 17.638 1.00 28.41 C
ATOM 1430 O ALA A 201 -27.939 -29.626 18.171 1.00 28.33 O
ATOM 1431 CB ALA A 201 -25.864 -27.873 16.494 1.00 27.37 C
ATOM 1432 N ASP A 202 -29.053 -28.058 16.978 1.00 27.06 N
ATOM 1433 CA ASP A 202 -30.190 -28.888 16.610 1.00 26.69 C
ATOM 1434 C ASP A 202 -30.254 -28.983 15.104 1.00 27.62 C
ATOM 1435 O ASP A 202 -30.105 -27.975 14.379 1.00 26.83 O
ATOM 1436 CB ASP A 202 -31.500 -28.307 17.156 1.00 27.14 C
ATOM 1437 CG ASP A 202 -31.504 -28.221 18.665 1.00 27.87 C
ATOM 1438 OD1 ASP A 202 -30.615 -28.842 19.269 1.00 27.29 O
ATOM 1439 OD2 ASP A 202 -32.390 -27.550 19.246 1.00 29.66 O
ATOM 1440 N GLY A 203 -30.442 -30.204 14.629 1.00 26.93 N
ATOM 1441 CA GLY A 203 -30.565 -30.443 13.202 1.00 27.43 C
ATOM 1442 C GLY A 203 -31.934 -30.983 12.878 1.00 28.50 C
ATOM 1443 O GLY A 203 -32.486 -31.788 13.639 1.00 28.72 O
ATOM 1444 N ASP A 204 -32.472 -30.544 11.744 1.00 28.27 N
ATOM 1445 CA ASP A 204 -33.729 -31.052 11.222 1.00 29.23 C
ATOM 1446 C ASP A 204 -33.638 -31.287 9.720 1.00 30.22 C
ATOM 1447 O ASP A 204 -32.903 -30.603 9.012 1.00 31.67 O
ATOM 1448 CB ASP A 204 -34.887 -30.107 11.556 1.00 29.20 C
ATOM 1449 CG ASP A 204 -35.137 -30.007 13.043 1.00 29.89 C
ATOM 1450 OD1 ASP A 204 -35.976 -30.782 13.560 1.00 32.15 O
ATOM 1451 OD2 ASP A 204 -34.472 -29.180 13.709 1.00 28.55 O
ATOM 1452 N VAL A 205 -34.358 -32.290 9.240 1.00 29.52 N
ATOM 1453 CA VAL A 205 -34.428 -32.555 7.810 1.00 29.47 C
ATOM 1454 C VAL A 205 -35.889 -32.470 7.418 1.00 29.81 C
ATOM 1455 O VAL A 205 -36.747 -33.078 8.056 1.00 31.71 O
ATOM 1456 CB VAL A 205 -33.806 -33.927 7.433 1.00 29.37 C
ATOM 1457 CG1 VAL A 205 -33.967 -34.233 5.941 1.00 27.70 C
ATOM 1458 CG2 VAL A 205 -32.335 -33.966 7.814 1.00 27.14 C
ATOM 1459 N THR A 206 -36.171 -31.674 6.394 1.00 29.97 N
ATOM 1460 CA THR A 206 -37.536 -31.501 5.894 1.00 29.46 C
ATOM 1461 C THR A 206 -37.704 -32.273 4.594 1.00 28.99 C
ATOM 1462 O THR A 206 -36.716 -32.643 3.954 1.00 26.92 O
ATOM 1463 CB THR A 206 -37.862 -30.020 5.635 1.00 29.10 C
ATOM 1464 OG1 THR A 206 -37.079 -29.548 4.536 1.00 29.73 O
ATOM 1465 CG2 THR A 206 -37.572 -29.182 6.868 1.00 28.97 C
ATOM 1466 N ALA A 207 -38.952 -32.487 4.192 1.00 29.01 N
ATOM 1467 CA ALA A 207 -39.269 -33.323 3.035 1.00 30.08 C
ATOM 1468 C ALA A 207 -39.547 -32.533 1.752 1.00 30.41 C
ATOM 1469 O ALA A 207 -39.553 -33.106 0.660 1.00 31.30 O
ATOM 1470 CB ALA A 207 -40.461 -34.223 3.359 1.00 30.06 C
ATOM 1471 N SER A 208 -39.781 -31.228 1.888 1.00 30.79 N
ATOM 1472 CA SER A 208 -40.246 -30.394 0.779 1.00 30.73 C
ATOM 1473 C SER A 208 -40.017 -28.919 1.082 1.00 29.89 C
ATOM 1474 O SER A 208 -39.784 -28.545 2.235 1.00 31.34 O
ATOM 1475 CB SER A 208 -41.747 -30.585 0.593 1.00 30.66 C
ATOM 1476 OG SER A 208 -42.433 -30.046 1.710 1.00 29.26 O
ATOM 1477 N LEU A 209 -40.133 -28.090 0.049 1.00 29.32 N
ATOM 1478 CA LEU A 209 -40.076 -26.633 0.194 1.00 28.13 C
ATOM 1479 C LEU A 209 -41.097 -26.103 1.211 1.00 27.64 C
ATOM 1480 O LEU A 209 -40.764 -25.286 2.067 1.00 27.08 O
ATOM 1481 CB LEU A 209 -40.286 -25.970 -1.171 1.00 27.51 C
ATOM 1482 CG LEU A 209 -40.292 -24.436 -1.230 1.00 27.10 C
ATOM 1483 CD1 LEU A 209 -38.968 -23.855 -0.767 1.00 26.60 C
ATOM 1484 CD2 LEU A 209 -40.633 -23.990 -2.648 1.00 26.92 C
ATOM 1485 N ASP A 210 -42.335 -26.584 1.126 1.00 27.66 N
ATOM 1486 CA ASP A 210 -43.396 -26.127 2.041 1.00 28.01 C
ATOM 1487 C ASP A 210 -43.026 -26.394 3.484 1.00 27.84 C
ATOM 1488 O ASP A 210 -43.295 -25.576 4.361 1.00 26.45 O
ATOM 1489 CB ASP A 210 -44.735 -26.789 1.716 1.00 29.33 C
ATOM 1490 CG ASP A 210 -45.417 -26.168 0.501 1.00 31.65 C
ATOM 1491 OD1 ASP A 210 -44.991 -25.077 0.040 1.00 31.42 O
ATOM 1492 OD2 ASP A 210 -46.388 -26.777 0.004 1.00 32.09 O
ATOM 1493 N GLU A 211 -42.396 -27.540 3.713 1.00 28.07 N
ATOM 1494 CA GLU A 211 -41.932 -27.936 5.034 1.00 29.34 C
ATOM 1495 C GLU A 211 -40.769 -27.065 5.508 1.00 27.16 C
ATOM 1496 O GLU A 211 -40.705 -26.688 6.668 1.00 25.58 O
ATOM 1497 CB GLU A 211 -41.475 -29.382 4.966 1.00 31.78 C
ATOM 1498 CG GLU A 211 -41.440 -30.111 6.286 1.00 38.79 C
ATOM 1499 CD GLU A 211 -41.631 -31.596 6.058 1.00 42.85 C
ATOM 1500 OE1 GLU A 211 -42.751 -31.986 5.637 1.00 45.20 O
ATOM 1501 OE2 GLU A 211 -40.659 -32.352 6.265 1.00 41.04 O
ATOM 1502 N THR A 212 -39.842 -26.770 4.604 1.00 27.78 N
ATOM 1503 CA THR A 212 -38.700 -25.898 4.917 1.00 26.32 C
ATOM 1504 C THR A 212 -39.177 -24.513 5.330 1.00 26.07 C
ATOM 1505 O THR A 212 -38.696 -23.952 6.312 1.00 25.67 O
ATOM 1506 CB THR A 212 -37.749 -25.785 3.716 1.00 25.89 C
ATOM 1507 OG1 THR A 212 -37.304 -27.095 3.354 1.00 25.17 O
ATOM 1508 CG2 THR A 212 -36.537 -24.885 4.034 1.00 24.84 C
ATOM 1509 N ILE A 213 -40.127 -23.971 4.577 1.00 27.32 N
ATOM 1510 CA ILE A 213 -40.729 -22.683 4.899 1.00 28.02 C
ATOM 1511 C ILE A 213 -41.474 -22.697 6.245 1.00 28.27 C
ATOM 1512 O ILE A 213 -41.323 -21.770 7.046 1.00 28.33 O
ATOM 1513 CB ILE A 213 -41.605 -22.178 3.727 1.00 28.17 C
ATOM 1514 CG1 ILE A 213 -40.694 -21.759 2.564 1.00 28.04 C
ATOM 1515 CG2 ILE A 213 -42.512 -21.024 4.155 1.00 28.09 C
ATOM 1516 CD1 ILE A 213 -41.393 -21.673 1.227 1.00 28.65 C
ATOM 1517 N ALA A 214 -42.252 -23.749 6.505 1.00 29.06 N
ATOM 1518 CA ALA A 214 -43.009 -23.838 7.769 1.00 28.44 C
ATOM 1519 C ALA A 214 -42.094 -23.831 9.007 1.00 29.07 C
ATOM 1520 O ALA A 214 -42.347 -23.109 9.981 1.00 29.68 O
ATOM 1521 CB ALA A 214 -43.924 -25.057 7.767 1.00 28.00 C
ATOM 1522 N LEU A 215 -41.020 -24.616 8.950 1.00 28.84 N
ATOM 1523 CA LEU A 215 -40.021 -24.660 10.012 1.00 30.16 C
ATOM 1524 C LEU A 215 -39.407 -23.283 10.293 1.00 30.53 C
ATOM 1525 O LEU A 215 -39.075 -22.970 11.434 1.00 31.43 O
ATOM 1526 CB LEU A 215 -38.922 -25.672 9.662 1.00 30.36 C
ATOM 1527 CG LEU A 215 -37.748 -25.842 10.636 1.00 30.63 C
ATOM 1528 CD1 LEU A 215 -37.254 -27.279 10.641 1.00 30.73 C
ATOM 1529 CD2 LEU A 215 -36.613 -24.887 10.293 1.00 30.96 C
ATOM 1530 N HIS A 216 -39.237 -22.473 9.253 1.00 30.41 N
ATOM 1531 CA HIS A 216 -38.654 -21.146 9.426 1.00 32.06 C
ATOM 1532 C HIS A 216 -39.679 -20.121 9.828 1.00 32.94 C
ATOM 1533 O HIS A 216 -39.325 -19.002 10.173 1.00 33.75 O
ATOM 1534 CB HIS A 216 -37.911 -20.713 8.165 1.00 30.09 C
ATOM 1535 CG HIS A 216 -36.594 -21.429 7.960 1.00 29.96 C
ATOM 1536 ND1 HIS A 216 -36.511 -22.658 7.414 1.00 29.57 N
ATOM 1537 CD2 HIS A 216 -35.286 -21.040 8.247 1.00 30.28 C
ATOM 1538 CE1 HIS A 216 -35.225 -23.041 7.354 1.00 28.80 C
ATOM 1539 NE2 HIS A 216 -34.473 -22.050 7.863 1.00 30.49 N
ATOM 1540 N SER A 217 -40.954 -20.507 9.809 1.00 34.01 N
ATOM 1541 CA SER A 217 -42.058 -19.588 10.078 1.00 34.21 C
ATOM 1542 C SER A 217 -42.858 -19.945 11.331 1.00 35.28 C
ATOM 1543 O SER A 217 -43.818 -19.261 11.660 1.00 38.23 O
ATOM 1544 CB SER A 217 -43.023 -19.552 8.893 1.00 34.17 C
ATOM 1545 OG SER A 217 -42.352 -19.397 7.664 1.00 33.03 O
ATOM 1546 N ASP A 218 -42.478 -21.006 12.030 1.00 34.59 N
ATOM 1547 CA ASP A 218 -43.266 -21.453 13.173 1.00 36.39 C
ATOM 1548 C ASP A 218 -42.834 -20.810 14.488 1.00 36.25 C
ATOM 1549 O ASP A 218 -43.333 -21.180 15.547 1.00 37.48 O
ATOM 1550 CB ASP A 218 -43.260 -22.993 13.282 1.00 37.43 C
ATOM 1551 CG ASP A 218 -41.897 -23.561 13.700 1.00 39.91 C
ATOM 1552 OD1 ASP A 218 -41.050 -22.808 14.225 1.00 41.40 O
ATOM 1553 OD2 ASP A 218 -41.670 -24.773 13.501 1.00 41.24 O
ATOM 1554 N GLY A 219 -41.893 -19.870 14.414 1.00 37.13 N
ATOM 1555 CA GLY A 219 -41.398 -19.167 15.596 1.00 32.86 C
ATOM 1556 C GLY A 219 -40.086 -19.707 16.143 1.00 33.28 C
ATOM 1557 O GLY A 219 -39.440 -19.056 16.963 1.00 32.25 O
ATOM 1558 N SER A 220 -39.671 -20.889 15.681 1.00 32.46 N
ATOM 1559 CA SER A 220 -38.500 -21.553 16.265 1.00 32.22 C
ATOM 1560 C SER A 220 -37.177 -20.823 16.018 1.00 31.99 C
ATOM 1561 O SER A 220 -36.212 -21.037 16.748 1.00 29.90 O
ATOM 1562 CB SER A 220 -38.400 -23.015 15.813 1.00 31.53 C
ATOM 1563 OG SER A 220 -38.328 -23.119 14.410 1.00 32.16 O
ATOM 1564 N GLU A 221 -37.141 -19.951 15.007 1.00 31.57 N
ATOM 1565 CA GLU A 221 -35.908 -19.227 14.667 1.00 32.03 C
ATOM 1566 C GLU A 221 -35.396 -18.347 15.813 1.00 31.94 C
ATOM 1567 O GLU A 221 -34.186 -18.195 15.995 1.00 31.20 O
ATOM 1568 CB GLU A 221 -36.077 -18.424 13.368 1.00 30.47 C
ATOM 1569 CG GLU A 221 -36.081 -19.308 12.125 1.00 30.27 C
ATOM 1570 CD GLU A 221 -34.686 -19.752 11.704 1.00 30.35 C
ATOM 1571 OE1 GLU A 221 -34.366 -20.953 11.799 1.00 28.08 O
ATOM 1572 OE2 GLU A 221 -33.891 -18.886 11.293 1.00 32.66 O
ATOM 1573 N ALA A 222 -36.325 -17.806 16.595 1.00 32.27 N
ATOM 1574 CA ALA A 222 -36.013 -16.968 17.753 1.00 33.17 C
ATOM 1575 C ALA A 222 -35.244 -17.684 18.875 1.00 33.47 C
ATOM 1576 O ALA A 222 -34.651 -17.037 19.735 1.00 33.64 O
ATOM 1577 CB ALA A 222 -37.290 -16.353 18.300 1.00 34.15 C
ATOM 1578 N ARG A 223 -35.244 -19.013 18.851 1.00 32.91 N
ATOM 1579 CA ARG A 223 -34.564 -19.814 19.872 1.00 32.84 C
ATOM 1580 C ARG A 223 -33.112 -20.130 19.499 1.00 31.62 C
ATOM 1581 O ARG A 223 -32.395 -20.773 20.265 1.00 30.78 O
ATOM 1582 CB ARG A 223 -35.350 -21.109 20.133 1.00 34.48 C
ATOM 1583 CG ARG A 223 -36.720 -20.840 20.748 1.00 38.56 C
ATOM 1584 CD ARG A 223 -37.387 -22.098 21.288 1.00 39.51 C
ATOM 1585 NE ARG A 223 -38.254 -22.747 20.301 1.00 43.62 N
ATOM 1586 CZ ARG A 223 -37.933 -23.843 19.612 1.00 43.82 C
ATOM 1587 NH1 ARG A 223 -36.757 -24.430 19.781 1.00 45.08 N
ATOM 1588 NH2 ARG A 223 -38.794 -24.355 18.747 1.00 43.44 N
ATOM 1589 N TYR A 224 -32.686 -19.659 18.327 1.00 29.00 N
ATOM 1590 CA TYR A 224 -31.351 -19.932 17.822 1.00 28.59 C
ATOM 1591 C TYR A 224 -30.676 -18.657 17.326 1.00 27.76 C
ATOM 1592 O TYR A 224 -31.239 -17.918 16.510 1.00 27.08 O
ATOM 1593 CB TYR A 224 -31.417 -20.929 16.664 1.00 28.19 C
ATOM 1594 CG TYR A 224 -32.044 -22.263 16.994 1.00 29.10 C
ATOM 1595 CD1 TYR A 224 -31.303 -23.263 17.627 1.00 30.08 C
ATOM 1596 CD2 TYR A 224 -33.370 -22.535 16.643 1.00 29.05 C
ATOM 1597 CE1 TYR A 224 -31.867 -24.494 17.917 1.00 31.33 C
ATOM 1598 CE2 TYR A 224 -33.950 -23.760 16.941 1.00 30.82 C
ATOM 1599 CZ TYR A 224 -33.190 -24.730 17.577 1.00 31.87 C
ATOM 1600 OH TYR A 224 -33.734 -25.945 17.864 1.00 32.15 O
ATOM 1601 N THR A 225 -29.464 -18.414 17.811 1.00 26.02 N
ATOM 1602 CA THR A 225 -28.692 -17.285 17.336 1.00 26.27 C
ATOM 1603 C THR A 225 -28.153 -17.577 15.932 1.00 25.57 C
ATOM 1604 O THR A 225 -27.979 -16.658 15.144 1.00 26.46 O
ATOM 1605 CB THR A 225 -27.548 -16.899 18.302 1.00 26.00 C
ATOM 1606 OG1 THR A 225 -26.890 -18.080 18.774 1.00 25.39 O
ATOM 1607 CG2 THR A 225 -28.084 -16.091 19.509 1.00 26.14 C
ATOM 1608 N TYR A 226 -27.919 -18.855 15.622 1.00 25.31 N
ATOM 1609 CA TYR A 226 -27.377 -19.261 14.317 1.00 24.46 C
ATOM 1610 C TYR A 226 -28.301 -20.241 13.595 1.00 24.03 C
ATOM 1611 O TYR A 226 -28.775 -21.211 14.196 1.00 23.45 O
ATOM 1612 CB TYR A 226 -26.007 -19.914 14.471 1.00 25.24 C
ATOM 1613 CG TYR A 226 -24.903 -19.004 14.946 1.00 25.92 C
ATOM 1614 CD1 TYR A 226 -23.888 -18.590 14.077 1.00 24.51 C
ATOM 1615 CD2 TYR A 226 -24.849 -18.581 16.273 1.00 24.88 C
ATOM 1616 CE1 TYR A 226 -22.869 -17.765 14.524 1.00 24.60 C
ATOM 1617 CE2 TYR A 226 -23.845 -17.745 16.716 1.00 25.49 C
ATOM 1618 CZ TYR A 226 -22.851 -17.351 15.841 1.00 25.76 C
ATOM 1619 OH TYR A 226 -21.846 -16.530 16.308 1.00 27.74 O
ATOM 1620 N SER A 227 -28.528 -20.003 12.304 1.00 22.55 N
ATOM 1621 CA SER A 227 -29.441 -20.834 11.512 1.00 24.04 C
ATOM 1622 C SER A 227 -29.157 -20.721 10.011 1.00 24.55 C
ATOM 1623 O SER A 227 -29.097 -19.615 9.466 1.00 24.25 O
ATOM 1624 CB SER A 227 -30.907 -20.448 11.831 1.00 23.61 C
ATOM 1625 OG SER A 227 -31.837 -21.276 11.151 1.00 25.85 O
ATOM 1626 N SER A 228 -28.925 -21.867 9.361 1.00 25.74 N
ATOM 1627 CA SER A 228 -28.846 -21.959 7.900 1.00 24.64 C
ATOM 1628 C SER A 228 -29.239 -23.366 7.457 1.00 25.94 C
ATOM 1629 O SER A 228 -29.358 -24.273 8.283 1.00 25.37 O
ATOM 1630 CB SER A 228 -27.440 -21.622 7.376 1.00 24.88 C
ATOM 1631 OG SER A 228 -26.496 -22.543 7.867 1.00 25.16 O
ATOM 1632 N ALA A 229 -29.415 -23.546 6.150 1.00 24.98 N
ATOM 1633 CA ALA A 229 -29.864 -24.818 5.609 1.00 25.35 C
ATOM 1634 C ALA A 229 -29.262 -25.067 4.223 1.00 26.88 C
ATOM 1635 O ALA A 229 -28.968 -24.119 3.484 1.00 27.46 O
ATOM 1636 CB ALA A 229 -31.387 -24.839 5.538 1.00 21.52 C
ATOM 1637 N TRP A 230 -29.062 -26.336 3.879 1.00 28.43 N
ATOM 1638 CA TRP A 230 -28.829 -26.700 2.482 1.00 31.22 C
ATOM 1639 C TRP A 230 -30.128 -27.197 1.929 1.00 30.60 C
ATOM 1640 O TRP A 230 -30.840 -27.945 2.604 1.00 31.09 O
ATOM 1641 CB TRP A 230 -27.750 -27.773 2.335 1.00 35.45 C
ATOM 1642 CG TRP A 230 -27.730 -28.373 0.943 1.00 39.85 C
ATOM 1643 CD1 TRP A 230 -26.952 -27.971 -0.146 1.00 39.62 C
ATOM 1644 CD2 TRP A 230 -28.572 -29.477 0.424 1.00 41.71 C
ATOM 1645 NE1 TRP A 230 -27.231 -28.728 -1.256 1.00 42.44 N
ATOM 1646 CE2 TRP A 230 -28.187 -29.656 -0.985 1.00 43.28 C
ATOM 1647 CE3 TRP A 230 -29.558 -30.303 0.965 1.00 41.22 C
ATOM 1648 CZ2 TRP A 230 -28.778 -30.628 -1.794 1.00 43.14 C
ATOM 1649 CZ3 TRP A 230 -30.144 -31.279 0.140 1.00 42.99 C
ATOM 1650 CH2 TRP A 230 -29.761 -31.436 -1.204 1.00 42.85 C
ATOM 1651 N PHE A 231 -30.467 -26.794 0.708 1.00 28.32 N
ATOM 1652 CA PHE A 231 -31.681 -27.294 0.096 1.00 28.56 C
ATOM 1653 C PHE A 231 -31.467 -27.943 -1.268 1.00 29.31 C
ATOM 1654 O PHE A 231 -30.450 -27.724 -1.935 1.00 28.13 O
ATOM 1655 CB PHE A 231 -32.801 -26.238 0.080 1.00 30.40 C
ATOM 1656 CG PHE A 231 -32.647 -25.186 -0.975 1.00 29.76 C
ATOM 1657 CD1 PHE A 231 -33.297 -25.314 -2.201 1.00 29.22 C
ATOM 1658 CD2 PHE A 231 -31.869 -24.056 -0.741 1.00 30.50 C
ATOM 1659 CE1 PHE A 231 -33.163 -24.342 -3.180 1.00 30.43 C
ATOM 1660 CE2 PHE A 231 -31.731 -23.076 -1.714 1.00 30.26 C
ATOM 1661 CZ PHE A 231 -32.379 -23.215 -2.934 1.00 30.27 C
ATOM 1662 N ASP A 232 -32.446 -28.748 -1.660 1.00 28.74 N
ATOM 1663 CA ASP A 232 -32.449 -29.449 -2.941 1.00 28.75 C
ATOM 1664 C ASP A 232 -33.097 -28.525 -3.986 1.00 26.97 C
ATOM 1665 O ASP A 232 -34.276 -28.199 -3.882 1.00 25.92 O
ATOM 1666 CB ASP A 232 -33.221 -30.767 -2.749 1.00 29.17 C
ATOM 1667 CG ASP A 232 -33.307 -31.627 -3.999 1.00 29.92 C
ATOM 1668 OD1 ASP A 232 -33.050 -31.154 -5.126 1.00 29.94 O
ATOM 1669 OD2 ASP A 232 -33.680 -32.809 -3.828 1.00 30.28 O
ATOM 1670 N ALA A 233 -32.299 -28.090 -4.964 1.00 26.57 N
ATOM 1671 CA ALA A 233 -32.749 -27.223 -6.065 1.00 27.79 C
ATOM 1672 C ALA A 233 -32.962 -27.964 -7.394 1.00 28.63 C
ATOM 1673 O ALA A 233 -33.291 -27.337 -8.408 1.00 27.09 O
ATOM 1674 CB ALA A 233 -31.751 -26.083 -6.278 1.00 27.74 C
ATOM 1675 N ILE A 234 -32.789 -29.285 -7.381 1.00 30.56 N
ATOM 1676 CA ILE A 234 -32.833 -30.096 -8.609 1.00 31.35 C
ATOM 1677 C ILE A 234 -34.070 -30.995 -8.719 1.00 32.68 C
ATOM 1678 O ILE A 234 -34.667 -31.102 -9.794 1.00 34.17 O
ATOM 1679 CB ILE A 234 -31.534 -30.917 -8.791 1.00 32.02 C
ATOM 1680 CG1 ILE A 234 -30.353 -29.962 -8.994 1.00 31.93 C
ATOM 1681 CG2 ILE A 234 -31.660 -31.895 -9.967 1.00 31.96 C
ATOM 1682 CD1 ILE A 234 -28.990 -30.614 -8.924 1.00 32.87 C
ATOM 1683 N SER A 235 -34.457 -31.628 -7.615 1.00 32.66 N
ATOM 1684 CA SER A 235 -35.595 -32.548 -7.620 1.00 34.46 C
ATOM 1685 C SER A 235 -36.908 -31.856 -7.952 1.00 33.96 C
ATOM 1686 O SER A 235 -37.184 -30.747 -7.488 1.00 32.16 O
ATOM 1687 CB SER A 235 -35.741 -33.259 -6.274 1.00 33.19 C
ATOM 1688 OG SER A 235 -34.554 -33.943 -5.911 1.00 34.60 O
ATOM 1689 N ALA A 236 -37.719 -32.542 -8.747 1.00 34.02 N
ATOM 1690 CA ALA A 236 -39.082 -32.122 -9.022 1.00 34.85 C
ATOM 1691 C ALA A 236 -39.853 -31.964 -7.709 1.00 33.02 C
ATOM 1692 O ALA A 236 -39.521 -32.613 -6.718 1.00 31.48 O
ATOM 1693 CB ALA A 236 -39.763 -33.142 -9.932 1.00 34.98 C
ATOM 1694 N PRO A 237 -40.873 -31.084 -7.689 1.00 32.92 N
ATOM 1695 CA PRO A 237 -41.777 -31.059 -6.540 1.00 32.38 C
ATOM 1696 C PRO A 237 -42.442 -32.437 -6.402 1.00 32.89 C
ATOM 1697 O PRO A 237 -42.753 -33.052 -7.416 1.00 33.39 O
ATOM 1698 CB PRO A 237 -42.837 -30.022 -6.948 1.00 33.03 C
ATOM 1699 CG PRO A 237 -42.195 -29.200 -8.012 1.00 32.34 C
ATOM 1700 CD PRO A 237 -41.296 -30.146 -8.744 1.00 32.09 C
ATOM 1701 N PRO A 238 -42.720 -32.896 -5.167 1.00 32.66 N
ATOM 1702 CA PRO A 238 -42.620 -32.196 -3.887 1.00 31.11 C
ATOM 1703 C PRO A 238 -41.252 -32.240 -3.196 1.00 29.98 C
ATOM 1704 O PRO A 238 -41.067 -31.572 -2.187 1.00 29.52 O
ATOM 1705 CB PRO A 238 -43.669 -32.915 -3.031 1.00 32.27 C
ATOM 1706 CG PRO A 238 -43.646 -34.315 -3.542 1.00 32.32 C
ATOM 1707 CD PRO A 238 -43.326 -34.233 -5.012 1.00 32.03 C
ATOM 1708 N LYS A 239 -40.305 -33.007 -3.726 1.00 29.05 N
ATOM 1709 CA LYS A 239 -38.980 -33.081 -3.125 1.00 30.12 C
ATOM 1710 C LYS A 239 -38.237 -31.742 -3.221 1.00 28.14 C
ATOM 1711 O LYS A 239 -37.480 -31.394 -2.321 1.00 26.71 O
ATOM 1712 CB LYS A 239 -38.153 -34.212 -3.746 1.00 32.68 C
ATOM 1713 CG LYS A 239 -38.668 -35.608 -3.412 1.00 37.23 C
ATOM 1714 CD LYS A 239 -37.846 -36.671 -4.125 1.00 40.43 C
ATOM 1715 CE LYS A 239 -38.454 -38.055 -3.962 1.00 42.98 C
ATOM 1716 NZ LYS A 239 -38.478 -38.444 -2.525 1.00 46.28 N
ATOM 1717 N LEU A 240 -38.466 -31.005 -4.309 1.00 26.64 N
ATOM 1718 CA LEU A 240 -37.952 -29.631 -4.462 1.00 26.28 C
ATOM 1719 C LEU A 240 -38.008 -28.839 -3.170 1.00 25.47 C
ATOM 1720 O LEU A 240 -39.077 -28.695 -2.567 1.00 24.34 O
ATOM 1721 CB LEU A 240 -38.740 -28.857 -5.529 1.00 25.94 C
ATOM 1722 CG LEU A 240 -38.255 -27.402 -5.746 1.00 25.59 C
ATOM 1723 CD1 LEU A 240 -36.777 -27.384 -6.116 1.00 23.80 C
ATOM 1724 CD2 LEU A 240 -39.089 -26.721 -6.823 1.00 25.29 C
ATOM 1725 N GLY A 241 -36.857 -28.329 -2.746 1.00 25.88 N
ATOM 1726 CA GLY A 241 -36.812 -27.442 -1.583 1.00 27.44 C
ATOM 1727 C GLY A 241 -36.769 -28.133 -0.228 1.00 28.16 C
ATOM 1728 O GLY A 241 -36.849 -27.459 0.820 1.00 26.90 O
ATOM 1729 N ARG A 242 -36.635 -29.464 -0.238 1.00 26.52 N
ATOM 1730 CA ARG A 242 -36.301 -30.198 0.987 1.00 27.69 C
ATOM 1731 C ARG A 242 -34.918 -29.746 1.451 1.00 26.88 C
ATOM 1732 O ARG A 242 -34.106 -29.283 0.637 1.00 30.09 O
ATOM 1733 CB ARG A 242 -36.360 -31.718 0.782 1.00 29.41 C
ATOM 1734 CG ARG A 242 -35.284 -32.301 -0.122 1.00 30.76 C
ATOM 1735 CD ARG A 242 -35.632 -33.738 -0.477 1.00 32.32 C
ATOM 1736 NE ARG A 242 -34.771 -34.274 -1.527 1.00 34.77 N
ATOM 1737 CZ ARG A 242 -34.610 -35.572 -1.782 1.00 38.03 C
ATOM 1738 NH1 ARG A 242 -35.248 -36.495 -1.065 1.00 39.69 N
ATOM 1739 NH2 ARG A 242 -33.807 -35.952 -2.760 1.00 40.45 N
ATOM 1740 N ALA A 243 -34.641 -29.880 2.739 1.00 25.28 N
ATOM 1741 CA ALA A 243 -33.504 -29.188 3.333 1.00 25.58 C
ATOM 1742 C ALA A 243 -32.896 -29.945 4.499 1.00 25.57 C
ATOM 1743 O ALA A 243 -33.614 -30.622 5.237 1.00 26.11 O
ATOM 1744 CB ALA A 243 -33.947 -27.802 3.806 1.00 24.70 C
ATOM 1745 N ALA A 244 -31.580 -29.818 4.666 1.00 24.55 N
ATOM 1746 CA ALA A 244 -30.932 -30.158 5.934 1.00 24.95 C
ATOM 1747 C ALA A 244 -30.630 -28.844 6.669 1.00 25.30 C
ATOM 1748 O ALA A 244 -29.827 -28.017 6.200 1.00 24.18 O
ATOM 1749 CB ALA A 244 -29.669 -30.969 5.711 1.00 25.14 C
ATOM 1750 N VAL A 245 -31.311 -28.649 7.795 1.00 23.01 N
ATOM 1751 CA VAL A 245 -31.249 -27.410 8.562 1.00 23.40 C
ATOM 1752 C VAL A 245 -30.334 -27.603 9.757 1.00 24.60 C
ATOM 1753 O VAL A 245 -30.436 -28.605 10.492 1.00 23.87 O
ATOM 1754 CB VAL A 245 -32.666 -26.996 9.071 1.00 23.04 C
ATOM 1755 CG1 VAL A 245 -32.665 -25.556 9.568 1.00 22.73 C
ATOM 1756 CG2 VAL A 245 -33.708 -27.161 7.968 1.00 21.82 C
ATOM 1757 N SER A 246 -29.440 -26.643 9.959 1.00 24.12 N
ATOM 1758 CA SER A 246 -28.517 -26.687 11.080 1.00 26.22 C
ATOM 1759 C SER A 246 -28.703 -25.408 11.896 1.00 27.27 C
ATOM 1760 O SER A 246 -28.517 -24.310 11.370 1.00 26.76 O
ATOM 1761 CB SER A 246 -27.079 -26.816 10.555 1.00 26.92 C
ATOM 1762 OG SER A 246 -26.124 -26.438 11.533 1.00 30.98 O
ATOM 1763 N ARG A 247 -29.101 -25.544 13.160 1.00 26.37 N
ATOM 1764 CA ARG A 247 -29.357 -24.364 14.001 1.00 26.36 C
ATOM 1765 C ARG A 247 -28.725 -24.536 15.371 1.00 26.42 C
ATOM 1766 O ARG A 247 -28.709 -25.632 15.923 1.00 28.67 O
ATOM 1767 CB ARG A 247 -30.866 -24.086 14.131 1.00 25.74 C
ATOM 1768 CG ARG A 247 -31.638 -24.201 12.822 1.00 27.02 C
ATOM 1769 CD ARG A 247 -33.051 -23.642 12.913 1.00 27.86 C
ATOM 1770 NE ARG A 247 -34.064 -24.565 13.444 1.00 27.62 N
ATOM 1771 CZ ARG A 247 -35.349 -24.241 13.568 1.00 29.01 C
ATOM 1772 NH1 ARG A 247 -35.757 -23.025 13.205 1.00 27.09 N
ATOM 1773 NH2 ARG A 247 -36.230 -25.115 14.062 1.00 27.76 N
ATOM 1774 N GLY A 248 -28.187 -23.461 15.924 1.00 26.00 N
ATOM 1775 CA GLY A 248 -27.596 -23.549 17.249 1.00 27.01 C
ATOM 1776 C GLY A 248 -27.291 -22.217 17.895 1.00 26.88 C
ATOM 1777 O GLY A 248 -27.835 -21.179 17.504 1.00 25.67 O
ATOM 1778 N ARG A 249 -26.417 -22.279 18.896 1.00 27.97 N
ATOM 1779 CA ARG A 249 -25.911 -21.119 19.617 1.00 28.47 C
ATOM 1780 C ARG A 249 -24.554 -21.504 20.175 1.00 27.87 C
ATOM 1781 O ARG A 249 -24.253 -22.691 20.304 1.00 27.41 O
ATOM 1782 CB ARG A 249 -26.870 -20.730 20.753 1.00 31.37 C
ATOM 1783 CG ARG A 249 -26.977 -21.770 21.856 1.00 34.70 C
ATOM 1784 CD ARG A 249 -28.207 -21.548 22.733 1.00 37.59 C
ATOM 1785 NE ARG A 249 -29.459 -21.753 21.994 1.00 43.52 N
ATOM 1786 CZ ARG A 249 -29.968 -22.943 21.650 1.00 45.44 C
ATOM 1787 NH1 ARG A 249 -29.337 -24.077 21.961 1.00 45.29 N
ATOM 1788 NH2 ARG A 249 -31.115 -23.001 20.981 1.00 44.18 N
ATOM 1789 N LEU A 250 -23.729 -20.515 20.505 1.00 27.13 N
ATOM 1790 CA LEU A 250 -22.442 -20.798 21.131 1.00 28.71 C
ATOM 1791 C LEU A 250 -22.663 -21.531 22.446 1.00 29.19 C
ATOM 1792 O LEU A 250 -23.584 -21.200 23.180 1.00 29.30 O
ATOM 1793 CB LEU A 250 -21.668 -19.516 21.389 1.00 27.31 C
ATOM 1794 CG LEU A 250 -21.166 -18.804 20.140 1.00 28.05 C
ATOM 1795 CD1 LEU A 250 -20.846 -17.371 20.516 1.00 27.03 C
ATOM 1796 CD2 LEU A 250 -19.947 -19.536 19.582 1.00 27.43 C
ATOM 1797 N ALA A 251 -21.831 -22.534 22.716 1.00 28.94 N
ATOM 1798 CA ALA A 251 -21.921 -23.319 23.950 1.00 31.61 C
ATOM 1799 C ALA A 251 -21.315 -22.542 25.119 1.00 32.17 C
ATOM 1800 O ALA A 251 -20.431 -21.713 24.912 1.00 28.95 O
ATOM 1801 CB ALA A 251 -21.193 -24.645 23.777 1.00 30.89 C
ATOM 1802 N THR A 252 -21.807 -22.808 26.331 1.00 32.70 N
ATOM 1803 CA THR A 252 -21.132 -22.376 27.562 1.00 35.46 C
ATOM 1804 C THR A 252 -20.259 -23.520 28.058 1.00 36.40 C
ATOM 1805 O THR A 252 -20.479 -24.673 27.686 1.00 37.89 O
ATOM 1806 CB THR A 252 -22.116 -22.004 28.694 1.00 36.98 C
ATOM 1807 OG1 THR A 252 -22.878 -23.160 29.063 1.00 37.51 O
ATOM 1808 CG2 THR A 252 -23.043 -20.868 28.282 1.00 35.57 C
ATOM 1809 N VAL A 253 -19.277 -23.198 28.900 1.00 38.22 N
ATOM 1810 CA VAL A 253 -18.319 -24.184 29.417 1.00 39.61 C
ATOM 1811 C VAL A 253 -18.988 -25.434 30.008 1.00 39.09 C
ATOM 1812 O VAL A 253 -18.600 -26.552 29.671 1.00 37.99 O
ATOM 1813 CB VAL A 253 -17.329 -23.561 30.429 1.00 40.37 C
ATOM 1814 CG1 VAL A 253 -16.514 -24.638 31.136 1.00 40.88 C
ATOM 1815 CG2 VAL A 253 -16.403 -22.584 29.724 1.00 40.57 C
ATOM 1816 N GLU A 254 -19.999 -25.252 30.854 1.00 40.88 N
ATOM 1817 CA GLU A 254 -20.652 -26.402 31.498 1.00 44.27 C
ATOM 1818 C GLU A 254 -21.420 -27.306 30.521 1.00 45.03 C
ATOM 1819 O GLU A 254 -21.685 -28.463 30.835 1.00 44.71 O
ATOM 1820 CB GLU A 254 -21.519 -25.980 32.703 1.00 47.44 C
ATOM 1821 CG GLU A 254 -22.733 -25.118 32.392 1.00 52.61 C
ATOM 1822 CD GLU A 254 -22.406 -23.641 32.215 1.00 57.20 C
ATOM 1823 OE1 GLU A 254 -21.270 -23.219 32.543 1.00 59.20 O
ATOM 1824 OE2 GLU A 254 -23.297 -22.894 31.745 1.00 57.15 O
ATOM 1825 N GLN A 255 -21.735 -26.791 29.329 1.00 42.34 N
ATOM 1826 CA GLN A 255 -22.403 -27.582 28.295 1.00 41.27 C
ATOM 1827 C GLN A 255 -21.441 -28.477 27.520 1.00 42.04 C
ATOM 1828 O GLN A 255 -21.859 -29.320 26.731 1.00 43.72 O
ATOM 1829 CB GLN A 255 -23.168 -26.676 27.334 1.00 41.89 C
ATOM 1830 CG GLN A 255 -24.376 -25.990 27.958 1.00 39.10 C
ATOM 1831 CD GLN A 255 -25.042 -25.022 27.000 1.00 40.99 C
ATOM 1832 OE1 GLN A 255 -24.390 -24.152 26.420 1.00 40.25 O
ATOM 1833 NE2 GLN A 255 -26.348 -25.172 26.825 1.00 40.80 N
ATOM 1834 N LEU A 256 -20.148 -28.293 27.747 1.00 41.52 N
ATOM 1835 CA LEU A 256 -19.143 -29.149 27.141 1.00 42.32 C
ATOM 1836 C LEU A 256 -19.021 -30.445 27.939 1.00 43.55 C
ATOM 1837 O LEU A 256 -19.176 -30.433 29.158 1.00 43.01 O
ATOM 1838 CB LEU A 256 -17.794 -28.426 27.126 1.00 41.55 C
ATOM 1839 CG LEU A 256 -17.394 -27.446 26.004 1.00 42.06 C
ATOM 1840 CD1 LEU A 256 -18.530 -26.988 25.092 1.00 40.37 C
ATOM 1841 CD2 LEU A 256 -16.657 -26.263 26.604 1.00 40.30 C
ATOM 1842 N PRO A 257 -18.742 -31.571 27.259 1.00 45.24 N
ATOM 1843 CA PRO A 257 -18.338 -32.761 28.008 1.00 47.44 C
ATOM 1844 C PRO A 257 -17.037 -32.475 28.761 1.00 49.06 C
ATOM 1845 O PRO A 257 -16.245 -31.636 28.308 1.00 48.00 O
ATOM 1846 CB PRO A 257 -18.103 -33.806 26.912 1.00 47.05 C
ATOM 1847 CG PRO A 257 -17.935 -33.028 25.648 1.00 47.44 C
ATOM 1848 CD PRO A 257 -18.813 -31.829 25.812 1.00 45.35 C
ATOM 1849 N ALA A 258 -16.824 -33.155 29.891 1.00 47.32 N
ATOM 1850 CA ALA A 258 -15.657 -32.906 30.754 1.00 48.42 C
ATOM 1851 C ALA A 258 -14.326 -32.906 29.987 1.00 48.50 C
ATOM 1852 O ALA A 258 -13.446 -32.087 30.255 1.00 48.63 O
ATOM 1853 CB ALA A 258 -15.621 -33.902 31.902 1.00 48.53 C
ATOM 1854 N LYS A 259 -14.219 -33.811 29.019 1.00 49.30 N
ATOM 1855 CA LYS A 259 -13.070 -33.932 28.121 1.00 51.61 C
ATOM 1856 C LYS A 259 -12.626 -32.600 27.507 1.00 52.84 C
ATOM 1857 O LYS A 259 -11.428 -32.339 27.379 1.00 53.66 O
ATOM 1858 CB LYS A 259 -13.426 -34.909 27.000 1.00 53.35 C
ATOM 1859 CG LYS A 259 -12.254 -35.605 26.338 1.00 54.45 C
ATOM 1860 CD LYS A 259 -12.743 -36.389 25.128 1.00 57.62 C
ATOM 1861 CE LYS A 259 -11.810 -37.537 24.780 1.00 60.93 C
ATOM 1862 NZ LYS A 259 -11.807 -38.600 25.827 1.00 63.46 N
ATOM 1863 N LEU A 260 -13.594 -31.764 27.134 1.00 51.46 N
ATOM 1864 CA LEU A 260 -13.315 -30.508 26.430 1.00 52.29 C
ATOM 1865 C LEU A 260 -13.266 -29.281 27.340 1.00 52.78 C
ATOM 1866 O LEU A 260 -12.910 -28.185 26.887 1.00 52.13 O
ATOM 1867 CB LEU A 260 -14.350 -30.288 25.323 1.00 51.96 C
ATOM 1868 CG LEU A 260 -14.119 -30.813 23.902 1.00 53.76 C
ATOM 1869 CD1 LEU A 260 -13.551 -32.224 23.833 1.00 54.58 C
ATOM 1870 CD2 LEU A 260 -15.420 -30.717 23.120 1.00 54.74 C
ATOM 1871 N ARG A 261 -13.618 -29.467 28.614 1.00 51.95 N
ATOM 1872 CA ARG A 261 -13.715 -28.360 29.571 1.00 50.86 C
ATOM 1873 C ARG A 261 -12.397 -27.714 29.978 1.00 49.40 C
ATOM 1874 O ARG A 261 -12.390 -26.574 30.445 1.00 47.81 O
ATOM 1875 CB ARG A 261 -14.453 -28.796 30.830 1.00 51.57 C
ATOM 1876 CG ARG A 261 -15.937 -28.537 30.766 1.00 52.38 C
ATOM 1877 CD ARG A 261 -16.576 -28.694 32.129 1.00 53.12 C
ATOM 1878 NE ARG A 261 -17.988 -29.013 31.973 1.00 55.83 N
ATOM 1879 CZ ARG A 261 -18.514 -30.215 32.182 1.00 54.32 C
ATOM 1880 NH1 ARG A 261 -17.751 -31.222 32.585 1.00 52.38 N
ATOM 1881 NH2 ARG A 261 -19.811 -30.405 31.993 1.00 54.83 N
ATOM 1882 N SER A 262 -11.295 -28.444 29.824 1.00 49.53 N
ATOM 1883 CA SER A 262 -9.981 -27.927 30.209 1.00 50.81 C
ATOM 1884 C SER A 262 -9.452 -26.884 29.221 1.00 49.19 C
ATOM 1885 O SER A 262 -8.686 -26.002 29.603 1.00 53.76 O
ATOM 1886 CB SER A 262 -8.977 -29.067 30.386 1.00 52.48 C
ATOM 1887 OG SER A 262 -8.816 -29.788 29.178 1.00 55.67 O
ATOM 1888 N GLU A 263 -9.861 -26.983 27.959 1.00 45.28 N
ATOM 1889 CA GLU A 263 -9.523 -25.964 26.963 1.00 44.80 C
ATOM 1890 C GLU A 263 -10.781 -25.512 26.226 1.00 38.08 C
ATOM 1891 O GLU A 263 -10.997 -25.903 25.087 1.00 35.27 O
ATOM 1892 CB GLU A 263 -8.488 -26.496 25.967 1.00 48.57 C
ATOM 1893 CG GLU A 263 -7.180 -26.953 26.597 1.00 58.23 C
ATOM 1894 CD GLU A 263 -6.086 -27.201 25.572 1.00 64.03 C
ATOM 1895 OE1 GLU A 263 -4.907 -26.932 25.895 1.00 67.50 O
ATOM 1896 OE2 GLU A 263 -6.400 -27.648 24.444 1.00 67.12 O
ATOM 1897 N PRO A 264 -11.624 -24.688 26.873 1.00 35.98 N
ATOM 1898 CA PRO A 264 -12.915 -24.475 26.207 1.00 35.93 C
ATOM 1899 C PRO A 264 -12.838 -23.560 24.979 1.00 34.01 C
ATOM 1900 O PRO A 264 -13.680 -23.654 24.094 1.00 33.64 O
ATOM 1901 CB PRO A 264 -13.797 -23.875 27.308 1.00 34.76 C
ATOM 1902 CG PRO A 264 -12.851 -23.322 28.321 1.00 35.23 C
ATOM 1903 CD PRO A 264 -11.568 -24.085 28.217 1.00 35.01 C
ATOM 1904 N LEU A 265 -11.809 -22.722 24.926 1.00 33.41 N
ATOM 1905 CA LEU A 265 -11.671 -21.703 23.885 1.00 36.05 C
ATOM 1906 C LEU A 265 -10.734 -22.124 22.755 1.00 39.33 C
ATOM 1907 O LEU A 265 -10.377 -21.315 21.899 1.00 43.68 O
ATOM 1908 CB LEU A 265 -11.216 -20.378 24.510 1.00 32.56 C
ATOM 1909 CG LEU A 265 -12.284 -19.727 25.401 1.00 32.12 C
ATOM 1910 CD1 LEU A 265 -11.668 -18.754 26.391 1.00 31.76 C
ATOM 1911 CD2 LEU A 265 -13.353 -19.041 24.564 1.00 31.06 C
ATOM 1912 N LYS A 266 -10.372 -23.402 22.734 1.00 42.51 N
ATOM 1913 CA LYS A 266 -9.405 -23.920 21.774 1.00 46.39 C
ATOM 1914 C LYS A 266 -10.025 -24.132 20.401 1.00 47.21 C
ATOM 1915 O LYS A 266 -11.137 -24.638 20.295 1.00 44.18 O
ATOM 1916 CB LYS A 266 -8.822 -25.243 22.289 1.00 50.00 C
ATOM 1917 CG LYS A 266 -7.353 -25.480 21.948 1.00 52.37 C
ATOM 1918 CD LYS A 266 -6.443 -24.351 22.431 1.00 54.60 C
ATOM 1919 CE LYS A 266 -6.396 -24.250 23.949 1.00 54.53 C
ATOM 1920 NZ LYS A 266 -5.910 -22.915 24.394 1.00 57.67 N
ATOM 1921 N PHE A 267 -9.314 -23.737 19.350 1.00 49.35 N
ATOM 1922 CA PHE A 267 -9.708 -24.162 18.011 1.00 58.10 C
ATOM 1923 C PHE A 267 -8.904 -25.382 17.558 1.00 59.40 C
ATOM 1924 O PHE A 267 -7.673 -25.360 17.555 1.00 60.76 O
ATOM 1925 CB PHE A 267 -9.610 -23.036 16.981 1.00 61.19 C
ATOM 1926 CG PHE A 267 -9.971 -23.476 15.590 1.00 64.72 C
ATOM 1927 CD1 PHE A 267 -9.024 -23.456 14.570 1.00 66.42 C
ATOM 1928 CD2 PHE A 267 -11.252 -23.954 15.307 1.00 66.91 C
ATOM 1929 CE1 PHE A 267 -9.354 -23.878 13.287 1.00 67.22 C
ATOM 1930 CE2 PHE A 267 -11.587 -24.378 14.029 1.00 69.00 C
ATOM 1931 CZ PHE A 267 -10.636 -24.338 13.017 1.00 67.62 C
ATOM 1932 N ASP A 268 -9.619 -26.441 17.183 1.00 64.85 N
ATOM 1933 CA ASP A 268 -9.006 -27.696 16.738 1.00 66.69 C
ATOM 1934 C ASP A 268 -8.432 -27.537 15.336 1.00 68.74 C
ATOM 1935 O ASP A 268 -8.993 -26.812 14.508 1.00 70.57 O
ATOM 1936 CB ASP A 268 -10.026 -28.845 16.728 1.00 68.30 C
ATOM 1937 CG ASP A 268 -11.363 -28.463 17.347 1.00 69.01 C
ATOM 1938 OD1 ASP A 268 -11.962 -27.457 16.904 1.00 67.12 O
ATOM 1939 OD2 ASP A 268 -11.827 -29.186 18.257 1.00 67.49 O
ATOM 1940 N ALA A 269 -7.322 -28.223 15.074 1.00 71.46 N
ATOM 1941 CA ALA A 269 -6.698 -28.228 13.750 1.00 72.64 C
ATOM 1942 C ALA A 269 -7.597 -28.922 12.718 1.00 72.97 C
ATOM 1943 O ALA A 269 -8.059 -30.043 12.963 1.00 69.38 O
ATOM 1944 CB ALA A 269 -5.333 -28.907 13.812 1.00 71.69 C
ATOM 1945 N PRO A 270 -7.875 -28.244 11.579 1.00 75.58 N
ATOM 1946 CA PRO A 270 -8.535 -28.907 10.449 1.00 75.74 C
ATOM 1947 C PRO A 270 -7.743 -30.149 10.053 1.00 76.94 C
ATOM 1948 O PRO A 270 -6.621 -30.024 9.559 1.00 77.82 O
ATOM 1949 CB PRO A 270 -8.469 -27.853 9.339 1.00 75.25 C
ATOM 1950 CG PRO A 270 -8.462 -26.551 10.064 1.00 74.13 C
ATOM 1951 CD PRO A 270 -7.704 -26.795 11.342 1.00 75.11 C
ATOM 1952 N GLN A 271 -8.318 -31.329 10.289 1.00 74.90 N
ATOM 1953 CA GLN A 271 -7.601 -32.603 10.120 1.00 74.76 C
ATOM 1954 C GLN A 271 -7.193 -32.915 8.671 1.00 73.39 C
ATOM 1955 O GLN A 271 -7.620 -32.236 7.730 1.00 72.74 O
ATOM 1956 CB GLN A 271 -8.381 -33.769 10.747 1.00 74.93 C
ATOM 1957 CG GLN A 271 -9.768 -34.004 10.167 1.00 76.86 C
ATOM 1958 CD GLN A 271 -10.663 -34.801 11.099 1.00 79.43 C
ATOM 1959 OE1 GLN A 271 -11.207 -35.838 10.718 1.00 81.22 O
ATOM 1960 NE2 GLN A 271 -10.821 -34.320 12.329 1.00 79.88 N
ATOM 1961 N LEU A 272 -6.361 -33.943 8.512 1.00 71.07 N
ATOM 1962 CA LEU A 272 -5.740 -34.264 7.226 1.00 70.17 C
ATOM 1963 C LEU A 272 -6.737 -34.811 6.204 1.00 68.35 C
ATOM 1964 O LEU A 272 -6.916 -34.232 5.127 1.00 66.08 O
ATOM 1965 CB LEU A 272 -4.593 -35.268 7.415 1.00 68.32 C
ATOM 1966 CG LEU A 272 -3.265 -35.053 6.670 1.00 68.49 C
ATOM 1967 CD1 LEU A 272 -2.670 -36.388 6.248 1.00 66.90 C
ATOM 1968 CD2 LEU A 272 -3.370 -34.098 5.486 1.00 66.98 C
ATOM 1969 N LEU A 273 -7.378 -35.924 6.554 1.00 65.81 N
ATOM 1970 CA LEU A 273 -8.243 -36.648 5.632 1.00 65.00 C
ATOM 1971 C LEU A 273 -9.636 -36.034 5.537 1.00 64.88 C
ATOM 1972 O LEU A 273 -10.274 -35.748 6.553 1.00 65.99 O
ATOM 1973 CB LEU A 273 -8.342 -38.128 6.028 1.00 63.47 C
ATOM 1974 CG LEU A 273 -7.052 -38.950 6.150 1.00 63.24 C
ATOM 1975 CD1 LEU A 273 -7.364 -40.359 6.630 1.00 62.22 C
ATOM 1976 CD2 LEU A 273 -6.278 -38.992 4.840 1.00 62.19 C
ATOM 1977 N THR A 274 -10.079 -35.825 4.299 1.00 62.09 N
ATOM 1978 CA THR A 274 -11.454 -35.436 3.996 1.00 59.98 C
ATOM 1979 C THR A 274 -12.154 -36.638 3.356 1.00 60.02 C
ATOM 1980 O THR A 274 -11.516 -37.665 3.093 1.00 57.59 O
ATOM 1981 CB THR A 274 -11.514 -34.208 3.058 1.00 57.66 C
ATOM 1982 OG1 THR A 274 -10.889 -34.520 1.806 1.00 58.64 O
ATOM 1983 CG2 THR A 274 -10.809 -33.012 3.686 1.00 58.41 C
ATOM 1984 N LEU A 275 -13.457 -36.515 3.105 1.00 59.12 N
ATOM 1985 CA LEU A 275 -14.240 -37.626 2.553 1.00 57.86 C
ATOM 1986 C LEU A 275 -13.761 -38.171 1.186 1.00 58.39 C
ATOM 1987 O LEU A 275 -13.771 -39.389 0.987 1.00 57.29 O
ATOM 1988 CB LEU A 275 -15.742 -37.305 2.544 1.00 58.17 C
ATOM 1989 CG LEU A 275 -16.450 -37.267 3.909 1.00 59.21 C
ATOM 1990 CD1 LEU A 275 -17.832 -36.647 3.769 1.00 59.17 C
ATOM 1991 CD2 LEU A 275 -16.546 -38.645 4.559 1.00 58.67 C
ATOM 1992 N PRO A 276 -13.341 -37.284 0.247 1.00 58.22 N
ATOM 1993 CA PRO A 276 -12.773 -37.784 -1.018 1.00 59.04 C
ATOM 1994 C PRO A 276 -11.544 -38.672 -0.826 1.00 59.59 C
ATOM 1995 O PRO A 276 -11.303 -39.579 -1.631 1.00 61.80 O
ATOM 1996 CB PRO A 276 -12.374 -36.505 -1.757 1.00 57.67 C
ATOM 1997 CG PRO A 276 -13.297 -35.471 -1.229 1.00 58.41 C
ATOM 1998 CD PRO A 276 -13.516 -35.818 0.216 1.00 57.86 C
ATOM 1999 N ASP A 277 -10.779 -38.405 0.228 1.00 58.19 N
ATOM 2000 CA ASP A 277 -9.600 -39.205 0.550 1.00 59.17 C
ATOM 2001 C ASP A 277 -9.998 -40.587 1.060 1.00 59.84 C
ATOM 2002 O ASP A 277 -9.375 -41.585 0.693 1.00 62.87 O
ATOM 2003 CB ASP A 277 -8.716 -38.484 1.575 1.00 55.92 C
ATOM 2004 CG ASP A 277 -8.436 -37.040 1.192 1.00 54.23 C
ATOM 2005 OD1 ASP A 277 -8.175 -36.765 0.000 1.00 51.75 O
ATOM 2006 OD2 ASP A 277 -8.482 -36.176 2.088 1.00 56.03 O
ATOM 2007 N VAL A 278 -11.047 -40.639 1.879 1.00 58.96 N
ATOM 2008 CA VAL A 278 -11.494 -41.893 2.499 1.00 60.39 C
ATOM 2009 C VAL A 278 -12.413 -42.714 1.587 1.00 59.89 C
ATOM 2010 O VAL A 278 -12.316 -43.942 1.547 1.00 58.83 O
ATOM 2011 CB VAL A 278 -12.164 -41.653 3.873 1.00 59.67 C
ATOM 2012 CG1 VAL A 278 -12.461 -42.978 4.564 1.00 60.88 C
ATOM 2013 CG2 VAL A 278 -11.269 -40.796 4.760 1.00 60.16 C
ATOM 2014 N PHE A 279 -13.295 -42.040 0.854 1.00 60.04 N
ATOM 2015 CA PHE A 279 -14.195 -42.724 -0.076 1.00 62.51 C
ATOM 2016 C PHE A 279 -14.059 -42.143 -1.488 1.00 64.54 C
ATOM 2017 O PHE A 279 -14.903 -41.349 -1.911 1.00 64.70 O
ATOM 2018 CB PHE A 279 -15.649 -42.648 0.414 1.00 63.10 C
ATOM 2019 CG PHE A 279 -15.826 -43.022 1.863 1.00 63.10 C
ATOM 2020 CD1 PHE A 279 -15.931 -44.356 2.246 1.00 63.28 C
ATOM 2021 CD2 PHE A 279 -15.888 -42.038 2.846 1.00 61.85 C
ATOM 2022 CE1 PHE A 279 -16.095 -44.701 3.581 1.00 62.89 C
ATOM 2023 CE2 PHE A 279 -16.049 -42.377 4.180 1.00 62.22 C
ATOM 2024 CZ PHE A 279 -16.151 -43.710 4.548 1.00 61.38 C
ATOM 2025 N PRO A 280 -12.996 -42.542 -2.226 1.00 63.52 N
ATOM 2026 CA PRO A 280 -12.703 -41.943 -3.536 1.00 61.41 C
ATOM 2027 C PRO A 280 -13.766 -42.236 -4.595 1.00 60.10 C
ATOM 2028 O PRO A 280 -13.959 -41.433 -5.507 1.00 58.89 O
ATOM 2029 CB PRO A 280 -11.363 -42.582 -3.934 1.00 61.22 C
ATOM 2030 CG PRO A 280 -10.816 -43.181 -2.683 1.00 62.97 C
ATOM 2031 CD PRO A 280 -12.018 -43.590 -1.885 1.00 62.96 C
ATOM 2032 N ASN A 281 -14.446 -43.372 -4.464 1.00 58.70 N
ATOM 2033 CA ASN A 281 -15.507 -43.758 -5.393 1.00 58.79 C
ATOM 2034 C ASN A 281 -16.865 -43.101 -5.098 1.00 58.74 C
ATOM 2035 O ASN A 281 -17.833 -43.311 -5.834 1.00 58.67 O
ATOM 2036 CB ASN A 281 -15.642 -45.285 -5.449 1.00 59.86 C
ATOM 2037 CG ASN A 281 -14.376 -45.971 -5.947 1.00 61.83 C
ATOM 2038 OD1 ASN A 281 -13.902 -46.929 -5.339 1.00 63.83 O
ATOM 2039 ND2 ASN A 281 -13.821 -45.479 -7.052 1.00 60.31 N
ATOM 2040 N GLY A 282 -16.932 -42.306 -4.030 1.00 57.54 N
ATOM 2041 CA GLY A 282 -18.155 -41.575 -3.680 1.00 58.13 C
ATOM 2042 C GLY A 282 -18.925 -42.181 -2.520 1.00 57.39 C
ATOM 2043 O GLY A 282 -18.472 -43.142 -1.893 1.00 57.83 O
ATOM 2044 N LEU A 283 -20.098 -41.621 -2.238 1.00 55.38 N
ATOM 2045 CA LEU A 283 -20.893 -42.043 -1.082 1.00 55.08 C
ATOM 2046 C LEU A 283 -22.136 -42.868 -1.438 1.00 51.86 C
ATOM 2047 O LEU A 283 -22.829 -43.355 -0.545 1.00 50.15 O
ATOM 2048 CB LEU A 283 -21.291 -40.828 -0.230 1.00 56.28 C
ATOM 2049 CG LEU A 283 -20.177 -40.060 0.493 1.00 58.86 C
ATOM 2050 CD1 LEU A 283 -20.715 -38.745 1.036 1.00 58.10 C
ATOM 2051 CD2 LEU A 283 -19.531 -40.886 1.603 1.00 58.72 C
ATOM 2052 N ALA A 284 -22.402 -43.032 -2.733 1.00 48.99 N
ATOM 2053 CA ALA A 284 -23.597 -43.738 -3.206 1.00 46.43 C
ATOM 2054 C ALA A 284 -23.500 -45.262 -3.072 1.00 45.27 C
ATOM 2055 O ALA A 284 -22.493 -45.875 -3.452 1.00 44.58 O
ATOM 2056 CB ALA A 284 -23.908 -43.349 -4.644 1.00 44.70 C
ATOM 2057 N ASN A 285 -24.550 -45.859 -2.506 1.00 41.06 N
ATOM 2058 CA ASN A 285 -24.725 -47.310 -2.499 1.00 37.94 C
ATOM 2059 C ASN A 285 -26.110 -47.644 -3.071 1.00 36.73 C
ATOM 2060 O ASN A 285 -26.783 -46.757 -3.605 1.00 35.70 O
ATOM 2061 CB ASN A 285 -24.479 -47.904 -1.098 1.00 36.95 C
ATOM 2062 CG ASN A 285 -25.356 -47.279 -0.017 1.00 39.84 C
ATOM 2063 OD1 ASN A 285 -26.579 -47.153 -0.170 1.00 37.41 O
ATOM 2064 ND2 ASN A 285 -24.734 -46.912 1.103 1.00 38.44 N
ATOM 2065 N LYS A 286 -26.542 -48.900 -2.979 1.00 34.87 N
ATOM 2066 CA LYS A 286 -27.800 -49.300 -3.625 1.00 34.58 C
ATOM 2067 C LYS A 286 -29.029 -48.749 -2.891 1.00 34.18 C
ATOM 2068 O LYS A 286 -30.136 -48.794 -3.422 1.00 35.41 O
ATOM 2069 CB LYS A 286 -27.898 -50.827 -3.785 1.00 33.67 C
ATOM 2070 CG LYS A 286 -27.943 -51.603 -2.473 1.00 35.01 C
ATOM 2071 CD LYS A 286 -28.238 -53.076 -2.732 1.00 34.95 C
ATOM 2072 CE LYS A 286 -28.322 -53.854 -1.436 1.00 34.73 C
ATOM 2073 NZ LYS A 286 -28.885 -55.208 -1.681 1.00 35.65 N
ATOM 2074 N TYR A 287 -28.814 -48.232 -1.682 1.00 33.12 N
ATOM 2075 CA TYR A 287 -29.893 -47.713 -0.835 1.00 35.66 C
ATOM 2076 C TYR A 287 -30.117 -46.210 -0.973 1.00 35.75 C
ATOM 2077 O TYR A 287 -31.187 -45.714 -0.629 1.00 35.82 O
ATOM 2078 CB TYR A 287 -29.594 -47.999 0.634 1.00 35.73 C
ATOM 2079 CG TYR A 287 -29.454 -49.454 0.991 1.00 36.56 C
ATOM 2080 CD1 TYR A 287 -30.577 -50.229 1.266 1.00 35.86 C
ATOM 2081 CD2 TYR A 287 -28.194 -50.047 1.089 1.00 36.54 C
ATOM 2082 CE1 TYR A 287 -30.458 -51.561 1.608 1.00 37.69 C
ATOM 2083 CE2 TYR A 287 -28.058 -51.382 1.431 1.00 38.82 C
ATOM 2084 CZ TYR A 287 -29.193 -52.133 1.691 1.00 39.75 C
ATOM 2085 OH TYR A 287 -29.068 -53.452 2.037 1.00 40.39 O
ATOM 2086 N THR A 288 -29.107 -45.499 -1.478 1.00 35.43 N
ATOM 2087 CA THR A 288 -29.036 -44.029 -1.413 1.00 35.40 C
ATOM 2088 C THR A 288 -30.268 -43.289 -1.936 1.00 35.44 C
ATOM 2089 O THR A 288 -30.724 -42.328 -1.317 1.00 37.41 O
ATOM 2090 CB THR A 288 -27.782 -43.491 -2.150 1.00 35.85 C
ATOM 2091 OG1 THR A 288 -26.628 -44.224 -1.726 1.00 35.05 O
ATOM 2092 CG2 THR A 288 -27.572 -41.993 -1.868 1.00 35.60 C
ATOM 2093 N PHE A 289 -30.794 -43.730 -3.072 1.00 36.75 N
ATOM 2094 CA PHE A 289 -31.851 -42.997 -3.754 1.00 37.69 C
ATOM 2095 C PHE A 289 -33.256 -43.559 -3.516 1.00 37.29 C
ATOM 2096 O PHE A 289 -34.224 -43.104 -4.124 1.00 37.56 O
ATOM 2097 CB PHE A 289 -31.531 -42.885 -5.248 1.00 40.14 C
ATOM 2098 CG PHE A 289 -30.212 -42.213 -5.526 1.00 44.24 C
ATOM 2099 CD1 PHE A 289 -30.082 -40.830 -5.409 1.00 45.45 C
ATOM 2100 CD2 PHE A 289 -29.093 -42.962 -5.879 1.00 45.22 C
ATOM 2101 CE1 PHE A 289 -28.864 -40.207 -5.655 1.00 47.19 C
ATOM 2102 CE2 PHE A 289 -27.874 -42.344 -6.128 1.00 45.25 C
ATOM 2103 CZ PHE A 289 -27.759 -40.967 -6.012 1.00 45.64 C
ATOM 2104 N GLY A 290 -33.366 -44.536 -2.622 1.00 34.35 N
ATOM 2105 CA GLY A 290 -34.657 -45.097 -2.292 1.00 31.67 C
ATOM 2106 C GLY A 290 -35.070 -44.782 -0.860 1.00 31.02 C
ATOM 2107 O GLY A 290 -34.408 -44.004 -0.161 1.00 30.07 O
ATOM 2108 N PRO A 291 -36.159 -45.412 -0.403 1.00 29.79 N
ATOM 2109 CA PRO A 291 -36.758 -45.145 0.907 1.00 29.42 C
ATOM 2110 C PRO A 291 -35.829 -45.361 2.100 1.00 29.26 C
ATOM 2111 O PRO A 291 -35.986 -44.679 3.108 1.00 27.66 O
ATOM 2112 CB PRO A 291 -37.961 -46.101 0.942 1.00 29.78 C
ATOM 2113 CG PRO A 291 -38.285 -46.334 -0.516 1.00 28.51 C
ATOM 2114 CD PRO A 291 -36.941 -46.398 -1.172 1.00 29.14 C
ATOM 2115 N ILE A 292 -34.866 -46.278 1.998 1.00 28.54 N
ATOM 2116 CA ILE A 292 -33.903 -46.471 3.095 1.00 29.54 C
ATOM 2117 C ILE A 292 -32.882 -45.325 3.138 1.00 29.34 C
ATOM 2118 O ILE A 292 -32.499 -44.887 4.219 1.00 30.51 O
ATOM 2119 CB ILE A 292 -33.219 -47.863 3.069 1.00 29.54 C
ATOM 2120 CG1 ILE A 292 -34.219 -48.957 3.448 1.00 31.17 C
ATOM 2121 CG2 ILE A 292 -32.040 -47.938 4.036 1.00 29.90 C
ATOM 2122 CD1 ILE A 292 -33.745 -50.348 3.079 1.00 32.65 C
ATOM 2123 N GLY A 293 -32.479 -44.835 1.968 1.00 30.27 N
ATOM 2124 CA GLY A 293 -31.635 -43.634 1.859 1.00 30.61 C
ATOM 2125 C GLY A 293 -32.298 -42.403 2.442 1.00 30.87 C
ATOM 2126 O GLY A 293 -31.708 -41.703 3.273 1.00 29.72 O
ATOM 2127 N GLU A 294 -33.544 -42.157 2.038 1.00 31.33 N
ATOM 2128 CA GLU A 294 -34.314 -41.037 2.568 1.00 32.32 C
ATOM 2129 C GLU A 294 -34.376 -41.100 4.090 1.00 31.00 C
ATOM 2130 O GLU A 294 -34.103 -40.115 4.771 1.00 28.79 O
ATOM 2131 CB GLU A 294 -35.716 -40.983 1.940 1.00 35.23 C
ATOM 2132 CG GLU A 294 -35.701 -40.496 0.496 1.00 39.72 C
ATOM 2133 CD GLU A 294 -37.074 -40.423 -0.162 1.00 43.96 C
ATOM 2134 OE1 GLU A 294 -38.111 -40.324 0.545 1.00 45.25 O
ATOM 2135 OE2 GLU A 294 -37.113 -40.444 -1.416 1.00 46.23 O
ATOM 2136 N LEU A 295 -34.693 -42.282 4.613 1.00 30.11 N
ATOM 2137 CA LEU A 295 -34.790 -42.511 6.047 1.00 30.39 C
ATOM 2138 C LEU A 295 -33.460 -42.286 6.766 1.00 30.69 C
ATOM 2139 O LEU A 295 -33.418 -41.675 7.838 1.00 28.99 O
ATOM 2140 CB LEU A 295 -35.279 -43.937 6.302 1.00 30.65 C
ATOM 2141 CG LEU A 295 -36.095 -44.250 7.541 1.00 31.97 C
ATOM 2142 CD1 LEU A 295 -37.125 -43.170 7.840 1.00 32.10 C
ATOM 2143 CD2 LEU A 295 -36.766 -45.598 7.307 1.00 32.09 C
ATOM 2144 N TRP A 296 -32.380 -42.788 6.173 1.00 30.18 N
ATOM 2145 CA TRP A 296 -31.066 -42.648 6.770 1.00 33.06 C
ATOM 2146 C TRP A 296 -30.669 -41.197 6.874 1.00 33.17 C
ATOM 2147 O TRP A 296 -30.191 -40.744 7.923 1.00 31.02 O
ATOM 2148 CB TRP A 296 -30.028 -43.435 5.975 1.00 35.38 C
ATOM 2149 CG TRP A 296 -28.643 -43.341 6.565 1.00 39.31 C
ATOM 2150 CD1 TRP A 296 -28.046 -44.204 7.485 1.00 41.31 C
ATOM 2151 CD2 TRP A 296 -27.635 -42.302 6.307 1.00 40.68 C
ATOM 2152 NE1 TRP A 296 -26.774 -43.783 7.795 1.00 40.83 N
ATOM 2153 CE2 TRP A 296 -26.466 -42.652 7.125 1.00 41.37 C
ATOM 2154 CE3 TRP A 296 -27.584 -41.164 5.508 1.00 41.97 C
ATOM 2155 CZ2 TRP A 296 -25.313 -41.879 7.130 1.00 42.30 C
ATOM 2156 CZ3 TRP A 296 -26.416 -40.389 5.522 1.00 43.76 C
ATOM 2157 CH2 TRP A 296 -25.309 -40.742 6.314 1.00 44.59 C
ATOM 2158 N TYR A 297 -30.865 -40.470 5.775 1.00 33.65 N
ATOM 2159 CA TYR A 297 -30.578 -39.048 5.698 1.00 36.07 C
ATOM 2160 C TYR A 297 -31.412 -38.273 6.721 1.00 34.02 C
ATOM 2161 O TYR A 297 -30.886 -37.442 7.449 1.00 32.49 O
ATOM 2162 CB TYR A 297 -30.843 -38.548 4.274 1.00 42.43 C
ATOM 2163 CG TYR A 297 -30.358 -37.147 3.996 1.00 48.92 C
ATOM 2164 CD1 TYR A 297 -29.014 -36.897 3.705 1.00 52.00 C
ATOM 2165 CD2 TYR A 297 -31.246 -36.068 4.013 1.00 52.22 C
ATOM 2166 CE1 TYR A 297 -28.568 -35.608 3.447 1.00 55.51 C
ATOM 2167 CE2 TYR A 297 -30.812 -34.776 3.755 1.00 56.09 C
ATOM 2168 CZ TYR A 297 -29.474 -34.552 3.473 1.00 57.03 C
ATOM 2169 OH TYR A 297 -29.043 -33.271 3.221 1.00 58.88 O
ATOM 2170 N ARG A 298 -32.706 -38.568 6.784 1.00 34.70 N
ATOM 2171 CA ARG A 298 -33.604 -37.940 7.756 1.00 36.86 C
ATOM 2172 C ARG A 298 -33.129 -38.163 9.208 1.00 36.39 C
ATOM 2173 O ARG A 298 -33.067 -37.219 9.997 1.00 35.41 O
ATOM 2174 CB ARG A 298 -35.047 -38.434 7.546 1.00 38.47 C
ATOM 2175 CG ARG A 298 -36.083 -37.751 8.426 1.00 43.87 C
ATOM 2176 CD ARG A 298 -37.518 -38.061 8.000 1.00 47.99 C
ATOM 2177 NE ARG A 298 -38.471 -37.576 9.005 1.00 52.28 N
ATOM 2178 CZ ARG A 298 -39.771 -37.882 9.053 1.00 54.02 C
ATOM 2179 NH1 ARG A 298 -40.338 -38.684 8.147 1.00 50.33 N
ATOM 2180 NH2 ARG A 298 -40.516 -37.373 10.023 1.00 54.18 N
ATOM 2181 N LYS A 299 -32.776 -39.405 9.541 1.00 36.08 N
ATOM 2182 CA LYS A 299 -32.303 -39.753 10.890 1.00 37.82 C
ATOM 2183 C LYS A 299 -30.953 -39.111 11.238 1.00 37.03 C
ATOM 2184 O LYS A 299 -30.775 -38.590 12.338 1.00 36.53 O
ATOM 2185 CB LYS A 299 -32.193 -41.274 11.058 1.00 41.73 C
ATOM 2186 CG LYS A 299 -33.518 -42.021 11.127 1.00 45.31 C
ATOM 2187 CD LYS A 299 -33.267 -43.518 11.235 1.00 47.96 C
ATOM 2188 CE LYS A 299 -34.558 -44.298 11.426 1.00 49.72 C
ATOM 2189 NZ LYS A 299 -34.319 -45.766 11.273 1.00 50.02 N
ATOM 2190 N SER A 300 -30.004 -39.149 10.308 1.00 34.99 N
ATOM 2191 CA SER A 300 -28.674 -38.619 10.594 1.00 35.22 C
ATOM 2192 C SER A 300 -28.654 -37.081 10.734 1.00 32.94 C
ATOM 2193 O SER A 300 -27.880 -36.543 11.525 1.00 30.74 O
ATOM 2194 CB SER A 300 -27.664 -39.102 9.550 1.00 36.56 C
ATOM 2195 OG SER A 300 -27.667 -38.249 8.425 1.00 43.78 O
ATOM 2196 N GLY A 301 -29.515 -36.386 9.986 1.00 30.67 N
ATOM 2197 CA GLY A 301 -29.584 -34.922 10.040 1.00 29.65 C
ATOM 2198 C GLY A 301 -30.593 -34.378 11.041 1.00 29.71 C
ATOM 2199 O GLY A 301 -30.842 -33.170 11.089 1.00 27.05 O
ATOM 2200 N THR A 302 -31.181 -35.271 11.837 1.00 29.58 N
ATOM 2201 CA THR A 302 -32.080 -34.871 12.925 1.00 29.80 C
ATOM 2202 C THR A 302 -31.414 -35.185 14.256 1.00 29.89 C
ATOM 2203 O THR A 302 -31.041 -36.324 14.512 1.00 30.82 O
ATOM 2204 CB THR A 302 -33.459 -35.568 12.820 1.00 29.95 C
ATOM 2205 OG1 THR A 302 -34.031 -35.297 11.535 1.00 31.41 O
ATOM 2206 CG2 THR A 302 -34.414 -35.074 13.897 1.00 30.78 C
ATOM 2207 N TYR A 303 -31.249 -34.167 15.094 1.00 29.65 N
ATOM 2208 CA TYR A 303 -30.559 -34.319 16.378 1.00 30.30 C
ATOM 2209 C TYR A 303 -30.818 -33.120 17.277 1.00 30.08 C
ATOM 2210 O TYR A 303 -31.267 -32.059 16.819 1.00 27.77 O
ATOM 2211 CB TYR A 303 -29.042 -34.535 16.188 1.00 30.54 C
ATOM 2212 CG TYR A 303 -28.373 -33.522 15.281 1.00 30.14 C
ATOM 2213 CD1 TYR A 303 -27.860 -32.320 15.792 1.00 29.73 C
ATOM 2214 CD2 TYR A 303 -28.235 -33.769 13.917 1.00 30.31 C
ATOM 2215 CE1 TYR A 303 -27.245 -31.397 14.965 1.00 29.15 C
ATOM 2216 CE2 TYR A 303 -27.628 -32.847 13.081 1.00 30.65 C
ATOM 2217 CZ TYR A 303 -27.134 -31.665 13.610 1.00 31.32 C
ATOM 2218 OH TYR A 303 -26.529 -30.753 12.773 1.00 31.37 O
ATOM 2219 N ARG A 304 -30.542 -33.298 18.565 1.00 28.97 N
ATOM 2220 CA ARG A 304 -30.729 -32.235 19.521 1.00 30.07 C
ATOM 2221 C ARG A 304 -29.552 -32.148 20.466 1.00 29.46 C
ATOM 2222 O ARG A 304 -29.042 -33.170 20.928 1.00 29.46 O
ATOM 2223 CB ARG A 304 -32.033 -32.437 20.315 1.00 30.43 C
ATOM 2224 CG ARG A 304 -33.301 -32.430 19.475 1.00 31.19 C
ATOM 2225 CD ARG A 304 -33.689 -31.018 19.066 1.00 31.91 C
ATOM 2226 NE ARG A 304 -34.880 -30.988 18.219 1.00 32.82 N
ATOM 2227 CZ ARG A 304 -34.869 -31.016 16.887 1.00 33.15 C
ATOM 2228 NH1 ARG A 304 -33.723 -31.082 16.212 1.00 32.08 N
ATOM 2229 NH2 ARG A 304 -36.016 -30.974 16.224 1.00 33.84 N
ATOM 2230 N GLY A 305 -29.133 -30.916 20.743 1.00 29.96 N
ATOM 2231 CA GLY A 305 -28.110 -30.632 21.738 1.00 30.29 C
ATOM 2232 C GLY A 305 -26.734 -31.182 21.416 1.00 31.74 C
ATOM 2233 O GLY A 305 -26.003 -31.558 22.327 1.00 31.94 O
ATOM 2234 N LYS A 306 -26.367 -31.218 20.135 1.00 32.09 N
ATOM 2235 CA LYS A 306 -25.056 -31.752 19.734 1.00 32.38 C
ATOM 2236 C LYS A 306 -23.947 -30.694 19.785 1.00 33.41 C
ATOM 2237 O LYS A 306 -24.028 -29.642 19.127 1.00 31.92 O
ATOM 2238 CB LYS A 306 -25.118 -32.393 18.341 1.00 33.21 C
ATOM 2239 CG LYS A 306 -23.860 -33.171 17.962 1.00 36.31 C
ATOM 2240 CD LYS A 306 -23.704 -33.342 16.456 1.00 37.51 C
ATOM 2241 CE LYS A 306 -24.615 -34.432 15.919 1.00 41.41 C
ATOM 2242 NZ LYS A 306 -24.355 -34.685 14.474 1.00 44.63 N
ATOM 2243 N VAL A 307 -22.904 -30.994 20.556 1.00 33.14 N
ATOM 2244 CA VAL A 307 -21.754 -30.113 20.684 1.00 35.09 C
ATOM 2245 C VAL A 307 -20.895 -30.252 19.428 1.00 34.74 C
ATOM 2246 O VAL A 307 -20.521 -31.357 19.046 1.00 35.18 O
ATOM 2247 CB VAL A 307 -20.919 -30.439 21.945 1.00 35.49 C
ATOM 2248 CG1 VAL A 307 -19.820 -29.398 22.160 1.00 35.65 C
ATOM 2249 CG2 VAL A 307 -21.813 -30.507 23.175 1.00 37.09 C
ATOM 2250 N GLN A 308 -20.608 -29.128 18.783 1.00 34.54 N
ATOM 2251 CA GLN A 308 -19.793 -29.115 17.568 1.00 34.12 C
ATOM 2252 C GLN A 308 -18.751 -27.997 17.626 1.00 34.37 C
ATOM 2253 O GLN A 308 -19.022 -26.926 18.167 1.00 32.07 O
ATOM 2254 CB GLN A 308 -20.680 -28.925 16.328 1.00 34.06 C
ATOM 2255 CG GLN A 308 -21.774 -29.977 16.153 1.00 34.91 C
ATOM 2256 CD GLN A 308 -22.572 -29.820 14.868 1.00 36.21 C
ATOM 2257 OE1 GLN A 308 -23.081 -28.738 14.557 1.00 36.94 O
ATOM 2258 NE2 GLN A 308 -22.705 -30.912 14.119 1.00 36.00 N
ATOM 2259 N ASN A 309 -17.564 -28.253 17.075 1.00 36.03 N
ATOM 2260 CA ASN A 309 -16.595 -27.184 16.823 1.00 37.13 C
ATOM 2261 C ASN A 309 -17.000 -26.331 15.614 1.00 37.53 C
ATOM 2262 O ASN A 309 -18.082 -26.518 15.041 1.00 33.87 O
ATOM 2263 CB ASN A 309 -15.162 -27.732 16.684 1.00 39.02 C
ATOM 2264 CG ASN A 309 -14.958 -28.599 15.445 1.00 41.06 C
ATOM 2265 OD1 ASN A 309 -15.667 -28.482 14.442 1.00 41.83 O
ATOM 2266 ND2 ASN A 309 -13.956 -29.467 15.507 1.00 42.79 N
ATOM 2267 N LEU A 310 -16.130 -25.397 15.234 1.00 39.32 N
ATOM 2268 CA LEU A 310 -16.419 -24.458 14.158 1.00 38.78 C
ATOM 2269 C LEU A 310 -16.617 -25.134 12.806 1.00 38.50 C
ATOM 2270 O LEU A 310 -17.592 -24.852 12.105 1.00 36.71 O
ATOM 2271 CB LEU A 310 -15.319 -23.400 14.062 1.00 41.37 C
ATOM 2272 CG LEU A 310 -15.512 -22.382 12.937 1.00 41.43 C
ATOM 2273 CD1 LEU A 310 -16.488 -21.276 13.333 1.00 41.49 C
ATOM 2274 CD2 LEU A 310 -14.158 -21.826 12.531 1.00 41.85 C
ATOM 2275 N THR A 311 -15.697 -26.023 12.440 1.00 39.15 N
ATOM 2276 CA THR A 311 -15.795 -26.754 11.174 1.00 39.15 C
ATOM 2277 C THR A 311 -17.106 -27.536 11.085 1.00 38.98 C
ATOM 2278 O THR A 311 -17.816 -27.442 10.086 1.00 39.32 O
ATOM 2279 CB THR A 311 -14.598 -27.709 10.975 1.00 40.87 C
ATOM 2280 OG1 THR A 311 -13.378 -26.973 11.104 1.00 39.13 O
ATOM 2281 CG2 THR A 311 -14.643 -28.360 9.596 1.00 41.71 C
ATOM 2282 N GLN A 312 -17.432 -28.282 12.139 1.00 38.00 N
ATOM 2283 CA GLN A 312 -18.626 -29.130 12.152 1.00 38.23 C
ATOM 2284 C GLN A 312 -19.906 -28.330 11.953 1.00 38.12 C
ATOM 2285 O GLN A 312 -20.730 -28.653 11.089 1.00 38.23 O
ATOM 2286 CB GLN A 312 -18.701 -29.926 13.459 1.00 40.09 C
ATOM 2287 CG GLN A 312 -17.695 -31.063 13.532 1.00 42.70 C
ATOM 2288 CD GLN A 312 -17.373 -31.499 14.950 1.00 44.26 C
ATOM 2289 OE1 GLN A 312 -17.385 -30.695 15.884 1.00 43.77 O
ATOM 2290 NE2 GLN A 312 -17.052 -32.781 15.112 1.00 45.25 N
ATOM 2291 N PHE A 313 -20.061 -27.283 12.757 1.00 37.38 N
ATOM 2292 CA PHE A 313 -21.263 -26.472 12.744 1.00 35.09 C
ATOM 2293 C PHE A 313 -21.273 -25.502 11.566 1.00 36.41 C
ATOM 2294 O PHE A 313 -22.301 -25.336 10.913 1.00 36.64 O
ATOM 2295 CB PHE A 313 -21.394 -25.699 14.064 1.00 33.16 C
ATOM 2296 CG PHE A 313 -22.657 -24.878 14.165 1.00 32.98 C
ATOM 2297 CD1 PHE A 313 -23.873 -25.490 14.445 1.00 30.49 C
ATOM 2298 CD2 PHE A 313 -22.633 -23.498 13.954 1.00 31.25 C
ATOM 2299 CE1 PHE A 313 -25.042 -24.746 14.532 1.00 33.17 C
ATOM 2300 CE2 PHE A 313 -23.797 -22.750 14.034 1.00 32.77 C
ATOM 2301 CZ PHE A 313 -25.007 -23.376 14.329 1.00 31.98 C
ATOM 2302 N TYR A 314 -20.129 -24.869 11.299 1.00 36.09 N
ATOM 2303 CA TYR A 314 -20.091 -23.688 10.434 1.00 37.54 C
ATOM 2304 C TYR A 314 -19.526 -23.933 9.038 1.00 39.12 C
ATOM 2305 O TYR A 314 -19.903 -23.259 8.081 1.00 39.42 O
ATOM 2306 CB TYR A 314 -19.323 -22.547 11.111 1.00 36.35 C
ATOM 2307 CG TYR A 314 -19.933 -21.206 10.833 1.00 34.93 C
ATOM 2308 CD1 TYR A 314 -20.788 -20.613 11.756 1.00 35.96 C
ATOM 2309 CD2 TYR A 314 -19.680 -20.537 9.638 1.00 35.37 C
ATOM 2310 CE1 TYR A 314 -21.372 -19.383 11.501 1.00 34.59 C
ATOM 2311 CE2 TYR A 314 -20.261 -19.309 9.375 1.00 35.37 C
ATOM 2312 CZ TYR A 314 -21.106 -18.739 10.313 1.00 33.60 C
ATOM 2313 OH TYR A 314 -21.683 -17.518 10.061 1.00 32.71 O
ATOM 2314 N HIS A 315 -18.625 -24.899 8.920 1.00 41.54 N
ATOM 2315 CA HIS A 315 -18.069 -25.231 7.620 1.00 44.64 C
ATOM 2316 C HIS A 315 -18.320 -26.683 7.262 1.00 46.14 C
ATOM 2317 O HIS A 315 -17.381 -27.396 6.913 1.00 43.30 O
ATOM 2318 CB HIS A 315 -16.579 -24.863 7.581 1.00 44.51 C
ATOM 2319 CG HIS A 315 -16.293 -23.411 7.938 1.00 45.67 C
ATOM 2320 ND1 HIS A 315 -16.609 -22.385 7.121 1.00 45.40 N
ATOM 2321 CD2 HIS A 315 -15.698 -22.842 9.066 1.00 44.02 C
ATOM 2322 CE1 HIS A 315 -16.237 -21.223 7.692 1.00 44.07 C
ATOM 2323 NE2 HIS A 315 -15.680 -21.504 8.881 1.00 44.91 N
ATOM 2324 N PRO A 316 -19.604 -27.136 7.313 1.00 49.87 N
ATOM 2325 CA PRO A 316 -19.885 -28.578 7.186 1.00 53.11 C
ATOM 2326 C PRO A 316 -19.535 -29.160 5.810 1.00 55.81 C
ATOM 2327 O PRO A 316 -19.417 -30.379 5.668 1.00 56.50 O
ATOM 2328 CB PRO A 316 -21.398 -28.668 7.438 1.00 53.23 C
ATOM 2329 CG PRO A 316 -21.930 -27.348 6.999 1.00 53.19 C
ATOM 2330 CD PRO A 316 -20.852 -26.342 7.319 1.00 51.76 C
ATOM 2331 N LEU A 317 -19.364 -28.289 4.818 1.00 57.73 N
ATOM 2332 CA LEU A 317 -19.011 -28.709 3.464 1.00 60.80 C
ATOM 2333 C LEU A 317 -17.496 -28.897 3.260 1.00 61.59 C
ATOM 2334 O LEU A 317 -17.074 -29.386 2.210 1.00 62.66 O
ATOM 2335 CB LEU A 317 -19.598 -27.738 2.426 1.00 62.64 C
ATOM 2336 CG LEU A 317 -21.055 -27.891 1.942 1.00 64.81 C
ATOM 2337 CD1 LEU A 317 -21.160 -28.938 0.841 1.00 65.36 C
ATOM 2338 CD2 LEU A 317 -22.050 -28.198 3.060 1.00 64.82 C
ATOM 2339 N ASP A 318 -16.695 -28.518 4.261 1.00 60.62 N
ATOM 2340 CA ASP A 318 -15.236 -28.723 4.237 1.00 62.36 C
ATOM 2341 C ASP A 318 -14.838 -30.200 4.117 1.00 64.95 C
ATOM 2342 O ASP A 318 -13.844 -30.530 3.465 1.00 64.83 O
ATOM 2343 CB ASP A 318 -14.571 -28.104 5.474 1.00 61.18 C
ATOM 2344 CG ASP A 318 -14.331 -26.603 5.331 1.00 58.35 C
ATOM 2345 OD1 ASP A 318 -14.683 -26.022 4.282 1.00 60.28 O
ATOM 2346 OD2 ASP A 318 -13.782 -26.003 6.275 1.00 56.34 O
ATOM 2347 N MET A 319 -15.624 -31.075 4.746 1.00 66.75 N
ATOM 2348 CA MET A 319 -15.413 -32.529 4.690 1.00 67.26 C
ATOM 2349 C MET A 319 -15.536 -33.097 3.270 1.00 65.23 C
ATOM 2350 O MET A 319 -14.937 -34.127 2.959 1.00 61.59 O
ATOM 2351 CB MET A 319 -16.382 -33.252 5.638 1.00 69.46 C
ATOM 2352 CG MET A 319 -17.853 -33.097 5.263 1.00 73.84 C
ATOM 2353 SD MET A 319 -19.034 -33.795 6.435 1.00 80.24 S
ATOM 2354 CE MET A 319 -18.778 -32.752 7.875 1.00 78.63 C
ATOM 2355 N PHE A 320 -16.309 -32.420 2.418 1.00 64.84 N
ATOM 2356 CA PHE A 320 -16.532 -32.870 1.041 1.00 66.67 C
ATOM 2357 C PHE A 320 -15.341 -32.634 0.101 1.00 67.05 C
ATOM 2358 O PHE A 320 -15.376 -33.042 -1.063 1.00 63.74 O
ATOM 2359 CB PHE A 320 -17.830 -32.280 0.467 1.00 67.87 C
ATOM 2360 CG PHE A 320 -19.082 -32.831 1.106 1.00 69.50 C
ATOM 2361 CD1 PHE A 320 -19.398 -34.188 1.008 1.00 69.47 C
ATOM 2362 CD2 PHE A 320 -19.947 -31.996 1.809 1.00 70.48 C
ATOM 2363 CE1 PHE A 320 -20.549 -34.696 1.599 1.00 68.91 C
ATOM 2364 CE2 PHE A 320 -21.101 -32.499 2.400 1.00 70.96 C
ATOM 2365 CZ PHE A 320 -21.402 -33.850 2.294 1.00 68.43 C
ATOM 2366 N GLY A 321 -14.303 -31.970 0.617 1.00 68.62 N
ATOM 2367 CA GLY A 321 -13.016 -31.804 -0.070 1.00 69.35 C
ATOM 2368 C GLY A 321 -13.086 -31.275 -1.490 1.00 71.35 C
ATOM 2369 O GLY A 321 -13.649 -30.206 -1.737 1.00 72.17 O
ATOM 2370 N GLU A 322 -12.519 -32.045 -2.419 1.00 73.67 N
ATOM 2371 CA GLU A 322 -12.427 -31.665 -3.832 1.00 73.51 C
ATOM 2372 C GLU A 322 -13.754 -31.799 -4.590 1.00 73.07 C
ATOM 2373 O GLU A 322 -13.872 -31.319 -5.722 1.00 73.17 O
ATOM 2374 CB GLU A 322 -11.329 -32.484 -4.534 1.00 77.04 C
ATOM 2375 CG GLU A 322 -11.795 -33.849 -5.064 1.00 80.07 C
ATOM 2376 CD GLU A 322 -10.652 -34.844 -5.233 1.00 80.51 C
ATOM 2377 OE1 GLU A 322 -9.521 -34.564 -4.775 1.00 81.05 O
ATOM 2378 OE2 GLU A 322 -10.895 -35.919 -5.823 1.00 79.91 O
ATOM 2379 N TRP A 323 -14.738 -32.448 -3.964 1.00 70.63 N
ATOM 2380 CA TRP A 323 -16.032 -32.729 -4.601 1.00 71.59 C
ATOM 2381 C TRP A 323 -16.903 -31.526 -4.857 1.00 70.82 C
ATOM 2382 O TRP A 323 -17.665 -31.514 -5.824 1.00 69.68 O
ATOM 2383 CB TRP A 323 -16.825 -33.759 -3.801 1.00 71.34 C
ATOM 2384 CG TRP A 323 -16.255 -35.159 -3.812 1.00 71.68 C
ATOM 2385 CD1 TRP A 323 -15.400 -35.733 -4.754 1.00 71.48 C
ATOM 2386 CD2 TRP A 323 -16.530 -36.232 -2.846 1.00 70.27 C
ATOM 2387 NE1 TRP A 323 -15.119 -37.036 -4.430 1.00 70.96 N
ATOM 2388 CE2 TRP A 323 -15.765 -37.400 -3.302 1.00 70.80 C
ATOM 2389 CE3 TRP A 323 -17.296 -36.336 -1.688 1.00 69.54 C
ATOM 2390 CZ2 TRP A 323 -15.786 -38.604 -2.615 1.00 69.94 C
ATOM 2391 CZ3 TRP A 323 -17.306 -37.556 -1.002 1.00 69.69 C
ATOM 2392 CH2 TRP A 323 -16.567 -38.661 -1.456 1.00 69.35 C
ATOM 2393 N ASN A 324 -16.828 -30.516 -3.993 1.00 71.65 N
ATOM 2394 CA ASN A 324 -17.621 -29.299 -4.190 1.00 72.63 C
ATOM 2395 C ASN A 324 -17.029 -28.372 -5.257 1.00 72.87 C
ATOM 2396 O ASN A 324 -15.818 -28.121 -5.270 1.00 70.87 O
ATOM 2397 CB ASN A 324 -17.887 -28.563 -2.863 1.00 72.69 C
ATOM 2398 CG ASN A 324 -16.658 -28.464 -1.977 1.00 70.25 C
ATOM 2399 OD1 ASN A 324 -15.631 -27.905 -2.369 1.00 72.72 O
ATOM 2400 ND2 ASN A 324 -16.769 -28.980 -0.760 1.00 67.67 N
ATOM 2401 N ARG A 325 -17.897 -27.888 -6.151 1.00 74.14 N
ATOM 2402 CA ARG A 325 -17.505 -27.066 -7.309 1.00 76.15 C
ATOM 2403 C ARG A 325 -16.451 -27.758 -8.185 1.00 77.86 C
ATOM 2404 O ARG A 325 -15.439 -27.161 -8.566 1.00 77.15 O
ATOM 2405 CB ARG A 325 -17.045 -25.668 -6.865 1.00 75.91 C
ATOM 2406 CG ARG A 325 -18.197 -24.719 -6.582 1.00 75.66 C
ATOM 2407 CD ARG A 325 -17.865 -23.719 -5.486 1.00 72.49 C
ATOM 2408 NE ARG A 325 -19.095 -23.207 -4.884 1.00 73.17 N
ATOM 2409 CZ ARG A 325 -19.166 -22.198 -4.019 1.00 71.04 C
ATOM 2410 NH1 ARG A 325 -18.068 -21.559 -3.632 1.00 67.56 N
ATOM 2411 NH2 ARG A 325 -20.351 -21.826 -3.545 1.00 68.16 N
ATOM 2412 N ALA A 326 -16.710 -29.022 -8.505 1.00 79.86 N
ATOM 2413 CA ALA A 326 -15.749 -29.844 -9.231 1.00 86.98 C
ATOM 2414 C ALA A 326 -16.155 -30.089 -10.685 1.00 91.48 C
ATOM 2415 O ALA A 326 -17.272 -29.758 -11.099 1.00 90.13 O
ATOM 2416 CB ALA A 326 -15.546 -31.171 -8.508 1.00 86.40 C
ATOM 2417 N TYR A 327 -15.209 -30.641 -11.449 1.00 94.91 N
ATOM 2418 CA TYR A 327 -15.456 -31.252 -12.764 1.00 96.86 C
ATOM 2419 C TYR A 327 -15.748 -30.284 -13.920 1.00 98.11 C
ATOM 2420 O TYR A 327 -15.704 -30.688 -15.085 1.00 98.54 O
ATOM 2421 CB TYR A 327 -16.566 -32.311 -12.667 1.00 98.76 C
ATOM 2422 CG TYR A 327 -16.158 -33.677 -13.168 1.00100.68 C
ATOM 2423 CD1 TYR A 327 -16.092 -33.954 -14.539 1.00100.33 C
ATOM 2424 CD2 TYR A 327 -15.835 -34.698 -12.268 1.00100.07 C
ATOM 2425 CE1 TYR A 327 -15.714 -35.208 -14.996 1.00 98.41 C
ATOM 2426 CE2 TYR A 327 -15.459 -35.955 -12.715 1.00 99.30 C
ATOM 2427 CZ TYR A 327 -15.400 -36.204 -14.078 1.00 98.92 C
ATOM 2428 OH TYR A 327 -15.026 -37.452 -14.521 1.00 98.21 O
ATOM 2429 N GLY A 328 -16.042 -29.022 -13.604 1.00 96.46 N
ATOM 2430 CA GLY A 328 -16.423 -28.040 -14.620 1.00 90.20 C
ATOM 2431 C GLY A 328 -15.266 -27.195 -15.123 1.00 87.85 C
ATOM 2432 O GLY A 328 -14.767 -26.338 -14.387 1.00 85.04 O
ATOM 2433 N PRO A 329 -14.826 -27.428 -16.381 1.00 85.57 N
ATOM 2434 CA PRO A 329 -13.781 -26.581 -16.971 1.00 83.50 C
ATOM 2435 C PRO A 329 -14.315 -25.197 -17.366 1.00 79.17 C
ATOM 2436 O PRO A 329 -13.559 -24.221 -17.361 1.00 76.84 O
ATOM 2437 CB PRO A 329 -13.338 -27.372 -18.208 1.00 81.43 C
ATOM 2438 CG PRO A 329 -14.527 -28.191 -18.581 1.00 82.20 C
ATOM 2439 CD PRO A 329 -15.256 -28.500 -17.302 1.00 83.50 C
ATOM 2440 N ALA A 330 -15.609 -25.129 -17.688 1.00 74.96 N
ATOM 2441 CA ALA A 330 -16.273 -23.880 -18.066 1.00 70.07 C
ATOM 2442 C ALA A 330 -16.425 -22.921 -16.878 1.00 68.60 C
ATOM 2443 O ALA A 330 -16.514 -21.702 -17.062 1.00 69.17 O
ATOM 2444 CB ALA A 330 -17.628 -24.174 -18.696 1.00 67.20 C
ATOM 2445 N GLY A 331 -16.444 -23.477 -15.666 1.00 62.24 N
ATOM 2446 CA GLY A 331 -16.617 -22.693 -14.451 1.00 53.30 C
ATOM 2447 C GLY A 331 -18.053 -22.743 -13.968 1.00 50.41 C
ATOM 2448 O GLY A 331 -18.878 -23.498 -14.492 1.00 46.03 O
ATOM 2449 N PHE A 332 -18.344 -21.929 -12.958 1.00 47.62 N
ATOM 2450 CA PHE A 332 -19.650 -21.897 -12.318 1.00 45.57 C
ATOM 2451 C PHE A 332 -20.092 -20.447 -12.193 1.00 40.50 C
ATOM 2452 O PHE A 332 -19.269 -19.546 -12.128 1.00 39.42 O
ATOM 2453 CB PHE A 332 -19.585 -22.545 -10.918 1.00 48.21 C
ATOM 2454 CG PHE A 332 -19.570 -24.057 -10.933 1.00 49.52 C
ATOM 2455 CD1 PHE A 332 -20.717 -24.783 -10.618 1.00 49.07 C
ATOM 2456 CD2 PHE A 332 -18.405 -24.761 -11.252 1.00 50.32 C
ATOM 2457 CE1 PHE A 332 -20.708 -26.174 -10.625 1.00 49.65 C
ATOM 2458 CE2 PHE A 332 -18.394 -26.150 -11.271 1.00 49.44 C
ATOM 2459 CZ PHE A 332 -19.546 -26.857 -10.954 1.00 48.72 C
ATOM 2460 N LEU A 333 -21.396 -20.220 -12.162 1.00 38.49 N
ATOM 2461 CA LEU A 333 -21.908 -18.889 -11.873 1.00 35.72 C
ATOM 2462 C LEU A 333 -22.622 -18.937 -10.526 1.00 33.86 C
ATOM 2463 O LEU A 333 -23.636 -19.623 -10.380 1.00 29.21 O
ATOM 2464 CB LEU A 333 -22.845 -18.426 -12.991 1.00 36.18 C
ATOM 2465 CG LEU A 333 -23.224 -16.949 -13.120 1.00 38.72 C
ATOM 2466 CD1 LEU A 333 -23.486 -16.603 -14.579 1.00 38.16 C
ATOM 2467 CD2 LEU A 333 -24.448 -16.621 -12.277 1.00 37.63 C
ATOM 2468 N GLN A 334 -22.071 -18.218 -9.550 1.00 32.48 N
ATOM 2469 CA GLN A 334 -22.679 -18.085 -8.223 1.00 34.07 C
ATOM 2470 C GLN A 334 -23.771 -17.000 -8.248 1.00 33.68 C
ATOM 2471 O GLN A 334 -23.539 -15.874 -8.688 1.00 33.44 O
ATOM 2472 CB GLN A 334 -21.586 -17.811 -7.164 1.00 36.28 C
ATOM 2473 CG GLN A 334 -22.044 -17.233 -5.827 1.00 41.90 C
ATOM 2474 CD GLN A 334 -22.757 -18.230 -4.919 1.00 43.72 C
ATOM 2475 OE1 GLN A 334 -23.537 -17.842 -4.044 1.00 49.30 O
ATOM 2476 NE2 GLN A 334 -22.493 -19.512 -5.120 1.00 43.71 N
ATOM 2477 N TYR A 335 -24.969 -17.363 -7.800 1.00 30.81 N
ATOM 2478 CA TYR A 335 -26.124 -16.474 -7.855 1.00 28.42 C
ATOM 2479 C TYR A 335 -26.801 -16.415 -6.490 1.00 27.77 C
ATOM 2480 O TYR A 335 -27.329 -17.429 -6.022 1.00 28.46 O
ATOM 2481 CB TYR A 335 -27.110 -16.973 -8.924 1.00 27.72 C
ATOM 2482 CG TYR A 335 -28.152 -15.955 -9.324 1.00 28.17 C
ATOM 2483 CD1 TYR A 335 -27.855 -14.951 -10.253 1.00 27.57 C
ATOM 2484 CD2 TYR A 335 -29.436 -15.986 -8.772 1.00 27.34 C
ATOM 2485 CE1 TYR A 335 -28.805 -14.004 -10.610 1.00 27.98 C
ATOM 2486 CE2 TYR A 335 -30.393 -15.040 -9.125 1.00 28.06 C
ATOM 2487 CZ TYR A 335 -30.072 -14.055 -10.038 1.00 27.92 C
ATOM 2488 OH TYR A 335 -31.013 -13.129 -10.389 1.00 28.91 O
ATOM 2489 N GLN A 336 -26.783 -15.238 -5.852 1.00 25.34 N
ATOM 2490 CA GLN A 336 -27.361 -15.076 -4.525 1.00 24.43 C
ATOM 2491 C GLN A 336 -28.385 -13.934 -4.507 1.00 24.48 C
ATOM 2492 O GLN A 336 -28.098 -12.825 -4.941 1.00 22.65 O
ATOM 2493 CB GLN A 336 -26.280 -14.854 -3.453 1.00 24.94 C
ATOM 2494 CG GLN A 336 -26.847 -14.567 -2.062 1.00 23.98 C
ATOM 2495 CD GLN A 336 -25.814 -14.600 -0.946 1.00 23.49 C
ATOM 2496 OE1 GLN A 336 -24.610 -14.720 -1.184 1.00 24.29 O
ATOM 2497 NE2 GLN A 336 -26.289 -14.518 0.288 1.00 21.54 N
ATOM 2498 N PHE A 337 -29.575 -14.222 -3.991 1.00 22.14 N
ATOM 2499 CA PHE A 337 -30.618 -13.221 -3.872 1.00 22.11 C
ATOM 2500 C PHE A 337 -31.386 -13.407 -2.574 1.00 21.38 C
ATOM 2501 O PHE A 337 -31.275 -14.446 -1.920 1.00 21.33 O
ATOM 2502 CB PHE A 337 -31.582 -13.281 -5.070 1.00 21.37 C
ATOM 2503 CG PHE A 337 -32.322 -14.589 -5.189 1.00 22.82 C
ATOM 2504 CD1 PHE A 337 -33.591 -14.747 -4.612 1.00 23.01 C
ATOM 2505 CD2 PHE A 337 -31.752 -15.666 -5.861 1.00 22.30 C
ATOM 2506 CE1 PHE A 337 -34.271 -15.954 -4.716 1.00 23.23 C
ATOM 2507 CE2 PHE A 337 -32.427 -16.873 -5.963 1.00 23.19 C
ATOM 2508 CZ PHE A 337 -33.689 -17.013 -5.396 1.00 23.47 C
ATOM 2509 N VAL A 338 -32.145 -12.380 -2.211 1.00 21.68 N
ATOM 2510 CA VAL A 338 -33.049 -12.430 -1.066 1.00 21.77 C
ATOM 2511 C VAL A 338 -34.420 -11.894 -1.496 1.00 22.77 C
ATOM 2512 O VAL A 338 -34.498 -10.937 -2.274 1.00 22.84 O
ATOM 2513 CB VAL A 338 -32.473 -11.640 0.142 1.00 21.91 C
ATOM 2514 CG1 VAL A 338 -32.106 -10.211 -0.257 1.00 20.74 C
ATOM 2515 CG2 VAL A 338 -33.437 -11.629 1.327 1.00 20.62 C
ATOM 2516 N ILE A 339 -35.495 -12.511 -0.994 1.00 22.80 N
ATOM 2517 CA ILE A 339 -36.859 -12.064 -1.254 1.00 22.74 C
ATOM 2518 C ILE A 339 -37.542 -11.698 0.081 1.00 23.90 C
ATOM 2519 O ILE A 339 -37.457 -12.459 1.044 1.00 23.75 O
ATOM 2520 CB ILE A 339 -37.678 -13.171 -1.980 1.00 23.63 C
ATOM 2521 CG1 ILE A 339 -36.992 -13.649 -3.282 1.00 23.71 C
ATOM 2522 CG2 ILE A 339 -39.121 -12.741 -2.233 1.00 23.87 C
ATOM 2523 CD1 ILE A 339 -36.930 -12.632 -4.413 1.00 23.72 C
ATOM 2524 N PRO A 340 -38.222 -10.536 0.141 1.00 23.57 N
ATOM 2525 CA PRO A 340 -38.847 -10.084 1.387 1.00 24.63 C
ATOM 2526 C PRO A 340 -39.711 -11.184 2.009 1.00 25.30 C
ATOM 2527 O PRO A 340 -40.411 -11.899 1.289 1.00 25.39 O
ATOM 2528 CB PRO A 340 -39.750 -8.919 0.950 1.00 24.93 C
ATOM 2529 CG PRO A 340 -39.260 -8.491 -0.383 1.00 25.50 C
ATOM 2530 CD PRO A 340 -38.412 -9.586 -0.975 1.00 24.12 C
ATOM 2531 N THR A 341 -39.662 -11.283 3.335 1.00 25.84 N
ATOM 2532 CA THR A 341 -40.336 -12.339 4.103 1.00 26.40 C
ATOM 2533 C THR A 341 -41.759 -12.600 3.640 1.00 27.20 C
ATOM 2534 O THR A 341 -42.132 -13.754 3.387 1.00 26.16 O
ATOM 2535 CB THR A 341 -40.328 -12.005 5.608 1.00 26.83 C
ATOM 2536 OG1 THR A 341 -39.000 -11.648 5.991 1.00 28.01 O
ATOM 2537 CG2 THR A 341 -40.779 -13.203 6.463 1.00 27.38 C
ATOM 2538 N GLU A 342 -42.533 -11.520 3.496 1.00 28.34 N
ATOM 2539 CA GLU A 342 -43.972 -11.594 3.191 1.00 28.31 C
ATOM 2540 C GLU A 342 -44.270 -12.201 1.822 1.00 28.42 C
ATOM 2541 O GLU A 342 -45.343 -12.753 1.608 1.00 29.11 O
ATOM 2542 CB GLU A 342 -44.641 -10.210 3.325 1.00 28.08 C
ATOM 2543 CG GLU A 342 -44.155 -9.156 2.336 1.00 29.65 C
ATOM 2544 CD GLU A 342 -42.969 -8.345 2.851 1.00 30.64 C
ATOM 2545 OE1 GLU A 342 -42.244 -8.828 3.749 1.00 30.95 O
ATOM 2546 OE2 GLU A 342 -42.767 -7.214 2.358 1.00 30.00 O
ATOM 2547 N ALA A 343 -43.308 -12.122 0.907 1.00 27.30 N
ATOM 2548 CA ALA A 343 -43.503 -12.615 -0.454 1.00 26.58 C
ATOM 2549 C ALA A 343 -43.200 -14.107 -0.571 1.00 27.60 C
ATOM 2550 O ALA A 343 -42.361 -14.542 -1.378 1.00 25.49 O
ATOM 2551 CB ALA A 343 -42.663 -11.808 -1.434 1.00 24.64 C
ATOM 2552 N VAL A 344 -43.920 -14.901 0.212 1.00 29.54 N
ATOM 2553 CA VAL A 344 -43.622 -16.324 0.320 1.00 31.21 C
ATOM 2554 C VAL A 344 -44.014 -17.123 -0.931 1.00 30.49 C
ATOM 2555 O VAL A 344 -43.238 -17.972 -1.381 1.00 31.55 O
ATOM 2556 CB VAL A 344 -44.145 -16.937 1.663 1.00 32.17 C
ATOM 2557 CG1 VAL A 344 -45.664 -16.938 1.734 1.00 33.20 C
ATOM 2558 CG2 VAL A 344 -43.583 -18.337 1.872 1.00 33.75 C
ATOM 2559 N ASP A 345 -45.185 -16.844 -1.503 1.00 30.69 N
ATOM 2560 CA ASP A 345 -45.607 -17.502 -2.747 1.00 31.56 C
ATOM 2561 C ASP A 345 -44.691 -17.144 -3.900 1.00 29.95 C
ATOM 2562 O ASP A 345 -44.364 -17.989 -4.739 1.00 28.49 O
ATOM 2563 CB ASP A 345 -47.037 -17.105 -3.120 1.00 34.69 C
ATOM 2564 CG ASP A 345 -48.047 -17.529 -2.077 1.00 37.16 C
ATOM 2565 OD1 ASP A 345 -47.890 -18.632 -1.514 1.00 37.78 O
ATOM 2566 OD2 ASP A 345 -48.990 -16.750 -1.818 1.00 40.34 O
ATOM 2567 N GLU A 346 -44.296 -15.877 -3.939 1.00 28.29 N
ATOM 2568 CA GLU A 346 -43.352 -15.386 -4.930 1.00 28.98 C
ATOM 2569 C GLU A 346 -42.013 -16.128 -4.786 1.00 27.32 C
ATOM 2570 O GLU A 346 -41.410 -16.556 -5.779 1.00 27.37 O
ATOM 2571 CB GLU A 346 -43.162 -13.868 -4.759 1.00 29.07 C
ATOM 2572 CG GLU A 346 -44.393 -13.013 -5.071 1.00 31.16 C
ATOM 2573 CD GLU A 346 -45.448 -12.984 -3.965 1.00 31.78 C
ATOM 2574 OE1 GLU A 346 -45.250 -13.584 -2.891 1.00 31.14 O
ATOM 2575 OE2 GLU A 346 -46.501 -12.347 -4.172 1.00 34.48 O
ATOM 2576 N PHE A 347 -41.555 -16.279 -3.545 1.00 27.62 N
ATOM 2577 CA PHE A 347 -40.317 -17.003 -3.265 1.00 28.63 C
ATOM 2578 C PHE A 347 -40.402 -18.451 -3.775 1.00 28.00 C
ATOM 2579 O PHE A 347 -39.472 -18.949 -4.400 1.00 24.66 O
ATOM 2580 CB PHE A 347 -39.986 -16.971 -1.764 1.00 28.46 C
ATOM 2581 CG PHE A 347 -38.817 -17.844 -1.383 1.00 30.01 C
ATOM 2582 CD1 PHE A 347 -37.551 -17.602 -1.904 1.00 29.73 C
ATOM 2583 CD2 PHE A 347 -38.978 -18.901 -0.486 1.00 30.21 C
ATOM 2584 CE1 PHE A 347 -36.479 -18.405 -1.554 1.00 29.86 C
ATOM 2585 CE2 PHE A 347 -37.903 -19.702 -0.129 1.00 29.89 C
ATOM 2586 CZ PHE A 347 -36.652 -19.457 -0.670 1.00 30.34 C
ATOM 2587 N LYS A 348 -41.534 -19.104 -3.513 1.00 28.09 N
ATOM 2588 CA LYS A 348 -41.760 -20.481 -3.973 1.00 29.87 C
ATOM 2589 C LYS A 348 -41.771 -20.564 -5.488 1.00 28.98 C
ATOM 2590 O LYS A 348 -41.206 -21.498 -6.068 1.00 28.91 O
ATOM 2591 CB LYS A 348 -43.066 -21.033 -3.381 1.00 31.14 C
ATOM 2592 CG LYS A 348 -42.931 -21.327 -1.894 1.00 33.18 C
ATOM 2593 CD LYS A 348 -44.238 -21.157 -1.136 1.00 36.27 C
ATOM 2594 CE LYS A 348 -45.162 -22.335 -1.328 1.00 36.44 C
ATOM 2595 NZ LYS A 348 -45.954 -22.486 -0.077 1.00 41.22 N
ATOM 2596 N LYS A 349 -42.379 -19.564 -6.123 1.00 28.41 N
ATOM 2597 CA LYS A 349 -42.393 -19.475 -7.584 1.00 29.99 C
ATOM 2598 C LYS A 349 -40.964 -19.432 -8.150 1.00 28.91 C
ATOM 2599 O LYS A 349 -40.641 -20.164 -9.084 1.00 27.60 O
ATOM 2600 CB LYS A 349 -43.230 -18.271 -8.042 1.00 31.63 C
ATOM 2601 CG LYS A 349 -43.356 -18.072 -9.549 1.00 35.30 C
ATOM 2602 CD LYS A 349 -43.948 -19.294 -10.250 1.00 38.17 C
ATOM 2603 CE LYS A 349 -43.969 -19.132 -11.768 1.00 40.80 C
ATOM 2604 NZ LYS A 349 -44.999 -18.139 -12.207 1.00 41.33 N
ATOM 2605 N ILE A 350 -40.102 -18.601 -7.569 1.00 28.95 N
ATOM 2606 CA ILE A 350 -38.731 -18.502 -8.063 1.00 28.93 C
ATOM 2607 C ILE A 350 -37.946 -19.823 -7.901 1.00 27.16 C
ATOM 2608 O ILE A 350 -37.183 -20.196 -8.782 1.00 26.72 O
ATOM 2609 CB ILE A 350 -37.982 -17.275 -7.489 1.00 31.21 C
ATOM 2610 CG1 ILE A 350 -36.594 -17.148 -8.114 1.00 32.30 C
ATOM 2611 CG2 ILE A 350 -37.846 -17.345 -5.977 1.00 31.99 C
ATOM 2612 CD1 ILE A 350 -36.077 -15.726 -8.124 1.00 37.59 C
ATOM 2613 N ILE A 351 -38.153 -20.535 -6.795 1.00 26.34 N
ATOM 2614 CA ILE A 351 -37.508 -21.844 -6.617 1.00 25.15 C
ATOM 2615 C ILE A 351 -37.990 -22.831 -7.691 1.00 24.90 C
ATOM 2616 O ILE A 351 -37.176 -23.548 -8.285 1.00 26.98 O
ATOM 2617 CB ILE A 351 -37.683 -22.412 -5.185 1.00 23.82 C
ATOM 2618 CG1 ILE A 351 -37.155 -21.434 -4.117 1.00 23.83 C
ATOM 2619 CG2 ILE A 351 -37.024 -23.792 -5.032 1.00 22.44 C
ATOM 2620 CD1 ILE A 351 -35.668 -21.114 -4.214 1.00 23.55 C
ATOM 2621 N GLY A 352 -39.299 -22.840 -7.955 1.00 24.44 N
ATOM 2622 CA GLY A 352 -39.889 -23.618 -9.060 1.00 25.71 C
ATOM 2623 C GLY A 352 -39.266 -23.304 -10.423 1.00 27.27 C
ATOM 2624 O GLY A 352 -38.920 -24.218 -11.194 1.00 27.96 O
ATOM 2625 N VAL A 353 -39.100 -22.016 -10.710 1.00 26.66 N
ATOM 2626 CA VAL A 353 -38.486 -21.579 -11.967 1.00 28.08 C
ATOM 2627 C VAL A 353 -37.071 -22.156 -12.130 1.00 27.22 C
ATOM 2628 O VAL A 353 -36.747 -22.712 -13.168 1.00 28.77 O
ATOM 2629 CB VAL A 353 -38.488 -20.040 -12.078 1.00 29.08 C
ATOM 2630 CG1 VAL A 353 -37.601 -19.574 -13.224 1.00 28.59 C
ATOM 2631 CG2 VAL A 353 -39.923 -19.525 -12.244 1.00 28.67 C
ATOM 2632 N ILE A 354 -36.257 -22.051 -11.081 1.00 27.71 N
ATOM 2633 CA ILE A 354 -34.898 -22.595 -11.060 1.00 27.39 C
ATOM 2634 C ILE A 354 -34.874 -24.100 -11.350 1.00 27.68 C
ATOM 2635 O ILE A 354 -34.073 -24.585 -12.159 1.00 28.34 O
ATOM 2636 CB ILE A 354 -34.187 -22.273 -9.712 1.00 26.87 C
ATOM 2637 CG1 ILE A 354 -33.887 -20.762 -9.639 1.00 25.86 C
ATOM 2638 CG2 ILE A 354 -32.911 -23.106 -9.558 1.00 25.84 C
ATOM 2639 CD1 ILE A 354 -33.515 -20.249 -8.262 1.00 25.85 C
ATOM 2640 N GLN A 355 -35.766 -24.824 -10.691 1.00 27.38 N
ATOM 2641 CA GLN A 355 -35.860 -26.264 -10.830 1.00 27.88 C
ATOM 2642 C GLN A 355 -36.278 -26.677 -12.241 1.00 28.07 C
ATOM 2643 O GLN A 355 -35.801 -27.688 -12.741 1.00 28.99 O
ATOM 2644 CB GLN A 355 -36.839 -26.836 -9.791 1.00 28.16 C
ATOM 2645 CG GLN A 355 -36.800 -28.360 -9.654 1.00 30.10 C
ATOM 2646 CD GLN A 355 -37.523 -29.083 -10.785 1.00 31.72 C
ATOM 2647 OE1 GLN A 355 -38.469 -28.556 -11.375 1.00 32.06 O
ATOM 2648 NE2 GLN A 355 -37.068 -30.288 -11.099 1.00 30.90 N
ATOM 2649 N ALA A 356 -37.165 -25.908 -12.867 1.00 27.60 N
ATOM 2650 CA ALA A 356 -37.669 -26.238 -14.201 1.00 29.02 C
ATOM 2651 C ALA A 356 -36.765 -25.712 -15.316 1.00 30.82 C
ATOM 2652 O ALA A 356 -37.038 -25.950 -16.492 1.00 32.97 O
ATOM 2653 CB ALA A 356 -39.097 -25.714 -14.387 1.00 28.55 C
ATOM 2654 N SER A 357 -35.697 -25.008 -14.947 1.00 30.25 N
ATOM 2655 CA SER A 357 -34.878 -24.275 -15.923 1.00 31.55 C
ATOM 2656 C SER A 357 -33.970 -25.161 -16.770 1.00 33.29 C
ATOM 2657 O SER A 357 -33.587 -24.778 -17.880 1.00 34.99 O
ATOM 2658 CB SER A 357 -34.015 -23.236 -15.212 1.00 28.93 C
ATOM 2659 OG SER A 357 -32.976 -23.847 -14.456 1.00 28.27 O
ATOM 2660 N GLY A 358 -33.599 -26.321 -16.240 1.00 33.03 N
ATOM 2661 CA GLY A 358 -32.621 -27.183 -16.910 1.00 33.87 C
ATOM 2662 C GLY A 358 -31.182 -26.842 -16.544 1.00 35.50 C
ATOM 2663 O GLY A 358 -30.241 -27.393 -17.119 1.00 36.25 O
ATOM 2664 N HIS A 359 -31.016 -25.917 -15.600 1.00 33.88 N
ATOM 2665 CA HIS A 359 -29.725 -25.623 -14.998 1.00 33.61 C
ATOM 2666 C HIS A 359 -29.703 -26.215 -13.614 1.00 34.39 C
ATOM 2667 O HIS A 359 -30.633 -26.004 -12.823 1.00 32.08 O
ATOM 2668 CB HIS A 359 -29.473 -24.118 -14.978 1.00 33.23 C
ATOM 2669 CG HIS A 359 -29.383 -23.511 -16.357 1.00 32.94 C
ATOM 2670 ND1 HIS A 359 -28.267 -23.593 -17.112 1.00 32.25 N
ATOM 2671 CD2 HIS A 359 -30.328 -22.837 -17.120 1.00 31.85 C
ATOM 2672 CE1 HIS A 359 -28.489 -22.992 -18.292 1.00 32.08 C
ATOM 2673 NE2 HIS A 359 -29.752 -22.531 -18.293 1.00 33.21 N
ATOM 2674 N TYR A 360 -28.651 -26.973 -13.314 1.00 33.58 N
ATOM 2675 CA TYR A 360 -28.625 -27.792 -12.098 1.00 36.24 C
ATOM 2676 C TYR A 360 -27.639 -27.304 -11.054 1.00 34.42 C
ATOM 2677 O TYR A 360 -26.425 -27.271 -11.292 1.00 33.49 O
ATOM 2678 CB TYR A 360 -28.351 -29.264 -12.437 1.00 39.12 C
ATOM 2679 CG TYR A 360 -29.214 -29.772 -13.567 1.00 41.30 C
ATOM 2680 CD1 TYR A 360 -30.608 -29.788 -13.451 1.00 41.83 C
ATOM 2681 CD2 TYR A 360 -28.640 -30.221 -14.757 1.00 41.66 C
ATOM 2682 CE1 TYR A 360 -31.404 -30.246 -14.489 1.00 43.60 C
ATOM 2683 CE2 TYR A 360 -29.427 -30.680 -15.801 1.00 43.06 C
ATOM 2684 CZ TYR A 360 -30.804 -30.694 -15.661 1.00 43.44 C
ATOM 2685 OH TYR A 360 -31.587 -31.143 -16.696 1.00 44.63 O
ATOM 2686 N SER A 361 -28.168 -26.914 -9.899 1.00 30.81 N
ATOM 2687 CA SER A 361 -27.315 -26.503 -8.790 1.00 31.34 C
ATOM 2688 C SER A 361 -27.342 -27.501 -7.641 1.00 31.74 C
ATOM 2689 O SER A 361 -28.409 -27.825 -7.108 1.00 28.53 O
ATOM 2690 CB SER A 361 -27.694 -25.110 -8.280 1.00 30.71 C
ATOM 2691 OG SER A 361 -26.829 -24.726 -7.219 1.00 29.78 O
ATOM 2692 N PHE A 362 -26.156 -27.975 -7.263 1.00 34.50 N
ATOM 2693 CA PHE A 362 -25.999 -28.896 -6.133 1.00 38.37 C
ATOM 2694 C PHE A 362 -25.699 -28.202 -4.795 1.00 36.77 C
ATOM 2695 O PHE A 362 -25.994 -28.742 -3.735 1.00 39.47 O
ATOM 2696 CB PHE A 362 -24.916 -29.941 -6.442 1.00 41.02 C
ATOM 2697 CG PHE A 362 -25.363 -31.012 -7.401 1.00 45.77 C
ATOM 2698 CD1 PHE A 362 -26.161 -32.075 -6.963 1.00 47.33 C
ATOM 2699 CD2 PHE A 362 -24.990 -30.967 -8.744 1.00 47.06 C
ATOM 2700 CE1 PHE A 362 -26.574 -33.068 -7.850 1.00 49.49 C
ATOM 2701 CE2 PHE A 362 -25.403 -31.957 -9.633 1.00 49.30 C
ATOM 2702 CZ PHE A 362 -26.196 -33.007 -9.188 1.00 48.34 C
ATOM 2703 N LEU A 363 -25.111 -27.014 -4.850 1.00 34.95 N
ATOM 2704 CA LEU A 363 -24.671 -26.316 -3.648 1.00 36.45 C
ATOM 2705 C LEU A 363 -25.616 -25.167 -3.325 1.00 34.50 C
ATOM 2706 O LEU A 363 -25.482 -24.074 -3.869 1.00 36.04 O
ATOM 2707 CB LEU A 363 -23.235 -25.805 -3.814 1.00 38.10 C
ATOM 2708 CG LEU A 363 -22.097 -26.815 -4.002 1.00 41.57 C
ATOM 2709 CD1 LEU A 363 -20.764 -26.100 -3.827 1.00 43.41 C
ATOM 2710 CD2 LEU A 363 -22.178 -27.997 -3.044 1.00 41.23 C
ATOM 2711 N ASN A 364 -26.579 -25.424 -2.446 1.00 32.83 N
ATOM 2712 CA ASN A 364 -27.668 -24.479 -2.222 1.00 32.27 C
ATOM 2713 C ASN A 364 -27.815 -24.020 -0.760 1.00 32.86 C
ATOM 2714 O ASN A 364 -28.103 -24.817 0.142 1.00 32.47 O
ATOM 2715 CB ASN A 364 -28.981 -25.054 -2.746 1.00 32.63 C
ATOM 2716 CG ASN A 364 -28.861 -25.596 -4.162 1.00 32.67 C
ATOM 2717 OD1 ASN A 364 -29.050 -26.785 -4.392 1.00 33.09 O
ATOM 2718 ND2 ASN A 364 -28.529 -24.730 -5.113 1.00 31.97 N
ATOM 2719 N VAL A 365 -27.607 -22.729 -0.547 1.00 29.96 N
ATOM 2720 CA VAL A 365 -27.719 -22.130 0.771 1.00 29.41 C
ATOM 2721 C VAL A 365 -29.109 -21.523 0.922 1.00 28.80 C
ATOM 2722 O VAL A 365 -29.638 -20.887 -0.003 1.00 29.60 O
ATOM 2723 CB VAL A 365 -26.627 -21.071 0.997 1.00 30.80 C
ATOM 2724 CG1 VAL A 365 -26.982 -20.138 2.156 1.00 31.78 C
ATOM 2725 CG2 VAL A 365 -25.289 -21.751 1.241 1.00 31.06 C
ATOM 2726 N PHE A 366 -29.709 -21.768 2.077 1.00 26.67 N
ATOM 2727 CA PHE A 366 -31.008 -21.219 2.415 1.00 24.75 C
ATOM 2728 C PHE A 366 -30.872 -20.619 3.813 1.00 25.34 C
ATOM 2729 O PHE A 366 -30.373 -21.271 4.740 1.00 24.89 O
ATOM 2730 CB PHE A 366 -32.059 -22.338 2.367 1.00 25.69 C
ATOM 2731 CG PHE A 366 -33.458 -21.911 2.730 1.00 26.62 C
ATOM 2732 CD1 PHE A 366 -34.479 -21.959 1.780 1.00 29.91 C
ATOM 2733 CD2 PHE A 366 -33.774 -21.523 4.020 1.00 27.05 C
ATOM 2734 CE1 PHE A 366 -35.782 -21.592 2.114 1.00 30.89 C
ATOM 2735 CE2 PHE A 366 -35.061 -21.144 4.359 1.00 27.67 C
ATOM 2736 CZ PHE A 366 -36.066 -21.177 3.408 1.00 29.63 C
ATOM 2737 N LYS A 367 -31.298 -19.369 3.966 1.00 24.70 N
ATOM 2738 CA LYS A 367 -31.327 -18.747 5.279 1.00 23.83 C
ATOM 2739 C LYS A 367 -32.422 -17.680 5.354 1.00 23.45 C
ATOM 2740 O LYS A 367 -32.696 -16.993 4.375 1.00 22.82 O
ATOM 2741 CB LYS A 367 -29.942 -18.213 5.677 1.00 25.34 C
ATOM 2742 CG LYS A 367 -29.965 -16.899 6.434 1.00 26.85 C
ATOM 2743 CD LYS A 367 -28.917 -16.812 7.512 1.00 27.18 C
ATOM 2744 CE LYS A 367 -29.514 -16.117 8.729 1.00 26.46 C
ATOM 2745 NZ LYS A 367 -30.123 -17.123 9.634 1.00 24.01 N
ATOM 2746 N LEU A 368 -33.084 -17.584 6.507 1.00 22.67 N
ATOM 2747 CA LEU A 368 -34.016 -16.479 6.742 1.00 21.64 C
ATOM 2748 C LEU A 368 -33.292 -15.290 7.387 1.00 20.29 C
ATOM 2749 O LEU A 368 -32.854 -15.364 8.535 1.00 20.97 O
ATOM 2750 CB LEU A 368 -35.215 -16.929 7.595 1.00 21.41 C
ATOM 2751 CG LEU A 368 -36.286 -15.876 7.930 1.00 21.41 C
ATOM 2752 CD1 LEU A 368 -36.890 -15.273 6.665 1.00 22.00 C
ATOM 2753 CD2 LEU A 368 -37.389 -16.484 8.801 1.00 21.82 C
ATOM 2754 N PHE A 369 -33.135 -14.202 6.630 1.00 21.53 N
ATOM 2755 CA PHE A 369 -32.509 -12.978 7.147 1.00 21.49 C
ATOM 2756 C PHE A 369 -33.403 -12.270 8.176 1.00 22.80 C
ATOM 2757 O PHE A 369 -34.635 -12.349 8.087 1.00 22.53 O
ATOM 2758 CB PHE A 369 -32.259 -11.998 6.006 1.00 22.32 C
ATOM 2759 CG PHE A 369 -30.993 -12.248 5.225 1.00 21.98 C
ATOM 2760 CD1 PHE A 369 -29.954 -13.007 5.746 1.00 21.90 C
ATOM 2761 CD2 PHE A 369 -30.830 -11.669 3.966 1.00 22.62 C
ATOM 2762 CE1 PHE A 369 -28.787 -13.213 5.023 1.00 22.59 C
ATOM 2763 CE2 PHE A 369 -29.668 -11.866 3.241 1.00 22.36 C
ATOM 2764 CZ PHE A 369 -28.637 -12.626 3.773 1.00 22.32 C
ATOM 2765 N GLY A 370 -32.788 -11.572 9.132 1.00 22.92 N
ATOM 2766 CA GLY A 370 -33.539 -10.694 10.033 1.00 23.96 C
ATOM 2767 C GLY A 370 -33.557 -9.231 9.575 1.00 24.16 C
ATOM 2768 O GLY A 370 -33.297 -8.949 8.410 1.00 23.42 O
ATOM 2769 N PRO A 371 -33.869 -8.292 10.500 1.00 24.55 N
ATOM 2770 CA PRO A 371 -33.894 -6.839 10.251 1.00 24.46 C
ATOM 2771 C PRO A 371 -32.661 -6.286 9.498 1.00 24.42 C
ATOM 2772 O PRO A 371 -31.536 -6.723 9.745 1.00 25.39 O
ATOM 2773 CB PRO A 371 -33.991 -6.249 11.673 1.00 25.10 C
ATOM 2774 CG PRO A 371 -34.777 -7.291 12.432 1.00 24.53 C
ATOM 2775 CD PRO A 371 -34.288 -8.618 11.884 1.00 24.08 C
ATOM 2776 N ARG A 372 -32.894 -5.338 8.586 1.00 23.59 N
ATOM 2777 CA ARG A 372 -31.828 -4.716 7.795 1.00 25.10 C
ATOM 2778 C ARG A 372 -31.141 -3.599 8.585 1.00 25.19 C
ATOM 2779 O ARG A 372 -31.582 -3.245 9.676 1.00 23.33 O
ATOM 2780 CB ARG A 372 -32.378 -4.194 6.453 1.00 24.92 C
ATOM 2781 CG ARG A 372 -33.436 -3.077 6.567 1.00 25.13 C
ATOM 2782 CD ARG A 372 -33.548 -2.302 5.250 1.00 25.64 C
ATOM 2783 NE ARG A 372 -32.275 -1.648 4.940 1.00 25.96 N
ATOM 2784 CZ ARG A 372 -31.753 -1.472 3.728 1.00 26.57 C
ATOM 2785 NH1 ARG A 372 -32.380 -1.879 2.628 1.00 25.37 N
ATOM 2786 NH2 ARG A 372 -30.577 -0.867 3.626 1.00 27.62 N
ATOM 2787 N ASN A 373 -30.039 -3.061 8.059 1.00 24.51 N
ATOM 2788 CA ASN A 373 -29.433 -1.900 8.702 1.00 23.49 C
ATOM 2789 C ASN A 373 -29.608 -0.619 7.884 1.00 23.53 C
ATOM 2790 O ASN A 373 -30.262 -0.605 6.835 1.00 22.12 O
ATOM 2791 CB ASN A 373 -27.967 -2.150 9.101 1.00 23.59 C
ATOM 2792 CG ASN A 373 -27.035 -2.280 7.895 1.00 22.27 C
ATOM 2793 OD1 ASN A 373 -27.296 -1.730 6.824 1.00 23.84 O
ATOM 2794 ND2 ASN A 373 -25.959 -3.024 8.065 1.00 24.02 N
ATOM 2795 N GLN A 374 -29.045 0.472 8.379 1.00 24.56 N
ATOM 2796 CA GLN A 374 -29.317 1.760 7.755 1.00 26.62 C
ATOM 2797 C GLN A 374 -28.385 2.063 6.564 1.00 25.06 C
ATOM 2798 O GLN A 374 -28.432 3.155 5.993 1.00 24.97 O
ATOM 2799 CB GLN A 374 -29.304 2.881 8.807 1.00 28.76 C
ATOM 2800 CG GLN A 374 -27.913 3.199 9.317 1.00 33.23 C
ATOM 2801 CD GLN A 374 -27.925 3.946 10.633 1.00 37.47 C
ATOM 2802 OE1 GLN A 374 -28.062 3.345 11.702 1.00 37.32 O
ATOM 2803 NE2 GLN A 374 -27.737 5.266 10.563 1.00 37.75 N
ATOM 2804 N ALA A 375 -27.556 1.101 6.164 1.00 23.92 N
ATOM 2805 CA ALA A 375 -26.665 1.329 5.006 1.00 22.43 C
ATOM 2806 C ALA A 375 -27.440 1.240 3.687 1.00 21.80 C
ATOM 2807 O ALA A 375 -28.026 0.194 3.384 1.00 22.08 O
ATOM 2808 CB ALA A 375 -25.506 0.342 5.014 1.00 22.39 C
ATOM 2809 N PRO A 376 -27.434 2.321 2.876 1.00 20.82 N
ATOM 2810 CA PRO A 376 -28.313 2.308 1.698 1.00 21.07 C
ATOM 2811 C PRO A 376 -28.022 1.242 0.647 1.00 21.02 C
ATOM 2812 O PRO A 376 -28.952 0.823 -0.025 1.00 21.07 O
ATOM 2813 CB PRO A 376 -28.175 3.717 1.117 1.00 21.30 C
ATOM 2814 CG PRO A 376 -26.972 4.311 1.759 1.00 20.64 C
ATOM 2815 CD PRO A 376 -26.775 3.623 3.068 1.00 21.02 C
ATOM 2816 N LEU A 377 -26.755 0.835 0.495 1.00 21.14 N
ATOM 2817 CA LEU A 377 -26.382 -0.249 -0.418 1.00 22.32 C
ATOM 2818 C LEU A 377 -26.198 -1.628 0.257 1.00 21.48 C
ATOM 2819 O LEU A 377 -25.757 -2.557 -0.398 1.00 22.26 O
ATOM 2820 CB LEU A 377 -25.108 0.090 -1.228 1.00 23.26 C
ATOM 2821 CG LEU A 377 -25.116 0.879 -2.544 1.00 25.34 C
ATOM 2822 CD1 LEU A 377 -23.902 0.498 -3.402 1.00 27.23 C
ATOM 2823 CD2 LEU A 377 -26.398 0.706 -3.343 1.00 24.20 C
ATOM 2824 N SER A 378 -26.499 -1.749 1.551 1.00 21.15 N
ATOM 2825 CA SER A 378 -26.486 -3.052 2.262 1.00 21.54 C
ATOM 2826 C SER A 378 -27.353 -4.063 1.498 1.00 20.21 C
ATOM 2827 O SER A 378 -28.451 -3.734 1.077 1.00 20.70 O
ATOM 2828 CB SER A 378 -27.038 -2.876 3.685 1.00 21.87 C
ATOM 2829 OG SER A 378 -26.920 -4.060 4.471 1.00 24.04 O
ATOM 2830 N PHE A 379 -26.850 -5.275 1.291 1.00 18.79 N
ATOM 2831 CA PHE A 379 -27.621 -6.315 0.630 1.00 18.41 C
ATOM 2832 C PHE A 379 -28.763 -6.898 1.501 1.00 18.33 C
ATOM 2833 O PHE A 379 -29.884 -7.001 1.014 1.00 17.09 O
ATOM 2834 CB PHE A 379 -26.690 -7.409 0.072 1.00 19.06 C
ATOM 2835 CG PHE A 379 -27.379 -8.722 -0.235 1.00 19.83 C
ATOM 2836 CD1 PHE A 379 -28.209 -8.857 -1.352 1.00 19.19 C
ATOM 2837 CD2 PHE A 379 -27.159 -9.839 0.577 1.00 19.32 C
ATOM 2838 CE1 PHE A 379 -28.826 -10.067 -1.633 1.00 20.07 C
ATOM 2839 CE2 PHE A 379 -27.759 -11.056 0.289 1.00 19.28 C
ATOM 2840 CZ PHE A 379 -28.608 -11.168 -0.811 1.00 19.27 C
ATOM 2841 N PRO A 380 -28.486 -7.266 2.771 1.00 18.23 N
ATOM 2842 CA PRO A 380 -29.540 -8.020 3.465 1.00 19.38 C
ATOM 2843 C PRO A 380 -30.782 -7.197 3.789 1.00 19.70 C
ATOM 2844 O PRO A 380 -30.687 -6.031 4.188 1.00 18.99 O
ATOM 2845 CB PRO A 380 -28.869 -8.455 4.767 1.00 18.99 C
ATOM 2846 CG PRO A 380 -27.406 -8.479 4.451 1.00 19.77 C
ATOM 2847 CD PRO A 380 -27.209 -7.315 3.517 1.00 18.88 C
ATOM 2848 N ILE A 381 -31.932 -7.818 3.571 1.00 21.34 N
ATOM 2849 CA ILE A 381 -33.221 -7.298 4.018 1.00 20.76 C
ATOM 2850 C ILE A 381 -33.917 -8.514 4.630 1.00 21.19 C
ATOM 2851 O ILE A 381 -33.584 -9.643 4.271 1.00 20.89 O
ATOM 2852 CB ILE A 381 -34.043 -6.698 2.856 1.00 20.27 C
ATOM 2853 CG1 ILE A 381 -34.336 -7.757 1.782 1.00 21.09 C
ATOM 2854 CG2 ILE A 381 -33.307 -5.503 2.249 1.00 20.52 C
ATOM 2855 CD1 ILE A 381 -35.413 -7.365 0.784 1.00 20.87 C
ATOM 2856 N PRO A 382 -34.846 -8.301 5.581 1.00 20.93 N
ATOM 2857 CA PRO A 382 -35.543 -9.482 6.133 1.00 21.39 C
ATOM 2858 C PRO A 382 -36.248 -10.328 5.057 1.00 21.28 C
ATOM 2859 O PRO A 382 -36.987 -9.805 4.229 1.00 23.48 O
ATOM 2860 CB PRO A 382 -36.547 -8.875 7.135 1.00 20.34 C
ATOM 2861 CG PRO A 382 -36.596 -7.399 6.825 1.00 21.07 C
ATOM 2862 CD PRO A 382 -35.225 -7.057 6.279 1.00 20.45 C
ATOM 2863 N GLY A 383 -35.999 -11.628 5.050 1.00 20.94 N
ATOM 2864 CA GLY A 383 -36.634 -12.477 4.063 1.00 21.14 C
ATOM 2865 C GLY A 383 -35.750 -13.625 3.628 1.00 21.72 C
ATOM 2866 O GLY A 383 -34.739 -13.913 4.253 1.00 22.05 O
ATOM 2867 N TRP A 384 -36.145 -14.251 2.529 1.00 21.96 N
ATOM 2868 CA TRP A 384 -35.658 -15.559 2.142 1.00 23.15 C
ATOM 2869 C TRP A 384 -34.440 -15.417 1.288 1.00 22.33 C
ATOM 2870 O TRP A 384 -34.538 -14.987 0.149 1.00 23.15 O
ATOM 2871 CB TRP A 384 -36.765 -16.282 1.384 1.00 23.99 C
ATOM 2872 CG TRP A 384 -38.067 -16.290 2.156 1.00 24.59 C
ATOM 2873 CD1 TRP A 384 -39.205 -15.517 1.933 1.00 24.97 C
ATOM 2874 CD2 TRP A 384 -38.369 -17.085 3.338 1.00 25.20 C
ATOM 2875 NE1 TRP A 384 -40.178 -15.790 2.866 1.00 25.64 N
ATOM 2876 CE2 TRP A 384 -39.737 -16.726 3.741 1.00 25.91 C
ATOM 2877 CE3 TRP A 384 -37.670 -18.033 4.082 1.00 26.04 C
ATOM 2878 CZ2 TRP A 384 -40.354 -17.312 4.831 1.00 26.05 C
ATOM 2879 CZ3 TRP A 384 -38.306 -18.614 5.185 1.00 26.51 C
ATOM 2880 CH2 TRP A 384 -39.611 -18.257 5.550 1.00 26.12 C
ATOM 2881 N ASN A 385 -33.291 -15.769 1.845 1.00 22.50 N
ATOM 2882 CA ASN A 385 -32.002 -15.622 1.161 1.00 23.57 C
ATOM 2883 C ASN A 385 -31.543 -16.971 0.605 1.00 24.47 C
ATOM 2884 O ASN A 385 -31.559 -17.978 1.316 1.00 25.64 O
ATOM 2885 CB ASN A 385 -30.947 -15.050 2.114 1.00 22.10 C
ATOM 2886 CG ASN A 385 -29.541 -15.103 1.540 1.00 22.94 C
ATOM 2887 OD1 ASN A 385 -29.130 -14.227 0.773 1.00 23.22 O
ATOM 2888 ND2 ASN A 385 -28.787 -16.133 1.920 1.00 23.09 N
ATOM 2889 N ILE A 386 -31.106 -16.954 -0.650 1.00 25.25 N
ATOM 2890 CA ILE A 386 -30.790 -18.139 -1.426 1.00 26.16 C
ATOM 2891 C ILE A 386 -29.447 -17.955 -2.137 1.00 25.90 C
ATOM 2892 O ILE A 386 -29.227 -16.921 -2.770 1.00 26.81 O
ATOM 2893 CB ILE A 386 -31.887 -18.366 -2.498 1.00 27.80 C
ATOM 2894 CG1 ILE A 386 -33.206 -18.808 -1.859 1.00 29.04 C
ATOM 2895 CG2 ILE A 386 -31.467 -19.387 -3.543 1.00 29.29 C
ATOM 2896 CD1 ILE A 386 -33.060 -19.945 -0.868 1.00 29.23 C
ATOM 2897 N CYS A 387 -28.561 -18.946 -2.040 1.00 25.80 N
ATOM 2898 CA CYS A 387 -27.384 -19.020 -2.929 1.00 27.63 C
ATOM 2899 C CYS A 387 -27.442 -20.278 -3.743 1.00 27.28 C
ATOM 2900 O CYS A 387 -27.676 -21.359 -3.198 1.00 26.37 O
ATOM 2901 CB CYS A 387 -26.077 -19.072 -2.160 1.00 30.59 C
ATOM 2902 SG CYS A 387 -25.918 -17.784 -0.946 1.00 36.62 S
ATOM 2903 N VAL A 388 -27.228 -20.134 -5.046 1.00 27.38 N
ATOM 2904 CA VAL A 388 -27.174 -21.275 -5.941 1.00 27.94 C
ATOM 2905 C VAL A 388 -25.911 -21.194 -6.786 1.00 28.26 C
ATOM 2906 O VAL A 388 -25.348 -20.122 -6.969 1.00 27.44 O
ATOM 2907 CB VAL A 388 -28.436 -21.404 -6.831 1.00 28.64 C
ATOM 2908 CG1 VAL A 388 -29.659 -21.733 -5.984 1.00 29.52 C
ATOM 2909 CG2 VAL A 388 -28.673 -20.130 -7.634 1.00 29.02 C
ATOM 2910 N ASP A 389 -25.481 -22.343 -7.291 1.00 30.02 N
ATOM 2911 CA ASP A 389 -24.278 -22.450 -8.108 1.00 33.10 C
ATOM 2912 C ASP A 389 -24.595 -23.146 -9.411 1.00 33.14 C
ATOM 2913 O ASP A 389 -24.803 -24.365 -9.424 1.00 33.67 O
ATOM 2914 CB ASP A 389 -23.211 -23.253 -7.370 1.00 37.11 C
ATOM 2915 CG ASP A 389 -22.013 -22.437 -7.044 1.00 42.77 C
ATOM 2916 OD1 ASP A 389 -21.167 -22.229 -7.950 1.00 45.84 O
ATOM 2917 OD2 ASP A 389 -21.915 -22.001 -5.882 1.00 47.64 O
ATOM 2918 N PHE A 390 -24.640 -22.387 -10.503 1.00 30.26 N
ATOM 2919 CA PHE A 390 -24.975 -22.982 -11.801 1.00 29.92 C
ATOM 2920 C PHE A 390 -23.712 -23.213 -12.623 1.00 29.87 C
ATOM 2921 O PHE A 390 -22.964 -22.272 -12.866 1.00 31.12 O
ATOM 2922 CB PHE A 390 -25.872 -22.079 -12.636 1.00 28.13 C
ATOM 2923 CG PHE A 390 -27.184 -21.722 -12.002 1.00 27.24 C
ATOM 2924 CD1 PHE A 390 -28.147 -22.692 -11.735 1.00 27.32 C
ATOM 2925 CD2 PHE A 390 -27.481 -20.394 -11.746 1.00 26.62 C
ATOM 2926 CE1 PHE A 390 -29.373 -22.336 -11.181 1.00 27.72 C
ATOM 2927 CE2 PHE A 390 -28.705 -20.028 -11.202 1.00 27.28 C
ATOM 2928 CZ PHE A 390 -29.653 -21.001 -10.920 1.00 26.19 C
ATOM 2929 N PRO A 391 -23.499 -24.455 -13.087 1.00 30.43 N
ATOM 2930 CA PRO A 391 -22.466 -24.739 -14.098 1.00 31.65 C
ATOM 2931 C PRO A 391 -22.682 -23.876 -15.350 1.00 31.83 C
ATOM 2932 O PRO A 391 -23.821 -23.727 -15.801 1.00 30.97 O
ATOM 2933 CB PRO A 391 -22.699 -26.219 -14.435 1.00 31.23 C
ATOM 2934 CG PRO A 391 -23.415 -26.782 -13.252 1.00 32.60 C
ATOM 2935 CD PRO A 391 -24.247 -25.661 -12.696 1.00 30.99 C
ATOM 2936 N ILE A 392 -21.611 -23.288 -15.880 1.00 32.03 N
ATOM 2937 CA ILE A 392 -21.714 -22.454 -17.072 1.00 33.00 C
ATOM 2938 C ILE A 392 -21.946 -23.342 -18.290 1.00 34.76 C
ATOM 2939 O ILE A 392 -21.168 -24.256 -18.565 1.00 35.16 O
ATOM 2940 CB ILE A 392 -20.473 -21.548 -17.281 1.00 33.91 C
ATOM 2941 CG1 ILE A 392 -20.397 -20.477 -16.183 1.00 34.81 C
ATOM 2942 CG2 ILE A 392 -20.508 -20.881 -18.651 1.00 32.50 C
ATOM 2943 CD1 ILE A 392 -19.121 -19.653 -16.217 1.00 35.50 C
ATOM 2944 N LYS A 393 -23.040 -23.068 -18.995 1.00 34.95 N
ATOM 2945 CA LYS A 393 -23.425 -23.800 -20.194 1.00 33.13 C
ATOM 2946 C LYS A 393 -24.394 -22.937 -21.004 1.00 33.02 C
ATOM 2947 O LYS A 393 -24.864 -21.906 -20.515 1.00 31.34 O
ATOM 2948 CB LYS A 393 -24.050 -25.143 -19.818 1.00 33.58 C
ATOM 2949 CG LYS A 393 -25.446 -25.067 -19.217 1.00 33.30 C
ATOM 2950 CD LYS A 393 -25.829 -26.405 -18.610 1.00 32.28 C
ATOM 2951 CE LYS A 393 -27.334 -26.570 -18.561 1.00 32.24 C
ATOM 2952 NZ LYS A 393 -27.699 -27.801 -17.810 1.00 30.63 N
ATOM 2953 N ASP A 394 -24.699 -23.351 -22.231 1.00 31.75 N
ATOM 2954 CA ASP A 394 -25.538 -22.535 -23.108 1.00 31.89 C
ATOM 2955 C ASP A 394 -26.866 -22.166 -22.473 1.00 31.34 C
ATOM 2956 O ASP A 394 -27.525 -23.004 -21.844 1.00 29.53 O
ATOM 2957 CB ASP A 394 -25.805 -23.245 -24.431 1.00 33.91 C
ATOM 2958 CG ASP A 394 -24.573 -23.335 -25.300 1.00 36.03 C
ATOM 2959 OD1 ASP A 394 -23.657 -22.494 -25.151 1.00 36.20 O
ATOM 2960 OD2 ASP A 394 -24.535 -24.246 -26.144 1.00 39.72 O
ATOM 2961 N GLY A 395 -27.253 -20.910 -22.654 1.00 29.76 N
ATOM 2962 CA GLY A 395 -28.537 -20.437 -22.176 1.00 29.97 C
ATOM 2963 C GLY A 395 -28.507 -19.851 -20.771 1.00 29.81 C
ATOM 2964 O GLY A 395 -29.473 -19.208 -20.365 1.00 27.77 O
ATOM 2965 N LEU A 396 -27.419 -20.075 -20.026 1.00 28.02 N
ATOM 2966 CA LEU A 396 -27.348 -19.609 -18.624 1.00 27.70 C
ATOM 2967 C LEU A 396 -27.431 -18.095 -18.474 1.00 27.12 C
ATOM 2968 O LEU A 396 -28.171 -17.607 -17.628 1.00 27.73 O
ATOM 2969 CB LEU A 396 -26.108 -20.143 -17.881 1.00 26.55 C
ATOM 2970 CG LEU A 396 -26.005 -19.747 -16.399 1.00 27.18 C
ATOM 2971 CD1 LEU A 396 -27.180 -20.312 -15.586 1.00 25.98 C
ATOM 2972 CD2 LEU A 396 -24.673 -20.163 -15.786 1.00 26.43 C
ATOM 2973 N GLY A 397 -26.677 -17.356 -19.285 1.00 26.91 N
ATOM 2974 CA GLY A 397 -26.679 -15.893 -19.207 1.00 27.82 C
ATOM 2975 C GLY A 397 -28.079 -15.326 -19.362 1.00 27.67 C
ATOM 2976 O GLY A 397 -28.506 -14.479 -18.595 1.00 28.34 O
ATOM 2977 N LYS A 398 -28.805 -15.805 -20.361 1.00 28.62 N
ATOM 2978 CA LYS A 398 -30.146 -15.305 -20.604 1.00 28.88 C
ATOM 2979 C LYS A 398 -31.141 -15.789 -19.549 1.00 28.46 C
ATOM 2980 O LYS A 398 -32.079 -15.074 -19.209 1.00 29.50 O
ATOM 2981 CB LYS A 398 -30.595 -15.621 -22.029 1.00 31.40 C
ATOM 2982 CG LYS A 398 -29.942 -14.704 -23.051 1.00 33.29 C
ATOM 2983 CD LYS A 398 -30.661 -14.771 -24.383 1.00 35.99 C
ATOM 2984 CE LYS A 398 -30.215 -13.664 -25.322 1.00 37.50 C
ATOM 2985 NZ LYS A 398 -28.757 -13.714 -25.616 1.00 39.56 N
ATOM 2986 N PHE A 399 -30.914 -16.969 -18.987 1.00 27.76 N
ATOM 2987 CA PHE A 399 -31.765 -17.429 -17.887 1.00 27.11 C
ATOM 2988 C PHE A 399 -31.563 -16.631 -16.589 1.00 27.43 C
ATOM 2989 O PHE A 399 -32.545 -16.267 -15.927 1.00 25.92 O
ATOM 2990 CB PHE A 399 -31.583 -18.915 -17.613 1.00 28.13 C
ATOM 2991 CG PHE A 399 -32.287 -19.376 -16.376 1.00 28.67 C
ATOM 2992 CD1 PHE A 399 -33.681 -19.433 -16.335 1.00 29.22 C
ATOM 2993 CD2 PHE A 399 -31.564 -19.728 -15.244 1.00 28.44 C
ATOM 2994 CE1 PHE A 399 -34.334 -19.845 -15.189 1.00 28.53 C
ATOM 2995 CE2 PHE A 399 -32.216 -20.144 -14.091 1.00 28.85 C
ATOM 2996 CZ PHE A 399 -33.598 -20.201 -14.065 1.00 28.44 C
ATOM 2997 N VAL A 400 -30.318 -16.344 -16.224 1.00 25.84 N
ATOM 2998 CA VAL A 400 -30.102 -15.527 -15.024 1.00 28.21 C
ATOM 2999 C VAL A 400 -30.600 -14.083 -15.202 1.00 27.42 C
ATOM 3000 O VAL A 400 -30.940 -13.430 -14.226 1.00 26.96 O
ATOM 3001 CB VAL A 400 -28.663 -15.597 -14.463 1.00 29.49 C
ATOM 3002 CG1 VAL A 400 -28.329 -17.021 -14.038 1.00 30.20 C
ATOM 3003 CG2 VAL A 400 -27.646 -15.070 -15.468 1.00 30.99 C
ATOM 3004 N SER A 401 -30.680 -13.596 -16.442 1.00 27.91 N
ATOM 3005 CA SER A 401 -31.330 -12.305 -16.682 1.00 28.93 C
ATOM 3006 C SER A 401 -32.823 -12.382 -16.394 1.00 29.36 C
ATOM 3007 O SER A 401 -33.412 -11.411 -15.915 1.00 30.26 O
ATOM 3008 CB SER A 401 -31.084 -11.805 -18.104 1.00 31.19 C
ATOM 3009 OG SER A 401 -29.727 -11.429 -18.246 1.00 33.79 O
ATOM 3010 N GLU A 402 -33.433 -13.530 -16.681 1.00 28.47 N
ATOM 3011 CA GLU A 402 -34.845 -13.727 -16.352 1.00 30.25 C
ATOM 3012 C GLU A 402 -35.042 -13.834 -14.855 1.00 28.89 C
ATOM 3013 O GLU A 402 -35.990 -13.244 -14.318 1.00 30.73 O
ATOM 3014 CB GLU A 402 -35.459 -14.928 -17.087 1.00 30.94 C
ATOM 3015 CG GLU A 402 -35.606 -14.711 -18.591 1.00 32.14 C
ATOM 3016 CD GLU A 402 -36.413 -13.468 -18.927 1.00 34.56 C
ATOM 3017 OE1 GLU A 402 -37.539 -13.313 -18.393 1.00 36.17 O
ATOM 3018 OE2 GLU A 402 -35.914 -12.636 -19.709 1.00 32.43 O
ATOM 3019 N LEU A 403 -34.150 -14.563 -14.183 1.00 26.03 N
ATOM 3020 CA LEU A 403 -34.173 -14.615 -12.731 1.00 26.98 C
ATOM 3021 C LEU A 403 -34.079 -13.219 -12.123 1.00 26.32 C
ATOM 3022 O LEU A 403 -34.833 -12.916 -11.195 1.00 27.37 O
ATOM 3023 CB LEU A 403 -33.062 -15.514 -12.160 1.00 27.97 C
ATOM 3024 CG LEU A 403 -33.204 -17.038 -12.132 1.00 30.16 C
ATOM 3025 CD1 LEU A 403 -32.021 -17.652 -11.383 1.00 29.23 C
ATOM 3026 CD2 LEU A 403 -34.530 -17.475 -11.513 1.00 29.77 C
ATOM 3027 N ASP A 404 -33.164 -12.381 -12.640 1.00 24.56 N
ATOM 3028 CA ASP A 404 -33.014 -10.992 -12.184 1.00 24.51 C
ATOM 3029 C ASP A 404 -34.369 -10.296 -12.159 1.00 25.28 C
ATOM 3030 O ASP A 404 -34.717 -9.646 -11.184 1.00 25.05 O
ATOM 3031 CB ASP A 404 -32.103 -10.170 -13.107 1.00 25.32 C
ATOM 3032 CG ASP A 404 -30.620 -10.492 -12.960 1.00 25.47 C
ATOM 3033 OD1 ASP A 404 -30.225 -11.332 -12.126 1.00 25.39 O
ATOM 3034 OD2 ASP A 404 -29.823 -9.870 -13.704 1.00 26.44 O
ATOM 3035 N ARG A 405 -35.119 -10.448 -13.252 1.00 26.00 N
ATOM 3036 CA ARG A 405 -36.392 -9.780 -13.448 1.00 27.44 C
ATOM 3037 C ARG A 405 -37.414 -10.250 -12.420 1.00 26.04 C
ATOM 3038 O ARG A 405 -38.154 -9.448 -11.879 1.00 25.94 O
ATOM 3039 CB ARG A 405 -36.896 -10.017 -14.887 1.00 28.43 C
ATOM 3040 CG ARG A 405 -38.307 -9.528 -15.167 1.00 33.10 C
ATOM 3041 CD ARG A 405 -38.773 -9.872 -16.587 1.00 38.08 C
ATOM 3042 NE ARG A 405 -38.779 -11.319 -16.840 1.00 42.45 N
ATOM 3043 CZ ARG A 405 -39.775 -12.158 -16.539 1.00 43.06 C
ATOM 3044 NH1 ARG A 405 -40.895 -11.721 -15.972 1.00 42.97 N
ATOM 3045 NH2 ARG A 405 -39.650 -13.455 -16.817 1.00 43.88 N
ATOM 3046 N ARG A 406 -37.438 -11.549 -12.145 1.00 27.04 N
ATOM 3047 CA ARG A 406 -38.341 -12.079 -11.120 1.00 28.76 C
ATOM 3048 C ARG A 406 -37.934 -11.630 -9.722 1.00 26.60 C
ATOM 3049 O ARG A 406 -38.797 -11.233 -8.936 1.00 24.70 O
ATOM 3050 CB ARG A 406 -38.435 -13.600 -11.204 1.00 31.93 C
ATOM 3051 CG ARG A 406 -39.179 -14.061 -12.442 1.00 36.73 C
ATOM 3052 CD ARG A 406 -39.117 -15.568 -12.579 1.00 42.73 C
ATOM 3053 NE ARG A 406 -40.203 -16.112 -13.397 1.00 47.46 N
ATOM 3054 CZ ARG A 406 -41.461 -15.673 -13.407 1.00 49.46 C
ATOM 3055 NH1 ARG A 406 -41.855 -14.665 -12.631 1.00 49.44 N
ATOM 3056 NH2 ARG A 406 -42.334 -16.264 -14.196 1.00 50.67 N
ATOM 3057 N VAL A 407 -36.630 -11.666 -9.436 1.00 24.63 N
ATOM 3058 CA VAL A 407 -36.076 -11.175 -8.159 1.00 25.16 C
ATOM 3059 C VAL A 407 -36.486 -9.707 -7.942 1.00 24.33 C
ATOM 3060 O VAL A 407 -37.005 -9.348 -6.885 1.00 25.87 O
ATOM 3061 CB VAL A 407 -34.530 -11.329 -8.080 1.00 24.57 C
ATOM 3062 CG1 VAL A 407 -33.958 -10.578 -6.885 1.00 24.96 C
ATOM 3063 CG2 VAL A 407 -34.121 -12.797 -7.985 1.00 26.20 C
ATOM 3064 N LEU A 408 -36.283 -8.881 -8.962 1.00 24.46 N
ATOM 3065 CA LEU A 408 -36.640 -7.459 -8.900 1.00 24.92 C
ATOM 3066 C LEU A 408 -38.144 -7.269 -8.702 1.00 26.31 C
ATOM 3067 O LEU A 408 -38.581 -6.605 -7.754 1.00 25.72 O
ATOM 3068 CB LEU A 408 -36.173 -6.742 -10.176 1.00 25.12 C
ATOM 3069 CG LEU A 408 -36.692 -5.332 -10.474 1.00 25.69 C
ATOM 3070 CD1 LEU A 408 -36.327 -4.397 -9.328 1.00 23.85 C
ATOM 3071 CD2 LEU A 408 -36.118 -4.838 -11.801 1.00 25.42 C
ATOM 3072 N GLU A 409 -38.931 -7.866 -9.591 1.00 27.35 N
ATOM 3073 CA GLU A 409 -40.387 -7.793 -9.501 1.00 30.46 C
ATOM 3074 C GLU A 409 -40.915 -8.213 -8.120 1.00 29.04 C
ATOM 3075 O GLU A 409 -41.899 -7.651 -7.627 1.00 27.25 O
ATOM 3076 CB GLU A 409 -41.010 -8.627 -10.629 1.00 33.97 C
ATOM 3077 CG GLU A 409 -42.406 -9.160 -10.377 1.00 39.38 C
ATOM 3078 CD GLU A 409 -42.993 -9.839 -11.597 1.00 43.17 C
ATOM 3079 OE1 GLU A 409 -42.316 -10.713 -12.189 1.00 45.83 O
ATOM 3080 OE2 GLU A 409 -44.132 -9.488 -11.963 1.00 47.33 O
ATOM 3081 N PHE A 410 -40.251 -9.181 -7.493 1.00 26.91 N
ATOM 3082 CA PHE A 410 -40.684 -9.660 -6.185 1.00 27.72 C
ATOM 3083 C PHE A 410 -40.067 -8.898 -4.994 1.00 26.52 C
ATOM 3084 O PHE A 410 -40.035 -9.412 -3.874 1.00 24.86 O
ATOM 3085 CB PHE A 410 -40.459 -11.176 -6.059 1.00 29.39 C
ATOM 3086 CG PHE A 410 -41.263 -12.001 -7.038 1.00 32.28 C
ATOM 3087 CD1 PHE A 410 -42.443 -11.509 -7.592 1.00 32.11 C
ATOM 3088 CD2 PHE A 410 -40.853 -13.295 -7.378 1.00 33.76 C
ATOM 3089 CE1 PHE A 410 -43.185 -12.276 -8.481 1.00 34.82 C
ATOM 3090 CE2 PHE A 410 -41.597 -14.072 -8.261 1.00 35.61 C
ATOM 3091 CZ PHE A 410 -42.763 -13.560 -8.817 1.00 35.70 C
ATOM 3092 N GLY A 411 -39.590 -7.673 -5.246 1.00 24.63 N
ATOM 3093 CA GLY A 411 -39.011 -6.825 -4.200 1.00 23.71 C
ATOM 3094 C GLY A 411 -37.654 -7.206 -3.633 1.00 22.93 C
ATOM 3095 O GLY A 411 -37.227 -6.640 -2.616 1.00 23.21 O
ATOM 3096 N GLY A 412 -36.966 -8.155 -4.270 1.00 22.47 N
ATOM 3097 CA GLY A 412 -35.674 -8.611 -3.774 1.00 21.63 C
ATOM 3098 C GLY A 412 -34.487 -7.973 -4.473 1.00 23.24 C
ATOM 3099 O GLY A 412 -34.642 -7.058 -5.296 1.00 24.46 O
ATOM 3100 N ARG A 413 -33.294 -8.476 -4.173 1.00 22.42 N
ATOM 3101 CA ARG A 413 -32.069 -7.946 -4.786 1.00 21.64 C
ATOM 3102 C ARG A 413 -31.002 -9.017 -4.918 1.00 21.35 C
ATOM 3103 O ARG A 413 -31.081 -10.066 -4.274 1.00 20.62 O
ATOM 3104 CB ARG A 413 -31.505 -6.778 -3.955 1.00 20.27 C
ATOM 3105 CG ARG A 413 -31.220 -7.132 -2.497 1.00 19.56 C
ATOM 3106 CD ARG A 413 -32.379 -6.727 -1.580 1.00 19.95 C
ATOM 3107 NE ARG A 413 -32.581 -5.287 -1.711 1.00 19.93 N
ATOM 3108 CZ ARG A 413 -31.861 -4.368 -1.076 1.00 19.22 C
ATOM 3109 NH1 ARG A 413 -30.943 -4.732 -0.195 1.00 18.89 N
ATOM 3110 NH2 ARG A 413 -32.084 -3.075 -1.309 1.00 19.53 N
ATOM 3111 N LEU A 414 -29.988 -8.720 -5.731 1.00 22.69 N
ATOM 3112 CA LEU A 414 -28.753 -9.516 -5.798 1.00 23.01 C
ATOM 3113 C LEU A 414 -27.683 -8.898 -4.916 1.00 22.84 C
ATOM 3114 O LEU A 414 -27.774 -7.735 -4.541 1.00 22.47 O
ATOM 3115 CB LEU A 414 -28.203 -9.534 -7.231 1.00 24.95 C
ATOM 3116 CG LEU A 414 -29.115 -10.016 -8.345 1.00 26.65 C
ATOM 3117 CD1 LEU A 414 -28.485 -9.739 -9.700 1.00 26.92 C
ATOM 3118 CD2 LEU A 414 -29.362 -11.498 -8.127 1.00 27.21 C
ATOM 3119 N TYR A 415 -26.628 -9.664 -4.658 1.00 22.97 N
ATOM 3120 CA TYR A 415 -25.528 -9.263 -3.788 1.00 23.32 C
ATOM 3121 C TYR A 415 -24.310 -8.894 -4.639 1.00 24.23 C
ATOM 3122 O TYR A 415 -23.882 -9.697 -5.476 1.00 23.14 O
ATOM 3123 CB TYR A 415 -25.197 -10.465 -2.902 1.00 23.87 C
ATOM 3124 CG TYR A 415 -24.209 -10.282 -1.764 1.00 24.03 C
ATOM 3125 CD1 TYR A 415 -23.819 -9.014 -1.306 1.00 23.33 C
ATOM 3126 CD2 TYR A 415 -23.698 -11.404 -1.112 1.00 24.80 C
ATOM 3127 CE1 TYR A 415 -22.930 -8.881 -0.249 1.00 23.63 C
ATOM 3128 CE2 TYR A 415 -22.806 -11.286 -0.060 1.00 24.27 C
ATOM 3129 CZ TYR A 415 -22.424 -10.032 0.376 1.00 24.52 C
ATOM 3130 OH TYR A 415 -21.553 -9.945 1.445 1.00 22.93 O
ATOM 3131 N THR A 416 -23.722 -7.721 -4.408 1.00 24.66 N
ATOM 3132 CA THR A 416 -22.532 -7.315 -5.202 1.00 26.39 C
ATOM 3133 C THR A 416 -21.333 -8.271 -5.072 1.00 27.12 C
ATOM 3134 O THR A 416 -20.585 -8.460 -6.036 1.00 28.62 O
ATOM 3135 CB THR A 416 -22.046 -5.892 -4.872 1.00 26.42 C
ATOM 3136 OG1 THR A 416 -21.685 -5.813 -3.483 1.00 28.20 O
ATOM 3137 CG2 THR A 416 -23.126 -4.870 -5.181 1.00 27.14 C
ATOM 3138 N ALA A 417 -21.152 -8.858 -3.887 1.00 26.18 N
ATOM 3139 CA ALA A 417 -20.043 -9.779 -3.611 1.00 26.91 C
ATOM 3140 C ALA A 417 -20.092 -11.053 -4.460 1.00 27.85 C
ATOM 3141 O ALA A 417 -19.083 -11.759 -4.580 1.00 29.36 O
ATOM 3142 CB ALA A 417 -20.011 -10.150 -2.132 1.00 25.81 C
ATOM 3143 N LYS A 418 -21.267 -11.350 -5.014 1.00 27.54 N
ATOM 3144 CA LYS A 418 -21.458 -12.512 -5.867 1.00 29.38 C
ATOM 3145 C LYS A 418 -21.641 -12.143 -7.346 1.00 29.83 C
ATOM 3146 O LYS A 418 -21.353 -12.956 -8.213 1.00 31.68 O
ATOM 3147 CB LYS A 418 -22.634 -13.391 -5.381 1.00 28.89 C
ATOM 3148 CG LYS A 418 -22.681 -13.685 -3.875 1.00 29.56 C
ATOM 3149 CD LYS A 418 -21.420 -14.366 -3.343 1.00 29.53 C
ATOM 3150 CE LYS A 418 -21.598 -14.894 -1.922 1.00 28.02 C
ATOM 3151 NZ LYS A 418 -22.501 -16.086 -1.917 1.00 28.29 N
ATOM 3152 N ASP A 419 -22.091 -10.923 -7.629 1.00 27.98 N
ATOM 3153 CA ASP A 419 -22.472 -10.543 -8.998 1.00 29.06 C
ATOM 3154 C ASP A 419 -21.332 -10.177 -9.939 1.00 29.66 C
ATOM 3155 O ASP A 419 -20.448 -9.402 -9.586 1.00 29.29 O
ATOM 3156 CB ASP A 419 -23.453 -9.375 -8.991 1.00 28.26 C
ATOM 3157 CG ASP A 419 -23.831 -8.943 -10.402 1.00 28.51 C
ATOM 3158 OD1 ASP A 419 -24.421 -9.776 -11.128 1.00 26.58 O
ATOM 3159 OD2 ASP A 419 -23.510 -7.793 -10.788 1.00 28.09 O
ATOM 3160 N SER A 420 -21.406 -10.678 -11.167 1.00 30.93 N
ATOM 3161 CA SER A 420 -20.464 -10.274 -12.206 1.00 32.61 C
ATOM 3162 C SER A 420 -21.169 -9.865 -13.498 1.00 32.97 C
ATOM 3163 O SER A 420 -20.518 -9.416 -14.440 1.00 33.08 O
ATOM 3164 CB SER A 420 -19.456 -11.394 -12.487 1.00 35.78 C
ATOM 3165 OG SER A 420 -20.130 -12.607 -12.785 1.00 40.27 O
ATOM 3166 N ARG A 421 -22.496 -9.988 -13.552 1.00 31.56 N
ATOM 3167 CA ARG A 421 -23.172 -9.774 -14.832 1.00 30.76 C
ATOM 3168 C ARG A 421 -24.561 -9.114 -14.879 1.00 29.84 C
ATOM 3169 O ARG A 421 -25.102 -8.959 -15.969 1.00 29.51 O
ATOM 3170 CB ARG A 421 -23.127 -11.042 -15.712 1.00 32.46 C
ATOM 3171 CG ARG A 421 -23.460 -12.359 -15.037 1.00 34.30 C
ATOM 3172 CD ARG A 421 -24.942 -12.655 -15.165 1.00 37.17 C
ATOM 3173 NE ARG A 421 -25.687 -12.264 -13.973 1.00 38.03 N
ATOM 3174 CZ ARG A 421 -26.925 -11.764 -13.964 1.00 36.59 C
ATOM 3175 NH1 ARG A 421 -27.592 -11.544 -15.097 1.00 35.70 N
ATOM 3176 NH2 ARG A 421 -27.491 -11.465 -12.802 1.00 33.32 N
ATOM 3177 N THR A 422 -25.146 -8.721 -13.745 1.00 27.74 N
ATOM 3178 CA THR A 422 -26.409 -7.977 -13.834 1.00 26.95 C
ATOM 3179 C THR A 422 -26.168 -6.591 -14.467 1.00 26.98 C
ATOM 3180 O THR A 422 -25.031 -6.160 -14.643 1.00 27.35 O
ATOM 3181 CB THR A 422 -27.186 -7.873 -12.496 1.00 26.57 C
ATOM 3182 OG1 THR A 422 -28.558 -7.549 -12.774 1.00 28.70 O
ATOM 3183 CG2 THR A 422 -26.601 -6.818 -11.552 1.00 25.24 C
ATOM 3184 N THR A 423 -27.245 -5.926 -14.844 1.00 27.74 N
ATOM 3185 CA THR A 423 -27.152 -4.612 -15.465 1.00 27.54 C
ATOM 3186 C THR A 423 -27.333 -3.521 -14.430 1.00 26.39 C
ATOM 3187 O THR A 423 -27.939 -3.748 -13.373 1.00 25.69 O
ATOM 3188 CB THR A 423 -28.235 -4.424 -16.540 1.00 27.50 C
ATOM 3189 OG1 THR A 423 -29.535 -4.548 -15.940 1.00 27.58 O
ATOM 3190 CG2 THR A 423 -28.078 -5.460 -17.632 1.00 29.31 C
ATOM 3191 N ALA A 424 -26.826 -2.335 -14.758 1.00 25.33 N
ATOM 3192 CA ALA A 424 -27.044 -1.124 -13.981 1.00 25.96 C
ATOM 3193 C ALA A 424 -28.534 -0.849 -13.756 1.00 27.12 C
ATOM 3194 O ALA A 424 -28.943 -0.535 -12.643 1.00 26.88 O
ATOM 3195 CB ALA A 424 -26.367 0.062 -14.660 1.00 26.62 C
ATOM 3196 N GLU A 425 -29.344 -0.982 -14.805 1.00 28.10 N
ATOM 3197 CA GLU A 425 -30.786 -0.727 -14.702 1.00 28.57 C
ATOM 3198 C GLU A 425 -31.445 -1.633 -13.648 1.00 27.45 C
ATOM 3199 O GLU A 425 -32.189 -1.161 -12.782 1.00 28.02 O
ATOM 3200 CB GLU A 425 -31.460 -0.884 -16.077 1.00 30.01 C
ATOM 3201 CG GLU A 425 -32.956 -0.598 -16.084 1.00 32.04 C
ATOM 3202 CD GLU A 425 -33.606 -0.793 -17.448 1.00 33.38 C
ATOM 3203 OE1 GLU A 425 -32.972 -1.338 -18.372 1.00 35.94 O
ATOM 3204 OE2 GLU A 425 -34.775 -0.417 -17.599 1.00 36.18 O
ATOM 3205 N THR A 426 -31.150 -2.925 -13.711 1.00 25.35 N
ATOM 3206 CA THR A 426 -31.673 -3.892 -12.744 1.00 24.83 C
ATOM 3207 C THR A 426 -31.160 -3.609 -11.336 1.00 24.00 C
ATOM 3208 O THR A 426 -31.939 -3.598 -10.375 1.00 23.62 O
ATOM 3209 CB THR A 426 -31.293 -5.326 -13.144 1.00 24.33 C
ATOM 3210 OG1 THR A 426 -31.918 -5.637 -14.386 1.00 25.63 O
ATOM 3211 CG2 THR A 426 -31.764 -6.336 -12.106 1.00 24.75 C
ATOM 3212 N PHE A 427 -29.853 -3.393 -11.217 1.00 22.11 N
ATOM 3213 CA PHE A 427 -29.248 -3.116 -9.932 1.00 22.88 C
ATOM 3214 C PHE A 427 -29.845 -1.874 -9.284 1.00 23.04 C
ATOM 3215 O PHE A 427 -30.124 -1.884 -8.082 1.00 22.11 O
ATOM 3216 CB PHE A 427 -27.725 -2.949 -10.022 1.00 22.93 C
ATOM 3217 CG PHE A 427 -27.062 -2.779 -8.679 1.00 23.17 C
ATOM 3218 CD1 PHE A 427 -26.623 -3.893 -7.961 1.00 22.95 C
ATOM 3219 CD2 PHE A 427 -26.886 -1.515 -8.125 1.00 22.39 C
ATOM 3220 CE1 PHE A 427 -26.022 -3.740 -6.720 1.00 23.37 C
ATOM 3221 CE2 PHE A 427 -26.287 -1.357 -6.880 1.00 23.75 C
ATOM 3222 CZ PHE A 427 -25.853 -2.475 -6.172 1.00 23.00 C
ATOM 3223 N HIS A 428 -30.005 -0.801 -10.063 1.00 22.83 N
ATOM 3224 CA HIS A 428 -30.571 0.427 -9.504 1.00 22.41 C
ATOM 3225 C HIS A 428 -31.992 0.245 -9.048 1.00 22.88 C
ATOM 3226 O HIS A 428 -32.377 0.812 -8.036 1.00 23.50 O
ATOM 3227 CB HIS A 428 -30.455 1.600 -10.467 1.00 22.17 C
ATOM 3228 CG HIS A 428 -29.055 2.140 -10.592 1.00 22.59 C
ATOM 3229 ND1 HIS A 428 -28.769 3.449 -10.471 1.00 22.81 N
ATOM 3230 CD2 HIS A 428 -27.840 1.493 -10.844 1.00 22.26 C
ATOM 3231 CE1 HIS A 428 -27.444 3.638 -10.644 1.00 22.96 C
ATOM 3232 NE2 HIS A 428 -26.879 2.441 -10.875 1.00 22.64 N
ATOM 3233 N ALA A 429 -32.778 -0.548 -9.770 1.00 22.26 N
ATOM 3234 CA ALA A 429 -34.176 -0.809 -9.363 1.00 22.68 C
ATOM 3235 C ALA A 429 -34.269 -1.677 -8.106 1.00 23.25 C
ATOM 3236 O ALA A 429 -35.195 -1.528 -7.287 1.00 24.04 O
ATOM 3237 CB ALA A 429 -34.950 -1.433 -10.509 1.00 22.41 C
ATOM 3238 N MET A 430 -33.304 -2.583 -7.954 1.00 22.41 N
ATOM 3239 CA MET A 430 -33.211 -3.460 -6.790 1.00 23.49 C
ATOM 3240 C MET A 430 -32.779 -2.714 -5.523 1.00 23.94 C
ATOM 3241 O MET A 430 -33.046 -3.172 -4.422 1.00 26.14 O
ATOM 3242 CB MET A 430 -32.218 -4.604 -7.066 1.00 22.93 C
ATOM 3243 CG MET A 430 -32.709 -5.689 -8.020 1.00 21.95 C
ATOM 3244 SD MET A 430 -31.318 -6.795 -8.330 1.00 23.53 S
ATOM 3245 CE MET A 430 -32.119 -8.108 -9.256 1.00 24.16 C
ATOM 3246 N TYR A 431 -32.089 -1.589 -5.692 1.00 23.65 N
ATOM 3247 CA TYR A 431 -31.603 -0.777 -4.584 1.00 23.07 C
ATOM 3248 C TYR A 431 -32.200 0.644 -4.658 1.00 24.34 C
ATOM 3249 O TYR A 431 -31.530 1.559 -5.141 1.00 23.37 O
ATOM 3250 CB TYR A 431 -30.053 -0.731 -4.616 1.00 22.73 C
ATOM 3251 CG TYR A 431 -29.392 -2.016 -4.142 1.00 21.95 C
ATOM 3252 CD1 TYR A 431 -28.847 -2.112 -2.867 1.00 21.94 C
ATOM 3253 CD2 TYR A 431 -29.343 -3.143 -4.958 1.00 21.70 C
ATOM 3254 CE1 TYR A 431 -28.258 -3.294 -2.425 1.00 21.52 C
ATOM 3255 CE2 TYR A 431 -28.762 -4.326 -4.529 1.00 20.88 C
ATOM 3256 CZ TYR A 431 -28.222 -4.392 -3.262 1.00 20.40 C
ATOM 3257 OH TYR A 431 -27.648 -5.555 -2.825 1.00 20.62 O
ATOM 3258 N PRO A 432 -33.456 0.845 -4.163 1.00 24.88 N
ATOM 3259 CA PRO A 432 -34.095 2.176 -4.332 1.00 25.08 C
ATOM 3260 C PRO A 432 -33.397 3.325 -3.604 1.00 25.77 C
ATOM 3261 O PRO A 432 -33.699 4.489 -3.872 1.00 26.64 O
ATOM 3262 CB PRO A 432 -35.524 1.998 -3.784 1.00 25.79 C
ATOM 3263 CG PRO A 432 -35.608 0.611 -3.226 1.00 25.61 C
ATOM 3264 CD PRO A 432 -34.315 -0.130 -3.470 1.00 24.49 C
ATOM 3265 N ARG A 433 -32.479 3.009 -2.696 1.00 25.33 N
ATOM 3266 CA ARG A 433 -31.668 4.039 -2.045 1.00 25.82 C
ATOM 3267 C ARG A 433 -30.340 4.286 -2.779 1.00 25.08 C
ATOM 3268 O ARG A 433 -29.454 4.937 -2.250 1.00 24.67 O
ATOM 3269 CB ARG A 433 -31.415 3.684 -0.583 1.00 24.59 C
ATOM 3270 CG ARG A 433 -32.685 3.611 0.273 1.00 24.69 C
ATOM 3271 CD ARG A 433 -32.339 3.111 1.652 1.00 25.70 C
ATOM 3272 NE ARG A 433 -31.597 4.103 2.428 1.00 25.87 N
ATOM 3273 CZ ARG A 433 -31.188 3.928 3.685 1.00 26.57 C
ATOM 3274 NH1 ARG A 433 -31.446 2.791 4.329 1.00 27.13 N
ATOM 3275 NH2 ARG A 433 -30.522 4.896 4.307 1.00 25.56 N
ATOM 3276 N VAL A 434 -30.206 3.779 -3.999 1.00 26.50 N
ATOM 3277 CA VAL A 434 -28.941 3.949 -4.752 1.00 25.78 C
ATOM 3278 C VAL A 434 -28.628 5.434 -5.039 1.00 27.24 C
ATOM 3279 O VAL A 434 -27.472 5.863 -4.923 1.00 28.77 O
ATOM 3280 CB VAL A 434 -28.905 3.102 -6.051 1.00 25.54 C
ATOM 3281 CG1 VAL A 434 -29.880 3.630 -7.111 1.00 23.54 C
ATOM 3282 CG2 VAL A 434 -27.473 2.991 -6.595 1.00 24.25 C
ATOM 3283 N ASP A 435 -29.643 6.217 -5.405 1.00 26.94 N
ATOM 3284 CA ASP A 435 -29.417 7.651 -5.700 1.00 28.70 C
ATOM 3285 C ASP A 435 -28.930 8.396 -4.459 1.00 27.32 C
ATOM 3286 O ASP A 435 -28.008 9.203 -4.540 1.00 27.85 O
ATOM 3287 CB ASP A 435 -30.671 8.316 -6.271 1.00 30.02 C
ATOM 3288 CG ASP A 435 -31.014 7.825 -7.665 1.00 31.24 C
ATOM 3289 OD1 ASP A 435 -30.136 7.292 -8.369 1.00 32.93 O
ATOM 3290 OD2 ASP A 435 -32.177 7.990 -8.074 1.00 33.30 O
ATOM 3291 N GLU A 436 -29.550 8.101 -3.314 1.00 26.93 N
ATOM 3292 CA GLU A 436 -29.091 8.587 -2.015 1.00 26.51 C
ATOM 3293 C GLU A 436 -27.615 8.245 -1.754 1.00 26.41 C
ATOM 3294 O GLU A 436 -26.831 9.094 -1.328 1.00 26.58 O
ATOM 3295 CB GLU A 436 -29.975 8.015 -0.902 1.00 25.68 C
ATOM 3296 CG GLU A 436 -29.359 8.083 0.488 1.00 25.37 C
ATOM 3297 CD GLU A 436 -30.090 7.220 1.502 1.00 25.78 C
ATOM 3298 OE1 GLU A 436 -31.108 6.587 1.135 1.00 24.67 O
ATOM 3299 OE2 GLU A 436 -29.640 7.170 2.668 1.00 25.79 O
ATOM 3300 N TRP A 437 -27.242 6.998 -2.016 1.00 26.76 N
ATOM 3301 CA TRP A 437 -25.851 6.566 -1.886 1.00 25.74 C
ATOM 3302 C TRP A 437 -24.934 7.266 -2.873 1.00 26.16 C
ATOM 3303 O TRP A 437 -23.853 7.724 -2.502 1.00 25.94 O
ATOM 3304 CB TRP A 437 -25.769 5.049 -2.043 1.00 25.18 C
ATOM 3305 CG TRP A 437 -24.381 4.516 -1.851 1.00 25.23 C
ATOM 3306 CD1 TRP A 437 -23.790 4.078 -0.669 1.00 24.21 C
ATOM 3307 CD2 TRP A 437 -23.354 4.350 -2.881 1.00 24.22 C
ATOM 3308 NE1 TRP A 437 -22.494 3.669 -0.898 1.00 25.87 N
ATOM 3309 CE2 TRP A 437 -22.174 3.804 -2.201 1.00 24.88 C
ATOM 3310 CE3 TRP A 437 -23.295 4.591 -4.248 1.00 25.09 C
ATOM 3311 CZ2 TRP A 437 -20.998 3.522 -2.883 1.00 24.44 C
ATOM 3312 CZ3 TRP A 437 -22.105 4.302 -4.923 1.00 24.62 C
ATOM 3313 CH2 TRP A 437 -20.990 3.779 -4.254 1.00 24.68 C
ATOM 3314 N ILE A 438 -25.346 7.341 -4.137 1.00 26.91 N
ATOM 3315 CA ILE A 438 -24.564 8.028 -5.180 1.00 27.28 C
ATOM 3316 C ILE A 438 -24.240 9.488 -4.808 1.00 28.54 C
ATOM 3317 O ILE A 438 -23.109 9.943 -5.011 1.00 27.98 O
ATOM 3318 CB ILE A 438 -25.253 7.930 -6.564 1.00 28.10 C
ATOM 3319 CG1 ILE A 438 -25.089 6.518 -7.142 1.00 27.27 C
ATOM 3320 CG2 ILE A 438 -24.699 8.959 -7.555 1.00 29.05 C
ATOM 3321 CD1 ILE A 438 -25.991 6.237 -8.336 1.00 25.38 C
ATOM 3322 N SER A 439 -25.217 10.208 -4.250 1.00 28.11 N
ATOM 3323 CA SER A 439 -24.996 11.595 -3.817 1.00 29.28 C
ATOM 3324 C SER A 439 -23.938 11.725 -2.735 1.00 29.85 C
ATOM 3325 O SER A 439 -23.173 12.694 -2.740 1.00 29.74 O
ATOM 3326 CB SER A 439 -26.286 12.237 -3.315 1.00 28.83 C
ATOM 3327 OG SER A 439 -27.259 12.239 -4.332 1.00 29.86 O
ATOM 3328 N VAL A 440 -23.911 10.782 -1.789 1.00 29.66 N
ATOM 3329 CA VAL A 440 -22.844 10.750 -0.790 1.00 30.15 C
ATOM 3330 C VAL A 440 -21.487 10.537 -1.478 1.00 31.13 C
ATOM 3331 O VAL A 440 -20.519 11.237 -1.180 1.00 29.78 O
ATOM 3332 CB VAL A 440 -23.068 9.669 0.292 1.00 30.00 C
ATOM 3333 CG1 VAL A 440 -21.908 9.666 1.275 1.00 29.04 C
ATOM 3334 CG2 VAL A 440 -24.382 9.903 1.030 1.00 29.30 C
ATOM 3335 N ARG A 441 -21.435 9.588 -2.411 1.00 32.56 N
ATOM 3336 CA ARG A 441 -20.194 9.262 -3.121 1.00 34.42 C
ATOM 3337 C ARG A 441 -19.631 10.430 -3.937 1.00 35.98 C
ATOM 3338 O ARG A 441 -18.415 10.620 -3.983 1.00 38.85 O
ATOM 3339 CB ARG A 441 -20.369 8.031 -4.011 1.00 34.98 C
ATOM 3340 CG ARG A 441 -19.368 7.971 -5.153 1.00 34.87 C
ATOM 3341 CD ARG A 441 -19.060 6.572 -5.628 1.00 34.30 C
ATOM 3342 NE ARG A 441 -18.354 6.636 -6.900 1.00 38.34 N
ATOM 3343 CZ ARG A 441 -17.040 6.837 -7.043 1.00 39.00 C
ATOM 3344 NH1 ARG A 441 -16.241 6.984 -5.986 1.00 35.06 N
ATOM 3345 NH2 ARG A 441 -16.528 6.888 -8.265 1.00 38.37 N
ATOM 3346 N ARG A 442 -20.507 11.200 -4.579 1.00 37.78 N
ATOM 3347 CA ARG A 442 -20.067 12.333 -5.402 1.00 40.26 C
ATOM 3348 C ARG A 442 -19.638 13.505 -4.541 1.00 40.37 C
ATOM 3349 O ARG A 442 -18.824 14.321 -4.957 1.00 42.10 O
ATOM 3350 CB ARG A 442 -21.153 12.771 -6.375 1.00 40.84 C
ATOM 3351 CG ARG A 442 -21.256 11.889 -7.602 1.00 42.41 C
ATOM 3352 CD ARG A 442 -22.503 12.240 -8.376 1.00 43.69 C
ATOM 3353 NE ARG A 442 -22.807 11.248 -9.398 1.00 45.93 N
ATOM 3354 CZ ARG A 442 -23.914 11.256 -10.133 1.00 47.20 C
ATOM 3355 NH1 ARG A 442 -24.828 12.206 -9.953 1.00 48.40 N
ATOM 3356 NH2 ARG A 442 -24.113 10.312 -11.046 1.00 48.58 N
ATOM 3357 N LYS A 443 -20.207 13.580 -3.343 1.00 41.38 N
ATOM 3358 CA LYS A 443 -19.822 14.574 -2.349 1.00 41.19 C
ATOM 3359 C LYS A 443 -18.428 14.269 -1.787 1.00 40.08 C
ATOM 3360 O LYS A 443 -17.664 15.184 -1.495 1.00 38.88 O
ATOM 3361 CB LYS A 443 -20.872 14.618 -1.236 1.00 40.72 C
ATOM 3362 CG LYS A 443 -20.757 15.775 -0.263 1.00 43.64 C
ATOM 3363 CD LYS A 443 -22.087 16.022 0.443 1.00 44.90 C
ATOM 3364 CE LYS A 443 -22.407 14.919 1.439 1.00 44.45 C
ATOM 3365 NZ LYS A 443 -23.814 14.991 1.916 1.00 47.82 N
ATOM 3366 N VAL A 444 -18.090 12.985 -1.668 1.00 38.78 N
ATOM 3367 CA VAL A 444 -16.825 12.576 -1.048 1.00 37.17 C
ATOM 3368 C VAL A 444 -15.744 12.244 -2.083 1.00 36.58 C
ATOM 3369 O VAL A 444 -14.557 12.182 -1.752 1.00 38.28 O
ATOM 3370 CB VAL A 444 -17.036 11.414 -0.031 1.00 38.05 C
ATOM 3371 CG1 VAL A 444 -17.008 10.053 -0.720 1.00 35.83 C
ATOM 3372 CG2 VAL A 444 -15.993 11.462 1.075 1.00 38.56 C
ATOM 3373 N ASP A 445 -16.151 12.038 -3.334 1.00 35.41 N
ATOM 3374 CA ASP A 445 -15.202 11.750 -4.411 1.00 34.38 C
ATOM 3375 C ASP A 445 -15.667 12.376 -5.737 1.00 33.11 C
ATOM 3376 O ASP A 445 -15.979 11.654 -6.697 1.00 30.40 O
ATOM 3377 CB ASP A 445 -14.981 10.234 -4.537 1.00 35.09 C
ATOM 3378 CG ASP A 445 -13.940 9.873 -5.579 1.00 37.47 C
ATOM 3379 OD1 ASP A 445 -13.195 10.779 -6.027 1.00 35.83 O
ATOM 3380 OD2 ASP A 445 -13.869 8.678 -5.965 1.00 37.25 O
ATOM 3381 N PRO A 446 -15.721 13.727 -5.791 1.00 34.06 N
ATOM 3382 CA PRO A 446 -16.220 14.434 -6.983 1.00 35.44 C
ATOM 3383 C PRO A 446 -15.458 14.093 -8.263 1.00 35.17 C
ATOM 3384 O PRO A 446 -16.052 14.081 -9.346 1.00 35.86 O
ATOM 3385 CB PRO A 446 -16.061 15.924 -6.624 1.00 35.79 C
ATOM 3386 CG PRO A 446 -15.203 15.971 -5.402 1.00 34.28 C
ATOM 3387 CD PRO A 446 -15.363 14.661 -4.703 1.00 34.67 C
ATOM 3388 N LEU A 447 -14.174 13.781 -8.126 1.00 35.34 N
ATOM 3389 CA LEU A 447 -13.314 13.454 -9.268 1.00 36.91 C
ATOM 3390 C LEU A 447 -13.260 11.975 -9.649 1.00 36.96 C
ATOM 3391 O LEU A 447 -12.540 11.608 -10.574 1.00 35.65 O
ATOM 3392 CB LEU A 447 -11.884 13.929 -9.003 1.00 38.64 C
ATOM 3393 CG LEU A 447 -11.569 15.409 -9.161 1.00 42.94 C
ATOM 3394 CD1 LEU A 447 -10.190 15.677 -8.566 1.00 43.37 C
ATOM 3395 CD2 LEU A 447 -11.635 15.812 -10.631 1.00 41.53 C
ATOM 3396 N ARG A 448 -14.007 11.119 -8.948 1.00 37.34 N
ATOM 3397 CA ARG A 448 -13.972 9.679 -9.246 1.00 36.60 C
ATOM 3398 C ARG A 448 -12.541 9.120 -9.118 1.00 34.67 C
ATOM 3399 O ARG A 448 -12.061 8.360 -9.960 1.00 33.63 O
ATOM 3400 CB ARG A 448 -14.568 9.373 -10.635 1.00 36.67 C
ATOM 3401 CG ARG A 448 -16.048 9.708 -10.804 1.00 39.93 C
ATOM 3402 CD ARG A 448 -16.307 11.145 -11.257 1.00 42.56 C
ATOM 3403 NE ARG A 448 -15.678 11.451 -12.546 1.00 44.87 N
ATOM 3404 CZ ARG A 448 -15.577 12.672 -13.076 1.00 46.15 C
ATOM 3405 NH1 ARG A 448 -16.063 13.729 -12.439 1.00 45.04 N
ATOM 3406 NH2 ARG A 448 -14.975 12.840 -14.248 1.00 47.34 N
ATOM 3407 N VAL A 449 -11.868 9.519 -8.045 1.00 33.85 N
ATOM 3408 CA VAL A 449 -10.580 8.960 -7.672 1.00 34.08 C
ATOM 3409 C VAL A 449 -10.726 7.453 -7.416 1.00 34.40 C
ATOM 3410 O VAL A 449 -9.832 6.658 -7.747 1.00 31.66 O
ATOM 3411 CB VAL A 449 -10.011 9.705 -6.445 1.00 34.15 C
ATOM 3412 CG1 VAL A 449 -8.728 9.058 -5.935 1.00 34.81 C
ATOM 3413 CG2 VAL A 449 -9.771 11.176 -6.789 1.00 34.86 C
ATOM 3414 N PHE A 450 -11.868 7.059 -6.852 1.00 32.75 N
ATOM 3415 CA PHE A 450 -12.140 5.641 -6.621 1.00 32.41 C
ATOM 3416 C PHE A 450 -13.117 5.093 -7.638 1.00 32.54 C
ATOM 3417 O PHE A 450 -14.206 5.633 -7.840 1.00 32.49 O
ATOM 3418 CB PHE A 450 -12.577 5.383 -5.175 1.00 31.82 C
ATOM 3419 CG PHE A 450 -11.549 5.814 -4.168 1.00 30.88 C
ATOM 3420 CD1 PHE A 450 -10.438 5.030 -3.918 1.00 31.18 C
ATOM 3421 CD2 PHE A 450 -11.669 7.030 -3.518 1.00 30.24 C
ATOM 3422 CE1 PHE A 450 -9.476 5.435 -3.012 1.00 31.01 C
ATOM 3423 CE2 PHE A 450 -10.709 7.447 -2.613 1.00 31.10 C
ATOM 3424 CZ PHE A 450 -9.615 6.648 -2.355 1.00 31.08 C
ATOM 3425 N ALA A 451 -12.688 4.027 -8.302 1.00 32.35 N
ATOM 3426 CA ALA A 451 -13.415 3.473 -9.419 1.00 31.88 C
ATOM 3427 C ALA A 451 -13.024 2.026 -9.578 1.00 31.42 C
ATOM 3428 O ALA A 451 -11.907 1.636 -9.239 1.00 33.26 O
ATOM 3429 CB ALA A 451 -13.096 4.250 -10.689 1.00 33.28 C
ATOM 3430 N SER A 452 -13.947 1.231 -10.105 1.00 30.13 N
ATOM 3431 CA SER A 452 -13.711 -0.185 -10.332 1.00 29.12 C
ATOM 3432 C SER A 452 -14.495 -0.648 -11.552 1.00 29.19 C
ATOM 3433 O SER A 452 -15.356 0.074 -12.059 1.00 32.08 O
ATOM 3434 CB SER A 452 -14.172 -0.976 -9.110 1.00 28.52 C
ATOM 3435 OG SER A 452 -15.577 -0.854 -8.972 1.00 27.91 O
ATOM 3436 N ASP A 453 -14.216 -1.858 -12.016 1.00 27.75 N
ATOM 3437 CA ASP A 453 -15.018 -2.449 -13.080 1.00 28.08 C
ATOM 3438 C ASP A 453 -16.510 -2.543 -12.705 1.00 27.37 C
ATOM 3439 O ASP A 453 -17.382 -2.270 -13.534 1.00 24.02 O
ATOM 3440 CB ASP A 453 -14.454 -3.813 -13.467 1.00 28.98 C
ATOM 3441 CG ASP A 453 -13.098 -3.699 -14.139 1.00 30.20 C
ATOM 3442 OD1 ASP A 453 -12.595 -2.564 -14.289 1.00 32.12 O
ATOM 3443 OD2 ASP A 453 -12.540 -4.732 -14.530 1.00 32.66 O
ATOM 3444 N MET A 454 -16.795 -2.907 -11.458 1.00 26.12 N
ATOM 3445 CA MET A 454 -18.191 -2.941 -11.011 1.00 27.66 C
ATOM 3446 C MET A 454 -18.833 -1.560 -11.044 1.00 26.94 C
ATOM 3447 O MET A 454 -19.967 -1.412 -11.519 1.00 29.35 O
ATOM 3448 CB MET A 454 -18.341 -3.557 -9.616 1.00 27.85 C
ATOM 3449 CG MET A 454 -19.804 -3.596 -9.171 1.00 29.74 C
ATOM 3450 SD MET A 454 -20.035 -4.464 -7.621 1.00 31.34 S
ATOM 3451 CE MET A 454 -19.732 -6.163 -8.148 1.00 32.58 C
ATOM 3452 N ALA A 455 -18.121 -0.555 -10.534 1.00 26.60 N
ATOM 3453 CA ALA A 455 -18.625 0.821 -10.551 1.00 26.76 C
ATOM 3454 C ALA A 455 -19.054 1.245 -11.952 1.00 26.96 C
ATOM 3455 O ALA A 455 -20.114 1.852 -12.123 1.00 25.63 O
ATOM 3456 CB ALA A 455 -17.601 1.795 -9.987 1.00 26.17 C
ATOM 3457 N ARG A 456 -18.241 0.906 -12.950 1.00 26.22 N
ATOM 3458 CA ARG A 456 -18.542 1.258 -14.345 1.00 29.31 C
ATOM 3459 C ARG A 456 -19.714 0.455 -14.926 1.00 28.91 C
ATOM 3460 O ARG A 456 -20.598 1.016 -15.560 1.00 30.28 O
ATOM 3461 CB ARG A 456 -17.272 1.176 -15.231 1.00 30.44 C
ATOM 3462 CG ARG A 456 -16.248 2.273 -14.917 1.00 31.23 C
ATOM 3463 CD ARG A 456 -14.995 2.228 -15.793 1.00 32.41 C
ATOM 3464 NE ARG A 456 -14.113 1.129 -15.405 1.00 34.93 N
ATOM 3465 CZ ARG A 456 -13.090 1.240 -14.559 1.00 34.37 C
ATOM 3466 NH1 ARG A 456 -12.770 2.410 -14.017 1.00 34.27 N
ATOM 3467 NH2 ARG A 456 -12.367 0.174 -14.273 1.00 36.28 N
ATOM 3468 N ARG A 457 -19.738 -0.851 -14.678 1.00 28.49 N
ATOM 3469 CA ARG A 457 -20.819 -1.719 -15.153 1.00 27.61 C
ATOM 3470 C ARG A 457 -22.195 -1.380 -14.523 1.00 26.50 C
ATOM 3471 O ARG A 457 -23.222 -1.353 -15.221 1.00 25.26 O
ATOM 3472 CB ARG A 457 -20.439 -3.183 -14.883 1.00 27.83 C
ATOM 3473 CG ARG A 457 -21.452 -4.223 -15.326 1.00 28.73 C
ATOM 3474 CD ARG A 457 -20.879 -5.631 -15.176 1.00 30.02 C
ATOM 3475 NE ARG A 457 -20.455 -5.902 -13.800 1.00 30.95 N
ATOM 3476 CZ ARG A 457 -21.259 -6.371 -12.850 1.00 30.88 C
ATOM 3477 NH1 ARG A 457 -22.534 -6.630 -13.124 1.00 30.33 N
ATOM 3478 NH2 ARG A 457 -20.789 -6.581 -11.623 1.00 31.87 N
ATOM 3479 N LEU A 458 -22.208 -1.123 -13.216 1.00 25.54 N
ATOM 3480 CA LEU A 458 -23.464 -0.841 -12.466 1.00 24.51 C
ATOM 3481 C LEU A 458 -23.778 0.665 -12.348 1.00 26.07 C
ATOM 3482 O LEU A 458 -24.729 1.087 -11.647 1.00 25.11 O
ATOM 3483 CB LEU A 458 -23.413 -1.518 -11.088 1.00 24.01 C
ATOM 3484 CG LEU A 458 -23.274 -3.053 -11.072 1.00 23.85 C
ATOM 3485 CD1 LEU A 458 -23.223 -3.595 -9.645 1.00 23.84 C
ATOM 3486 CD2 LEU A 458 -24.378 -3.748 -11.853 1.00 23.74 C
ATOM 3487 N GLU A 459 -22.989 1.469 -13.059 1.00 27.02 N
ATOM 3488 CA GLU A 459 -23.125 2.928 -13.080 1.00 27.67 C
ATOM 3489 C GLU A 459 -23.251 3.498 -11.674 1.00 28.08 C
ATOM 3490 O GLU A 459 -24.188 4.219 -11.349 1.00 28.22 O
ATOM 3491 CB GLU A 459 -24.253 3.378 -14.026 1.00 28.36 C
ATOM 3492 CG GLU A 459 -24.034 2.879 -15.449 1.00 29.01 C
ATOM 3493 CD GLU A 459 -25.203 3.107 -16.391 1.00 30.60 C
ATOM 3494 OE1 GLU A 459 -25.964 4.084 -16.219 1.00 30.81 O
ATOM 3495 OE2 GLU A 459 -25.350 2.297 -17.329 1.00 31.72 O
ATOM 3496 N LEU A 460 -22.292 3.115 -10.839 1.00 29.77 N
ATOM 3497 CA LEU A 460 -22.141 3.646 -9.496 1.00 31.47 C
ATOM 3498 C LEU A 460 -21.025 4.677 -9.484 1.00 36.26 C
ATOM 3499 O LEU A 460 -20.854 5.400 -8.505 1.00 36.74 O
ATOM 3500 CB LEU A 460 -21.797 2.522 -8.529 1.00 29.06 C
ATOM 3501 CG LEU A 460 -22.841 1.417 -8.402 1.00 28.74 C
ATOM 3502 CD1 LEU A 460 -22.317 0.396 -7.421 1.00 29.39 C
ATOM 3503 CD2 LEU A 460 -24.182 1.985 -7.947 1.00 27.99 C
ATOM 3504 N LEU A 461 -20.263 4.716 -10.579 1.00 40.23 N
ATOM 3505 CA LEU A 461 -19.096 5.592 -10.708 1.00 44.59 C
ATOM 3506 C LEU A 461 -19.469 7.056 -10.513 1.00 45.60 C
ATOM 3507 O LEU A 461 -18.754 7.777 -9.824 1.00 47.32 O
ATOM 3508 CB LEU A 461 -18.430 5.386 -12.071 1.00 44.71 C
ATOM 3509 CG LEU A 461 -17.081 6.052 -12.360 1.00 48.06 C
ATOM 3510 CD1 LEU A 461 -15.978 5.368 -11.572 1.00 48.26 C
ATOM 3511 CD2 LEU A 461 -16.767 6.032 -13.854 1.00 46.83 C
ATOM 3512 OXT LEU A 461 -20.489 7.545 -11.016 1.00 48.46 O
TER 3513 LEU A 461
ATOM 3514 N THR B 7 -16.855 -22.011 52.342 1.00 80.16 N
ATOM 3515 CA THR B 7 -16.160 -21.378 51.178 1.00 80.93 C
ATOM 3516 C THR B 7 -14.754 -21.960 50.921 1.00 81.42 C
ATOM 3517 O THR B 7 -14.329 -22.071 49.769 1.00 83.59 O
ATOM 3518 CB THR B 7 -16.136 -19.827 51.287 1.00 81.92 C
ATOM 3519 OG1 THR B 7 -15.495 -19.263 50.134 1.00 81.92 O
ATOM 3520 CG2 THR B 7 -15.422 -19.348 52.561 1.00 80.76 C
ATOM 3521 N THR B 8 -14.049 -22.338 51.988 1.00 79.67 N
ATOM 3522 CA THR B 8 -12.685 -22.877 51.873 1.00 77.13 C
ATOM 3523 C THR B 8 -12.632 -24.396 52.069 1.00 74.72 C
ATOM 3524 O THR B 8 -13.519 -24.981 52.690 1.00 75.92 O
ATOM 3525 CB THR B 8 -11.703 -22.198 52.860 1.00 78.59 C
ATOM 3526 OG1 THR B 8 -12.033 -22.559 54.208 1.00 81.27 O
ATOM 3527 CG2 THR B 8 -11.737 -20.676 52.714 1.00 76.85 C
ATOM 3528 N THR B 9 -11.588 -25.023 51.529 1.00 72.26 N
ATOM 3529 CA THR B 9 -11.369 -26.463 51.663 1.00 69.73 C
ATOM 3530 C THR B 9 -10.049 -26.725 52.385 1.00 70.45 C
ATOM 3531 O THR B 9 -9.003 -26.199 51.991 1.00 70.88 O
ATOM 3532 CB THR B 9 -11.362 -27.162 50.282 1.00 68.76 C
ATOM 3533 OG1 THR B 9 -12.653 -27.038 49.675 1.00 69.06 O
ATOM 3534 CG2 THR B 9 -11.014 -28.645 50.403 1.00 66.59 C
ATOM 3535 N ALA B 10 -10.103 -27.524 53.450 1.00 68.26 N
ATOM 3536 CA ALA B 10 -8.895 -27.961 54.144 1.00 65.70 C
ATOM 3537 C ALA B 10 -8.130 -28.916 53.229 1.00 64.02 C
ATOM 3538 O ALA B 10 -8.653 -29.961 52.844 1.00 63.76 O
ATOM 3539 CB ALA B 10 -9.244 -28.627 55.469 1.00 64.50 C
ATOM 3540 N THR B 11 -6.905 -28.542 52.859 1.00 62.40 N
ATOM 3541 CA THR B 11 -6.128 -29.318 51.886 1.00 60.98 C
ATOM 3542 C THR B 11 -4.685 -29.551 52.327 1.00 61.03 C
ATOM 3543 O THR B 11 -4.036 -28.652 52.876 1.00 59.40 O
ATOM 3544 CB THR B 11 -6.120 -28.654 50.488 1.00 59.30 C
ATOM 3545 OG1 THR B 11 -7.390 -28.046 50.223 1.00 57.90 O
ATOM 3546 CG2 THR B 11 -5.818 -29.678 49.399 1.00 58.79 C
ATOM 3547 N ARG B 12 -4.205 -30.770 52.073 1.00 61.78 N
ATOM 3548 CA ARG B 12 -2.812 -31.155 52.284 1.00 63.15 C
ATOM 3549 C ARG B 12 -1.969 -30.667 51.105 1.00 62.99 C
ATOM 3550 O ARG B 12 -2.123 -31.141 49.975 1.00 62.35 O
ATOM 3551 CB ARG B 12 -2.704 -32.676 52.428 1.00 64.67 C
ATOM 3552 CG ARG B 12 -1.340 -33.184 52.866 1.00 69.73 C
ATOM 3553 CD ARG B 12 -1.234 -34.688 52.653 1.00 72.87 C
ATOM 3554 NE ARG B 12 0.149 -35.167 52.679 1.00 74.54 N
ATOM 3555 CZ ARG B 12 1.013 -35.045 51.672 1.00 76.35 C
ATOM 3556 NH1 ARG B 12 0.651 -34.441 50.545 1.00 78.56 N
ATOM 3557 NH2 ARG B 12 2.249 -35.514 51.794 1.00 74.99 N
ATOM 3558 N LEU B 13 -1.080 -29.718 51.373 1.00 61.50 N
ATOM 3559 CA LEU B 13 -0.289 -29.095 50.315 1.00 60.36 C
ATOM 3560 C LEU B 13 1.197 -29.394 50.444 1.00 60.39 C
ATOM 3561 O LEU B 13 1.720 -29.503 51.557 1.00 59.26 O
ATOM 3562 CB LEU B 13 -0.502 -27.578 50.314 1.00 58.21 C
ATOM 3563 CG LEU B 13 -1.912 -27.052 50.046 1.00 58.78 C
ATOM 3564 CD1 LEU B 13 -2.005 -25.582 50.430 1.00 57.52 C
ATOM 3565 CD2 LEU B 13 -2.309 -27.268 48.592 1.00 59.08 C
ATOM 3566 N THR B 14 1.865 -29.529 49.299 1.00 58.40 N
ATOM 3567 CA THR B 14 3.333 -29.553 49.241 1.00 59.19 C
ATOM 3568 C THR B 14 3.835 -28.663 48.096 1.00 58.87 C
ATOM 3569 O THR B 14 3.049 -28.206 47.263 1.00 57.06 O
ATOM 3570 CB THR B 14 3.907 -30.980 49.051 1.00 58.64 C
ATOM 3571 OG1 THR B 14 3.684 -31.423 47.705 1.00 57.23 O
ATOM 3572 CG2 THR B 14 3.294 -31.976 50.036 1.00 57.51 C
ATOM 3573 N GLY B 15 5.143 -28.421 48.057 1.00 58.66 N
ATOM 3574 CA GLY B 15 5.771 -27.830 46.879 1.00 55.88 C
ATOM 3575 C GLY B 15 5.887 -28.875 45.781 1.00 57.99 C
ATOM 3576 O GLY B 15 5.412 -30.007 45.935 1.00 56.54 O
ATOM 3577 N TRP B 16 6.520 -28.497 44.671 1.00 57.00 N
ATOM 3578 CA TRP B 16 6.748 -29.410 43.548 1.00 55.01 C
ATOM 3579 C TRP B 16 7.646 -30.547 43.948 1.00 56.05 C
ATOM 3580 O TRP B 16 7.541 -31.651 43.408 1.00 57.31 O
ATOM 3581 CB TRP B 16 7.341 -28.662 42.354 1.00 52.37 C
ATOM 3582 CG TRP B 16 7.218 -29.411 41.045 1.00 49.88 C
ATOM 3583 CD1 TRP B 16 8.230 -30.045 40.327 1.00 47.78 C
ATOM 3584 CD2 TRP B 16 5.996 -29.631 40.252 1.00 48.16 C
ATOM 3585 NE1 TRP B 16 7.734 -30.620 39.182 1.00 45.78 N
ATOM 3586 CE2 TRP B 16 6.405 -30.411 39.076 1.00 47.26 C
ATOM 3587 CE3 TRP B 16 4.658 -29.274 40.394 1.00 48.16 C
ATOM 3588 CZ2 TRP B 16 5.494 -30.807 38.101 1.00 48.27 C
ATOM 3589 CZ3 TRP B 16 3.750 -29.681 39.405 1.00 48.14 C
ATOM 3590 CH2 TRP B 16 4.161 -30.427 38.286 1.00 47.37 C
ATOM 3591 N GLY B 17 8.532 -30.283 44.909 1.00 57.16 N
ATOM 3592 CA GLY B 17 9.439 -31.296 45.450 1.00 59.80 C
ATOM 3593 C GLY B 17 8.745 -32.437 46.180 1.00 60.51 C
ATOM 3594 O GLY B 17 9.380 -33.442 46.500 1.00 57.80 O
ATOM 3595 N ARG B 18 7.444 -32.280 46.444 1.00 63.18 N
ATOM 3596 CA ARG B 18 6.641 -33.308 47.114 1.00 66.58 C
ATOM 3597 C ARG B 18 7.266 -33.637 48.479 1.00 67.59 C
ATOM 3598 O ARG B 18 7.578 -34.790 48.789 1.00 70.93 O
ATOM 3599 CB ARG B 18 6.493 -34.545 46.205 1.00 69.32 C
ATOM 3600 CG ARG B 18 5.748 -35.743 46.784 1.00 73.65 C
ATOM 3601 CD ARG B 18 4.268 -35.472 46.998 1.00 75.50 C
ATOM 3602 NE ARG B 18 3.516 -36.714 47.177 1.00 77.95 N
ATOM 3603 CZ ARG B 18 2.348 -36.805 47.810 1.00 78.29 C
ATOM 3604 NH1 ARG B 18 1.788 -35.726 48.344 1.00 76.21 N
ATOM 3605 NH2 ARG B 18 1.740 -37.980 47.916 1.00 77.93 N
ATOM 3606 N THR B 19 7.463 -32.591 49.277 1.00 65.52 N
ATOM 3607 CA THR B 19 8.095 -32.705 50.586 1.00 64.80 C
ATOM 3608 C THR B 19 7.446 -31.728 51.570 1.00 63.18 C
ATOM 3609 O THR B 19 6.771 -30.783 51.156 1.00 62.07 O
ATOM 3610 CB THR B 19 9.628 -32.472 50.498 1.00 66.63 C
ATOM 3611 OG1 THR B 19 10.275 -33.064 51.630 1.00 68.98 O
ATOM 3612 CG2 THR B 19 9.977 -30.975 50.425 1.00 65.50 C
ATOM 3613 N ALA B 20 7.656 -31.974 52.864 1.00 62.05 N
ATOM 3614 CA ALA B 20 7.128 -31.143 53.959 1.00 60.51 C
ATOM 3615 C ALA B 20 5.632 -30.779 53.839 1.00 59.59 C
ATOM 3616 O ALA B 20 5.291 -29.595 53.714 1.00 58.58 O
ATOM 3617 CB ALA B 20 7.988 -29.892 54.147 1.00 58.87 C
ATOM 3618 N PRO B 21 4.735 -31.793 53.894 1.00 59.34 N
ATOM 3619 CA PRO B 21 3.293 -31.538 53.749 1.00 58.95 C
ATOM 3620 C PRO B 21 2.748 -30.590 54.811 1.00 59.70 C
ATOM 3621 O PRO B 21 3.296 -30.518 55.916 1.00 58.28 O
ATOM 3622 CB PRO B 21 2.662 -32.928 53.908 1.00 60.35 C
ATOM 3623 CG PRO B 21 3.696 -33.764 54.583 1.00 58.75 C
ATOM 3624 CD PRO B 21 5.016 -33.225 54.120 1.00 59.09 C
ATOM 3625 N SER B 22 1.675 -29.877 54.470 1.00 60.79 N
ATOM 3626 CA SER B 22 1.085 -28.872 55.354 1.00 62.23 C
ATOM 3627 C SER B 22 -0.396 -28.646 55.040 1.00 62.53 C
ATOM 3628 O SER B 22 -0.753 -28.317 53.905 1.00 63.40 O
ATOM 3629 CB SER B 22 1.857 -27.557 55.235 1.00 63.28 C
ATOM 3630 OG SER B 22 1.362 -26.584 56.132 1.00 65.18 O
ATOM 3631 N VAL B 23 -1.245 -28.817 56.055 1.00 62.78 N
ATOM 3632 CA VAL B 23 -2.703 -28.710 55.901 1.00 61.03 C
ATOM 3633 C VAL B 23 -3.175 -27.264 56.025 1.00 59.51 C
ATOM 3634 O VAL B 23 -2.987 -26.621 57.064 1.00 58.67 O
ATOM 3635 CB VAL B 23 -3.473 -29.586 56.921 1.00 61.14 C
ATOM 3636 CG1 VAL B 23 -4.948 -29.685 56.539 1.00 61.09 C
ATOM 3637 CG2 VAL B 23 -2.857 -30.975 57.018 1.00 60.98 C
ATOM 3638 N ALA B 24 -3.798 -26.764 54.961 1.00 56.81 N
ATOM 3639 CA ALA B 24 -4.259 -25.383 54.922 1.00 54.66 C
ATOM 3640 C ALA B 24 -5.693 -25.248 54.425 1.00 53.75 C
ATOM 3641 O ALA B 24 -6.205 -26.104 53.702 1.00 54.46 O
ATOM 3642 CB ALA B 24 -3.327 -24.545 54.063 1.00 55.17 C
ATOM 3643 N ASN B 25 -6.336 -24.160 54.824 1.00 52.19 N
ATOM 3644 CA ASN B 25 -7.607 -23.785 54.232 1.00 55.82 C
ATOM 3645 C ASN B 25 -7.358 -23.153 52.864 1.00 54.35 C
ATOM 3646 O ASN B 25 -6.663 -22.143 52.755 1.00 55.27 O
ATOM 3647 CB ASN B 25 -8.374 -22.833 55.151 1.00 55.52 C
ATOM 3648 CG ASN B 25 -8.649 -23.434 56.523 1.00 59.39 C
ATOM 3649 OD1 ASN B 25 -8.794 -24.655 56.673 1.00 57.25 O
ATOM 3650 ND2 ASN B 25 -8.727 -22.573 57.534 1.00 59.39 N
ATOM 3651 N VAL B 26 -7.915 -23.772 51.828 1.00 53.19 N
ATOM 3652 CA VAL B 26 -7.733 -23.317 50.449 1.00 53.90 C
ATOM 3653 C VAL B 26 -8.989 -22.640 49.889 1.00 53.71 C
ATOM 3654 O VAL B 26 -10.052 -23.262 49.765 1.00 53.15 O
ATOM 3655 CB VAL B 26 -7.275 -24.473 49.526 1.00 51.99 C
ATOM 3656 CG1 VAL B 26 -7.262 -24.039 48.066 1.00 51.79 C
ATOM 3657 CG2 VAL B 26 -5.898 -24.967 49.948 1.00 52.30 C
ATOM 3658 N LEU B 27 -8.853 -21.357 49.567 1.00 54.18 N
ATOM 3659 CA LEU B 27 -9.893 -20.617 48.868 1.00 52.13 C
ATOM 3660 C LEU B 27 -9.626 -20.681 47.370 1.00 52.82 C
ATOM 3661 O LEU B 27 -8.504 -20.418 46.919 1.00 51.04 O
ATOM 3662 CB LEU B 27 -9.931 -19.166 49.349 1.00 53.07 C
ATOM 3663 CG LEU B 27 -10.930 -18.211 48.694 1.00 54.03 C
ATOM 3664 CD1 LEU B 27 -12.361 -18.713 48.838 1.00 55.81 C
ATOM 3665 CD2 LEU B 27 -10.783 -16.817 49.283 1.00 53.46 C
ATOM 3666 N ARG B 28 -10.652 -21.040 46.602 1.00 52.28 N
ATOM 3667 CA ARG B 28 -10.503 -21.178 45.153 1.00 54.52 C
ATOM 3668 C ARG B 28 -11.679 -20.560 44.400 1.00 54.58 C
ATOM 3669 O ARG B 28 -12.669 -21.233 44.105 1.00 55.51 O
ATOM 3670 CB ARG B 28 -10.311 -22.644 44.762 1.00 55.56 C
ATOM 3671 CG ARG B 28 -9.818 -22.812 43.341 1.00 59.50 C
ATOM 3672 CD ARG B 28 -10.053 -24.211 42.806 1.00 61.27 C
ATOM 3673 NE ARG B 28 -10.007 -24.212 41.345 1.00 66.35 N
ATOM 3674 CZ ARG B 28 -8.890 -24.248 40.621 1.00 68.07 C
ATOM 3675 NH1 ARG B 28 -7.702 -24.291 41.212 1.00 67.38 N
ATOM 3676 NH2 ARG B 28 -8.961 -24.240 39.296 1.00 71.44 N
ATOM 3677 N THR B 29 -11.550 -19.279 44.078 1.00 52.58 N
ATOM 3678 CA THR B 29 -12.646 -18.527 43.482 1.00 53.53 C
ATOM 3679 C THR B 29 -12.181 -17.634 42.319 1.00 52.82 C
ATOM 3680 O THR B 29 -11.103 -17.042 42.387 1.00 53.34 O
ATOM 3681 CB THR B 29 -13.367 -17.681 44.556 1.00 54.16 C
ATOM 3682 OG1 THR B 29 -14.410 -16.909 43.950 1.00 56.76 O
ATOM 3683 CG2 THR B 29 -12.385 -16.745 45.276 1.00 53.01 C
ATOM 3684 N PRO B 30 -12.982 -17.552 41.236 1.00 51.67 N
ATOM 3685 CA PRO B 30 -12.700 -16.532 40.217 1.00 49.52 C
ATOM 3686 C PRO B 30 -13.213 -15.154 40.637 1.00 49.94 C
ATOM 3687 O PRO B 30 -13.072 -14.179 39.898 1.00 50.41 O
ATOM 3688 CB PRO B 30 -13.444 -17.045 38.980 1.00 49.77 C
ATOM 3689 CG PRO B 30 -14.507 -17.948 39.508 1.00 49.90 C
ATOM 3690 CD PRO B 30 -13.980 -18.540 40.783 1.00 51.47 C
ATOM 3691 N ASP B 31 -13.785 -15.080 41.833 1.00 51.88 N
ATOM 3692 CA ASP B 31 -14.391 -13.857 42.340 1.00 54.78 C
ATOM 3693 C ASP B 31 -13.374 -13.041 43.138 1.00 55.53 C
ATOM 3694 O ASP B 31 -13.028 -13.396 44.269 1.00 55.73 O
ATOM 3695 CB ASP B 31 -15.603 -14.221 43.207 1.00 58.34 C
ATOM 3696 CG ASP B 31 -16.566 -13.071 43.397 1.00 58.84 C
ATOM 3697 OD1 ASP B 31 -16.145 -11.897 43.327 1.00 59.40 O
ATOM 3698 OD2 ASP B 31 -17.760 -13.353 43.637 1.00 63.38 O
ATOM 3699 N ALA B 32 -12.903 -11.946 42.543 1.00 55.62 N
ATOM 3700 CA ALA B 32 -11.897 -11.084 43.168 1.00 56.86 C
ATOM 3701 C ALA B 32 -12.431 -10.419 44.432 1.00 58.84 C
ATOM 3702 O ALA B 32 -11.670 -10.122 45.355 1.00 58.58 O
ATOM 3703 CB ALA B 32 -11.398 -10.039 42.182 1.00 54.91 C
ATOM 3704 N GLU B 33 -13.745 -10.202 44.457 1.00 60.39 N
ATOM 3705 CA GLU B 33 -14.450 -9.645 45.607 1.00 61.70 C
ATOM 3706 C GLU B 33 -14.320 -10.566 46.823 1.00 59.02 C
ATOM 3707 O GLU B 33 -14.127 -10.099 47.948 1.00 55.49 O
ATOM 3708 CB GLU B 33 -15.928 -9.428 45.252 1.00 65.03 C
ATOM 3709 CG GLU B 33 -16.650 -8.415 46.126 1.00 72.19 C
ATOM 3710 CD GLU B 33 -16.014 -7.038 46.078 1.00 75.62 C
ATOM 3711 OE1 GLU B 33 -15.744 -6.473 47.161 1.00 77.39 O
ATOM 3712 OE2 GLU B 33 -15.777 -6.526 44.961 1.00 75.82 O
ATOM 3713 N MET B 34 -14.412 -11.871 46.573 1.00 58.18 N
ATOM 3714 CA MET B 34 -14.250 -12.901 47.593 1.00 59.09 C
ATOM 3715 C MET B 34 -12.842 -12.884 48.200 1.00 58.68 C
ATOM 3716 O MET B 34 -12.677 -12.993 49.420 1.00 57.40 O
ATOM 3717 CB MET B 34 -14.543 -14.276 46.984 1.00 61.21 C
ATOM 3718 CG MET B 34 -15.412 -15.185 47.837 1.00 66.72 C
ATOM 3719 SD MET B 34 -17.162 -14.739 47.750 1.00 74.99 S
ATOM 3720 CE MET B 34 -17.328 -13.573 49.103 1.00 66.76 C
ATOM 3721 N ILE B 35 -11.835 -12.736 47.343 1.00 56.83 N
ATOM 3722 CA ILE B 35 -10.438 -12.711 47.776 1.00 54.84 C
ATOM 3723 C ILE B 35 -10.191 -11.532 48.720 1.00 53.49 C
ATOM 3724 O ILE B 35 -9.488 -11.676 49.716 1.00 54.87 O
ATOM 3725 CB ILE B 35 -9.465 -12.717 46.568 1.00 54.80 C
ATOM 3726 CG1 ILE B 35 -9.617 -14.022 45.771 1.00 53.29 C
ATOM 3727 CG2 ILE B 35 -8.019 -12.542 47.017 1.00 53.78 C
ATOM 3728 CD1 ILE B 35 -9.003 -13.991 44.386 1.00 53.86 C
ATOM 3729 N VAL B 36 -10.797 -10.386 48.419 1.00 54.33 N
ATOM 3730 CA VAL B 36 -10.728 -9.210 49.293 1.00 55.99 C
ATOM 3731 C VAL B 36 -11.356 -9.484 50.667 1.00 58.50 C
ATOM 3732 O VAL B 36 -10.815 -9.058 51.691 1.00 59.76 O
ATOM 3733 CB VAL B 36 -11.380 -7.966 48.642 1.00 55.49 C
ATOM 3734 CG1 VAL B 36 -11.343 -6.765 49.582 1.00 55.09 C
ATOM 3735 CG2 VAL B 36 -10.685 -7.623 47.334 1.00 55.57 C
ATOM 3736 N LYS B 37 -12.480 -10.203 50.687 1.00 59.65 N
ATOM 3737 CA LYS B 37 -13.179 -10.506 51.948 1.00 61.17 C
ATOM 3738 C LYS B 37 -12.408 -11.495 52.816 1.00 58.53 C
ATOM 3739 O LYS B 37 -12.367 -11.345 54.035 1.00 59.27 O
ATOM 3740 CB LYS B 37 -14.615 -11.015 51.712 1.00 63.21 C
ATOM 3741 CG LYS B 37 -15.522 -10.096 50.897 1.00 67.96 C
ATOM 3742 CD LYS B 37 -15.446 -8.643 51.348 1.00 70.47 C
ATOM 3743 CE LYS B 37 -15.836 -7.700 50.221 1.00 74.43 C
ATOM 3744 NZ LYS B 37 -15.186 -6.366 50.370 1.00 76.52 N
ATOM 3745 N ALA B 38 -11.803 -12.500 52.183 1.00 57.37 N
ATOM 3746 CA ALA B 38 -11.028 -13.516 52.895 1.00 56.48 C
ATOM 3747 C ALA B 38 -9.820 -12.921 53.614 1.00 56.53 C
ATOM 3748 O ALA B 38 -9.494 -13.338 54.721 1.00 57.78 O
ATOM 3749 CB ALA B 38 -10.598 -14.619 51.948 1.00 55.72 C
ATOM 3750 N VAL B 39 -9.168 -11.943 52.986 1.00 56.97 N
ATOM 3751 CA VAL B 39 -8.070 -11.207 53.620 1.00 55.44 C
ATOM 3752 C VAL B 39 -8.571 -10.433 54.849 1.00 57.12 C
ATOM 3753 O VAL B 39 -7.991 -10.541 55.933 1.00 54.32 O
ATOM 3754 CB VAL B 39 -7.349 -10.271 52.617 1.00 55.10 C
ATOM 3755 CG1 VAL B 39 -6.361 -9.348 53.324 1.00 54.25 C
ATOM 3756 CG2 VAL B 39 -6.636 -11.088 51.549 1.00 52.97 C
ATOM 3757 N ALA B 40 -9.655 -9.675 54.681 1.00 57.45 N
ATOM 3758 CA ALA B 40 -10.269 -8.939 55.791 1.00 58.47 C
ATOM 3759 C ALA B 40 -10.670 -9.884 56.930 1.00 58.38 C
ATOM 3760 O ALA B 40 -10.499 -9.552 58.105 1.00 60.31 O
ATOM 3761 CB ALA B 40 -11.467 -8.136 55.304 1.00 57.21 C
ATOM 3762 N ARG B 41 -11.182 -11.059 56.563 1.00 58.38 N
ATOM 3763 CA ARG B 41 -11.518 -12.129 57.507 1.00 61.30 C
ATOM 3764 C ARG B 41 -10.301 -12.578 58.325 1.00 61.98 C
ATOM 3765 O ARG B 41 -10.402 -12.783 59.538 1.00 61.67 O
ATOM 3766 CB ARG B 41 -12.129 -13.318 56.754 1.00 64.51 C
ATOM 3767 CG ARG B 41 -12.655 -14.441 57.635 1.00 68.01 C
ATOM 3768 CD ARG B 41 -13.494 -15.422 56.833 1.00 71.45 C
ATOM 3769 NE ARG B 41 -14.091 -16.444 57.691 1.00 76.60 N
ATOM 3770 CZ ARG B 41 -14.963 -17.368 57.290 1.00 78.50 C
ATOM 3771 NH1 ARG B 41 -15.367 -17.421 56.024 1.00 79.61 N
ATOM 3772 NH2 ARG B 41 -15.435 -18.246 58.164 1.00 79.72 N
ATOM 3773 N VAL B 42 -9.159 -12.725 57.652 1.00 61.44 N
ATOM 3774 CA VAL B 42 -7.888 -13.052 58.304 1.00 58.83 C
ATOM 3775 C VAL B 42 -7.384 -11.860 59.123 1.00 58.96 C
ATOM 3776 O VAL B 42 -6.803 -12.040 60.193 1.00 60.17 O
ATOM 3777 CB VAL B 42 -6.826 -13.516 57.275 1.00 58.17 C
ATOM 3778 CG1 VAL B 42 -5.450 -13.653 57.914 1.00 57.07 C
ATOM 3779 CG2 VAL B 42 -7.240 -14.836 56.639 1.00 56.06 C
ATOM 3780 N ALA B 43 -7.633 -10.649 58.627 1.00 60.55 N
ATOM 3781 CA ALA B 43 -7.267 -9.416 59.336 1.00 64.66 C
ATOM 3782 C ALA B 43 -8.166 -9.114 60.547 1.00 70.99 C
ATOM 3783 O ALA B 43 -7.838 -8.251 61.369 1.00 72.02 O
ATOM 3784 CB ALA B 43 -7.249 -8.234 58.379 1.00 63.28 C
ATOM 3785 N GLU B 44 -9.299 -9.811 60.638 1.00 76.32 N
ATOM 3786 CA GLU B 44 -10.164 -9.764 61.822 1.00 78.86 C
ATOM 3787 C GLU B 44 -9.871 -10.956 62.742 1.00 79.63 C
ATOM 3788 O GLU B 44 -10.029 -10.866 63.963 1.00 75.96 O
ATOM 3789 CB GLU B 44 -11.643 -9.742 61.420 1.00 80.18 C
ATOM 3790 CG GLU B 44 -12.592 -9.441 62.575 1.00 83.61 C
ATOM 3791 CD GLU B 44 -14.046 -9.336 62.148 1.00 85.39 C
ATOM 3792 OE1 GLU B 44 -14.481 -10.117 61.272 1.00 85.76 O
ATOM 3793 OE2 GLU B 44 -14.758 -8.471 62.704 1.00 84.81 O
ATOM 3794 N SER B 45 -9.436 -12.063 62.141 1.00 81.88 N
ATOM 3795 CA SER B 45 -8.979 -13.246 62.874 1.00 84.51 C
ATOM 3796 C SER B 45 -7.886 -12.894 63.891 1.00 85.98 C
ATOM 3797 O SER B 45 -7.740 -13.566 64.914 1.00 87.75 O
ATOM 3798 CB SER B 45 -8.468 -14.305 61.891 1.00 84.03 C
ATOM 3799 OG SER B 45 -8.474 -15.598 62.468 1.00 85.26 O
ATOM 3800 N GLY B 46 -7.126 -11.838 63.600 1.00 86.87 N
ATOM 3801 CA GLY B 46 -6.102 -11.326 64.508 1.00 85.68 C
ATOM 3802 C GLY B 46 -4.682 -11.510 64.003 1.00 87.60 C
ATOM 3803 O GLY B 46 -3.724 -11.344 64.764 1.00 87.90 O
ATOM 3804 N GLY B 47 -4.544 -11.849 62.721 1.00 84.38 N
ATOM 3805 CA GLY B 47 -3.235 -12.084 62.114 1.00 79.69 C
ATOM 3806 C GLY B 47 -2.979 -13.557 61.867 1.00 76.79 C
ATOM 3807 O GLY B 47 -3.479 -14.119 60.891 1.00 74.41 O
ATOM 3808 N GLY B 48 -2.197 -14.178 62.754 1.00 75.97 N
ATOM 3809 CA GLY B 48 -1.906 -15.614 62.687 1.00 69.20 C
ATOM 3810 C GLY B 48 -3.204 -16.398 62.652 1.00 69.70 C
ATOM 3811 O GLY B 48 -4.132 -16.083 63.402 1.00 71.79 O
ATOM 3812 N ARG B 49 -3.288 -17.427 61.810 1.00 66.48 N
ATOM 3813 CA ARG B 49 -2.150 -18.001 61.088 1.00 64.55 C
ATOM 3814 C ARG B 49 -1.959 -17.473 59.654 1.00 60.29 C
ATOM 3815 O ARG B 49 -1.420 -18.176 58.795 1.00 59.63 O
ATOM 3816 CB ARG B 49 -2.293 -19.525 61.066 1.00 68.15 C
ATOM 3817 CG ARG B 49 -2.552 -20.151 62.430 1.00 70.42 C
ATOM 3818 CD ARG B 49 -1.258 -20.621 63.064 1.00 74.59 C
ATOM 3819 NE ARG B 49 -0.720 -21.785 62.361 1.00 77.83 N
ATOM 3820 CZ ARG B 49 0.574 -22.072 62.253 1.00 77.63 C
ATOM 3821 NH1 ARG B 49 1.491 -21.280 62.796 1.00 82.08 N
ATOM 3822 NH2 ARG B 49 0.956 -23.157 61.594 1.00 78.40 N
ATOM 3823 N GLY B 50 -2.409 -16.243 59.409 1.00 56.16 N
ATOM 3824 CA GLY B 50 -2.170 -15.538 58.147 1.00 51.96 C
ATOM 3825 C GLY B 50 -2.724 -16.158 56.873 1.00 48.22 C
ATOM 3826 O GLY B 50 -3.449 -17.152 56.903 1.00 45.55 O
ATOM 3827 N ALA B 51 -2.364 -15.556 55.744 1.00 47.68 N
ATOM 3828 CA ALA B 51 -2.754 -16.059 54.425 1.00 45.54 C
ATOM 3829 C ALA B 51 -1.573 -16.012 53.467 1.00 42.61 C
ATOM 3830 O ALA B 51 -0.684 -15.185 53.620 1.00 43.69 O
ATOM 3831 CB ALA B 51 -3.906 -15.237 53.870 1.00 45.05 C
ATOM 3832 N ILE B 52 -1.563 -16.899 52.479 1.00 42.46 N
ATOM 3833 CA ILE B 52 -0.582 -16.817 51.392 1.00 41.61 C
ATOM 3834 C ILE B 52 -1.220 -17.165 50.044 1.00 41.00 C
ATOM 3835 O ILE B 52 -2.035 -18.083 49.960 1.00 41.40 O
ATOM 3836 CB ILE B 52 0.657 -17.716 51.650 1.00 40.88 C
ATOM 3837 CG1 ILE B 52 1.834 -17.315 50.748 1.00 39.71 C
ATOM 3838 CG2 ILE B 52 0.330 -19.193 51.467 1.00 40.50 C
ATOM 3839 CD1 ILE B 52 2.571 -16.074 51.204 1.00 39.66 C
ATOM 3840 N ALA B 53 -0.836 -16.443 48.992 1.00 39.56 N
ATOM 3841 CA ALA B 53 -1.287 -16.788 47.647 1.00 38.12 C
ATOM 3842 C ALA B 53 -0.567 -18.033 47.152 1.00 37.48 C
ATOM 3843 O ALA B 53 0.571 -18.301 47.546 1.00 39.58 O
ATOM 3844 CB ALA B 53 -1.081 -15.622 46.685 1.00 35.83 C
ATOM 3845 N ARG B 54 -1.244 -18.796 46.301 1.00 35.71 N
ATOM 3846 CA ARG B 54 -0.643 -19.929 45.607 1.00 36.25 C
ATOM 3847 C ARG B 54 -0.927 -19.833 44.099 1.00 35.96 C
ATOM 3848 O ARG B 54 -2.029 -19.462 43.686 1.00 36.32 O
ATOM 3849 CB ARG B 54 -1.191 -21.236 46.174 1.00 35.14 C
ATOM 3850 CG ARG B 54 -0.636 -22.506 45.550 1.00 36.49 C
ATOM 3851 CD ARG B 54 -1.350 -23.721 46.128 1.00 37.22 C
ATOM 3852 NE ARG B 54 -0.747 -24.985 45.709 1.00 38.01 N
ATOM 3853 CZ ARG B 54 0.255 -25.590 46.341 1.00 38.32 C
ATOM 3854 NH1 ARG B 54 0.794 -25.044 47.425 1.00 39.71 N
ATOM 3855 NH2 ARG B 54 0.733 -26.736 45.878 1.00 39.26 N
ATOM 3856 N GLY B 55 0.072 -20.161 43.286 1.00 36.08 N
ATOM 3857 CA GLY B 55 -0.085 -20.173 41.835 1.00 34.31 C
ATOM 3858 C GLY B 55 -0.291 -21.593 41.365 1.00 36.40 C
ATOM 3859 O GLY B 55 -1.205 -22.271 41.828 1.00 36.56 O
ATOM 3860 N LEU B 56 0.570 -22.059 40.462 1.00 34.75 N
ATOM 3861 CA LEU B 56 0.460 -23.416 39.941 1.00 34.97 C
ATOM 3862 C LEU B 56 1.303 -24.433 40.716 1.00 36.10 C
ATOM 3863 O LEU B 56 1.450 -25.581 40.284 1.00 37.37 O
ATOM 3864 CB LEU B 56 0.803 -23.452 38.445 1.00 35.19 C
ATOM 3865 CG LEU B 56 -0.358 -23.206 37.476 1.00 36.10 C
ATOM 3866 CD1 LEU B 56 0.142 -22.700 36.132 1.00 35.51 C
ATOM 3867 CD2 LEU B 56 -1.211 -24.462 37.298 1.00 37.21 C
ATOM 3868 N GLY B 57 1.862 -24.003 41.849 1.00 36.73 N
ATOM 3869 CA GLY B 57 2.606 -24.891 42.754 1.00 36.20 C
ATOM 3870 C GLY B 57 3.900 -25.466 42.194 1.00 35.90 C
ATOM 3871 O GLY B 57 4.293 -26.572 42.557 1.00 34.66 O
ATOM 3872 N ARG B 58 4.576 -24.710 41.331 1.00 34.57 N
ATOM 3873 CA ARG B 58 5.827 -25.181 40.721 1.00 35.10 C
ATOM 3874 C ARG B 58 7.104 -24.924 41.530 1.00 33.91 C
ATOM 3875 O ARG B 58 8.140 -25.515 41.236 1.00 35.43 O
ATOM 3876 CB ARG B 58 5.984 -24.651 39.292 1.00 34.77 C
ATOM 3877 CG ARG B 58 5.567 -25.639 38.212 1.00 36.88 C
ATOM 3878 CD ARG B 58 4.100 -26.038 38.309 1.00 38.53 C
ATOM 3879 NE ARG B 58 3.733 -27.007 37.273 1.00 41.33 N
ATOM 3880 CZ ARG B 58 2.512 -27.511 37.105 1.00 41.68 C
ATOM 3881 NH1 ARG B 58 1.515 -27.157 37.907 1.00 42.11 N
ATOM 3882 NH2 ARG B 58 2.289 -28.376 36.130 1.00 43.96 N
ATOM 3883 N SER B 59 7.046 -24.046 42.530 1.00 34.54 N
ATOM 3884 CA SER B 59 8.159 -23.932 43.473 1.00 34.85 C
ATOM 3885 C SER B 59 8.295 -25.253 44.221 1.00 36.10 C
ATOM 3886 O SER B 59 7.288 -25.850 44.608 1.00 35.59 O
ATOM 3887 CB SER B 59 7.935 -22.799 44.465 1.00 33.98 C
ATOM 3888 OG SER B 59 7.822 -21.562 43.798 1.00 34.87 O
ATOM 3889 N TYR B 60 9.532 -25.701 44.415 1.00 37.01 N
ATOM 3890 CA TYR B 60 9.826 -27.010 45.017 1.00 40.19 C
ATOM 3891 C TYR B 60 9.631 -27.043 46.536 1.00 41.55 C
ATOM 3892 O TYR B 60 9.366 -28.102 47.107 1.00 43.55 O
ATOM 3893 CB TYR B 60 11.263 -27.432 44.699 1.00 40.89 C
ATOM 3894 CG TYR B 60 11.516 -27.831 43.265 1.00 43.49 C
ATOM 3895 CD1 TYR B 60 11.824 -29.153 42.938 1.00 44.91 C
ATOM 3896 CD2 TYR B 60 11.460 -26.890 42.229 1.00 45.50 C
ATOM 3897 CE1 TYR B 60 12.068 -29.526 41.626 1.00 45.71 C
ATOM 3898 CE2 TYR B 60 11.705 -27.251 40.909 1.00 45.07 C
ATOM 3899 CZ TYR B 60 12.007 -28.570 40.614 1.00 47.58 C
ATOM 3900 OH TYR B 60 12.248 -28.944 39.308 1.00 46.39 O
ATOM 3901 N GLY B 61 9.786 -25.890 47.180 1.00 41.85 N
ATOM 3902 CA GLY B 61 9.744 -25.802 48.639 1.00 43.45 C
ATOM 3903 C GLY B 61 8.398 -25.388 49.200 1.00 42.69 C
ATOM 3904 O GLY B 61 7.356 -25.736 48.654 1.00 42.16 O
ATOM 3905 N ASP B 62 8.438 -24.609 50.275 1.00 44.02 N
ATOM 3906 CA ASP B 62 7.272 -24.350 51.122 1.00 42.54 C
ATOM 3907 C ASP B 62 6.803 -22.893 51.125 1.00 41.46 C
ATOM 3908 O ASP B 62 6.226 -22.427 52.116 1.00 42.32 O
ATOM 3909 CB ASP B 62 7.589 -24.803 52.562 1.00 44.70 C
ATOM 3910 CG ASP B 62 8.852 -24.133 53.137 1.00 47.18 C
ATOM 3911 OD1 ASP B 62 9.604 -23.472 52.380 1.00 46.24 O
ATOM 3912 OD2 ASP B 62 9.094 -24.266 54.357 1.00 47.53 O
ATOM 3913 N ASN B 63 7.050 -22.164 50.038 1.00 40.55 N
ATOM 3914 CA ASN B 63 6.645 -20.752 49.983 1.00 38.67 C
ATOM 3915 C ASN B 63 5.177 -20.534 49.610 1.00 37.74 C
ATOM 3916 O ASN B 63 4.607 -19.488 49.923 1.00 36.67 O
ATOM 3917 CB ASN B 63 7.580 -19.912 49.094 1.00 38.00 C
ATOM 3918 CG ASN B 63 7.751 -20.484 47.701 1.00 38.21 C
ATOM 3919 OD1 ASN B 63 7.390 -21.630 47.436 1.00 38.57 O
ATOM 3920 ND2 ASN B 63 8.322 -19.682 46.800 1.00 35.99 N
ATOM 3921 N ALA B 64 4.576 -21.532 48.964 1.00 38.39 N
ATOM 3922 CA ALA B 64 3.185 -21.451 48.506 1.00 42.68 C
ATOM 3923 C ALA B 64 2.231 -22.298 49.353 1.00 45.10 C
ATOM 3924 O ALA B 64 1.206 -22.770 48.851 1.00 46.21 O
ATOM 3925 CB ALA B 64 3.084 -21.845 47.032 1.00 41.42 C
ATOM 3926 N GLN B 65 2.577 -22.492 50.628 1.00 46.04 N
ATOM 3927 CA GLN B 65 1.705 -23.186 51.583 1.00 47.50 C
ATOM 3928 C GLN B 65 1.750 -22.540 52.972 1.00 47.10 C
ATOM 3929 O GLN B 65 2.729 -21.877 53.330 1.00 46.72 O
ATOM 3930 CB GLN B 65 2.026 -24.684 51.645 1.00 46.97 C
ATOM 3931 CG GLN B 65 3.391 -25.028 52.212 1.00 47.90 C
ATOM 3932 CD GLN B 65 3.880 -26.388 51.752 1.00 49.84 C
ATOM 3933 OE1 GLN B 65 4.141 -26.598 50.570 1.00 52.94 O
ATOM 3934 NE2 GLN B 65 4.017 -27.316 52.688 1.00 51.45 N
ATOM 3935 N ASN B 66 0.680 -22.733 53.742 1.00 45.36 N
ATOM 3936 CA ASN B 66 0.523 -22.068 55.031 1.00 45.20 C
ATOM 3937 C ASN B 66 -0.264 -22.959 56.001 1.00 45.18 C
ATOM 3938 O ASN B 66 -1.475 -22.789 56.166 1.00 43.94 O
ATOM 3939 CB ASN B 66 -0.166 -20.710 54.825 1.00 44.05 C
ATOM 3940 CG ASN B 66 -0.211 -19.864 56.087 1.00 44.35 C
ATOM 3941 OD1 ASN B 66 0.483 -20.137 57.064 1.00 44.06 O
ATOM 3942 ND2 ASN B 66 -1.032 -18.816 56.063 1.00 44.25 N
ATOM 3943 N GLY B 67 0.436 -23.906 56.628 1.00 46.23 N
ATOM 3944 CA GLY B 67 -0.165 -24.866 57.567 1.00 48.08 C
ATOM 3945 C GLY B 67 -1.019 -24.229 58.642 1.00 48.30 C
ATOM 3946 O GLY B 67 -0.583 -23.299 59.322 1.00 49.35 O
ATOM 3947 N GLY B 68 -2.248 -24.720 58.778 1.00 50.14 N
ATOM 3948 CA GLY B 68 -3.196 -24.183 59.757 1.00 50.96 C
ATOM 3949 C GLY B 68 -3.672 -22.779 59.430 1.00 51.03 C
ATOM 3950 O GLY B 68 -4.269 -22.106 60.271 1.00 51.15 O
ATOM 3951 N GLY B 69 -3.410 -22.335 58.202 1.00 51.50 N
ATOM 3952 CA GLY B 69 -3.789 -20.995 57.776 1.00 49.57 C
ATOM 3953 C GLY B 69 -4.485 -20.987 56.433 1.00 49.32 C
ATOM 3954 O GLY B 69 -4.851 -22.042 55.904 1.00 48.36 O
ATOM 3955 N LEU B 70 -4.659 -19.788 55.882 1.00 49.45 N
ATOM 3956 CA LEU B 70 -5.302 -19.624 54.583 1.00 48.74 C
ATOM 3957 C LEU B 70 -4.300 -19.621 53.426 1.00 49.06 C
ATOM 3958 O LEU B 70 -3.245 -18.975 53.498 1.00 46.28 O
ATOM 3959 CB LEU B 70 -6.150 -18.349 54.550 1.00 48.59 C
ATOM 3960 CG LEU B 70 -6.971 -18.079 53.277 1.00 46.14 C
ATOM 3961 CD1 LEU B 70 -8.081 -19.104 53.089 1.00 44.66 C
ATOM 3962 CD2 LEU B 70 -7.532 -16.666 53.294 1.00 44.64 C
ATOM 3963 N VAL B 71 -4.659 -20.359 52.376 1.00 48.84 N
ATOM 3964 CA VAL B 71 -3.956 -20.377 51.099 1.00 47.57 C
ATOM 3965 C VAL B 71 -4.968 -20.044 50.003 1.00 47.88 C
ATOM 3966 O VAL B 71 -5.927 -20.792 49.789 1.00 48.40 O
ATOM 3967 CB VAL B 71 -3.331 -21.761 50.820 1.00 47.86 C
ATOM 3968 CG1 VAL B 71 -2.886 -21.883 49.367 1.00 47.77 C
ATOM 3969 CG2 VAL B 71 -2.162 -22.019 51.755 1.00 47.95 C
ATOM 3970 N ILE B 72 -4.764 -18.912 49.331 1.00 43.62 N
ATOM 3971 CA ILE B 72 -5.656 -18.484 48.255 1.00 43.17 C
ATOM 3972 C ILE B 72 -5.082 -18.885 46.893 1.00 43.94 C
ATOM 3973 O ILE B 72 -4.124 -18.273 46.409 1.00 42.55 O
ATOM 3974 CB ILE B 72 -5.938 -16.964 48.321 1.00 43.63 C
ATOM 3975 CG1 ILE B 72 -6.605 -16.608 49.653 1.00 43.47 C
ATOM 3976 CG2 ILE B 72 -6.798 -16.509 47.143 1.00 43.09 C
ATOM 3977 CD1 ILE B 72 -6.790 -15.122 49.881 1.00 44.23 C
ATOM 3978 N ASP B 73 -5.669 -19.928 46.301 1.00 42.59 N
ATOM 3979 CA ASP B 73 -5.335 -20.389 44.954 1.00 44.69 C
ATOM 3980 C ASP B 73 -5.783 -19.342 43.928 1.00 44.04 C
ATOM 3981 O ASP B 73 -6.978 -19.065 43.790 1.00 44.48 O
ATOM 3982 CB ASP B 73 -5.994 -21.750 44.684 1.00 44.93 C
ATOM 3983 CG ASP B 73 -5.697 -22.301 43.289 1.00 47.77 C
ATOM 3984 OD1 ASP B 73 -5.155 -21.580 42.423 1.00 47.76 O
ATOM 3985 OD2 ASP B 73 -6.020 -23.482 43.052 1.00 49.66 O
ATOM 3986 N MET B 74 -4.810 -18.769 43.221 1.00 42.89 N
ATOM 3987 CA MET B 74 -5.057 -17.650 42.314 1.00 40.93 C
ATOM 3988 C MET B 74 -5.330 -18.063 40.873 1.00 38.86 C
ATOM 3989 O MET B 74 -5.609 -17.207 40.034 1.00 40.57 O
ATOM 3990 CB MET B 74 -3.879 -16.663 42.343 1.00 42.60 C
ATOM 3991 CG MET B 74 -3.709 -15.919 43.656 1.00 42.56 C
ATOM 3992 SD MET B 74 -5.140 -14.916 44.079 1.00 44.05 S
ATOM 3993 CE MET B 74 -4.989 -13.590 42.882 1.00 43.41 C
ATOM 3994 N THR B 75 -5.251 -19.357 40.582 1.00 38.30 N
ATOM 3995 CA THR B 75 -5.389 -19.849 39.202 1.00 40.22 C
ATOM 3996 C THR B 75 -6.758 -19.582 38.527 1.00 43.13 C
ATOM 3997 O THR B 75 -6.813 -19.454 37.300 1.00 43.54 O
ATOM 3998 CB THR B 75 -5.021 -21.340 39.063 1.00 40.86 C
ATOM 3999 OG1 THR B 75 -5.885 -22.123 39.895 1.00 41.44 O
ATOM 4000 CG2 THR B 75 -3.563 -21.586 39.454 1.00 38.91 C
ATOM 4001 N PRO B 76 -7.864 -19.518 39.310 1.00 43.25 N
ATOM 4002 CA PRO B 76 -9.140 -19.141 38.685 1.00 42.47 C
ATOM 4003 C PRO B 76 -9.167 -17.695 38.189 1.00 41.44 C
ATOM 4004 O PRO B 76 -9.977 -17.359 37.328 1.00 39.91 O
ATOM 4005 CB PRO B 76 -10.149 -19.304 39.828 1.00 42.73 C
ATOM 4006 CG PRO B 76 -9.538 -20.343 40.704 1.00 43.86 C
ATOM 4007 CD PRO B 76 -8.075 -20.016 40.684 1.00 44.04 C
ATOM 4008 N LEU B 77 -8.300 -16.848 38.735 1.00 39.99 N
ATOM 4009 CA LEU B 77 -8.250 -15.453 38.318 1.00 39.95 C
ATOM 4010 C LEU B 77 -7.291 -15.350 37.131 1.00 38.75 C
ATOM 4011 O LEU B 77 -6.151 -14.921 37.280 1.00 38.66 O
ATOM 4012 CB LEU B 77 -7.818 -14.560 39.487 1.00 41.31 C
ATOM 4013 CG LEU B 77 -8.158 -13.071 39.433 1.00 44.36 C
ATOM 4014 CD1 LEU B 77 -9.587 -12.821 39.893 1.00 43.79 C
ATOM 4015 CD2 LEU B 77 -7.181 -12.266 40.276 1.00 45.27 C
ATOM 4016 N ASN B 78 -7.770 -15.757 35.957 1.00 35.65 N
ATOM 4017 CA ASN B 78 -6.911 -15.944 34.790 1.00 35.05 C
ATOM 4018 C ASN B 78 -7.367 -15.155 33.561 1.00 33.53 C
ATOM 4019 O ASN B 78 -7.202 -15.613 32.436 1.00 32.09 O
ATOM 4020 CB ASN B 78 -6.840 -17.433 34.440 1.00 34.09 C
ATOM 4021 CG ASN B 78 -8.181 -17.983 33.974 1.00 36.32 C
ATOM 4022 OD1 ASN B 78 -9.232 -17.366 34.192 1.00 34.82 O
ATOM 4023 ND2 ASN B 78 -8.151 -19.135 33.313 1.00 34.46 N
ATOM 4024 N THR B 79 -7.941 -13.975 33.775 1.00 32.95 N
ATOM 4025 CA THR B 79 -8.397 -13.153 32.661 1.00 33.41 C
ATOM 4026 C THR B 79 -7.257 -12.363 32.033 1.00 31.94 C
ATOM 4027 O THR B 79 -6.517 -11.665 32.730 1.00 31.41 O
ATOM 4028 CB THR B 79 -9.519 -12.181 33.087 1.00 34.43 C
ATOM 4029 OG1 THR B 79 -10.662 -12.938 33.488 1.00 36.21 O
ATOM 4030 CG2 THR B 79 -9.913 -11.250 31.937 1.00 35.54 C
ATOM 4031 N ILE B 80 -7.136 -12.480 30.714 1.00 31.98 N
ATOM 4032 CA ILE B 80 -6.298 -11.580 29.921 1.00 32.05 C
ATOM 4033 C ILE B 80 -7.144 -10.364 29.512 1.00 30.39 C
ATOM 4034 O ILE B 80 -8.020 -10.461 28.648 1.00 29.85 O
ATOM 4035 CB ILE B 80 -5.686 -12.303 28.688 1.00 33.21 C
ATOM 4036 CG1 ILE B 80 -4.729 -13.409 29.152 1.00 34.22 C
ATOM 4037 CG2 ILE B 80 -4.973 -11.310 27.779 1.00 33.93 C
ATOM 4038 CD1 ILE B 80 -4.287 -14.374 28.070 1.00 33.68 C
ATOM 4039 N HIS B 81 -6.885 -9.223 30.146 1.00 28.50 N
ATOM 4040 CA HIS B 81 -7.674 -8.016 29.911 1.00 28.89 C
ATOM 4041 C HIS B 81 -7.399 -7.365 28.582 1.00 28.38 C
ATOM 4042 O HIS B 81 -8.329 -7.010 27.849 1.00 27.82 O
ATOM 4043 CB HIS B 81 -7.475 -7.020 31.058 1.00 28.90 C
ATOM 4044 CG HIS B 81 -7.933 -7.547 32.393 1.00 29.91 C
ATOM 4045 ND1 HIS B 81 -9.231 -7.535 32.775 1.00 32.44 N
ATOM 4046 CD2 HIS B 81 -7.224 -8.141 33.430 1.00 30.26 C
ATOM 4047 CE1 HIS B 81 -9.344 -8.086 33.998 1.00 31.25 C
ATOM 4048 NE2 HIS B 81 -8.115 -8.460 34.399 1.00 32.18 N
ATOM 4049 N SER B 82 -6.120 -7.193 28.258 1.00 26.62 N
ATOM 4050 CA SER B 82 -5.745 -6.534 27.013 1.00 25.83 C
ATOM 4051 C SER B 82 -4.319 -6.852 26.637 1.00 24.52 C
ATOM 4052 O SER B 82 -3.475 -7.123 27.504 1.00 25.34 O
ATOM 4053 CB SER B 82 -5.928 -5.005 27.083 1.00 25.51 C
ATOM 4054 OG SER B 82 -4.874 -4.387 27.812 1.00 25.68 O
ATOM 4055 N ILE B 83 -4.079 -6.828 25.332 1.00 24.09 N
ATOM 4056 CA ILE B 83 -2.746 -6.937 24.758 1.00 24.30 C
ATOM 4057 C ILE B 83 -2.660 -5.890 23.658 1.00 24.47 C
ATOM 4058 O ILE B 83 -3.586 -5.755 22.868 1.00 24.79 O
ATOM 4059 CB ILE B 83 -2.477 -8.344 24.175 1.00 23.73 C
ATOM 4060 CG1 ILE B 83 -2.563 -9.412 25.272 1.00 22.39 C
ATOM 4061 CG2 ILE B 83 -1.113 -8.394 23.489 1.00 22.73 C
ATOM 4062 CD1 ILE B 83 -2.084 -10.792 24.855 1.00 23.36 C
ATOM 4063 N ASP B 84 -1.546 -5.167 23.594 1.00 26.38 N
ATOM 4064 CA ASP B 84 -1.387 -4.079 22.623 1.00 27.23 C
ATOM 4065 C ASP B 84 -0.032 -4.157 21.912 1.00 28.76 C
ATOM 4066 O ASP B 84 0.999 -3.971 22.539 1.00 28.20 O
ATOM 4067 CB ASP B 84 -1.530 -2.744 23.365 1.00 28.43 C
ATOM 4068 CG ASP B 84 -1.579 -1.541 22.442 1.00 29.18 C
ATOM 4069 OD1 ASP B 84 -0.669 -1.340 21.599 1.00 30.84 O
ATOM 4070 OD2 ASP B 84 -2.533 -0.764 22.590 1.00 29.40 O
ATOM 4071 N ALA B 85 -0.055 -4.412 20.604 1.00 28.65 N
ATOM 4072 CA ALA B 85 1.159 -4.533 19.799 1.00 31.62 C
ATOM 4073 C ALA B 85 1.949 -3.221 19.687 1.00 30.92 C
ATOM 4074 O ALA B 85 3.151 -3.250 19.440 1.00 31.83 O
ATOM 4075 CB ALA B 85 0.827 -5.074 18.409 1.00 31.63 C
ATOM 4076 N ASP B 86 1.276 -2.085 19.870 1.00 30.04 N
ATOM 4077 CA ASP B 86 1.938 -0.787 19.750 1.00 30.49 C
ATOM 4078 C ASP B 86 2.638 -0.378 21.034 1.00 29.36 C
ATOM 4079 O ASP B 86 3.771 0.068 20.989 1.00 28.66 O
ATOM 4080 CB ASP B 86 0.971 0.299 19.274 1.00 31.05 C
ATOM 4081 CG ASP B 86 0.370 -0.017 17.923 1.00 33.30 C
ATOM 4082 OD1 ASP B 86 1.129 -0.318 16.978 1.00 36.25 O
ATOM 4083 OD2 ASP B 86 -0.862 0.037 17.799 1.00 32.85 O
ATOM 4084 N THR B 87 1.979 -0.540 22.177 1.00 28.64 N
ATOM 4085 CA THR B 87 2.624 -0.228 23.450 1.00 27.95 C
ATOM 4086 C THR B 87 3.455 -1.426 23.933 1.00 29.23 C
ATOM 4087 O THR B 87 4.281 -1.279 24.833 1.00 28.68 O
ATOM 4088 CB THR B 87 1.615 0.149 24.541 1.00 28.35 C
ATOM 4089 OG1 THR B 87 0.817 -0.993 24.834 1.00 25.98 O
ATOM 4090 CG2 THR B 87 0.695 1.316 24.092 1.00 27.92 C
ATOM 4091 N LYS B 88 3.232 -2.601 23.326 1.00 27.96 N
ATOM 4092 CA LYS B 88 3.887 -3.856 23.730 1.00 28.62 C
ATOM 4093 C LYS B 88 3.474 -4.299 25.141 1.00 28.11 C
ATOM 4094 O LYS B 88 4.119 -5.149 25.760 1.00 27.91 O
ATOM 4095 CB LYS B 88 5.414 -3.744 23.581 1.00 30.01 C
ATOM 4096 CG LYS B 88 5.845 -3.328 22.177 1.00 32.10 C
ATOM 4097 CD LYS B 88 7.357 -3.246 22.017 1.00 35.37 C
ATOM 4098 CE LYS B 88 7.927 -2.002 22.688 1.00 38.75 C
ATOM 4099 NZ LYS B 88 9.418 -2.029 22.749 1.00 40.69 N
ATOM 4100 N LEU B 89 2.364 -3.741 25.624 1.00 25.86 N
ATOM 4101 CA LEU B 89 1.876 -4.013 26.978 1.00 25.78 C
ATOM 4102 C LEU B 89 0.764 -5.071 27.046 1.00 26.08 C
ATOM 4103 O LEU B 89 -0.171 -5.074 26.234 1.00 24.29 O
ATOM 4104 CB LEU B 89 1.373 -2.705 27.613 1.00 25.89 C
ATOM 4105 CG LEU B 89 2.228 -1.850 28.552 1.00 27.74 C
ATOM 4106 CD1 LEU B 89 3.729 -1.937 28.277 1.00 27.31 C
ATOM 4107 CD2 LEU B 89 1.732 -0.407 28.578 1.00 27.13 C
ATOM 4108 N VAL B 90 0.877 -5.958 28.032 1.00 25.66 N
ATOM 4109 CA VAL B 90 -0.190 -6.877 28.382 1.00 26.20 C
ATOM 4110 C VAL B 90 -0.710 -6.550 29.786 1.00 26.99 C
ATOM 4111 O VAL B 90 0.060 -6.250 30.695 1.00 27.39 O
ATOM 4112 CB VAL B 90 0.248 -8.360 28.301 1.00 26.37 C
ATOM 4113 CG1 VAL B 90 0.708 -8.724 26.892 1.00 26.07 C
ATOM 4114 CG2 VAL B 90 1.334 -8.674 29.323 1.00 25.62 C
ATOM 4115 N ASP B 91 -2.028 -6.601 29.941 1.00 27.29 N
ATOM 4116 CA ASP B 91 -2.691 -6.340 31.216 1.00 28.16 C
ATOM 4117 C ASP B 91 -3.410 -7.654 31.513 1.00 29.04 C
ATOM 4118 O ASP B 91 -4.310 -8.054 30.772 1.00 28.14 O
ATOM 4119 CB ASP B 91 -3.640 -5.141 31.052 1.00 27.44 C
ATOM 4120 CG ASP B 91 -4.448 -4.811 32.309 1.00 29.19 C
ATOM 4121 OD1 ASP B 91 -4.295 -5.464 33.361 1.00 26.62 O
ATOM 4122 OD2 ASP B 91 -5.270 -3.875 32.212 1.00 29.64 O
ATOM 4123 N ILE B 92 -2.949 -8.364 32.542 1.00 28.79 N
ATOM 4124 CA ILE B 92 -3.491 -9.683 32.868 1.00 30.32 C
ATOM 4125 C ILE B 92 -3.625 -9.876 34.373 1.00 31.45 C
ATOM 4126 O ILE B 92 -2.884 -9.264 35.143 1.00 32.58 O
ATOM 4127 CB ILE B 92 -2.616 -10.848 32.303 1.00 31.83 C
ATOM 4128 CG1 ILE B 92 -1.323 -11.061 33.123 1.00 30.56 C
ATOM 4129 CG2 ILE B 92 -2.358 -10.694 30.805 1.00 31.46 C
ATOM 4130 CD1 ILE B 92 -0.235 -10.024 32.920 1.00 30.90 C
ATOM 4131 N ASP B 93 -4.566 -10.732 34.778 1.00 32.90 N
ATOM 4132 CA ASP B 93 -4.702 -11.163 36.167 1.00 33.87 C
ATOM 4133 C ASP B 93 -3.523 -12.036 36.575 1.00 34.34 C
ATOM 4134 O ASP B 93 -2.989 -12.791 35.750 1.00 30.56 O
ATOM 4135 CB ASP B 93 -5.965 -12.008 36.346 1.00 36.29 C
ATOM 4136 CG ASP B 93 -7.237 -11.222 36.187 1.00 36.56 C
ATOM 4137 OD1 ASP B 93 -7.220 -9.970 36.258 1.00 39.12 O
ATOM 4138 OD2 ASP B 93 -8.271 -11.886 36.003 1.00 39.00 O
ATOM 4139 N ALA B 94 -3.155 -11.966 37.859 1.00 34.56 N
ATOM 4140 CA ALA B 94 -1.986 -12.687 38.375 1.00 33.44 C
ATOM 4141 C ALA B 94 -2.072 -14.193 38.181 1.00 33.27 C
ATOM 4142 O ALA B 94 -1.048 -14.891 38.191 1.00 33.46 O
ATOM 4143 CB ALA B 94 -1.752 -12.350 39.840 1.00 34.47 C
ATOM 4144 N GLY B 95 -3.289 -14.696 37.993 1.00 32.06 N
ATOM 4145 CA GLY B 95 -3.500 -16.126 37.831 1.00 31.84 C
ATOM 4146 C GLY B 95 -3.261 -16.634 36.420 1.00 31.45 C
ATOM 4147 O GLY B 95 -3.218 -17.838 36.198 1.00 32.60 O
ATOM 4148 N VAL B 96 -3.113 -15.724 35.460 1.00 30.37 N
ATOM 4149 CA VAL B 96 -2.781 -16.119 34.085 1.00 28.88 C
ATOM 4150 C VAL B 96 -1.437 -16.840 34.132 1.00 28.53 C
ATOM 4151 O VAL B 96 -0.539 -16.440 34.879 1.00 26.75 O
ATOM 4152 CB VAL B 96 -2.699 -14.893 33.139 1.00 29.22 C
ATOM 4153 CG1 VAL B 96 -2.106 -15.263 31.780 1.00 26.69 C
ATOM 4154 CG2 VAL B 96 -4.073 -14.251 32.964 1.00 27.98 C
ATOM 4155 N ASN B 97 -1.311 -17.917 33.362 1.00 29.18 N
ATOM 4156 CA ASN B 97 -0.040 -18.621 33.281 1.00 28.26 C
ATOM 4157 C ASN B 97 0.749 -18.263 32.016 1.00 29.29 C
ATOM 4158 O ASN B 97 0.186 -17.717 31.053 1.00 28.20 O
ATOM 4159 CB ASN B 97 -0.214 -20.145 33.486 1.00 28.68 C
ATOM 4160 CG ASN B 97 -0.791 -20.852 32.269 1.00 29.61 C
ATOM 4161 OD1 ASN B 97 -0.133 -20.970 31.240 1.00 30.01 O
ATOM 4162 ND2 ASN B 97 -2.016 -21.356 32.395 1.00 29.09 N
ATOM 4163 N LEU B 98 2.050 -18.574 32.032 1.00 27.34 N
ATOM 4164 CA LEU B 98 2.972 -18.122 30.989 1.00 27.10 C
ATOM 4165 C LEU B 98 2.752 -18.805 29.651 1.00 26.90 C
ATOM 4166 O LEU B 98 3.007 -18.209 28.611 1.00 25.62 O
ATOM 4167 CB LEU B 98 4.439 -18.270 31.436 1.00 26.96 C
ATOM 4168 CG LEU B 98 4.902 -17.402 32.619 1.00 26.93 C
ATOM 4169 CD1 LEU B 98 6.418 -17.460 32.773 1.00 27.37 C
ATOM 4170 CD2 LEU B 98 4.443 -15.958 32.480 1.00 27.88 C
ATOM 4171 N ASP B 99 2.299 -20.056 29.679 1.00 27.46 N
ATOM 4172 CA ASP B 99 1.908 -20.751 28.452 1.00 29.71 C
ATOM 4173 C ASP B 99 0.692 -20.081 27.804 1.00 27.85 C
ATOM 4174 O ASP B 99 0.700 -19.786 26.612 1.00 25.62 O
ATOM 4175 CB ASP B 99 1.621 -22.236 28.721 1.00 32.99 C
ATOM 4176 CG ASP B 99 1.546 -23.053 27.441 1.00 36.37 C
ATOM 4177 OD1 ASP B 99 2.572 -23.163 26.740 1.00 39.88 O
ATOM 4178 OD2 ASP B 99 0.462 -23.578 27.123 1.00 38.88 O
ATOM 4179 N GLN B 100 -0.347 -19.850 28.608 1.00 28.84 N
ATOM 4180 CA GLN B 100 -1.549 -19.125 28.178 1.00 29.60 C
ATOM 4181 C GLN B 100 -1.179 -17.746 27.621 1.00 29.26 C
ATOM 4182 O GLN B 100 -1.677 -17.349 26.563 1.00 30.09 O
ATOM 4183 CB GLN B 100 -2.521 -18.998 29.359 1.00 30.40 C
ATOM 4184 CG GLN B 100 -3.820 -18.241 29.100 1.00 31.98 C
ATOM 4185 CD GLN B 100 -4.496 -17.830 30.397 1.00 32.55 C
ATOM 4186 OE1 GLN B 100 -4.020 -18.171 31.485 1.00 33.20 O
ATOM 4187 NE2 GLN B 100 -5.602 -17.101 30.296 1.00 32.29 N
ATOM 4188 N LEU B 101 -0.282 -17.037 28.316 1.00 27.38 N
ATOM 4189 CA LEU B 101 0.135 -15.708 27.887 1.00 26.32 C
ATOM 4190 C LEU B 101 0.923 -15.742 26.565 1.00 26.28 C
ATOM 4191 O LEU B 101 0.631 -14.969 25.647 1.00 25.36 O
ATOM 4192 CB LEU B 101 0.929 -14.977 28.984 1.00 24.79 C
ATOM 4193 CG LEU B 101 1.435 -13.556 28.664 1.00 25.36 C
ATOM 4194 CD1 LEU B 101 0.339 -12.649 28.115 1.00 25.38 C
ATOM 4195 CD2 LEU B 101 2.077 -12.899 29.883 1.00 24.72 C
ATOM 4196 N MET B 102 1.906 -16.632 26.481 1.00 25.89 N
ATOM 4197 CA MET B 102 2.686 -16.810 25.248 1.00 27.46 C
ATOM 4198 C MET B 102 1.795 -17.016 24.022 1.00 25.79 C
ATOM 4199 O MET B 102 1.922 -16.310 23.036 1.00 25.05 O
ATOM 4200 CB MET B 102 3.656 -17.986 25.375 1.00 29.50 C
ATOM 4201 CG MET B 102 4.262 -18.378 24.038 1.00 33.31 C
ATOM 4202 SD MET B 102 5.291 -19.835 24.142 1.00 41.89 S
ATOM 4203 CE MET B 102 4.057 -21.135 24.085 1.00 40.67 C
ATOM 4204 N LYS B 103 0.889 -17.984 24.103 1.00 26.84 N
ATOM 4205 CA LYS B 103 -0.030 -18.279 23.005 1.00 27.46 C
ATOM 4206 C LYS B 103 -0.916 -17.092 22.638 1.00 26.18 C
ATOM 4207 O LYS B 103 -1.119 -16.820 21.470 1.00 26.76 O
ATOM 4208 CB LYS B 103 -0.847 -19.541 23.313 1.00 29.24 C
ATOM 4209 CG LYS B 103 0.069 -20.761 23.421 1.00 33.46 C
ATOM 4210 CD LYS B 103 -0.654 -22.066 23.698 1.00 34.96 C
ATOM 4211 CE LYS B 103 0.332 -23.224 23.640 1.00 36.38 C
ATOM 4212 NZ LYS B 103 -0.069 -24.324 24.571 1.00 39.90 N
ATOM 4213 N ALA B 104 -1.409 -16.369 23.636 1.00 26.14 N
ATOM 4214 CA ALA B 104 -2.270 -15.216 23.384 1.00 25.91 C
ATOM 4215 C ALA B 104 -1.517 -14.043 22.773 1.00 25.65 C
ATOM 4216 O ALA B 104 -2.068 -13.319 21.949 1.00 24.26 O
ATOM 4217 CB ALA B 104 -2.980 -14.783 24.664 1.00 26.92 C
ATOM 4218 N ALA B 105 -0.253 -13.879 23.162 1.00 25.64 N
ATOM 4219 CA ALA B 105 0.535 -12.711 22.766 1.00 26.06 C
ATOM 4220 C ALA B 105 1.217 -12.845 21.398 1.00 25.06 C
ATOM 4221 O ALA B 105 1.463 -11.844 20.728 1.00 25.05 O
ATOM 4222 CB ALA B 105 1.551 -12.373 23.850 1.00 25.15 C
ATOM 4223 N LEU B 106 1.509 -14.075 20.984 1.00 25.73 N
ATOM 4224 CA LEU B 106 2.178 -14.330 19.700 1.00 25.96 C
ATOM 4225 C LEU B 106 1.565 -13.645 18.457 1.00 26.71 C
ATOM 4226 O LEU B 106 2.302 -13.079 17.661 1.00 28.12 O
ATOM 4227 CB LEU B 106 2.379 -15.836 19.452 1.00 26.38 C
ATOM 4228 CG LEU B 106 3.688 -16.366 20.024 1.00 27.21 C
ATOM 4229 CD1 LEU B 106 3.719 -17.896 20.020 1.00 28.70 C
ATOM 4230 CD2 LEU B 106 4.880 -15.776 19.284 1.00 24.66 C
ATOM 4231 N PRO B 107 0.226 -13.699 18.282 1.00 27.65 N
ATOM 4232 CA PRO B 107 -0.383 -13.047 17.107 1.00 28.61 C
ATOM 4233 C PRO B 107 -0.251 -11.518 17.083 1.00 28.65 C
ATOM 4234 O PRO B 107 -0.640 -10.891 16.097 1.00 29.11 O
ATOM 4235 CB PRO B 107 -1.864 -13.442 17.221 1.00 28.81 C
ATOM 4236 CG PRO B 107 -1.831 -14.723 17.978 1.00 29.11 C
ATOM 4237 CD PRO B 107 -0.769 -14.500 19.015 1.00 27.52 C
ATOM 4238 N PHE B 108 0.281 -10.936 18.162 1.00 27.74 N
ATOM 4239 CA PHE B 108 0.577 -9.501 18.231 1.00 27.37 C
ATOM 4240 C PHE B 108 2.053 -9.211 17.944 1.00 27.61 C
ATOM 4241 O PHE B 108 2.498 -8.063 18.028 1.00 28.81 O
ATOM 4242 CB PHE B 108 0.221 -8.943 19.608 1.00 27.15 C
ATOM 4243 CG PHE B 108 -1.241 -9.069 19.966 1.00 26.80 C
ATOM 4244 CD1 PHE B 108 -2.119 -8.014 19.747 1.00 26.51 C
ATOM 4245 CD2 PHE B 108 -1.734 -10.238 20.529 1.00 27.38 C
ATOM 4246 CE1 PHE B 108 -3.459 -8.129 20.081 1.00 27.49 C
ATOM 4247 CE2 PHE B 108 -3.074 -10.357 20.867 1.00 27.37 C
ATOM 4248 CZ PHE B 108 -3.936 -9.306 20.641 1.00 26.85 C
ATOM 4249 N GLY B 109 2.824 -10.243 17.626 1.00 27.48 N
ATOM 4250 CA GLY B 109 4.272 -10.060 17.429 1.00 27.21 C
ATOM 4251 C GLY B 109 4.993 -9.767 18.739 1.00 27.07 C
ATOM 4252 O GLY B 109 5.980 -9.015 18.762 1.00 27.16 O
ATOM 4253 N LEU B 110 4.503 -10.370 19.823 1.00 25.18 N
ATOM 4254 CA LEU B 110 5.044 -10.172 21.171 1.00 24.56 C
ATOM 4255 C LEU B 110 5.490 -11.480 21.817 1.00 24.50 C
ATOM 4256 O LEU B 110 4.893 -12.534 21.583 1.00 24.66 O
ATOM 4257 CB LEU B 110 3.995 -9.504 22.069 1.00 23.79 C
ATOM 4258 CG LEU B 110 3.465 -8.123 21.659 1.00 23.63 C
ATOM 4259 CD1 LEU B 110 2.375 -7.662 22.622 1.00 23.89 C
ATOM 4260 CD2 LEU B 110 4.590 -7.105 21.612 1.00 23.40 C
ATOM 4261 N TRP B 111 6.509 -11.386 22.669 1.00 24.51 N
ATOM 4262 CA TRP B 111 7.177 -12.539 23.268 1.00 25.50 C
ATOM 4263 C TRP B 111 7.317 -12.323 24.760 1.00 26.19 C
ATOM 4264 O TRP B 111 7.692 -11.225 25.196 1.00 25.88 O
ATOM 4265 CB TRP B 111 8.542 -12.747 22.584 1.00 25.63 C
ATOM 4266 CG TRP B 111 9.185 -14.063 22.926 1.00 25.41 C
ATOM 4267 CD1 TRP B 111 10.216 -14.291 23.822 1.00 25.99 C
ATOM 4268 CD2 TRP B 111 8.827 -15.395 22.406 1.00 26.05 C
ATOM 4269 NE1 TRP B 111 10.510 -15.630 23.900 1.00 26.78 N
ATOM 4270 CE2 TRP B 111 9.715 -16.347 23.076 1.00 26.52 C
ATOM 4271 CE3 TRP B 111 7.893 -15.872 21.491 1.00 25.86 C
ATOM 4272 CZ2 TRP B 111 9.660 -17.712 22.823 1.00 26.55 C
ATOM 4273 CZ3 TRP B 111 7.838 -17.249 21.253 1.00 26.56 C
ATOM 4274 CH2 TRP B 111 8.710 -18.145 21.898 1.00 27.39 C
ATOM 4275 N VAL B 112 6.953 -13.335 25.562 1.00 25.23 N
ATOM 4276 CA VAL B 112 7.136 -13.286 27.014 1.00 25.17 C
ATOM 4277 C VAL B 112 8.630 -13.062 27.295 1.00 26.51 C
ATOM 4278 O VAL B 112 9.459 -13.896 26.918 1.00 25.56 O
ATOM 4279 CB VAL B 112 6.629 -14.572 27.720 1.00 25.60 C
ATOM 4280 CG1 VAL B 112 6.863 -14.496 29.223 1.00 24.97 C
ATOM 4281 CG2 VAL B 112 5.150 -14.805 27.442 1.00 24.23 C
ATOM 4282 N PRO B 113 8.971 -11.923 27.939 1.00 26.45 N
ATOM 4283 CA PRO B 113 10.369 -11.477 28.015 1.00 25.51 C
ATOM 4284 C PRO B 113 11.277 -12.352 28.874 1.00 25.86 C
ATOM 4285 O PRO B 113 12.484 -12.366 28.646 1.00 25.40 O
ATOM 4286 CB PRO B 113 10.262 -10.061 28.610 1.00 25.44 C
ATOM 4287 CG PRO B 113 8.969 -10.068 29.365 1.00 24.68 C
ATOM 4288 CD PRO B 113 8.047 -10.945 28.558 1.00 24.31 C
ATOM 4289 N VAL B 114 10.707 -13.085 29.830 1.00 24.39 N
ATOM 4290 CA VAL B 114 11.468 -14.046 30.620 1.00 24.77 C
ATOM 4291 C VAL B 114 10.657 -15.329 30.753 1.00 26.69 C
ATOM 4292 O VAL B 114 9.562 -15.333 31.337 1.00 27.74 O
ATOM 4293 CB VAL B 114 11.842 -13.495 32.028 1.00 22.88 C
ATOM 4294 CG1 VAL B 114 12.409 -14.596 32.917 1.00 21.95 C
ATOM 4295 CG2 VAL B 114 12.825 -12.340 31.934 1.00 22.47 C
ATOM 4296 N LEU B 115 11.186 -16.414 30.201 1.00 28.47 N
ATOM 4297 CA LEU B 115 10.559 -17.722 30.324 1.00 30.79 C
ATOM 4298 C LEU B 115 11.452 -18.687 31.103 1.00 32.31 C
ATOM 4299 O LEU B 115 12.641 -18.808 30.800 1.00 33.15 O
ATOM 4300 CB LEU B 115 10.230 -18.284 28.936 1.00 31.68 C
ATOM 4301 CG LEU B 115 9.016 -17.651 28.254 1.00 31.46 C
ATOM 4302 CD1 LEU B 115 9.047 -17.849 26.746 1.00 30.15 C
ATOM 4303 CD2 LEU B 115 7.722 -18.205 28.847 1.00 31.15 C
ATOM 4304 N PRO B 116 10.889 -19.372 32.116 1.00 32.01 N
ATOM 4305 CA PRO B 116 11.671 -20.339 32.875 1.00 31.50 C
ATOM 4306 C PRO B 116 11.676 -21.695 32.150 1.00 34.42 C
ATOM 4307 O PRO B 116 11.119 -21.801 31.054 1.00 35.18 O
ATOM 4308 CB PRO B 116 10.908 -20.424 34.196 1.00 30.97 C
ATOM 4309 CG PRO B 116 9.481 -20.165 33.818 1.00 31.14 C
ATOM 4310 CD PRO B 116 9.472 -19.379 32.527 1.00 30.21 C
ATOM 4311 N GLY B 117 12.289 -22.715 32.750 1.00 35.75 N
ATOM 4312 CA GLY B 117 12.361 -24.053 32.132 1.00 37.23 C
ATOM 4313 C GLY B 117 11.039 -24.809 32.004 1.00 39.89 C
ATOM 4314 O GLY B 117 11.014 -25.933 31.508 1.00 43.04 O
ATOM 4315 N THR B 118 9.950 -24.204 32.475 1.00 39.58 N
ATOM 4316 CA THR B 118 8.597 -24.746 32.332 1.00 39.63 C
ATOM 4317 C THR B 118 7.644 -23.570 32.148 1.00 39.54 C
ATOM 4318 O THR B 118 7.854 -22.516 32.738 1.00 38.68 O
ATOM 4319 CB THR B 118 8.161 -25.590 33.556 1.00 41.02 C
ATOM 4320 OG1 THR B 118 6.848 -26.115 33.331 1.00 43.99 O
ATOM 4321 CG2 THR B 118 8.124 -24.756 34.843 1.00 40.88 C
ATOM 4322 N ARG B 119 6.607 -23.735 31.332 1.00 39.50 N
ATOM 4323 CA ARG B 119 5.669 -22.635 31.088 1.00 39.16 C
ATOM 4324 C ARG B 119 4.454 -22.699 32.005 1.00 39.09 C
ATOM 4325 O ARG B 119 3.613 -21.786 32.003 1.00 37.46 O
ATOM 4326 CB ARG B 119 5.232 -22.592 29.621 1.00 42.34 C
ATOM 4327 CG ARG B 119 6.348 -22.254 28.634 1.00 44.51 C
ATOM 4328 CD ARG B 119 5.816 -22.049 27.220 1.00 46.00 C
ATOM 4329 NE ARG B 119 5.050 -23.201 26.740 1.00 47.98 N
ATOM 4330 CZ ARG B 119 5.536 -24.177 25.972 1.00 49.89 C
ATOM 4331 NH1 ARG B 119 6.801 -24.153 25.567 1.00 49.88 N
ATOM 4332 NH2 ARG B 119 4.749 -25.176 25.598 1.00 48.54 N
ATOM 4333 N GLN B 120 4.352 -23.772 32.789 1.00 36.62 N
ATOM 4334 CA GLN B 120 3.256 -23.889 33.749 1.00 37.78 C
ATOM 4335 C GLN B 120 3.564 -23.126 35.049 1.00 36.01 C
ATOM 4336 O GLN B 120 3.741 -23.718 36.121 1.00 37.32 O
ATOM 4337 CB GLN B 120 2.884 -25.361 33.997 1.00 40.17 C
ATOM 4338 CG GLN B 120 2.283 -26.054 32.776 1.00 42.71 C
ATOM 4339 CD GLN B 120 0.912 -25.510 32.400 1.00 47.25 C
ATOM 4340 OE1 GLN B 120 0.017 -25.399 33.245 1.00 50.30 O
ATOM 4341 NE2 GLN B 120 0.737 -25.174 31.124 1.00 48.24 N
ATOM 4342 N VAL B 121 3.617 -21.800 34.920 1.00 34.06 N
ATOM 4343 CA VAL B 121 3.917 -20.871 36.010 1.00 32.95 C
ATOM 4344 C VAL B 121 2.963 -19.677 35.878 1.00 33.07 C
ATOM 4345 O VAL B 121 2.736 -19.201 34.767 1.00 32.93 O
ATOM 4346 CB VAL B 121 5.390 -20.402 35.921 1.00 32.74 C
ATOM 4347 CG1 VAL B 121 5.648 -19.186 36.792 1.00 34.50 C
ATOM 4348 CG2 VAL B 121 6.349 -21.534 36.289 1.00 32.63 C
ATOM 4349 N THR B 122 2.401 -19.201 36.994 1.00 33.66 N
ATOM 4350 CA THR B 122 1.505 -18.038 36.962 1.00 31.99 C
ATOM 4351 C THR B 122 2.321 -16.745 36.919 1.00 31.85 C
ATOM 4352 O THR B 122 3.493 -16.736 37.299 1.00 32.56 O
ATOM 4353 CB THR B 122 0.517 -17.996 38.158 1.00 33.44 C
ATOM 4354 OG1 THR B 122 1.230 -17.764 39.378 1.00 33.72 O
ATOM 4355 CG2 THR B 122 -0.296 -19.300 38.274 1.00 31.74 C
ATOM 4356 N VAL B 123 1.706 -15.667 36.438 1.00 29.02 N
ATOM 4357 CA VAL B 123 2.318 -14.336 36.464 1.00 28.01 C
ATOM 4358 C VAL B 123 2.626 -13.937 37.920 1.00 28.26 C
ATOM 4359 O VAL B 123 3.678 -13.368 38.211 1.00 27.32 O
ATOM 4360 CB VAL B 123 1.398 -13.280 35.809 1.00 26.40 C
ATOM 4361 CG1 VAL B 123 1.938 -11.875 36.026 1.00 25.51 C
ATOM 4362 CG2 VAL B 123 1.199 -13.573 34.323 1.00 26.71 C
ATOM 4363 N GLY B 124 1.696 -14.246 38.822 1.00 27.78 N
ATOM 4364 CA GLY B 124 1.889 -14.046 40.264 1.00 28.68 C
ATOM 4365 C GLY B 124 3.117 -14.750 40.827 1.00 28.51 C
ATOM 4366 O GLY B 124 3.909 -14.135 41.526 1.00 29.77 O
ATOM 4367 N GLY B 125 3.274 -16.034 40.511 1.00 28.76 N
ATOM 4368 CA GLY B 125 4.468 -16.800 40.882 1.00 28.58 C
ATOM 4369 C GLY B 125 5.751 -16.319 40.218 1.00 29.61 C
ATOM 4370 O GLY B 125 6.816 -16.334 40.827 1.00 29.06 O
ATOM 4371 N ALA B 126 5.637 -15.909 38.955 1.00 28.11 N
ATOM 4372 CA ALA B 126 6.737 -15.353 38.193 1.00 27.14 C
ATOM 4373 C ALA B 126 7.310 -14.090 38.848 1.00 27.75 C
ATOM 4374 O ALA B 126 8.531 -13.910 38.913 1.00 27.11 O
ATOM 4375 CB ALA B 126 6.256 -15.038 36.788 1.00 27.96 C
ATOM 4376 N ILE B 127 6.414 -13.221 39.322 1.00 27.95 N
ATOM 4377 CA ILE B 127 6.788 -11.980 39.995 1.00 27.43 C
ATOM 4378 C ILE B 127 7.311 -12.242 41.406 1.00 27.70 C
ATOM 4379 O ILE B 127 8.379 -11.746 41.776 1.00 25.85 O
ATOM 4380 CB ILE B 127 5.610 -10.971 40.038 1.00 27.71 C
ATOM 4381 CG1 ILE B 127 5.226 -10.551 38.614 1.00 28.04 C
ATOM 4382 CG2 ILE B 127 5.985 -9.742 40.856 1.00 27.66 C
ATOM 4383 CD1 ILE B 127 3.973 -9.699 38.511 1.00 27.92 C
ATOM 4384 N ALA B 128 6.567 -13.039 42.176 1.00 27.68 N
ATOM 4385 CA ALA B 128 6.907 -13.311 43.573 1.00 28.33 C
ATOM 4386 C ALA B 128 8.228 -14.059 43.771 1.00 28.98 C
ATOM 4387 O ALA B 128 8.825 -13.977 44.842 1.00 29.42 O
ATOM 4388 CB ALA B 128 5.772 -14.052 44.264 1.00 27.56 C
ATOM 4389 N CYS B 129 8.654 -14.810 42.756 1.00 27.50 N
ATOM 4390 CA CYS B 129 9.947 -15.485 42.792 1.00 28.33 C
ATOM 4391 C CYS B 129 10.955 -14.779 41.895 1.00 27.44 C
ATOM 4392 O CYS B 129 12.096 -15.212 41.802 1.00 28.18 O
ATOM 4393 CB CYS B 129 9.826 -16.964 42.411 1.00 28.76 C
ATOM 4394 SG CYS B 129 9.179 -17.995 43.757 1.00 30.81 S
ATOM 4395 N ASP B 130 10.524 -13.681 41.268 1.00 26.47 N
ATOM 4396 CA ASP B 130 11.356 -12.912 40.341 1.00 25.56 C
ATOM 4397 C ASP B 130 12.130 -13.890 39.459 1.00 25.25 C
ATOM 4398 O ASP B 130 13.358 -13.931 39.498 1.00 27.33 O
ATOM 4399 CB ASP B 130 12.310 -11.998 41.112 1.00 24.38 C
ATOM 4400 CG ASP B 130 12.991 -10.963 40.221 1.00 23.61 C
ATOM 4401 OD1 ASP B 130 12.540 -10.733 39.072 1.00 23.05 O
ATOM 4402 OD2 ASP B 130 13.971 -10.366 40.691 1.00 22.88 O
ATOM 4403 N ILE B 131 11.401 -14.685 38.683 1.00 24.34 N
ATOM 4404 CA ILE B 131 11.993 -15.841 37.997 1.00 24.43 C
ATOM 4405 C ILE B 131 12.970 -15.400 36.905 1.00 23.85 C
ATOM 4406 O ILE B 131 12.870 -14.290 36.376 1.00 23.62 O
ATOM 4407 CB ILE B 131 10.923 -16.815 37.439 1.00 23.64 C
ATOM 4408 CG1 ILE B 131 10.026 -16.118 36.407 1.00 23.33 C
ATOM 4409 CG2 ILE B 131 10.077 -17.394 38.577 1.00 23.78 C
ATOM 4410 CD1 ILE B 131 9.205 -17.078 35.563 1.00 22.89 C
ATOM 4411 N HIS B 132 13.927 -16.272 36.606 1.00 25.06 N
ATOM 4412 CA HIS B 132 14.941 -16.019 35.603 1.00 25.23 C
ATOM 4413 C HIS B 132 14.850 -17.078 34.553 1.00 25.68 C
ATOM 4414 O HIS B 132 14.120 -18.061 34.708 1.00 25.21 O
ATOM 4415 CB HIS B 132 16.330 -16.027 36.225 1.00 25.84 C
ATOM 4416 CG HIS B 132 16.632 -17.270 37.038 1.00 26.90 C
ATOM 4417 ND1 HIS B 132 17.178 -18.388 36.495 1.00 28.52 N
ATOM 4418 CD2 HIS B 132 16.460 -17.534 38.382 1.00 24.86 C
ATOM 4419 CE1 HIS B 132 17.324 -19.319 37.453 1.00 26.14 C
ATOM 4420 NE2 HIS B 132 16.888 -18.795 38.606 1.00 28.26 N
ATOM 4421 N GLY B 133 15.584 -16.891 33.465 1.00 24.20 N
ATOM 4422 CA GLY B 133 15.546 -17.850 32.382 1.00 25.17 C
ATOM 4423 C GLY B 133 16.843 -17.852 31.614 1.00 25.84 C
ATOM 4424 O GLY B 133 17.819 -17.229 32.025 1.00 23.70 O
ATOM 4425 N LYS B 134 16.807 -18.534 30.476 1.00 26.52 N
ATOM 4426 CA LYS B 134 17.955 -18.759 29.609 1.00 26.89 C
ATOM 4427 C LYS B 134 18.504 -17.434 29.050 1.00 25.40 C
ATOM 4428 O LYS B 134 19.660 -17.345 28.635 1.00 24.55 O
ATOM 4429 CB LYS B 134 17.504 -19.713 28.495 1.00 29.36 C
ATOM 4430 CG LYS B 134 18.605 -20.457 27.766 1.00 30.36 C
ATOM 4431 CD LYS B 134 18.014 -21.432 26.754 1.00 32.28 C
ATOM 4432 CE LYS B 134 19.087 -21.996 25.813 1.00 32.93 C
ATOM 4433 NZ LYS B 134 18.468 -22.946 24.839 1.00 34.91 N
ATOM 4434 N ASN B 135 17.674 -16.396 29.073 1.00 24.18 N
ATOM 4435 CA ASN B 135 18.063 -15.076 28.589 1.00 24.00 C
ATOM 4436 C ASN B 135 18.408 -14.060 29.690 1.00 24.94 C
ATOM 4437 O ASN B 135 18.469 -12.847 29.425 1.00 25.30 O
ATOM 4438 CB ASN B 135 16.981 -14.500 27.667 1.00 23.28 C
ATOM 4439 CG ASN B 135 15.691 -14.215 28.407 1.00 23.79 C
ATOM 4440 OD1 ASN B 135 15.519 -14.653 29.540 1.00 23.00 O
ATOM 4441 ND2 ASN B 135 14.789 -13.497 27.772 1.00 22.07 N
ATOM 4442 N HIS B 136 18.652 -14.537 30.911 1.00 24.14 N
ATOM 4443 CA HIS B 136 18.935 -13.609 32.017 1.00 24.85 C
ATOM 4444 C HIS B 136 20.045 -12.623 31.746 1.00 26.44 C
ATOM 4445 O HIS B 136 19.943 -11.450 32.112 1.00 25.70 O
ATOM 4446 CB HIS B 136 19.226 -14.323 33.329 1.00 23.70 C
ATOM 4447 CG HIS B 136 19.404 -13.365 34.481 1.00 24.86 C
ATOM 4448 ND1 HIS B 136 20.604 -12.837 34.808 1.00 24.79 N
ATOM 4449 CD2 HIS B 136 18.467 -12.782 35.336 1.00 23.87 C
ATOM 4450 CE1 HIS B 136 20.442 -11.982 35.836 1.00 25.95 C
ATOM 4451 NE2 HIS B 136 19.130 -11.948 36.152 1.00 23.55 N
ATOM 4452 N HIS B 137 21.122 -13.085 31.118 1.00 26.87 N
ATOM 4453 CA HIS B 137 22.289 -12.231 30.892 1.00 28.45 C
ATOM 4454 C HIS B 137 22.025 -11.094 29.944 1.00 28.98 C
ATOM 4455 O HIS B 137 22.765 -10.113 29.933 1.00 30.52 O
ATOM 4456 CB HIS B 137 23.463 -13.061 30.386 1.00 27.69 C
ATOM 4457 CG HIS B 137 23.254 -13.622 29.009 1.00 28.33 C
ATOM 4458 ND1 HIS B 137 22.411 -14.636 28.765 1.00 29.23 N
ATOM 4459 CD2 HIS B 137 23.825 -13.280 27.785 1.00 29.13 C
ATOM 4460 CE1 HIS B 137 22.419 -14.925 27.451 1.00 28.83 C
ATOM 4461 NE2 HIS B 137 23.294 -14.096 26.852 1.00 30.23 N
ATOM 4462 N SER B 138 20.991 -11.223 29.115 1.00 29.22 N
ATOM 4463 CA SER B 138 20.610 -10.136 28.212 1.00 29.60 C
ATOM 4464 C SER B 138 19.299 -9.447 28.606 1.00 28.61 C
ATOM 4465 O SER B 138 19.042 -8.340 28.172 1.00 29.79 O
ATOM 4466 CB SER B 138 20.521 -10.632 26.763 1.00 29.82 C
ATOM 4467 OG SER B 138 19.449 -11.550 26.596 1.00 30.39 O
ATOM 4468 N ALA B 139 18.476 -10.087 29.430 1.00 28.72 N
ATOM 4469 CA ALA B 139 17.142 -9.553 29.693 1.00 28.83 C
ATOM 4470 C ALA B 139 16.803 -9.313 31.169 1.00 28.94 C
ATOM 4471 O ALA B 139 15.752 -8.745 31.467 1.00 29.43 O
ATOM 4472 CB ALA B 139 16.086 -10.444 29.040 1.00 28.69 C
ATOM 4473 N GLY B 140 17.679 -9.748 32.079 1.00 28.08 N
ATOM 4474 CA GLY B 140 17.400 -9.715 33.515 1.00 26.67 C
ATOM 4475 C GLY B 140 16.316 -10.716 33.893 1.00 26.27 C
ATOM 4476 O GLY B 140 16.027 -11.651 33.139 1.00 26.59 O
ATOM 4477 N SER B 141 15.708 -10.527 35.057 1.00 24.67 N
ATOM 4478 CA SER B 141 14.668 -11.451 35.509 1.00 24.44 C
ATOM 4479 C SER B 141 13.274 -10.884 35.248 1.00 23.66 C
ATOM 4480 O SER B 141 13.134 -9.802 34.688 1.00 23.75 O
ATOM 4481 CB SER B 141 14.887 -11.874 36.975 1.00 23.74 C
ATOM 4482 OG SER B 141 14.853 -10.774 37.869 1.00 23.87 O
ATOM 4483 N PHE B 142 12.245 -11.630 35.636 1.00 23.87 N
ATOM 4484 CA PHE B 142 10.872 -11.278 35.330 1.00 24.07 C
ATOM 4485 C PHE B 142 10.478 -9.897 35.870 1.00 25.14 C
ATOM 4486 O PHE B 142 9.786 -9.138 35.189 1.00 25.75 O
ATOM 4487 CB PHE B 142 9.929 -12.353 35.873 1.00 24.03 C
ATOM 4488 CG PHE B 142 8.598 -12.376 35.195 1.00 24.37 C
ATOM 4489 CD1 PHE B 142 8.410 -13.128 34.039 1.00 24.09 C
ATOM 4490 CD2 PHE B 142 7.518 -11.642 35.714 1.00 23.57 C
ATOM 4491 CE1 PHE B 142 7.176 -13.164 33.402 1.00 24.49 C
ATOM 4492 CE2 PHE B 142 6.291 -11.662 35.075 1.00 23.62 C
ATOM 4493 CZ PHE B 142 6.112 -12.421 33.922 1.00 24.34 C
ATOM 4494 N GLY B 143 10.940 -9.580 37.081 1.00 24.97 N
ATOM 4495 CA GLY B 143 10.667 -8.301 37.726 1.00 24.90 C
ATOM 4496 C GLY B 143 11.044 -7.087 36.902 1.00 25.51 C
ATOM 4497 O GLY B 143 10.358 -6.073 36.983 1.00 26.47 O
ATOM 4498 N ASN B 144 12.120 -7.198 36.105 1.00 24.45 N
ATOM 4499 CA ASN B 144 12.595 -6.119 35.221 1.00 25.10 C
ATOM 4500 C ASN B 144 11.582 -5.645 34.182 1.00 24.05 C
ATOM 4501 O ASN B 144 11.753 -4.570 33.603 1.00 23.94 O
ATOM 4502 CB ASN B 144 13.875 -6.531 34.442 1.00 26.14 C
ATOM 4503 CG ASN B 144 15.090 -6.793 35.333 1.00 26.70 C
ATOM 4504 OD1 ASN B 144 16.186 -6.314 35.042 1.00 29.15 O
ATOM 4505 ND2 ASN B 144 14.925 -7.593 36.370 1.00 25.28 N
ATOM 4506 N HIS B 145 10.555 -6.453 33.922 1.00 22.25 N
ATOM 4507 CA HIS B 145 9.644 -6.221 32.802 1.00 22.22 C
ATOM 4508 C HIS B 145 8.253 -5.845 33.262 1.00 23.24 C
ATOM 4509 O HIS B 145 7.361 -5.598 32.454 1.00 22.83 O
ATOM 4510 CB HIS B 145 9.623 -7.466 31.916 1.00 22.39 C
ATOM 4511 CG HIS B 145 11.004 -7.854 31.418 1.00 21.67 C
ATOM 4512 ND1 HIS B 145 11.613 -7.204 30.399 1.00 22.93 N
ATOM 4513 CD2 HIS B 145 11.914 -8.791 31.884 1.00 22.36 C
ATOM 4514 CE1 HIS B 145 12.850 -7.714 30.208 1.00 21.34 C
ATOM 4515 NE2 HIS B 145 13.039 -8.688 31.108 1.00 22.20 N
ATOM 4516 N VAL B 146 8.058 -5.815 34.570 1.00 23.54 N
ATOM 4517 CA VAL B 146 6.745 -5.499 35.128 1.00 25.85 C
ATOM 4518 C VAL B 146 6.632 -3.988 35.179 1.00 27.44 C
ATOM 4519 O VAL B 146 7.517 -3.320 35.723 1.00 29.14 O
ATOM 4520 CB VAL B 146 6.559 -6.117 36.521 1.00 25.49 C
ATOM 4521 CG1 VAL B 146 5.207 -5.720 37.113 1.00 25.57 C
ATOM 4522 CG2 VAL B 146 6.691 -7.635 36.454 1.00 24.27 C
ATOM 4523 N ARG B 147 5.572 -3.451 34.576 1.00 29.02 N
ATOM 4524 CA ARG B 147 5.397 -1.999 34.487 1.00 30.69 C
ATOM 4525 C ARG B 147 4.444 -1.478 35.558 1.00 31.00 C
ATOM 4526 O ARG B 147 4.513 -0.316 35.955 1.00 32.23 O
ATOM 4527 CB ARG B 147 4.947 -1.590 33.082 1.00 31.65 C
ATOM 4528 CG ARG B 147 5.978 -1.910 31.994 1.00 32.38 C
ATOM 4529 CD ARG B 147 7.286 -1.152 32.192 1.00 33.33 C
ATOM 4530 NE ARG B 147 8.373 -1.675 31.353 1.00 33.54 N
ATOM 4531 CZ ARG B 147 9.417 -2.385 31.796 1.00 33.18 C
ATOM 4532 NH1 ARG B 147 9.545 -2.684 33.088 1.00 29.10 N
ATOM 4533 NH2 ARG B 147 10.349 -2.795 30.935 1.00 31.93 N
ATOM 4534 N SER B 148 3.564 -2.351 36.022 1.00 30.52 N
ATOM 4535 CA SER B 148 2.716 -2.051 37.169 1.00 31.32 C
ATOM 4536 C SER B 148 2.169 -3.349 37.716 1.00 31.94 C
ATOM 4537 O SER B 148 2.102 -4.360 37.007 1.00 31.63 O
ATOM 4538 CB SER B 148 1.556 -1.133 36.771 1.00 31.72 C
ATOM 4539 OG SER B 148 0.588 -1.855 36.027 1.00 31.53 O
ATOM 4540 N MET B 149 1.799 -3.331 38.992 1.00 32.37 N
ATOM 4541 CA MET B 149 0.982 -4.392 39.550 1.00 32.59 C
ATOM 4542 C MET B 149 0.037 -3.845 40.615 1.00 34.04 C
ATOM 4543 O MET B 149 0.333 -2.850 41.289 1.00 33.95 O
ATOM 4544 CB MET B 149 1.813 -5.577 40.075 1.00 31.25 C
ATOM 4545 CG MET B 149 3.008 -5.205 40.928 1.00 33.75 C
ATOM 4546 SD MET B 149 3.923 -6.659 41.509 1.00 36.35 S
ATOM 4547 CE MET B 149 5.496 -5.918 41.919 1.00 34.31 C
ATOM 4548 N ASP B 150 -1.111 -4.493 40.735 1.00 35.82 N
ATOM 4549 CA ASP B 150 -2.085 -4.148 41.755 1.00 37.35 C
ATOM 4550 C ASP B 150 -1.930 -5.158 42.875 1.00 37.12 C
ATOM 4551 O ASP B 150 -2.089 -6.351 42.655 1.00 35.89 O
ATOM 4552 CB ASP B 150 -3.498 -4.215 41.181 1.00 39.08 C
ATOM 4553 CG ASP B 150 -3.702 -3.268 40.015 1.00 42.74 C
ATOM 4554 OD1 ASP B 150 -3.028 -2.213 39.947 1.00 43.89 O
ATOM 4555 OD2 ASP B 150 -4.553 -3.585 39.162 1.00 46.41 O
ATOM 4556 N LEU B 151 -1.617 -4.667 44.071 1.00 38.64 N
ATOM 4557 CA LEU B 151 -1.347 -5.528 45.222 1.00 38.58 C
ATOM 4558 C LEU B 151 -2.405 -5.360 46.310 1.00 39.21 C
ATOM 4559 O LEU B 151 -2.573 -4.260 46.858 1.00 38.56 O
ATOM 4560 CB LEU B 151 0.033 -5.205 45.805 1.00 37.28 C
ATOM 4561 CG LEU B 151 0.437 -5.955 47.075 1.00 36.64 C
ATOM 4562 CD1 LEU B 151 0.870 -7.368 46.728 1.00 36.33 C
ATOM 4563 CD2 LEU B 151 1.549 -5.213 47.796 1.00 36.81 C
ATOM 4564 N LEU B 152 -3.102 -6.451 46.623 1.00 39.15 N
ATOM 4565 CA LEU B 152 -4.078 -6.462 47.718 1.00 40.88 C
ATOM 4566 C LEU B 152 -3.364 -6.442 49.068 1.00 42.00 C
ATOM 4567 O LEU B 152 -2.889 -7.473 49.553 1.00 41.82 O
ATOM 4568 CB LEU B 152 -5.012 -7.671 47.613 1.00 40.09 C
ATOM 4569 CG LEU B 152 -5.952 -8.011 48.783 1.00 41.80 C
ATOM 4570 CD1 LEU B 152 -6.871 -6.853 49.162 1.00 40.12 C
ATOM 4571 CD2 LEU B 152 -6.759 -9.253 48.452 1.00 39.37 C
ATOM 4572 N THR B 153 -3.301 -5.252 49.656 1.00 43.33 N
ATOM 4573 CA THR B 153 -2.601 -5.007 50.915 1.00 45.73 C
ATOM 4574 C THR B 153 -3.374 -5.529 52.146 1.00 47.39 C
ATOM 4575 O THR B 153 -4.573 -5.816 52.067 1.00 43.07 O
ATOM 4576 CB THR B 153 -2.228 -3.506 51.006 1.00 49.01 C
ATOM 4577 OG1 THR B 153 -0.912 -3.319 50.471 1.00 52.03 O
ATOM 4578 CG2 THR B 153 -2.248 -2.990 52.412 1.00 51.86 C
ATOM 4579 N ALA B 154 -2.663 -5.671 53.267 1.00 48.51 N
ATOM 4580 CA ALA B 154 -3.192 -6.254 54.509 1.00 46.82 C
ATOM 4581 C ALA B 154 -4.435 -5.562 55.080 1.00 47.84 C
ATOM 4582 O ALA B 154 -5.288 -6.218 55.675 1.00 45.27 O
ATOM 4583 CB ALA B 154 -2.096 -6.319 55.565 1.00 46.23 C
ATOM 4584 N ASP B 155 -4.527 -4.246 54.900 1.00 49.87 N
ATOM 4585 CA ASP B 155 -5.688 -3.481 55.359 1.00 54.12 C
ATOM 4586 C ASP B 155 -6.821 -3.434 54.325 1.00 55.32 C
ATOM 4587 O ASP B 155 -7.760 -2.651 54.458 1.00 56.51 O
ATOM 4588 CB ASP B 155 -5.272 -2.066 55.792 1.00 56.58 C
ATOM 4589 CG ASP B 155 -4.625 -1.262 54.670 1.00 58.65 C
ATOM 4590 OD1 ASP B 155 -4.184 -0.126 54.942 1.00 60.89 O
ATOM 4591 OD2 ASP B 155 -4.560 -1.747 53.521 1.00 57.32 O
ATOM 4592 N GLY B 156 -6.720 -4.272 53.297 1.00 55.58 N
ATOM 4593 CA GLY B 156 -7.777 -4.418 52.302 1.00 55.85 C
ATOM 4594 C GLY B 156 -7.715 -3.485 51.103 1.00 55.62 C
ATOM 4595 O GLY B 156 -8.506 -3.632 50.175 1.00 58.49 O
ATOM 4596 N GLU B 157 -6.794 -2.525 51.110 1.00 56.42 N
ATOM 4597 CA GLU B 157 -6.672 -1.601 49.979 1.00 59.13 C
ATOM 4598 C GLU B 157 -5.755 -2.143 48.877 1.00 60.71 C
ATOM 4599 O GLU B 157 -4.866 -2.964 49.135 1.00 61.43 O
ATOM 4600 CB GLU B 157 -6.237 -0.197 50.428 1.00 61.37 C
ATOM 4601 CG GLU B 157 -4.750 -0.022 50.712 1.00 61.74 C
ATOM 4602 CD GLU B 157 -4.243 1.366 50.348 1.00 63.87 C
ATOM 4603 OE1 GLU B 157 -3.581 2.012 51.192 1.00 61.09 O
ATOM 4604 OE2 GLU B 157 -4.501 1.813 49.210 1.00 64.51 O
ATOM 4605 N ILE B 158 -5.991 -1.680 47.650 1.00 57.71 N
ATOM 4606 CA ILE B 158 -5.208 -2.096 46.491 1.00 53.94 C
ATOM 4607 C ILE B 158 -4.202 -1.002 46.136 1.00 53.90 C
ATOM 4608 O ILE B 158 -4.572 0.075 45.666 1.00 54.33 O
ATOM 4609 CB ILE B 158 -6.105 -2.418 45.271 1.00 53.76 C
ATOM 4610 CG1 ILE B 158 -7.297 -3.309 45.668 1.00 53.64 C
ATOM 4611 CG2 ILE B 158 -5.287 -3.039 44.145 1.00 54.44 C
ATOM 4612 CD1 ILE B 158 -6.958 -4.742 46.023 1.00 50.65 C
ATOM 4613 N ARG B 159 -2.929 -1.276 46.387 1.00 51.18 N
ATOM 4614 CA ARG B 159 -1.876 -0.344 46.027 1.00 51.77 C
ATOM 4615 C ARG B 159 -1.522 -0.564 44.560 1.00 50.52 C
ATOM 4616 O ARG B 159 -1.356 -1.704 44.115 1.00 51.43 O
ATOM 4617 CB ARG B 159 -0.644 -0.527 46.923 1.00 52.93 C
ATOM 4618 CG ARG B 159 -0.922 -0.544 48.425 1.00 53.48 C
ATOM 4619 CD ARG B 159 -0.923 0.854 49.023 1.00 52.43 C
ATOM 4620 NE ARG B 159 0.425 1.414 49.126 1.00 52.23 N
ATOM 4621 CZ ARG B 159 1.192 1.339 50.212 1.00 50.58 C
ATOM 4622 NH1 ARG B 159 0.755 0.720 51.304 1.00 50.33 N
ATOM 4623 NH2 ARG B 159 2.402 1.879 50.204 1.00 49.59 N
ATOM 4624 N HIS B 160 -1.449 0.524 43.801 1.00 48.04 N
ATOM 4625 CA HIS B 160 -0.989 0.450 42.428 1.00 45.03 C
ATOM 4626 C HIS B 160 0.483 0.687 42.449 1.00 44.47 C
ATOM 4627 O HIS B 160 0.941 1.812 42.661 1.00 46.55 O
ATOM 4628 CB HIS B 160 -1.700 1.464 41.542 1.00 44.61 C
ATOM 4629 CG HIS B 160 -1.452 1.257 40.067 1.00 45.22 C
ATOM 4630 ND1 HIS B 160 -2.042 0.271 39.366 1.00 44.74 N
ATOM 4631 CD2 HIS B 160 -0.635 1.946 39.168 1.00 44.14 C
ATOM 4632 CE1 HIS B 160 -1.636 0.329 38.081 1.00 44.26 C
ATOM 4633 NE2 HIS B 160 -0.773 1.354 37.963 1.00 44.04 N
ATOM 4634 N LEU B 161 1.243 -0.385 42.259 1.00 42.12 N
ATOM 4635 CA LEU B 161 2.699 -0.319 42.347 1.00 40.18 C
ATOM 4636 C LEU B 161 3.335 -0.192 40.973 1.00 38.48 C
ATOM 4637 O LEU B 161 2.966 -0.910 40.044 1.00 37.67 O
ATOM 4638 CB LEU B 161 3.251 -1.555 43.064 1.00 39.51 C
ATOM 4639 CG LEU B 161 2.584 -2.003 44.364 1.00 39.70 C
ATOM 4640 CD1 LEU B 161 3.290 -3.232 44.909 1.00 38.32 C
ATOM 4641 CD2 LEU B 161 2.586 -0.885 45.399 1.00 38.15 C
ATOM 4642 N THR B 162 4.279 0.738 40.855 1.00 38.33 N
ATOM 4643 CA THR B 162 5.088 0.900 39.653 1.00 36.74 C
ATOM 4644 C THR B 162 6.551 0.933 40.097 1.00 36.23 C
ATOM 4645 O THR B 162 6.836 1.348 41.227 1.00 35.28 O
ATOM 4646 CB THR B 162 4.729 2.184 38.855 1.00 38.85 C
ATOM 4647 OG1 THR B 162 5.358 3.329 39.444 1.00 37.00 O
ATOM 4648 CG2 THR B 162 3.208 2.406 38.793 1.00 36.27 C
ATOM 4649 N PRO B 163 7.476 0.463 39.230 1.00 34.99 N
ATOM 4650 CA PRO B 163 8.903 0.378 39.551 1.00 35.81 C
ATOM 4651 C PRO B 163 9.573 1.699 39.923 1.00 39.58 C
ATOM 4652 O PRO B 163 10.468 1.695 40.764 1.00 40.69 O
ATOM 4653 CB PRO B 163 9.532 -0.164 38.252 1.00 32.90 C
ATOM 4654 CG PRO B 163 8.518 0.098 37.182 1.00 32.95 C
ATOM 4655 CD PRO B 163 7.202 -0.084 37.889 1.00 34.51 C
ATOM 4656 N THR B 164 9.167 2.804 39.295 1.00 42.37 N
ATOM 4657 CA THR B 164 9.833 4.099 39.512 1.00 45.83 C
ATOM 4658 C THR B 164 8.938 5.174 40.131 1.00 47.95 C
ATOM 4659 O THR B 164 9.361 6.323 40.275 1.00 49.66 O
ATOM 4660 CB THR B 164 10.425 4.685 38.209 1.00 45.73 C
ATOM 4661 OG1 THR B 164 9.361 5.059 37.326 1.00 46.12 O
ATOM 4662 CG2 THR B 164 11.347 3.690 37.514 1.00 47.20 C
ATOM 4663 N GLY B 165 7.714 4.807 40.492 1.00 48.29 N
ATOM 4664 CA GLY B 165 6.767 5.766 41.060 1.00 51.27 C
ATOM 4665 C GLY B 165 6.975 6.002 42.544 1.00 52.65 C
ATOM 4666 O GLY B 165 8.042 5.697 43.086 1.00 51.82 O
ATOM 4667 N GLU B 166 5.947 6.541 43.199 1.00 53.79 N
ATOM 4668 CA GLU B 166 6.004 6.851 44.631 1.00 55.15 C
ATOM 4669 C GLU B 166 6.035 5.583 45.488 1.00 52.85 C
ATOM 4670 O GLU B 166 6.563 5.591 46.600 1.00 53.73 O
ATOM 4671 CB GLU B 166 4.829 7.750 45.043 1.00 57.65 C
ATOM 4672 CG GLU B 166 3.496 7.021 45.205 1.00 59.63 C
ATOM 4673 CD GLU B 166 2.330 7.960 45.422 1.00 61.72 C
ATOM 4674 OE1 GLU B 166 2.307 9.033 44.784 1.00 62.52 O
ATOM 4675 OE2 GLU B 166 1.428 7.618 46.223 1.00 63.53 O
ATOM 4676 N ASP B 167 5.463 4.502 44.962 1.00 48.82 N
ATOM 4677 CA ASP B 167 5.466 3.214 45.643 1.00 47.61 C
ATOM 4678 C ASP B 167 6.562 2.266 45.128 1.00 42.62 C
ATOM 4679 O ASP B 167 6.423 1.048 45.208 1.00 43.11 O
ATOM 4680 CB ASP B 167 4.079 2.559 45.568 1.00 50.27 C
ATOM 4681 CG ASP B 167 3.357 2.556 46.909 1.00 53.02 C
ATOM 4682 OD1 ASP B 167 4.027 2.457 47.954 1.00 57.23 O
ATOM 4683 OD2 ASP B 167 2.112 2.633 46.926 1.00 53.82 O
ATOM 4684 N ALA B 168 7.647 2.842 44.617 1.00 40.06 N
ATOM 4685 CA ALA B 168 8.802 2.095 44.101 1.00 39.67 C
ATOM 4686 C ALA B 168 9.350 1.066 45.091 1.00 40.69 C
ATOM 4687 O ALA B 168 9.682 -0.057 44.709 1.00 40.74 O
ATOM 4688 CB ALA B 168 9.908 3.058 43.689 1.00 39.30 C
ATOM 4689 N GLU B 169 9.443 1.462 46.359 1.00 41.04 N
ATOM 4690 CA GLU B 169 9.989 0.623 47.422 1.00 39.96 C
ATOM 4691 C GLU B 169 9.122 -0.616 47.703 1.00 38.28 C
ATOM 4692 O GLU B 169 9.643 -1.725 47.849 1.00 37.45 O
ATOM 4693 CB GLU B 169 10.206 1.478 48.681 1.00 43.37 C
ATOM 4694 CG GLU B 169 10.462 0.718 49.967 1.00 45.84 C
ATOM 4695 CD GLU B 169 10.598 1.651 51.161 1.00 48.49 C
ATOM 4696 OE1 GLU B 169 11.684 2.244 51.334 1.00 50.00 O
ATOM 4697 OE2 GLU B 169 9.621 1.789 51.925 1.00 48.65 O
ATOM 4698 N LEU B 170 7.805 -0.441 47.772 1.00 35.56 N
ATOM 4699 CA LEU B 170 6.921 -1.594 47.929 1.00 34.06 C
ATOM 4700 C LEU B 170 6.878 -2.479 46.659 1.00 31.94 C
ATOM 4701 O LEU B 170 6.758 -3.693 46.749 1.00 30.69 O
ATOM 4702 CB LEU B 170 5.511 -1.159 48.352 1.00 34.18 C
ATOM 4703 CG LEU B 170 4.498 -2.274 48.650 1.00 34.39 C
ATOM 4704 CD1 LEU B 170 5.030 -3.282 49.667 1.00 34.67 C
ATOM 4705 CD2 LEU B 170 3.165 -1.690 49.118 1.00 34.62 C
ATOM 4706 N PHE B 171 6.969 -1.857 45.492 1.00 32.90 N
ATOM 4707 CA PHE B 171 7.062 -2.585 44.226 1.00 34.00 C
ATOM 4708 C PHE B 171 8.230 -3.573 44.283 1.00 32.52 C
ATOM 4709 O PHE B 171 8.052 -4.782 44.098 1.00 31.18 O
ATOM 4710 CB PHE B 171 7.248 -1.609 43.056 1.00 34.44 C
ATOM 4711 CG PHE B 171 7.349 -2.280 41.706 1.00 35.51 C
ATOM 4712 CD1 PHE B 171 6.213 -2.481 40.930 1.00 35.17 C
ATOM 4713 CD2 PHE B 171 8.579 -2.716 41.214 1.00 34.94 C
ATOM 4714 CE1 PHE B 171 6.301 -3.095 39.687 1.00 35.30 C
ATOM 4715 CE2 PHE B 171 8.669 -3.336 39.974 1.00 35.42 C
ATOM 4716 CZ PHE B 171 7.529 -3.528 39.212 1.00 33.92 C
ATOM 4717 N TRP B 172 9.413 -3.047 44.573 1.00 31.97 N
ATOM 4718 CA TRP B 172 10.631 -3.850 44.578 1.00 31.89 C
ATOM 4719 C TRP B 172 10.766 -4.831 45.717 1.00 32.38 C
ATOM 4720 O TRP B 172 11.596 -5.736 45.649 1.00 32.43 O
ATOM 4721 CB TRP B 172 11.846 -2.956 44.425 1.00 31.13 C
ATOM 4722 CG TRP B 172 11.925 -2.409 43.027 1.00 31.35 C
ATOM 4723 CD1 TRP B 172 11.697 -1.103 42.606 1.00 30.85 C
ATOM 4724 CD2 TRP B 172 12.231 -3.158 41.800 1.00 31.44 C
ATOM 4725 NE1 TRP B 172 11.848 -0.994 41.249 1.00 31.02 N
ATOM 4726 CE2 TRP B 172 12.172 -2.189 40.704 1.00 31.66 C
ATOM 4727 CE3 TRP B 172 12.551 -4.486 41.514 1.00 32.97 C
ATOM 4728 CZ2 TRP B 172 12.426 -2.552 39.386 1.00 30.46 C
ATOM 4729 CZ3 TRP B 172 12.794 -4.840 40.181 1.00 31.64 C
ATOM 4730 CH2 TRP B 172 12.729 -3.896 39.146 1.00 31.42 C
ATOM 4731 N ALA B 173 9.938 -4.689 46.754 1.00 32.03 N
ATOM 4732 CA ALA B 173 9.870 -5.695 47.819 1.00 32.00 C
ATOM 4733 C ALA B 173 8.913 -6.827 47.446 1.00 31.56 C
ATOM 4734 O ALA B 173 9.029 -7.958 47.941 1.00 31.08 O
ATOM 4735 CB ALA B 173 9.460 -5.061 49.145 1.00 33.23 C
ATOM 4736 N THR B 174 7.969 -6.513 46.570 1.00 30.48 N
ATOM 4737 CA THR B 174 7.000 -7.492 46.097 1.00 31.29 C
ATOM 4738 C THR B 174 7.644 -8.416 45.046 1.00 29.74 C
ATOM 4739 O THR B 174 7.372 -9.617 45.016 1.00 29.83 O
ATOM 4740 CB THR B 174 5.730 -6.777 45.586 1.00 32.72 C
ATOM 4741 OG1 THR B 174 5.213 -5.949 46.641 1.00 33.38 O
ATOM 4742 CG2 THR B 174 4.652 -7.775 45.156 1.00 31.29 C
ATOM 4743 N VAL B 175 8.508 -7.844 44.210 1.00 28.96 N
ATOM 4744 CA VAL B 175 9.352 -8.613 43.284 1.00 29.02 C
ATOM 4745 C VAL B 175 10.257 -9.513 44.123 1.00 28.12 C
ATOM 4746 O VAL B 175 10.986 -9.034 44.990 1.00 28.68 O
ATOM 4747 CB VAL B 175 10.190 -7.678 42.372 1.00 29.09 C
ATOM 4748 CG1 VAL B 175 11.251 -8.450 41.592 1.00 28.32 C
ATOM 4749 CG2 VAL B 175 9.292 -6.921 41.402 1.00 28.38 C
ATOM 4750 N GLY B 176 10.172 -10.819 43.899 1.00 27.54 N
ATOM 4751 CA GLY B 176 10.954 -11.780 44.677 1.00 30.23 C
ATOM 4752 C GLY B 176 10.541 -11.868 46.144 1.00 31.90 C
ATOM 4753 O GLY B 176 11.184 -12.563 46.936 1.00 31.60 O
ATOM 4754 N GLY B 177 9.452 -11.182 46.500 1.00 32.05 N
ATOM 4755 CA GLY B 177 8.960 -11.157 47.876 1.00 32.14 C
ATOM 4756 C GLY B 177 8.193 -12.371 48.372 1.00 33.45 C
ATOM 4757 O GLY B 177 7.688 -12.371 49.511 1.00 33.79 O
ATOM 4758 N ASN B 178 8.084 -13.397 47.532 1.00 31.89 N
ATOM 4759 CA ASN B 178 7.429 -14.669 47.899 1.00 33.45 C
ATOM 4760 C ASN B 178 5.996 -14.581 48.458 1.00 36.05 C
ATOM 4761 O ASN B 178 5.594 -15.398 49.298 1.00 37.80 O
ATOM 4762 CB ASN B 178 8.333 -15.494 48.832 1.00 32.55 C
ATOM 4763 CG ASN B 178 9.544 -16.056 48.110 1.00 31.84 C
ATOM 4764 OD1 ASN B 178 9.525 -17.189 47.655 1.00 33.07 O
ATOM 4765 ND2 ASN B 178 10.587 -15.245 47.970 1.00 33.48 N
ATOM 4766 N GLY B 179 5.232 -13.605 47.972 1.00 35.80 N
ATOM 4767 CA GLY B 179 3.830 -13.425 48.372 1.00 38.84 C
ATOM 4768 C GLY B 179 3.611 -12.767 49.732 1.00 39.55 C
ATOM 4769 O GLY B 179 2.485 -12.726 50.231 1.00 42.11 O
ATOM 4770 N LEU B 180 4.675 -12.237 50.327 1.00 38.68 N
ATOM 4771 CA LEU B 180 4.627 -11.819 51.725 1.00 39.07 C
ATOM 4772 C LEU B 180 4.395 -10.335 51.914 1.00 40.68 C
ATOM 4773 O LEU B 180 4.477 -9.831 53.034 1.00 44.34 O
ATOM 4774 CB LEU B 180 5.888 -12.268 52.467 1.00 38.14 C
ATOM 4775 CG LEU B 180 6.118 -13.779 52.548 1.00 38.91 C
ATOM 4776 CD1 LEU B 180 7.545 -14.080 52.983 1.00 38.96 C
ATOM 4777 CD2 LEU B 180 5.108 -14.463 53.464 1.00 39.47 C
ATOM 4778 N THR B 181 4.118 -9.630 50.822 1.00 38.23 N
ATOM 4779 CA THR B 181 3.704 -8.235 50.910 1.00 37.86 C
ATOM 4780 C THR B 181 2.211 -8.116 50.626 1.00 36.60 C
ATOM 4781 O THR B 181 1.645 -7.028 50.712 1.00 37.17 O
ATOM 4782 CB THR B 181 4.452 -7.343 49.907 1.00 36.37 C
ATOM 4783 OG1 THR B 181 4.153 -7.788 48.580 1.00 35.77 O
ATOM 4784 CG2 THR B 181 5.952 -7.384 50.156 1.00 37.04 C
ATOM 4785 N GLY B 182 1.590 -9.240 50.276 1.00 37.79 N
ATOM 4786 CA GLY B 182 0.180 -9.274 49.908 1.00 38.40 C
ATOM 4787 C GLY B 182 -0.085 -10.111 48.673 1.00 39.50 C
ATOM 4788 O GLY B 182 0.774 -10.885 48.235 1.00 39.53 O
ATOM 4789 N ILE B 183 -1.281 -9.947 48.110 1.00 39.15 N
ATOM 4790 CA ILE B 183 -1.705 -10.697 46.929 1.00 38.71 C
ATOM 4791 C ILE B 183 -1.680 -9.812 45.678 1.00 37.89 C
ATOM 4792 O ILE B 183 -2.398 -8.810 45.601 1.00 36.92 O
ATOM 4793 CB ILE B 183 -3.105 -11.319 47.132 1.00 40.26 C
ATOM 4794 CG1 ILE B 183 -3.066 -12.345 48.270 1.00 41.18 C
ATOM 4795 CG2 ILE B 183 -3.598 -11.981 45.850 1.00 38.73 C
ATOM 4796 CD1 ILE B 183 -4.428 -12.768 48.766 1.00 41.78 C
ATOM 4797 N ILE B 184 -0.816 -10.169 44.725 1.00 37.12 N
ATOM 4798 CA ILE B 184 -0.777 -9.510 43.419 1.00 34.95 C
ATOM 4799 C ILE B 184 -2.050 -9.946 42.714 1.00 34.28 C
ATOM 4800 O ILE B 184 -2.316 -11.142 42.589 1.00 33.91 O
ATOM 4801 CB ILE B 184 0.464 -9.928 42.594 1.00 34.57 C
ATOM 4802 CG1 ILE B 184 1.748 -9.638 43.385 1.00 33.47 C
ATOM 4803 CG2 ILE B 184 0.488 -9.199 41.256 1.00 33.98 C
ATOM 4804 CD1 ILE B 184 2.887 -10.598 43.106 1.00 34.22 C
ATOM 4805 N MET B 185 -2.862 -8.976 42.305 1.00 34.06 N
ATOM 4806 CA MET B 185 -4.161 -9.285 41.705 1.00 35.75 C
ATOM 4807 C MET B 185 -4.074 -9.243 40.187 1.00 34.57 C
ATOM 4808 O MET B 185 -4.770 -9.973 39.488 1.00 34.79 O
ATOM 4809 CB MET B 185 -5.232 -8.292 42.183 1.00 37.20 C
ATOM 4810 CG MET B 185 -5.409 -8.208 43.695 1.00 39.33 C
ATOM 4811 SD MET B 185 -6.206 -9.658 44.419 1.00 42.46 S
ATOM 4812 CE MET B 185 -7.892 -9.462 43.835 1.00 40.81 C
ATOM 4813 N ARG B 186 -3.197 -8.384 39.688 1.00 35.50 N
ATOM 4814 CA ARG B 186 -3.198 -8.015 38.287 1.00 36.18 C
ATOM 4815 C ARG B 186 -1.882 -7.303 38.016 1.00 35.15 C
ATOM 4816 O ARG B 186 -1.295 -6.700 38.925 1.00 36.96 O
ATOM 4817 CB ARG B 186 -4.383 -7.072 38.034 1.00 35.89 C
ATOM 4818 CG ARG B 186 -4.729 -6.788 36.584 1.00 36.77 C
ATOM 4819 CD ARG B 186 -6.059 -6.059 36.506 1.00 35.91 C
ATOM 4820 NE ARG B 186 -6.250 -5.415 35.208 1.00 35.13 N
ATOM 4821 CZ ARG B 186 -7.409 -4.926 34.768 1.00 36.25 C
ATOM 4822 NH1 ARG B 186 -8.512 -5.021 35.514 1.00 32.31 N
ATOM 4823 NH2 ARG B 186 -7.469 -4.351 33.572 1.00 33.72 N
ATOM 4824 N ALA B 187 -1.421 -7.381 36.771 1.00 32.30 N
ATOM 4825 CA ALA B 187 -0.153 -6.784 36.386 1.00 29.65 C
ATOM 4826 C ALA B 187 -0.158 -6.311 34.938 1.00 29.27 C
ATOM 4827 O ALA B 187 -0.944 -6.791 34.121 1.00 27.06 O
ATOM 4828 CB ALA B 187 0.977 -7.774 36.619 1.00 29.35 C
ATOM 4829 N THR B 188 0.717 -5.356 34.631 1.00 28.93 N
ATOM 4830 CA THR B 188 1.016 -5.027 33.245 1.00 30.13 C
ATOM 4831 C THR B 188 2.480 -5.329 32.999 1.00 29.49 C
ATOM 4832 O THR B 188 3.335 -4.869 33.744 1.00 29.85 O
ATOM 4833 CB THR B 188 0.700 -3.564 32.862 1.00 31.71 C
ATOM 4834 OG1 THR B 188 1.478 -2.678 33.669 1.00 37.91 O
ATOM 4835 CG2 THR B 188 -0.775 -3.251 33.059 1.00 30.74 C
ATOM 4836 N ILE B 189 2.743 -6.117 31.957 1.00 28.10 N
ATOM 4837 CA ILE B 189 4.083 -6.564 31.600 1.00 27.48 C
ATOM 4838 C ILE B 189 4.454 -5.973 30.238 1.00 28.31 C
ATOM 4839 O ILE B 189 3.651 -5.991 29.293 1.00 27.66 O
ATOM 4840 CB ILE B 189 4.147 -8.115 31.525 1.00 27.55 C
ATOM 4841 CG1 ILE B 189 3.480 -8.784 32.750 1.00 28.34 C
ATOM 4842 CG2 ILE B 189 5.569 -8.627 31.288 1.00 27.72 C
ATOM 4843 CD1 ILE B 189 4.192 -8.592 34.071 1.00 28.91 C
ATOM 4844 N GLU B 190 5.664 -5.443 30.130 1.00 27.93 N
ATOM 4845 CA GLU B 190 6.150 -5.044 28.838 1.00 27.32 C
ATOM 4846 C GLU B 190 6.785 -6.263 28.163 1.00 27.41 C
ATOM 4847 O GLU B 190 7.748 -6.845 28.679 1.00 25.10 O
ATOM 4848 CB GLU B 190 7.149 -3.889 28.929 1.00 28.30 C
ATOM 4849 CG GLU B 190 7.479 -3.330 27.560 1.00 29.41 C
ATOM 4850 CD GLU B 190 8.525 -2.227 27.576 1.00 31.27 C
ATOM 4851 OE1 GLU B 190 8.796 -1.643 28.641 1.00 33.57 O
ATOM 4852 OE2 GLU B 190 9.062 -1.930 26.499 1.00 32.30 O
ATOM 4853 N MET B 191 6.235 -6.608 27.000 1.00 26.78 N
ATOM 4854 CA MET B 191 6.655 -7.774 26.223 1.00 27.50 C
ATOM 4855 C MET B 191 7.823 -7.436 25.309 1.00 27.43 C
ATOM 4856 O MET B 191 8.112 -6.256 25.054 1.00 27.53 O
ATOM 4857 CB MET B 191 5.468 -8.302 25.395 1.00 25.79 C
ATOM 4858 CG MET B 191 4.229 -8.593 26.231 1.00 26.98 C
ATOM 4859 SD MET B 191 4.429 -9.988 27.354 1.00 28.49 S
ATOM 4860 CE MET B 191 4.137 -11.348 26.222 1.00 28.86 C
ATOM 4861 N THR B 192 8.501 -8.473 24.829 1.00 27.67 N
ATOM 4862 CA THR B 192 9.587 -8.308 23.862 1.00 27.74 C
ATOM 4863 C THR B 192 9.011 -8.472 22.448 1.00 28.01 C
ATOM 4864 O THR B 192 8.341 -9.467 22.166 1.00 27.67 O
ATOM 4865 CB THR B 192 10.714 -9.333 24.122 1.00 28.54 C
ATOM 4866 O |
