*** 4fdo v/s 4FF6 ***
Job options:
ID = 20122707512611839
JOBID = 4fdo v/s 4FF6
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 4FF6
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-MAY-12 4FF6
TITLE MYCOBACTERIUM TUBERCULOSIS DPRE1 IN COMPLEX WITH CT325 - MONOCLINIC
TITLE 2 CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE DECAPRENYLPHOSPHORYL-BETA-D-RIBOSE OXIDASE;
COMPND 3 CHAIN: A, B;
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 4FF6 1 JRNL
REVDAT 1 04-JUL-12 4FF6 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. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 31565
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1581
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 29.9278 - 5.7697 1.00 2801 146 0.1653 0.2091
REMARK 3 2 5.7697 - 4.5849 1.00 2757 146 0.1547 0.2181
REMARK 3 3 4.5849 - 4.0069 1.00 2748 145 0.1534 0.1641
REMARK 3 4 4.0069 - 3.6412 1.00 2728 144 0.1813 0.2359
REMARK 3 5 3.6412 - 3.3806 1.00 2706 142 0.2121 0.2486
REMARK 3 6 3.3806 - 3.1815 1.00 2745 145 0.2323 0.3445
REMARK 3 7 3.1815 - 3.0224 1.00 2704 142 0.2357 0.2984
REMARK 3 8 3.0224 - 2.8909 1.00 2718 143 0.2537 0.3016
REMARK 3 9 2.8909 - 2.7797 1.00 2728 144 0.2450 0.3416
REMARK 3 10 2.7797 - 2.6838 1.00 2701 144 0.2503 0.2952
REMARK 3 11 2.6838 - 2.6000 0.98 2648 140 0.2710 0.3148
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.30
REMARK 3 B_SOL : 29.35
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.190
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) : 5.15950
REMARK 3 B22 (A**2) : 5.27050
REMARK 3 B33 (A**2) : -10.43000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -12.36220
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 : 0.009 6647
REMARK 3 ANGLE : 1.278 9052
REMARK 3 CHIRALITY : 0.086 1015
REMARK 3 PLANARITY : 0.006 1155
REMARK 3 DIHEDRAL : 15.467 2343
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND (RESID 7:461 OR RESID 501:501 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4032 -11.8560 36.5610
REMARK 3 T TENSOR
REMARK 3 T11: 0.1836 T22: 0.1574
REMARK 3 T33: 0.2492 T12: -0.0074
REMARK 3 T13: 0.0623 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 1.6223 L22: 0.9699
REMARK 3 L33: 2.5882 L12: -0.1516
REMARK 3 L13: 1.4668 L23: 0.1990
REMARK 3 S TENSOR
REMARK 3 S11: 0.0639 S12: -0.1231 S13: -0.1067
REMARK 3 S21: 0.0363 S22: 0.0754 S23: -0.0271
REMARK 3 S31: 0.1126 S32: -0.0682 S33: -0.0661
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND (RESID 7:461 OR RESID 501:501 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.5328 -18.5940 0.6185
REMARK 3 T TENSOR
REMARK 3 T11: 0.3272 T22: 0.3073
REMARK 3 T33: 0.3000 T12: 0.0393
REMARK 3 T13: 0.0158 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 3.4693 L22: 1.9050
REMARK 3 L33: 2.3615 L12: 1.1265
REMARK 3 L13: 1.9494 L23: 0.2313
REMARK 3 S TENSOR
REMARK 3 S11: 0.1229 S12: 0.6111 S13: -0.2708
REMARK 3 S21: -0.0698 S22: 0.2225 S23: 0.0299
REMARK 3 S31: 0.4925 S32: 0.2410 S33: -0.1589
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 3
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain 'A' and resid 7:260 and backbone
REMARK 3 SELECTION : chain 'B' and resid 7:260 and backbone
REMARK 3 ATOM PAIRS NUMBER : 1008
REMARK 3 RMSD : 0.050
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain 'A' and resid 303:314 and backbone
REMARK 3 SELECTION : chain 'B' and resid 303:314 and backbone
REMARK 3 ATOM PAIRS NUMBER : 48
REMARK 3 RMSD : 0.051
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain 'A' and resid 332:461 and backbone
REMARK 3 SELECTION : chain 'B' and resid 332:461 and backbone
REMARK 3 ATOM PAIRS NUMBER : 520
REMARK 3 RMSD : 0.068
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FF6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB072824.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
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 : MULTILAYER FOCUSSING OPTICS
REMARK 200 OPTICS : NULL
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 : 31582
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 29.926
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : 0.07700
REMARK 200 FOR THE DATA SET : 26.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.10
REMARK 200 R MERGE FOR SHELL (I) : 0.58000
REMARK 200 R SYM FOR SHELL (I) : 0.58000
REMARK 200 FOR SHELL : 3.600
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: 4FDP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M IMIDAZOLE, 31% V/V POLYPROPYLENE
REMARK 280 GLYCOL, PH 7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 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 42.26500
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 GLY A 46
REMARK 465 GLY A 47
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 PRO A 316
REMARK 465 LEU A 317
REMARK 465 ASP A 318
REMARK 465 MET A 319
REMARK 465 PHE A 320
REMARK 465 GLY A 321
REMARK 465 GLU A 322
REMARK 465 TRP A 323
REMARK 465 ASN A 324
REMARK 465 ARG A 325
REMARK 465 ALA A 326
REMARK 465 TYR A 327
REMARK 465 GLY A 328
REMARK 465 PRO A 329
REMARK 465 ALA A 330
REMARK 465 MET B -19
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 GLY B 46
REMARK 465 GLY B 47
REMARK 465 ALA B 269
REMARK 465 PRO B 270
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 PRO B 316
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 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 ARG A 18 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 37 CE NZ
REMARK 470 ARG A 41 NE CZ NH1 NH2
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 CG CD CE NZ
REMARK 470 ASP A 268 CG OD1 OD2
REMARK 470 GLU A 294 CD OE1 OE2
REMARK 470 ARG A 298 CD NE CZ NH1 NH2
REMARK 470 LYS A 299 CE NZ
REMARK 470 HIS A 315 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 362 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR B 7 OG1 CG2
REMARK 470 LYS B 37 CE NZ
REMARK 470 ARG B 41 NE CZ NH1 NH2
REMARK 470 TRP B 230 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 230 CZ3 CH2
REMARK 470 GLU B 254 CG CD OE1 OE2
REMARK 470 LYS B 259 CG CD CE NZ
REMARK 470 GLU B 263 CG CD OE1 OE2
REMARK 470 LYS B 266 CG CD CE NZ
REMARK 470 PHE B 267 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 295 CG CD1 CD2
REMARK 470 LYS B 299 CG CD CE NZ
REMARK 470 HIS B 315 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 334 CG CD OE1 NE2
REMARK 470 LYS B 349 CE NZ
REMARK 470 LYS B 393 CE NZ
REMARK 470 LYS B 398 CE NZ
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 THR A 19 O HOH A 632 1.87
REMARK 500 OE2 GLU A 402 NH1 ARG A 405 1.88
REMARK 500 O HOH A 610 O HOH A 622 2.04
REMARK 500 OH TYR A 431 O HOH A 653 2.09
REMARK 500 OG1 THR A 87 O HOH A 657 2.11
REMARK 500 OD2 ASP B 99 NH1 ARG B 119 2.12
REMARK 500 O HOH A 626 O HOH A 651 2.13
REMARK 500 O GLY A 140 O HOH A 605 2.13
REMARK 500 O HOH B 629 O HOH B 630 2.14
REMARK 500 OE2 GLU A 221 O HOH A 601 2.15
REMARK 500 O LEU A 250 O HOH A 658 2.15
REMARK 500 O PRO A 291 O HOH A 627 2.16
REMARK 500 O HOH A 638 O HOH A 639 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 159 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
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 TYR A 431 79.23 -115.99
REMARK 500 ARG B 49 -0.60 68.03
REMARK 500 GLU B 254 1.12 -63.87
REMARK 500 ALA B 343 48.75 -77.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 0T4 B 502
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 0T4 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 IMD A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FDP RELATED DB: PDB
REMARK 900 RELATED ID: 4FEH RELATED DB: PDB
REMARK 900 RELATED ID: 4FDN RELATED DB: PDB
REMARK 900 RELATED ID: 4FDO RELATED DB: PDB
DBREF 4FF6 A 1 461 UNP P72056 DPRE1_MYCTU 1 461
DBREF 4FF6 B 1 461 UNP P72056 DPRE1_MYCTU 1 461
SEQADV 4FF6 MET A -19 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 GLY A -18 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 SER A -17 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 SER A -16 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS A -15 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS A -14 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS A -13 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS A -12 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS A -11 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS A -10 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 SER A -9 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 SER A -8 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 GLY A -7 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 LEU A -6 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 VAL A -5 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 PRO A -4 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 ARG A -3 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 GLY A -2 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 SER A -1 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS A 0 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 MET B -19 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 GLY B -18 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 SER B -17 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 SER B -16 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS B -15 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS B -14 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS B -13 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS B -12 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS B -11 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS B -10 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 SER B -9 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 SER B -8 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 GLY B -7 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 LEU B -6 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 VAL B -5 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 PRO B -4 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 ARG B -3 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 GLY B -2 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 SER B -1 UNP P72056 EXPRESSION TAG
SEQADV 4FF6 HIS B 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
SEQRES 1 B 481 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 481 LEU VAL PRO ARG GLY SER HIS MET LEU SER VAL GLY ALA
SEQRES 3 B 481 THR THR THR ALA THR ARG LEU THR GLY TRP GLY ARG THR
SEQRES 4 B 481 ALA PRO SER VAL ALA ASN VAL LEU ARG THR PRO ASP ALA
SEQRES 5 B 481 GLU MET ILE VAL LYS ALA VAL ALA ARG VAL ALA GLU SER
SEQRES 6 B 481 GLY GLY GLY ARG GLY ALA ILE ALA ARG GLY LEU GLY ARG
SEQRES 7 B 481 SER TYR GLY ASP ASN ALA GLN ASN GLY GLY GLY LEU VAL
SEQRES 8 B 481 ILE ASP MET THR PRO LEU ASN THR ILE HIS SER ILE ASP
SEQRES 9 B 481 ALA ASP THR LYS LEU VAL ASP ILE ASP ALA GLY VAL ASN
SEQRES 10 B 481 LEU ASP GLN LEU MET LYS ALA ALA LEU PRO PHE GLY LEU
SEQRES 11 B 481 TRP VAL PRO VAL LEU PRO GLY THR ARG GLN VAL THR VAL
SEQRES 12 B 481 GLY GLY ALA ILE ALA CYS ASP ILE HIS GLY LYS ASN HIS
SEQRES 13 B 481 HIS SER ALA GLY SER PHE GLY ASN HIS VAL ARG SER MET
SEQRES 14 B 481 ASP LEU LEU THR ALA ASP GLY GLU ILE ARG HIS LEU THR
SEQRES 15 B 481 PRO THR GLY GLU ASP ALA GLU LEU PHE TRP ALA THR VAL
SEQRES 16 B 481 GLY GLY ASN GLY LEU THR GLY ILE ILE MET ARG ALA THR
SEQRES 17 B 481 ILE GLU MET THR PRO THR SER THR ALA TYR PHE ILE ALA
SEQRES 18 B 481 ASP GLY ASP VAL THR ALA SER LEU ASP GLU THR ILE ALA
SEQRES 19 B 481 LEU HIS SER ASP GLY SER GLU ALA ARG TYR THR TYR SER
SEQRES 20 B 481 SER ALA TRP PHE ASP ALA ILE SER ALA PRO PRO LYS LEU
SEQRES 21 B 481 GLY ARG ALA ALA VAL SER ARG GLY ARG LEU ALA THR VAL
SEQRES 22 B 481 GLU GLN LEU PRO ALA LYS LEU ARG SER GLU PRO LEU LYS
SEQRES 23 B 481 PHE ASP ALA PRO GLN LEU LEU THR LEU PRO ASP VAL PHE
SEQRES 24 B 481 PRO ASN GLY LEU ALA ASN LYS TYR THR PHE GLY PRO ILE
SEQRES 25 B 481 GLY GLU LEU TRP TYR ARG LYS SER GLY THR TYR ARG GLY
SEQRES 26 B 481 LYS VAL GLN ASN LEU THR GLN PHE TYR HIS PRO LEU ASP
SEQRES 27 B 481 MET PHE GLY GLU TRP ASN ARG ALA TYR GLY PRO ALA GLY
SEQRES 28 B 481 PHE LEU GLN TYR GLN PHE VAL ILE PRO THR GLU ALA VAL
SEQRES 29 B 481 ASP GLU PHE LYS LYS ILE ILE GLY VAL ILE GLN ALA SER
SEQRES 30 B 481 GLY HIS TYR SER PHE LEU ASN VAL PHE LYS LEU PHE GLY
SEQRES 31 B 481 PRO ARG ASN GLN ALA PRO LEU SER PHE PRO ILE PRO GLY
SEQRES 32 B 481 TRP ASN ILE CYS VAL ASP PHE PRO ILE LYS ASP GLY LEU
SEQRES 33 B 481 GLY LYS PHE VAL SER GLU LEU ASP ARG ARG VAL LEU GLU
SEQRES 34 B 481 PHE GLY GLY ARG LEU TYR THR ALA LYS ASP SER ARG THR
SEQRES 35 B 481 THR ALA GLU THR PHE HIS ALA MET TYR PRO ARG VAL ASP
SEQRES 36 B 481 GLU TRP ILE SER VAL ARG ARG LYS VAL ASP PRO LEU ARG
SEQRES 37 B 481 VAL PHE ALA SER ASP MET ALA ARG ARG LEU GLU LEU LEU
HET FAD A 501 53
HET 0T4 A 502 23
HET IMD A 503 5
HET IMD A 504 5
HET FAD B 501 53
HET 0T4 B 502 15
HET IMD B 503 5
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM 0T4 3-(HYDROXYAMINO)-N-[(1R)-1-PHENYLETHYL]-5-
HETNAM 2 0T4 (TRIFLUOROMETHYL)BENZAMIDE
HETNAM IMD IMIDAZOLE
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 0T4 2(C16 H15 F3 N2 O2)
FORMUL 5 IMD 3(C3 H5 N2 1+)
FORMUL 10 HOH *122(H2 O)
HELIX 1 1 ASP A 31 GLU A 44 1 14
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 ASP A 218 1 11
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 GLY A 290 THR A 302 1 13
HELIX 11 11 LEU A 310 HIS A 315 1 6
HELIX 12 12 ALA A 343 SER A 357 1 15
HELIX 13 13 GLY A 395 PHE A 410 1 16
HELIX 14 14 THR A 423 TYR A 431 1 9
HELIX 15 15 ARG A 433 ASP A 445 1 13
HELIX 16 16 SER A 452 LEU A 458 1 7
HELIX 17 17 ASP B 31 GLU B 44 1 14
HELIX 18 18 ASN B 97 LEU B 106 1 10
HELIX 19 19 THR B 122 CYS B 129 1 8
HELIX 20 20 ASN B 135 GLY B 140 1 6
HELIX 21 21 SER B 141 ASN B 144 5 4
HELIX 22 22 ASP B 167 VAL B 175 1 9
HELIX 23 23 SER B 208 SER B 217 1 10
HELIX 24 24 GLY B 219 TYR B 224 5 6
HELIX 25 25 THR B 252 LEU B 256 5 5
HELIX 26 26 GLU B 294 THR B 302 1 9
HELIX 27 27 ASN B 309 HIS B 315 1 7
HELIX 28 28 ALA B 343 SER B 357 1 15
HELIX 29 29 GLY B 395 PHE B 410 1 16
HELIX 30 30 THR B 423 TYR B 431 1 9
HELIX 31 31 ARG B 433 ASP B 445 1 13
HELIX 32 32 SER B 452 LEU B 458 1 7
SHEET 1 A 4 THR A 8 LEU A 13 0
SHEET 2 A 4 SER A 22 ARG A 28 -1 O ALA A 24 N THR A 11
SHEET 3 A 4 LEU A 70 ASP A 73 1 O ASP A 73 N LEU A 27
SHEET 4 A 4 ALA A 51 ARG A 54 1 N ILE A 52 O ILE A 72
SHEET 1 B10 ILE A 158 LEU A 161 0
SHEET 2 B10 VAL A 146 LEU A 152 -1 N MET A 149 O LEU A 161
SHEET 3 B10 ILE A 183 GLU A 190 -1 O ILE A 183 N LEU A 152
SHEET 4 B10 LEU A 89 ASP A 93 -1 N VAL A 90 O ILE A 189
SHEET 5 B10 ILE A 80 ASP A 84 -1 N SER A 82 O ASP A 91
SHEET 6 B10 ILE B 80 ASP B 84 -1 O ILE B 83 N ILE A 83
SHEET 7 B10 LEU B 89 ASP B 93 -1 O ASP B 91 N SER B 82
SHEET 8 B10 ILE B 183 GLU B 190 -1 O ILE B 189 N VAL B 90
SHEET 9 B10 VAL B 146 LEU B 152 -1 N LEU B 152 O ILE B 183
SHEET 10 B10 ILE B 158 LEU B 161 -1 O LEU B 161 N MET B 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 TYR A 226 O GLY A 248
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 TYR A 335 O VAL A 388
SHEET 8 D 8 ARG A 413 LEU A 414 -1 O ARG A 413 N VAL A 338
SHEET 1 E 4 THR B 8 LEU B 13 0
SHEET 2 E 4 SER B 22 ARG B 28 -1 O ALA B 24 N THR B 11
SHEET 3 E 4 LEU B 70 ASP B 73 1 O ASP B 73 N LEU B 27
SHEET 4 E 4 ALA B 51 ARG B 54 1 N ILE B 52 O ILE B 72
SHEET 1 F 2 LEU B 110 TRP B 111 0
SHEET 2 F 2 THR B 192 PRO B 193 -1 O THR B 192 N TRP B 111
SHEET 1 G 8 TYR B 303 GLN B 308 0
SHEET 2 G 8 PHE B 199 VAL B 205 -1 N ALA B 201 O LYS B 306
SHEET 3 G 8 ALA B 243 LEU B 250 -1 O ARG B 247 N ASP B 202
SHEET 4 G 8 TYR B 226 PHE B 231 -1 N TRP B 230 O ALA B 244
SHEET 5 G 8 VAL B 365 PHE B 369 -1 O PHE B 366 N ALA B 229
SHEET 6 G 8 GLY B 383 PRO B 391 -1 O ASN B 385 N LYS B 367
SHEET 7 G 8 PHE B 332 PRO B 340 -1 N LEU B 333 O PHE B 390
SHEET 8 G 8 ARG B 413 LEU B 414 -1 O ARG B 413 N VAL B 338
LINK SG CYS A 387 N8 0T4 A 502 1555 1555 1.90
CISPEP 1 PRO A 237 PRO A 238 0 -6.39
CISPEP 2 PRO B 237 PRO B 238 0 -1.26
SITE 1 AC1 34 TRP A 16 ILE A 52 ALA A 53 ARG A 54
SITE 2 AC1 34 GLY A 55 LEU A 56 GLY A 57 ARG A 58
SITE 3 AC1 34 SER A 59 TYR A 60 ASN A 63 ALA A 64
SITE 4 AC1 34 MET A 74 ALA A 94 PRO A 116 GLY A 117
SITE 5 AC1 34 THR A 118 VAL A 121 THR A 122 GLY A 124
SITE 6 AC1 34 GLY A 125 ALA A 128 CYS A 129 ILE A 131
SITE 7 AC1 34 HIS A 132 ASN A 178 GLY A 179 GLY A 182
SITE 8 AC1 34 ILE A 184 TYR A 415 ALA A 417 0T4 A 502
SITE 9 AC1 34 HOH A 608 HOH A 611
SITE 1 AC2 11 GLY A 117 GLY A 133 LYS A 134 TRP A 230
SITE 2 AC2 11 GLN A 336 VAL A 365 ASN A 385 ILE A 386
SITE 3 AC2 11 CYS A 387 FAD A 501 HOH A 655
SITE 1 AC3 4 SER A 82 ASP A 84 SER B 82 ASP B 84
SITE 1 AC4 6 MET A 102 ALA A 105 LEU A 106 LEU A 110
SITE 2 AC4 6 TRP A 111 VAL A 112
SITE 1 AC5 31 TRP B 16 ALA B 53 ARG B 54 GLY B 55
SITE 2 AC5 31 LEU B 56 GLY B 57 ARG B 58 SER B 59
SITE 3 AC5 31 TYR B 60 ASN B 63 ALA B 64 MET B 74
SITE 4 AC5 31 ALA B 94 PRO B 116 GLY B 117 THR B 118
SITE 5 AC5 31 VAL B 121 THR B 122 GLY B 124 GLY B 125
SITE 6 AC5 31 ALA B 128 CYS B 129 ILE B 131 HIS B 132
SITE 7 AC5 31 ASN B 178 GLY B 179 GLY B 182 ILE B 184
SITE 8 AC5 31 TYR B 415 ALA B 417 0T4 B 502
SITE 1 AC6 11 GLY B 117 HIS B 132 GLY B 133 LYS B 134
SITE 2 AC6 11 GLN B 336 VAL B 365 LYS B 367 ASN B 385
SITE 3 AC6 11 ILE B 386 CYS B 387 FAD B 501
SITE 1 AC7 6 MET B 102 LEU B 106 LEU B 110 TRP B 111
SITE 2 AC7 6 VAL B 112 MET B 191
CRYST1 78.260 84.530 80.850 90.00 103.54 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 0.012778 0.000000 0.003077 0.00000
SCALE2 0.000000 0.011830 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012722 0.00000
ATOM 1 N THR A 7 -16.190 -0.342 47.565 1.00 92.43 N
ATOM 2 CA THR A 7 -15.591 -0.930 46.367 1.00 97.75 C
ATOM 3 C THR A 7 -14.322 -1.740 46.699 1.00 96.22 C
ATOM 4 O THR A 7 -13.949 -2.663 45.966 1.00 92.29 O
ATOM 5 CB THR A 7 -15.304 0.140 45.286 1.00 78.94 C
ATOM 6 N THR A 8 -13.679 -1.405 47.816 1.00 97.65 N
ATOM 7 CA THR A 8 -12.476 -2.108 48.257 1.00 91.01 C
ATOM 8 C THR A 8 -12.793 -3.191 49.292 1.00 87.98 C
ATOM 9 O THR A 8 -13.806 -3.119 49.989 1.00 91.61 O
ATOM 10 CB THR A 8 -11.437 -1.126 48.841 1.00 84.82 C
ATOM 11 OG1 THR A 8 -11.773 -0.813 50.198 1.00 88.16 O
ATOM 12 CG2 THR A 8 -11.400 0.162 48.021 1.00 78.55 C
ATOM 13 N THR A 9 -11.924 -4.192 49.383 1.00 84.88 N
ATOM 14 CA THR A 9 -12.104 -5.286 50.330 1.00 84.23 C
ATOM 15 C THR A 9 -10.816 -5.553 51.118 1.00 90.98 C
ATOM 16 O THR A 9 -9.770 -5.843 50.531 1.00 89.44 O
ATOM 17 CB THR A 9 -12.614 -6.570 49.620 1.00 81.13 C
ATOM 18 OG1 THR A 9 -12.298 -7.722 50.411 1.00 81.98 O
ATOM 19 CG2 THR A 9 -11.987 -6.719 48.238 1.00 79.10 C
ATOM 20 N ALA A 10 -10.891 -5.423 52.444 1.00 93.75 N
ATOM 21 CA ALA A 10 -9.761 -5.739 53.317 1.00 91.45 C
ATOM 22 C ALA A 10 -9.313 -7.190 53.118 1.00 91.42 C
ATOM 23 O ALA A 10 -10.040 -8.131 53.448 1.00 83.91 O
ATOM 24 CB ALA A 10 -10.119 -5.483 54.775 1.00 79.60 C
ATOM 25 N THR A 11 -8.116 -7.363 52.564 1.00 89.03 N
ATOM 26 CA THR A 11 -7.601 -8.696 52.264 1.00 90.53 C
ATOM 27 C THR A 11 -6.227 -8.911 52.902 1.00 82.20 C
ATOM 28 O THR A 11 -5.465 -7.959 53.096 1.00 79.25 O
ATOM 29 CB THR A 11 -7.503 -8.933 50.735 1.00 85.28 C
ATOM 30 OG1 THR A 11 -8.597 -8.289 50.070 1.00 76.49 O
ATOM 31 CG2 THR A 11 -7.514 -10.425 50.410 1.00 78.25 C
ATOM 32 N ARG A 12 -5.925 -10.162 53.236 1.00 78.27 N
ATOM 33 CA ARG A 12 -4.610 -10.516 53.762 1.00 92.32 C
ATOM 34 C ARG A 12 -3.708 -11.001 52.626 1.00 93.23 C
ATOM 35 O ARG A 12 -3.995 -12.008 51.969 1.00 94.01 O
ATOM 36 CB ARG A 12 -4.714 -11.569 54.876 1.00 96.29 C
ATOM 37 CG ARG A 12 -3.386 -11.897 55.562 1.00 86.77 C
ATOM 38 CD ARG A 12 -3.555 -12.961 56.644 1.00 96.02 C
ATOM 39 NE ARG A 12 -2.326 -13.720 56.881 1.00 94.70 N
ATOM 40 CZ ARG A 12 -2.039 -14.887 56.305 1.00104.38 C
ATOM 41 NH1 ARG A 12 -2.894 -15.443 55.455 1.00107.22 N
ATOM 42 NH2 ARG A 12 -0.896 -15.503 56.580 1.00106.71 N
ATOM 43 N LEU A 13 -2.614 -10.277 52.404 1.00 87.38 N
ATOM 44 CA LEU A 13 -1.750 -10.514 51.250 1.00 85.88 C
ATOM 45 C LEU A 13 -0.358 -11.023 51.604 1.00 82.35 C
ATOM 46 O LEU A 13 0.224 -10.620 52.607 1.00 84.28 O
ATOM 47 CB LEU A 13 -1.596 -9.224 50.454 1.00 78.22 C
ATOM 48 CG LEU A 13 -2.873 -8.666 49.852 1.00 65.89 C
ATOM 49 CD1 LEU A 13 -2.660 -7.214 49.517 1.00 59.22 C
ATOM 50 CD2 LEU A 13 -3.231 -9.483 48.621 1.00 68.74 C
ATOM 51 N THR A 14 0.168 -11.909 50.762 1.00 79.32 N
ATOM 52 CA THR A 14 1.568 -12.317 50.826 1.00 80.50 C
ATOM 53 C THR A 14 2.111 -12.366 49.407 1.00 76.25 C
ATOM 54 O THR A 14 1.344 -12.361 48.450 1.00 81.65 O
ATOM 55 CB THR A 14 1.755 -13.726 51.443 1.00 78.58 C
ATOM 56 OG1 THR A 14 1.250 -14.725 50.545 1.00 77.06 O
ATOM 57 CG2 THR A 14 1.046 -13.843 52.773 1.00 80.95 C
ATOM 58 N GLY A 15 3.429 -12.421 49.266 1.00 71.71 N
ATOM 59 CA GLY A 15 4.020 -12.712 47.978 1.00 57.73 C
ATOM 60 C GLY A 15 3.861 -14.198 47.725 1.00 66.03 C
ATOM 61 O GLY A 15 3.083 -14.871 48.399 1.00 71.78 O
ATOM 62 N TRP A 16 4.615 -14.721 46.769 1.00 59.89 N
ATOM 63 CA TRP A 16 4.534 -16.135 46.405 1.00 62.61 C
ATOM 64 C TRP A 16 5.220 -17.010 47.458 1.00 68.22 C
ATOM 65 O TRP A 16 5.041 -18.229 47.483 1.00 66.46 O
ATOM 66 CB TRP A 16 5.176 -16.338 45.028 1.00 48.43 C
ATOM 67 CG TRP A 16 4.791 -17.589 44.289 1.00 54.85 C
ATOM 68 CD1 TRP A 16 5.593 -18.664 44.028 1.00 53.25 C
ATOM 69 CD2 TRP A 16 3.516 -17.883 43.690 1.00 49.34 C
ATOM 70 NE1 TRP A 16 4.898 -19.612 43.307 1.00 54.64 N
ATOM 71 CE2 TRP A 16 3.620 -19.160 43.087 1.00 53.94 C
ATOM 72 CE3 TRP A 16 2.294 -17.196 43.614 1.00 44.93 C
ATOM 73 CZ2 TRP A 16 2.546 -19.770 42.412 1.00 49.29 C
ATOM 74 CZ3 TRP A 16 1.225 -17.798 42.949 1.00 39.64 C
ATOM 75 CH2 TRP A 16 1.361 -19.074 42.354 1.00 49.71 C
ATOM 76 N GLY A 17 6.008 -16.373 48.323 1.00 76.01 N
ATOM 77 CA GLY A 17 6.727 -17.075 49.370 1.00 77.33 C
ATOM 78 C GLY A 17 5.816 -17.396 50.537 1.00 83.35 C
ATOM 79 O GLY A 17 6.218 -18.096 51.469 1.00 87.77 O
ATOM 80 N ARG A 18 4.588 -16.882 50.467 1.00 81.70 N
ATOM 81 CA ARG A 18 3.563 -17.093 51.490 1.00 85.10 C
ATOM 82 C ARG A 18 4.054 -16.640 52.874 1.00 90.69 C
ATOM 83 O ARG A 18 3.743 -17.245 53.906 1.00 89.27 O
ATOM 84 CB ARG A 18 3.069 -18.547 51.486 1.00 85.12 C
ATOM 85 N THR A 19 4.815 -15.550 52.877 1.00 89.62 N
ATOM 86 CA THR A 19 5.431 -15.040 54.095 1.00 86.68 C
ATOM 87 C THR A 19 5.312 -13.518 54.207 1.00 86.74 C
ATOM 88 O THR A 19 4.999 -12.834 53.232 1.00 87.87 O
ATOM 89 CB THR A 19 6.930 -15.431 54.170 1.00 83.61 C
ATOM 90 OG1 THR A 19 7.390 -15.331 55.523 1.00 89.03 O
ATOM 91 CG2 THR A 19 7.777 -14.525 53.276 1.00 70.26 C
ATOM 92 N ALA A 20 5.593 -13.005 55.402 1.00 87.66 N
ATOM 93 CA ALA A 20 5.439 -11.582 55.737 1.00 86.94 C
ATOM 94 C ALA A 20 4.058 -10.996 55.399 1.00 88.02 C
ATOM 95 O ALA A 20 3.972 -9.942 54.761 1.00 86.81 O
ATOM 96 CB ALA A 20 6.566 -10.742 55.110 1.00 64.73 C
ATOM 97 N PRO A 21 2.976 -11.661 55.857 1.00 87.35 N
ATOM 98 CA PRO A 21 1.632 -11.254 55.434 1.00 82.62 C
ATOM 99 C PRO A 21 1.220 -9.907 56.010 1.00 85.12 C
ATOM 100 O PRO A 21 1.676 -9.529 57.086 1.00 86.00 O
ATOM 101 CB PRO A 21 0.740 -12.371 55.979 1.00 82.92 C
ATOM 102 CG PRO A 21 1.470 -12.888 57.159 1.00 89.80 C
ATOM 103 CD PRO A 21 2.930 -12.748 56.856 1.00 86.86 C
ATOM 104 N SER A 22 0.358 -9.200 55.291 1.00 83.94 N
ATOM 105 CA SER A 22 -0.044 -7.853 55.665 1.00 82.61 C
ATOM 106 C SER A 22 -1.477 -7.600 55.172 1.00 84.54 C
ATOM 107 O SER A 22 -1.898 -8.179 54.171 1.00 88.31 O
ATOM 108 CB SER A 22 0.981 -6.865 55.086 1.00 68.44 C
ATOM 109 OG SER A 22 0.404 -5.654 54.689 1.00 69.54 O
ATOM 110 N VAL A 23 -2.241 -6.776 55.887 1.00 82.91 N
ATOM 111 CA VAL A 23 -3.635 -6.525 55.510 1.00 85.92 C
ATOM 112 C VAL A 23 -3.812 -5.177 54.825 1.00 81.19 C
ATOM 113 O VAL A 23 -3.414 -4.132 55.364 1.00 66.33 O
ATOM 114 CB VAL A 23 -4.611 -6.643 56.707 1.00 87.56 C
ATOM 115 CG1 VAL A 23 -6.018 -6.215 56.295 1.00 79.37 C
ATOM 116 CG2 VAL A 23 -4.631 -8.069 57.227 1.00 79.56 C
ATOM 117 N ALA A 24 -4.409 -5.223 53.634 1.00 78.13 N
ATOM 118 CA ALA A 24 -4.666 -4.023 52.848 1.00 76.78 C
ATOM 119 C ALA A 24 -6.070 -4.009 52.232 1.00 78.05 C
ATOM 120 O ALA A 24 -6.768 -5.028 52.187 1.00 70.60 O
ATOM 121 CB ALA A 24 -3.607 -3.867 51.768 1.00 65.78 C
ATOM 122 N ASN A 25 -6.474 -2.834 51.764 1.00 78.31 N
ATOM 123 CA ASN A 25 -7.742 -2.666 51.065 1.00 82.34 C
ATOM 124 C ASN A 25 -7.574 -2.886 49.565 1.00 77.79 C
ATOM 125 O ASN A 25 -7.017 -2.037 48.868 1.00 70.35 O
ATOM 126 CB ASN A 25 -8.303 -1.268 51.332 1.00 74.57 C
ATOM 127 CG ASN A 25 -8.565 -1.030 52.798 1.00 89.22 C
ATOM 128 OD1 ASN A 25 -7.836 -0.286 53.460 1.00 84.59 O
ATOM 129 ND2 ASN A 25 -9.604 -1.677 53.324 1.00 92.35 N
ATOM 130 N VAL A 26 -8.065 -4.022 49.077 1.00 73.92 N
ATOM 131 CA VAL A 26 -7.841 -4.422 47.693 1.00 70.11 C
ATOM 132 C VAL A 26 -8.959 -4.025 46.739 1.00 73.40 C
ATOM 133 O VAL A 26 -9.992 -4.697 46.652 1.00 74.74 O
ATOM 134 CB VAL A 26 -7.596 -5.933 47.568 1.00 71.45 C
ATOM 135 CG1 VAL A 26 -7.369 -6.311 46.110 1.00 58.79 C
ATOM 136 CG2 VAL A 26 -6.402 -6.345 48.428 1.00 69.87 C
ATOM 137 N LEU A 27 -8.741 -2.927 46.022 1.00 72.74 N
ATOM 138 CA LEU A 27 -9.623 -2.525 44.934 1.00 66.18 C
ATOM 139 C LEU A 27 -9.458 -3.462 43.737 1.00 68.32 C
ATOM 140 O LEU A 27 -8.335 -3.761 43.326 1.00 64.75 O
ATOM 141 CB LEU A 27 -9.321 -1.089 44.510 1.00 55.16 C
ATOM 142 CG LEU A 27 -10.054 -0.570 43.263 1.00 62.99 C
ATOM 143 CD1 LEU A 27 -11.578 -0.692 43.387 1.00 42.69 C
ATOM 144 CD2 LEU A 27 -9.652 0.869 42.993 1.00 56.32 C
ATOM 145 N ARG A 28 -10.573 -3.937 43.190 1.00 68.05 N
ATOM 146 CA ARG A 28 -10.536 -4.752 41.979 1.00 67.07 C
ATOM 147 C ARG A 28 -11.597 -4.324 40.980 1.00 66.81 C
ATOM 148 O ARG A 28 -12.758 -4.717 41.079 1.00 72.98 O
ATOM 149 CB ARG A 28 -10.708 -6.236 42.283 1.00 65.15 C
ATOM 150 CG ARG A 28 -10.651 -7.060 41.016 1.00 68.19 C
ATOM 151 CD ARG A 28 -11.128 -8.472 41.205 1.00 70.35 C
ATOM 152 NE ARG A 28 -10.820 -9.250 40.015 1.00 75.89 N
ATOM 153 CZ ARG A 28 -9.652 -9.857 39.820 1.00 87.46 C
ATOM 154 NH1 ARG A 28 -8.706 -9.774 40.760 1.00 72.13 N
ATOM 155 NH2 ARG A 28 -9.431 -10.548 38.698 1.00 74.89 N
ATOM 156 N THR A 29 -11.197 -3.522 40.006 1.00 65.18 N
ATOM 157 CA THR A 29 -12.145 -3.044 39.011 1.00 68.14 C
ATOM 158 C THR A 29 -11.535 -3.086 37.604 1.00 68.56 C
ATOM 159 O THR A 29 -10.379 -2.709 37.417 1.00 72.28 O
ATOM 160 CB THR A 29 -12.639 -1.617 39.382 1.00 60.15 C
ATOM 161 OG1 THR A 29 -13.561 -1.134 38.398 1.00 75.93 O
ATOM 162 CG2 THR A 29 -11.473 -0.659 39.487 1.00 63.76 C
ATOM 163 N PRO A 30 -12.299 -3.586 36.617 1.00 66.17 N
ATOM 164 CA PRO A 30 -11.929 -3.484 35.198 1.00 60.04 C
ATOM 165 C PRO A 30 -12.074 -2.054 34.679 1.00 58.36 C
ATOM 166 O PRO A 30 -11.718 -1.775 33.535 1.00 53.71 O
ATOM 167 CB PRO A 30 -12.949 -4.390 34.513 1.00 61.38 C
ATOM 168 CG PRO A 30 -14.116 -4.431 35.473 1.00 53.05 C
ATOM 169 CD PRO A 30 -13.482 -4.438 36.815 1.00 60.66 C
ATOM 170 N ASP A 31 -12.580 -1.158 35.521 1.00 54.11 N
ATOM 171 CA ASP A 31 -12.844 0.212 35.105 1.00 58.13 C
ATOM 172 C ASP A 31 -11.706 1.161 35.460 1.00 64.15 C
ATOM 173 O ASP A 31 -11.531 1.529 36.622 1.00 66.51 O
ATOM 174 CB ASP A 31 -14.162 0.719 35.712 1.00 63.09 C
ATOM 175 CG ASP A 31 -14.556 2.125 35.212 1.00 70.86 C
ATOM 176 OD1 ASP A 31 -14.070 2.571 34.143 1.00 67.71 O
ATOM 177 OD2 ASP A 31 -15.374 2.784 35.891 1.00 67.48 O
ATOM 178 N ALA A 32 -10.952 1.578 34.449 1.00 59.25 N
ATOM 179 CA ALA A 32 -9.848 2.510 34.652 1.00 59.06 C
ATOM 180 C ALA A 32 -10.281 3.799 35.333 1.00 66.25 C
ATOM 181 O ALA A 32 -9.468 4.485 35.931 1.00 78.00 O
ATOM 182 CB ALA A 32 -9.138 2.815 33.341 1.00 45.92 C
ATOM 183 N GLU A 33 -11.562 4.124 35.258 1.00 70.84 N
ATOM 184 CA GLU A 33 -12.039 5.345 35.875 1.00 71.93 C
ATOM 185 C GLU A 33 -12.101 5.204 37.389 1.00 70.77 C
ATOM 186 O GLU A 33 -11.691 6.109 38.107 1.00 72.62 O
ATOM 187 CB GLU A 33 -13.383 5.771 35.278 1.00 82.15 C
ATOM 188 CG GLU A 33 -13.709 7.250 35.467 1.00 98.66 C
ATOM 189 CD GLU A 33 -12.655 8.195 34.876 1.00108.36 C
ATOM 190 OE1 GLU A 33 -11.734 7.735 34.158 1.00 97.60 O
ATOM 191 OE2 GLU A 33 -12.756 9.416 35.134 1.00107.51 O
ATOM 192 N MET A 34 -12.592 4.062 37.865 1.00 71.44 N
ATOM 193 CA MET A 34 -12.624 3.772 39.296 1.00 75.70 C
ATOM 194 C MET A 34 -11.201 3.809 39.853 1.00 75.67 C
ATOM 195 O MET A 34 -10.967 4.260 40.978 1.00 68.81 O
ATOM 196 CB MET A 34 -13.237 2.388 39.559 1.00 78.26 C
ATOM 197 CG MET A 34 -14.710 2.217 39.177 1.00 80.61 C
ATOM 198 SD MET A 34 -15.882 3.021 40.297 1.00114.69 S
ATOM 199 CE MET A 34 -16.229 4.554 39.418 1.00 88.63 C
ATOM 200 N ILE A 35 -10.253 3.337 39.046 1.00 73.03 N
ATOM 201 CA ILE A 35 -8.847 3.308 39.438 1.00 65.06 C
ATOM 202 C ILE A 35 -8.248 4.709 39.574 1.00 65.67 C
ATOM 203 O ILE A 35 -7.683 5.032 40.619 1.00 68.11 O
ATOM 204 CB ILE A 35 -8.004 2.449 38.472 1.00 55.55 C
ATOM 205 CG1 ILE A 35 -8.266 0.971 38.730 1.00 56.70 C
ATOM 206 CG2 ILE A 35 -6.525 2.730 38.632 1.00 45.11 C
ATOM 207 CD1 ILE A 35 -7.601 0.074 37.732 1.00 55.29 C
ATOM 208 N VAL A 36 -8.381 5.536 38.535 1.00 65.15 N
ATOM 209 CA VAL A 36 -7.859 6.905 38.569 1.00 65.45 C
ATOM 210 C VAL A 36 -8.403 7.689 39.758 1.00 75.16 C
ATOM 211 O VAL A 36 -7.687 8.483 40.378 1.00 75.89 O
ATOM 212 CB VAL A 36 -8.210 7.692 37.295 1.00 64.46 C
ATOM 213 CG1 VAL A 36 -7.564 9.071 37.337 1.00 63.34 C
ATOM 214 CG2 VAL A 36 -7.742 6.948 36.068 1.00 57.82 C
ATOM 215 N LYS A 37 -9.673 7.453 40.077 1.00 76.32 N
ATOM 216 CA LYS A 37 -10.347 8.199 41.132 1.00 76.73 C
ATOM 217 C LYS A 37 -10.024 7.651 42.517 1.00 74.99 C
ATOM 218 O LYS A 37 -10.131 8.372 43.511 1.00 76.65 O
ATOM 219 CB LYS A 37 -11.868 8.237 40.902 1.00 73.24 C
ATOM 220 CG LYS A 37 -12.363 9.478 40.142 1.00 75.53 C
ATOM 221 CD LYS A 37 -12.578 9.215 38.649 1.00 71.11 C
ATOM 222 N ALA A 38 -9.626 6.383 42.578 1.00 71.04 N
ATOM 223 CA ALA A 38 -9.206 5.771 43.837 1.00 64.43 C
ATOM 224 C ALA A 38 -7.833 6.289 44.237 1.00 74.06 C
ATOM 225 O ALA A 38 -7.501 6.365 45.427 1.00 72.38 O
ATOM 226 CB ALA A 38 -9.162 4.279 43.703 1.00 63.40 C
ATOM 227 N VAL A 39 -7.034 6.628 43.228 1.00 71.04 N
ATOM 228 CA VAL A 39 -5.718 7.219 43.447 1.00 71.08 C
ATOM 229 C VAL A 39 -5.862 8.669 43.865 1.00 74.92 C
ATOM 230 O VAL A 39 -5.164 9.129 44.760 1.00 82.20 O
ATOM 231 CB VAL A 39 -4.806 7.110 42.201 1.00 66.36 C
ATOM 232 CG1 VAL A 39 -3.652 8.100 42.272 1.00 64.07 C
ATOM 233 CG2 VAL A 39 -4.279 5.695 42.060 1.00 65.83 C
ATOM 234 N ALA A 40 -6.775 9.388 43.223 1.00 79.72 N
ATOM 235 CA ALA A 40 -7.070 10.752 43.628 1.00 79.94 C
ATOM 236 C ALA A 40 -7.653 10.784 45.052 1.00 83.66 C
ATOM 237 O ALA A 40 -7.494 11.776 45.760 1.00 87.51 O
ATOM 238 CB ALA A 40 -8.008 11.410 42.625 1.00 84.84 C
ATOM 239 N ARG A 41 -8.295 9.685 45.467 1.00 79.87 N
ATOM 240 CA ARG A 41 -8.880 9.543 46.811 1.00 78.25 C
ATOM 241 C ARG A 41 -7.828 9.181 47.856 1.00 84.23 C
ATOM 242 O ARG A 41 -8.091 9.200 49.059 1.00 91.56 O
ATOM 243 CB ARG A 41 -9.989 8.480 46.813 1.00 85.26 C
ATOM 244 CG ARG A 41 -10.809 8.386 48.110 1.00 81.77 C
ATOM 245 CD ARG A 41 -11.292 6.964 48.382 1.00 66.12 C
ATOM 246 N VAL A 42 -6.631 8.849 47.393 1.00 89.89 N
ATOM 247 CA VAL A 42 -5.512 8.568 48.285 1.00 86.40 C
ATOM 248 C VAL A 42 -4.621 9.810 48.376 1.00 83.56 C
ATOM 249 O VAL A 42 -3.959 10.044 49.386 1.00 91.18 O
ATOM 250 CB VAL A 42 -4.720 7.323 47.786 1.00 73.47 C
ATOM 251 CG1 VAL A 42 -3.392 7.190 48.501 1.00 68.42 C
ATOM 252 CG2 VAL A 42 -5.545 6.053 47.966 1.00 62.04 C
ATOM 253 N ALA A 43 -4.658 10.630 47.331 1.00 77.21 N
ATOM 254 CA ALA A 43 -3.781 11.798 47.234 1.00 90.40 C
ATOM 255 C ALA A 43 -4.230 13.049 48.012 1.00104.33 C
ATOM 256 O ALA A 43 -3.419 13.938 48.272 1.00101.42 O
ATOM 257 CB ALA A 43 -3.516 12.147 45.770 1.00 74.48 C
ATOM 258 N GLU A 44 -5.506 13.127 48.378 1.00108.48 N
ATOM 259 CA GLU A 44 -6.000 14.286 49.125 1.00110.13 C
ATOM 260 C GLU A 44 -6.035 13.987 50.626 1.00110.50 C
ATOM 261 O GLU A 44 -6.159 14.894 51.448 1.00116.42 O
ATOM 262 CB GLU A 44 -7.372 14.741 48.594 1.00118.20 C
ATOM 263 CG GLU A 44 -8.589 14.062 49.220 1.00115.35 C
ATOM 264 CD GLU A 44 -8.788 12.640 48.743 1.00110.80 C
ATOM 265 OE1 GLU A 44 -7.779 11.948 48.483 1.00102.80 O
ATOM 266 OE2 GLU A 44 -9.958 12.214 48.629 1.00114.34 O
ATOM 267 N SER A 45 -5.915 12.709 50.971 1.00104.57 N
ATOM 268 CA SER A 45 -5.722 12.303 52.357 1.00105.14 C
ATOM 269 C SER A 45 -4.233 12.311 52.687 1.00101.83 C
ATOM 270 O SER A 45 -3.811 11.806 53.729 1.00100.65 O
ATOM 271 CB SER A 45 -6.301 10.906 52.589 1.00101.20 C
ATOM 272 OG SER A 45 -7.632 10.819 52.110 1.00 93.42 O
ATOM 273 N GLY A 48 -1.202 8.930 53.680 1.00 83.06 N
ATOM 274 CA GLY A 48 -1.516 7.975 54.727 1.00 87.71 C
ATOM 275 C GLY A 48 -1.367 6.548 54.241 1.00 88.17 C
ATOM 276 O GLY A 48 -2.351 5.891 53.896 1.00 91.03 O
ATOM 277 N ARG A 49 -0.123 6.079 54.205 1.00 78.88 N
ATOM 278 CA ARG A 49 0.219 4.728 53.741 1.00 79.56 C
ATOM 279 C ARG A 49 -0.036 4.443 52.259 1.00 63.22 C
ATOM 280 O ARG A 49 0.199 3.332 51.795 1.00 61.32 O
ATOM 281 CB ARG A 49 -0.395 3.652 54.638 1.00 73.76 C
ATOM 282 CG ARG A 49 0.246 3.669 56.005 1.00 74.32 C
ATOM 283 CD ARG A 49 -0.228 2.546 56.880 1.00 73.60 C
ATOM 284 NE ARG A 49 0.538 1.318 56.689 1.00 76.77 N
ATOM 285 CZ ARG A 49 1.781 1.130 57.127 1.00 72.83 C
ATOM 286 NH1 ARG A 49 2.431 2.107 57.755 1.00 62.98 N
ATOM 287 NH2 ARG A 49 2.384 -0.036 56.918 1.00 73.68 N
ATOM 288 N GLY A 50 -0.497 5.455 51.534 1.00 63.43 N
ATOM 289 CA GLY A 50 -0.621 5.403 50.084 1.00 64.52 C
ATOM 290 C GLY A 50 -1.207 4.175 49.393 1.00 61.13 C
ATOM 291 O GLY A 50 -2.093 3.490 49.926 1.00 60.56 O
ATOM 292 N ALA A 51 -0.694 3.891 48.194 1.00 57.83 N
ATOM 293 CA ALA A 51 -1.249 2.827 47.353 1.00 59.52 C
ATOM 294 C ALA A 51 -0.196 2.094 46.538 1.00 50.48 C
ATOM 295 O ALA A 51 0.779 2.695 46.084 1.00 53.61 O
ATOM 296 CB ALA A 51 -2.313 3.403 46.416 1.00 50.88 C
ATOM 297 N ILE A 52 -0.405 0.800 46.329 1.00 46.70 N
ATOM 298 CA ILE A 52 0.447 0.040 45.411 1.00 49.82 C
ATOM 299 C ILE A 52 -0.359 -0.823 44.416 1.00 51.46 C
ATOM 300 O ILE A 52 -1.405 -1.389 44.753 1.00 50.59 O
ATOM 301 CB ILE A 52 1.502 -0.819 46.176 1.00 40.63 C
ATOM 302 CG1 ILE A 52 2.799 -0.958 45.378 1.00 31.11 C
ATOM 303 CG2 ILE A 52 0.941 -2.166 46.566 1.00 45.84 C
ATOM 304 CD1 ILE A 52 3.412 0.371 45.004 1.00 33.49 C
ATOM 305 N ALA A 53 0.123 -0.899 43.178 1.00 49.16 N
ATOM 306 CA ALA A 53 -0.447 -1.816 42.190 1.00 40.93 C
ATOM 307 C ALA A 53 -0.022 -3.256 42.484 1.00 41.68 C
ATOM 308 O ALA A 53 1.087 -3.499 42.953 1.00 43.85 O
ATOM 309 CB ALA A 53 0.003 -1.430 40.814 1.00 39.07 C
ATOM 310 N ARG A 54 -0.909 -4.207 42.220 1.00 41.32 N
ATOM 311 CA ARG A 54 -0.568 -5.620 42.310 1.00 36.14 C
ATOM 312 C ARG A 54 -0.940 -6.312 40.999 1.00 47.06 C
ATOM 313 O ARG A 54 -1.949 -5.972 40.382 1.00 44.45 O
ATOM 314 CB ARG A 54 -1.304 -6.289 43.473 1.00 38.79 C
ATOM 315 CG ARG A 54 -0.972 -7.778 43.658 1.00 40.79 C
ATOM 316 CD ARG A 54 -1.898 -8.424 44.673 1.00 44.67 C
ATOM 317 NE ARG A 54 -1.490 -9.764 45.105 1.00 47.62 N
ATOM 318 CZ ARG A 54 -0.617 -10.015 46.089 1.00 58.09 C
ATOM 319 NH1 ARG A 54 -0.015 -9.014 46.730 1.00 46.83 N
ATOM 320 NH2 ARG A 54 -0.329 -11.271 46.425 1.00 45.48 N
ATOM 321 N GLY A 55 -0.133 -7.278 40.570 1.00 43.93 N
ATOM 322 CA GLY A 55 -0.448 -8.053 39.380 1.00 30.56 C
ATOM 323 C GLY A 55 -0.959 -9.420 39.788 1.00 36.22 C
ATOM 324 O GLY A 55 -1.897 -9.532 40.570 1.00 42.30 O
ATOM 325 N LEU A 56 -0.323 -10.466 39.280 1.00 36.16 N
ATOM 326 CA LEU A 56 -0.682 -11.837 39.636 1.00 33.36 C
ATOM 327 C LEU A 56 0.020 -12.373 40.899 1.00 40.02 C
ATOM 328 O LEU A 56 -0.061 -13.569 41.206 1.00 39.01 O
ATOM 329 CB LEU A 56 -0.424 -12.768 38.437 1.00 34.18 C
ATOM 330 CG LEU A 56 -1.529 -12.690 37.367 1.00 41.13 C
ATOM 331 CD1 LEU A 56 -1.094 -13.231 35.999 1.00 34.41 C
ATOM 332 CD2 LEU A 56 -2.718 -13.452 37.882 1.00 30.00 C
ATOM 333 N GLY A 57 0.725 -11.492 41.608 1.00 43.40 N
ATOM 334 CA GLY A 57 1.350 -11.827 42.879 1.00 36.40 C
ATOM 335 C GLY A 57 2.422 -12.911 42.836 1.00 43.66 C
ATOM 336 O GLY A 57 2.641 -13.618 43.818 1.00 44.71 O
ATOM 337 N ARG A 58 3.092 -13.048 41.698 1.00 44.82 N
ATOM 338 CA ARG A 58 4.121 -14.074 41.539 1.00 45.36 C
ATOM 339 C ARG A 58 5.438 -13.660 42.190 1.00 42.29 C
ATOM 340 O ARG A 58 6.334 -14.473 42.359 1.00 41.41 O
ATOM 341 CB ARG A 58 4.340 -14.399 40.051 1.00 37.31 C
ATOM 342 CG ARG A 58 3.647 -15.678 39.577 1.00 37.96 C
ATOM 343 CD ARG A 58 2.248 -15.794 40.178 1.00 40.43 C
ATOM 344 NE ARG A 58 1.540 -16.989 39.720 1.00 45.13 N
ATOM 345 CZ ARG A 58 0.214 -17.113 39.742 1.00 43.94 C
ATOM 346 NH1 ARG A 58 -0.535 -16.122 40.213 1.00 39.07 N
ATOM 347 NH2 ARG A 58 -0.368 -18.221 39.304 1.00 38.08 N
ATOM 348 N SER A 59 5.562 -12.382 42.524 1.00 39.88 N
ATOM 349 CA SER A 59 6.772 -11.891 43.163 1.00 44.31 C
ATOM 350 C SER A 59 6.782 -12.442 44.584 1.00 47.07 C
ATOM 351 O SER A 59 5.775 -12.381 45.287 1.00 51.92 O
ATOM 352 CB SER A 59 6.810 -10.355 43.125 1.00 38.99 C
ATOM 353 OG SER A 59 7.886 -9.817 43.861 1.00 54.88 O
ATOM 354 N TYR A 60 7.905 -13.021 44.986 1.00 43.86 N
ATOM 355 CA TYR A 60 8.024 -13.646 46.299 1.00 54.19 C
ATOM 356 C TYR A 60 8.067 -12.620 47.449 1.00 57.54 C
ATOM 357 O TYR A 60 7.641 -12.901 48.579 1.00 53.77 O
ATOM 358 CB TYR A 60 9.273 -14.520 46.341 1.00 50.03 C
ATOM 359 CG TYR A 60 9.252 -15.734 45.432 1.00 56.90 C
ATOM 360 CD1 TYR A 60 8.842 -16.978 45.911 1.00 56.52 C
ATOM 361 CD2 TYR A 60 9.669 -15.651 44.096 1.00 58.39 C
ATOM 362 CE1 TYR A 60 8.849 -18.116 45.091 1.00 58.93 C
ATOM 363 CE2 TYR A 60 9.674 -16.784 43.260 1.00 54.84 C
ATOM 364 CZ TYR A 60 9.259 -18.016 43.768 1.00 63.37 C
ATOM 365 OH TYR A 60 9.249 -19.144 42.961 1.00 60.81 O
ATOM 366 N GLY A 61 8.571 -11.427 47.145 1.00 52.97 N
ATOM 367 CA GLY A 61 8.794 -10.418 48.156 1.00 55.30 C
ATOM 368 C GLY A 61 7.545 -9.719 48.634 1.00 50.77 C
ATOM 369 O GLY A 61 6.441 -10.232 48.511 1.00 49.73 O
ATOM 370 N ASP A 62 7.745 -8.525 49.174 1.00 51.18 N
ATOM 371 CA ASP A 62 6.668 -7.723 49.715 1.00 50.31 C
ATOM 372 C ASP A 62 6.455 -6.434 48.922 1.00 44.34 C
ATOM 373 O ASP A 62 6.027 -5.420 49.472 1.00 41.43 O
ATOM 374 CB ASP A 62 6.929 -7.417 51.194 1.00 52.85 C
ATOM 375 CG ASP A 62 8.307 -6.806 51.446 1.00 50.17 C
ATOM 376 OD1 ASP A 62 9.035 -6.474 50.483 1.00 44.89 O
ATOM 377 OD2 ASP A 62 8.650 -6.638 52.633 1.00 53.56 O
ATOM 378 N ASN A 63 6.743 -6.481 47.625 1.00 43.09 N
ATOM 379 CA ASN A 63 6.561 -5.306 46.768 1.00 44.45 C
ATOM 380 C ASN A 63 5.124 -5.057 46.273 1.00 44.13 C
ATOM 381 O ASN A 63 4.793 -3.938 45.875 1.00 40.31 O
ATOM 382 CB ASN A 63 7.530 -5.336 45.588 1.00 42.97 C
ATOM 383 CG ASN A 63 7.605 -6.705 44.917 1.00 44.33 C
ATOM 384 OD1 ASN A 63 7.182 -7.724 45.479 1.00 44.32 O
ATOM 385 ND2 ASN A 63 8.178 -6.734 43.720 1.00 31.49 N
ATOM 386 N ALA A 64 4.283 -6.090 46.303 1.00 41.77 N
ATOM 387 CA ALA A 64 2.891 -5.960 45.847 1.00 45.96 C
ATOM 388 C ALA A 64 1.904 -6.061 46.992 1.00 55.48 C
ATOM 389 O ALA A 64 0.807 -6.592 46.822 1.00 56.03 O
ATOM 390 CB ALA A 64 2.555 -7.004 44.800 1.00 34.52 C
ATOM 391 N GLN A 65 2.316 -5.589 48.164 1.00 56.48 N
ATOM 392 CA GLN A 65 1.436 -5.472 49.320 1.00 54.56 C
ATOM 393 C GLN A 65 1.711 -4.160 50.015 1.00 54.70 C
ATOM 394 O GLN A 65 2.810 -3.608 49.921 1.00 51.71 O
ATOM 395 CB GLN A 65 1.605 -6.639 50.293 1.00 51.81 C
ATOM 396 CG GLN A 65 3.030 -7.083 50.554 1.00 45.19 C
ATOM 397 CD GLN A 65 3.092 -8.417 51.295 1.00 56.91 C
ATOM 398 OE1 GLN A 65 2.444 -8.592 52.321 1.00 69.64 O
ATOM 399 NE2 GLN A 65 3.868 -9.357 50.779 1.00 59.80 N
ATOM 400 N ASN A 66 0.706 -3.651 50.706 1.00 55.95 N
ATOM 401 CA ASN A 66 0.851 -2.364 51.350 1.00 58.67 C
ATOM 402 C ASN A 66 0.036 -2.329 52.641 1.00 62.01 C
ATOM 403 O ASN A 66 -1.095 -1.863 52.652 1.00 68.38 O
ATOM 404 CB ASN A 66 0.434 -1.275 50.364 1.00 48.93 C
ATOM 405 CG ASN A 66 0.519 0.108 50.949 1.00 52.77 C
ATOM 406 OD1 ASN A 66 1.340 0.377 51.830 1.00 58.96 O
ATOM 407 ND2 ASN A 66 -0.339 1.004 50.465 1.00 47.32 N
ATOM 408 N GLY A 67 0.619 -2.859 53.716 1.00 64.27 N
ATOM 409 CA GLY A 67 -0.016 -2.912 55.029 1.00 66.51 C
ATOM 410 C GLY A 67 -0.815 -1.698 55.434 1.00 63.56 C
ATOM 411 O GLY A 67 -0.303 -0.583 55.419 1.00 62.51 O
ATOM 412 N GLY A 68 -2.081 -1.914 55.773 1.00 63.17 N
ATOM 413 CA GLY A 68 -2.964 -0.820 56.134 1.00 62.55 C
ATOM 414 C GLY A 68 -3.003 0.304 55.111 1.00 65.70 C
ATOM 415 O GLY A 68 -3.078 1.484 55.466 1.00 62.88 O
ATOM 416 N GLY A 69 -2.943 -0.063 53.833 1.00 71.77 N
ATOM 417 CA GLY A 69 -3.050 0.900 52.749 1.00 63.35 C
ATOM 418 C GLY A 69 -3.884 0.357 51.608 1.00 64.45 C
ATOM 419 O GLY A 69 -4.553 -0.672 51.746 1.00 64.04 O
ATOM 420 N LEU A 70 -3.843 1.041 50.471 1.00 62.83 N
ATOM 421 CA LEU A 70 -4.571 0.576 49.299 1.00 60.76 C
ATOM 422 C LEU A 70 -3.690 -0.301 48.419 1.00 58.20 C
ATOM 423 O LEU A 70 -2.578 0.083 48.062 1.00 56.83 O
ATOM 424 CB LEU A 70 -5.104 1.766 48.494 1.00 61.71 C
ATOM 425 CG LEU A 70 -5.963 1.497 47.247 1.00 61.75 C
ATOM 426 CD1 LEU A 70 -7.336 0.925 47.597 1.00 56.20 C
ATOM 427 CD2 LEU A 70 -6.105 2.758 46.405 1.00 56.94 C
ATOM 428 N VAL A 71 -4.193 -1.486 48.091 1.00 58.61 N
ATOM 429 CA VAL A 71 -3.595 -2.336 47.065 1.00 54.84 C
ATOM 430 C VAL A 71 -4.550 -2.496 45.864 1.00 60.24 C
ATOM 431 O VAL A 71 -5.652 -3.028 45.992 1.00 60.74 O
ATOM 432 CB VAL A 71 -3.195 -3.710 47.636 1.00 58.62 C
ATOM 433 CG1 VAL A 71 -2.917 -4.698 46.515 1.00 54.47 C
ATOM 434 CG2 VAL A 71 -1.984 -3.570 48.548 1.00 48.08 C
ATOM 435 N ILE A 72 -4.128 -2.019 44.698 1.00 56.80 N
ATOM 436 CA ILE A 72 -4.972 -2.050 43.503 1.00 54.56 C
ATOM 437 C ILE A 72 -4.698 -3.254 42.587 1.00 54.17 C
ATOM 438 O ILE A 72 -3.673 -3.297 41.908 1.00 56.34 O
ATOM 439 CB ILE A 72 -4.789 -0.768 42.696 1.00 52.35 C
ATOM 440 CG1 ILE A 72 -5.119 0.439 43.576 1.00 57.22 C
ATOM 441 CG2 ILE A 72 -5.649 -0.795 41.436 1.00 48.45 C
ATOM 442 CD1 ILE A 72 -4.974 1.767 42.879 1.00 49.33 C
ATOM 443 N ASP A 73 -5.606 -4.230 42.570 1.00 52.61 N
ATOM 444 CA ASP A 73 -5.440 -5.385 41.693 1.00 47.84 C
ATOM 445 C ASP A 73 -5.683 -4.979 40.252 1.00 53.51 C
ATOM 446 O ASP A 73 -6.747 -4.458 39.918 1.00 61.81 O
ATOM 447 CB ASP A 73 -6.380 -6.521 42.069 1.00 43.37 C
ATOM 448 CG ASP A 73 -6.039 -7.808 41.350 1.00 54.24 C
ATOM 449 OD1 ASP A 73 -5.705 -7.757 40.148 1.00 56.88 O
ATOM 450 OD2 ASP A 73 -6.080 -8.882 41.983 1.00 62.54 O
ATOM 451 N MET A 74 -4.695 -5.245 39.401 1.00 55.81 N
ATOM 452 CA MET A 74 -4.701 -4.802 38.004 1.00 53.91 C
ATOM 453 C MET A 74 -5.146 -5.876 37.000 1.00 48.35 C
ATOM 454 O MET A 74 -5.368 -5.585 35.826 1.00 44.71 O
ATOM 455 CB MET A 74 -3.309 -4.300 37.624 1.00 44.91 C
ATOM 456 CG MET A 74 -2.957 -2.980 38.257 1.00 45.21 C
ATOM 457 SD MET A 74 -4.238 -1.768 37.927 1.00 53.88 S
ATOM 458 CE MET A 74 -3.701 -1.054 36.384 1.00 36.86 C
ATOM 459 N THR A 75 -5.266 -7.113 37.460 1.00 44.56 N
ATOM 460 CA THR A 75 -5.641 -8.200 36.568 1.00 51.48 C
ATOM 461 C THR A 75 -6.998 -8.056 35.836 1.00 53.52 C
ATOM 462 O THR A 75 -7.142 -8.561 34.725 1.00 52.78 O
ATOM 463 CB THR A 75 -5.499 -9.578 37.247 1.00 46.57 C
ATOM 464 OG1 THR A 75 -6.411 -9.686 38.342 1.00 53.38 O
ATOM 465 CG2 THR A 75 -4.107 -9.745 37.766 1.00 46.30 C
ATOM 466 N PRO A 76 -7.994 -7.380 36.441 1.00 60.31 N
ATOM 467 CA PRO A 76 -9.201 -7.133 35.637 1.00 53.89 C
ATOM 468 C PRO A 76 -8.965 -6.298 34.375 1.00 53.99 C
ATOM 469 O PRO A 76 -9.718 -6.439 33.397 1.00 54.54 O
ATOM 470 CB PRO A 76 -10.130 -6.380 36.602 1.00 55.12 C
ATOM 471 CG PRO A 76 -9.279 -6.023 37.792 1.00 65.74 C
ATOM 472 CD PRO A 76 -8.236 -7.089 37.863 1.00 58.36 C
ATOM 473 N LEU A 77 -7.948 -5.444 34.395 1.00 45.16 N
ATOM 474 CA LEU A 77 -7.637 -4.606 33.246 1.00 43.68 C
ATOM 475 C LEU A 77 -6.752 -5.379 32.289 1.00 46.29 C
ATOM 476 O LEU A 77 -5.564 -5.120 32.203 1.00 44.84 O
ATOM 477 CB LEU A 77 -6.898 -3.370 33.712 1.00 40.09 C
ATOM 478 CG LEU A 77 -7.417 -2.023 33.249 1.00 49.91 C
ATOM 479 CD1 LEU A 77 -7.566 -1.124 34.454 1.00 52.63 C
ATOM 480 CD2 LEU A 77 -6.444 -1.420 32.259 1.00 50.18 C
ATOM 481 N ASN A 78 -7.326 -6.334 31.574 1.00 41.89 N
ATOM 482 CA ASN A 78 -6.524 -7.234 30.765 1.00 40.22 C
ATOM 483 C ASN A 78 -6.962 -7.280 29.309 1.00 44.48 C
ATOM 484 O ASN A 78 -7.032 -8.357 28.717 1.00 36.73 O
ATOM 485 CB ASN A 78 -6.588 -8.631 31.349 1.00 42.50 C
ATOM 486 CG ASN A 78 -7.999 -9.171 31.372 1.00 47.29 C
ATOM 487 OD1 ASN A 78 -8.973 -8.415 31.254 1.00 35.96 O
ATOM 488 ND2 ASN A 78 -8.120 -10.483 31.513 1.00 43.63 N
ATOM 489 N THR A 79 -7.244 -6.109 28.741 1.00 41.47 N
ATOM 490 CA THR A 79 -7.595 -6.005 27.338 1.00 35.15 C
ATOM 491 C THR A 79 -6.356 -5.926 26.442 1.00 38.46 C
ATOM 492 O THR A 79 -5.495 -5.062 26.619 1.00 42.08 O
ATOM 493 CB THR A 79 -8.503 -4.776 27.073 1.00 37.86 C
ATOM 494 OG1 THR A 79 -9.812 -5.042 27.572 1.00 46.62 O
ATOM 495 CG2 THR A 79 -8.592 -4.451 25.573 1.00 30.41 C
ATOM 496 N ILE A 80 -6.276 -6.842 25.484 1.00 36.82 N
ATOM 497 CA ILE A 80 -5.351 -6.736 24.364 1.00 34.77 C
ATOM 498 C ILE A 80 -5.999 -5.850 23.312 1.00 40.94 C
ATOM 499 O ILE A 80 -7.029 -6.217 22.740 1.00 38.93 O
ATOM 500 CB ILE A 80 -5.038 -8.134 23.763 1.00 29.19 C
ATOM 501 CG1 ILE A 80 -4.261 -8.975 24.805 1.00 42.01 C
ATOM 502 CG2 ILE A 80 -4.242 -7.988 22.505 1.00 25.20 C
ATOM 503 CD1 ILE A 80 -3.662 -10.291 24.293 1.00 34.88 C
ATOM 504 N HIS A 81 -5.407 -4.678 23.076 1.00 39.00 N
ATOM 505 CA HIS A 81 -5.972 -3.681 22.169 1.00 31.50 C
ATOM 506 C HIS A 81 -5.663 -3.943 20.709 1.00 34.14 C
ATOM 507 O HIS A 81 -6.546 -3.862 19.871 1.00 36.46 O
ATOM 508 CB HIS A 81 -5.502 -2.286 22.563 1.00 38.43 C
ATOM 509 CG HIS A 81 -6.016 -1.844 23.890 1.00 41.25 C
ATOM 510 ND1 HIS A 81 -7.329 -1.481 24.091 1.00 45.36 N
ATOM 511 CD2 HIS A 81 -5.410 -1.739 25.094 1.00 44.39 C
ATOM 512 CE1 HIS A 81 -7.505 -1.149 25.356 1.00 43.23 C
ATOM 513 NE2 HIS A 81 -6.354 -1.301 25.988 1.00 47.07 N
ATOM 514 N SER A 82 -4.411 -4.244 20.402 1.00 34.66 N
ATOM 515 CA SER A 82 -4.049 -4.637 19.048 1.00 32.03 C
ATOM 516 C SER A 82 -2.719 -5.357 19.038 1.00 35.79 C
ATOM 517 O SER A 82 -1.914 -5.217 19.958 1.00 32.64 O
ATOM 518 CB SER A 82 -3.938 -3.421 18.129 1.00 30.29 C
ATOM 519 OG SER A 82 -2.820 -2.607 18.469 1.00 26.06 O
ATOM 520 N ILE A 83 -2.502 -6.114 17.968 1.00 34.37 N
ATOM 521 CA ILE A 83 -1.237 -6.754 17.665 1.00 27.75 C
ATOM 522 C ILE A 83 -1.025 -6.488 16.173 1.00 32.43 C
ATOM 523 O ILE A 83 -1.974 -6.552 15.394 1.00 32.17 O
ATOM 524 CB ILE A 83 -1.325 -8.274 17.911 1.00 27.87 C
ATOM 525 CG1 ILE A 83 -1.536 -8.588 19.395 1.00 24.13 C
ATOM 526 CG2 ILE A 83 -0.098 -8.988 17.368 1.00 30.26 C
ATOM 527 CD1 ILE A 83 -1.537 -10.089 19.695 1.00 26.02 C
ATOM 528 N ASP A 84 0.206 -6.184 15.769 1.00 33.31 N
ATOM 529 CA ASP A 84 0.504 -5.858 14.375 1.00 28.12 C
ATOM 530 C ASP A 84 1.743 -6.643 13.978 1.00 34.79 C
ATOM 531 O ASP A 84 2.812 -6.455 14.570 1.00 37.37 O
ATOM 532 CB ASP A 84 0.759 -4.356 14.257 1.00 34.02 C
ATOM 533 CG ASP A 84 0.837 -3.862 12.824 1.00 34.73 C
ATOM 534 OD1 ASP A 84 1.589 -4.441 12.001 1.00 35.82 O
ATOM 535 OD2 ASP A 84 0.153 -2.855 12.534 1.00 32.91 O
ATOM 536 N ALA A 85 1.602 -7.533 12.994 1.00 32.11 N
ATOM 537 CA ALA A 85 2.719 -8.352 12.543 1.00 31.84 C
ATOM 538 C ALA A 85 3.776 -7.537 11.778 1.00 39.30 C
ATOM 539 O ALA A 85 4.927 -7.973 11.616 1.00 40.04 O
ATOM 540 CB ALA A 85 2.218 -9.509 11.693 1.00 31.63 C
ATOM 541 N ASP A 86 3.385 -6.358 11.305 1.00 35.42 N
ATOM 542 CA ASP A 86 4.248 -5.577 10.426 1.00 39.46 C
ATOM 543 C ASP A 86 5.194 -4.686 11.232 1.00 41.86 C
ATOM 544 O ASP A 86 6.402 -4.630 10.955 1.00 37.85 O
ATOM 545 CB ASP A 86 3.402 -4.735 9.453 1.00 39.06 C
ATOM 546 CG ASP A 86 2.594 -5.597 8.462 1.00 45.68 C
ATOM 547 OD1 ASP A 86 3.135 -6.616 7.966 1.00 41.06 O
ATOM 548 OD2 ASP A 86 1.414 -5.255 8.180 1.00 40.73 O
ATOM 549 N THR A 87 4.631 -3.994 12.223 1.00 31.00 N
ATOM 550 CA THR A 87 5.413 -3.184 13.144 1.00 34.73 C
ATOM 551 C THR A 87 5.992 -4.012 14.302 1.00 42.12 C
ATOM 552 O THR A 87 6.872 -3.542 15.035 1.00 41.77 O
ATOM 553 CB THR A 87 4.554 -2.089 13.760 1.00 38.50 C
ATOM 554 OG1 THR A 87 3.412 -2.694 14.376 1.00 34.53 O
ATOM 555 CG2 THR A 87 4.119 -1.058 12.698 1.00 25.25 C
ATOM 556 N LYS A 88 5.490 -5.238 14.453 1.00 37.36 N
ATOM 557 CA LYS A 88 5.833 -6.128 15.562 1.00 35.03 C
ATOM 558 C LYS A 88 5.359 -5.602 16.899 1.00 31.33 C
ATOM 559 O LYS A 88 5.791 -6.088 17.931 1.00 34.27 O
ATOM 560 CB LYS A 88 7.333 -6.446 15.631 1.00 38.53 C
ATOM 561 CG LYS A 88 7.792 -7.539 14.677 1.00 40.71 C
ATOM 562 CD LYS A 88 8.313 -6.951 13.383 1.00 47.98 C
ATOM 563 CE LYS A 88 9.592 -6.156 13.623 1.00 53.25 C
ATOM 564 NZ LYS A 88 10.734 -7.048 13.984 1.00 65.23 N
ATOM 565 N LEU A 89 4.462 -4.619 16.881 1.00 33.52 N
ATOM 566 CA LEU A 89 4.005 -3.988 18.124 1.00 29.87 C
ATOM 567 C LEU A 89 2.731 -4.582 18.696 1.00 34.78 C
ATOM 568 O LEU A 89 1.805 -4.926 17.984 1.00 40.29 O
ATOM 569 CB LEU A 89 3.818 -2.475 17.974 1.00 24.60 C
ATOM 570 CG LEU A 89 5.043 -1.630 17.611 1.00 38.93 C
ATOM 571 CD1 LEU A 89 4.675 -0.166 17.618 1.00 30.93 C
ATOM 572 CD2 LEU A 89 6.192 -1.878 18.587 1.00 38.76 C
ATOM 573 N VAL A 90 2.691 -4.662 20.013 1.00 36.53 N
ATOM 574 CA VAL A 90 1.541 -5.145 20.732 1.00 32.39 C
ATOM 575 C VAL A 90 1.148 -4.021 21.695 1.00 35.73 C
ATOM 576 O VAL A 90 2.010 -3.377 22.290 1.00 39.05 O
ATOM 577 CB VAL A 90 1.948 -6.422 21.495 1.00 38.46 C
ATOM 578 CG1 VAL A 90 1.239 -6.515 22.785 1.00 42.18 C
ATOM 579 CG2 VAL A 90 1.722 -7.661 20.640 1.00 32.53 C
ATOM 580 N ASP A 91 -0.146 -3.773 21.835 1.00 36.00 N
ATOM 581 CA ASP A 91 -0.653 -2.679 22.653 1.00 32.94 C
ATOM 582 C ASP A 91 -1.676 -3.270 23.610 1.00 34.14 C
ATOM 583 O ASP A 91 -2.765 -3.653 23.203 1.00 41.24 O
ATOM 584 CB ASP A 91 -1.283 -1.603 21.752 1.00 27.33 C
ATOM 585 CG ASP A 91 -2.035 -0.523 22.538 1.00 37.92 C
ATOM 586 OD1 ASP A 91 -1.911 -0.452 23.780 1.00 33.29 O
ATOM 587 OD2 ASP A 91 -2.748 0.281 21.902 1.00 37.16 O
ATOM 588 N ILE A 92 -1.319 -3.377 24.882 1.00 40.88 N
ATOM 589 CA ILE A 92 -2.166 -4.086 25.836 1.00 35.85 C
ATOM 590 C ILE A 92 -2.252 -3.388 27.186 1.00 41.73 C
ATOM 591 O ILE A 92 -1.427 -2.533 27.536 1.00 40.74 O
ATOM 592 CB ILE A 92 -1.689 -5.535 26.092 1.00 36.28 C
ATOM 593 CG1 ILE A 92 -0.426 -5.558 26.965 1.00 37.86 C
ATOM 594 CG2 ILE A 92 -1.473 -6.290 24.794 1.00 27.14 C
ATOM 595 CD1 ILE A 92 0.870 -5.426 26.196 1.00 36.25 C
ATOM 596 N ASP A 93 -3.269 -3.774 27.939 1.00 36.97 N
ATOM 597 CA ASP A 93 -3.467 -3.283 29.278 1.00 35.51 C
ATOM 598 C ASP A 93 -2.434 -3.941 30.189 1.00 38.82 C
ATOM 599 O ASP A 93 -1.986 -5.052 29.931 1.00 36.79 O
ATOM 600 CB ASP A 93 -4.876 -3.659 29.740 1.00 40.77 C
ATOM 601 CG ASP A 93 -5.972 -2.728 29.189 1.00 44.09 C
ATOM 602 OD1 ASP A 93 -5.674 -1.590 28.758 1.00 39.51 O
ATOM 603 OD2 ASP A 93 -7.157 -3.133 29.232 1.00 42.89 O
ATOM 604 N ALA A 94 -2.060 -3.263 31.266 1.00 46.24 N
ATOM 605 CA ALA A 94 -1.058 -3.784 32.192 1.00 36.60 C
ATOM 606 C ALA A 94 -1.481 -5.102 32.844 1.00 36.40 C
ATOM 607 O ALA A 94 -0.639 -5.900 33.239 1.00 40.71 O
ATOM 608 CB ALA A 94 -0.739 -2.764 33.239 1.00 38.01 C
ATOM 609 N GLY A 95 -2.781 -5.335 32.929 1.00 35.07 N
ATOM 610 CA GLY A 95 -3.301 -6.555 33.503 1.00 31.16 C
ATOM 611 C GLY A 95 -3.153 -7.811 32.669 1.00 34.14 C
ATOM 612 O GLY A 95 -3.351 -8.914 33.195 1.00 35.95 O
ATOM 613 N VAL A 96 -2.815 -7.689 31.386 1.00 31.51 N
ATOM 614 CA VAL A 96 -2.674 -8.907 30.581 1.00 35.98 C
ATOM 615 C VAL A 96 -1.420 -9.679 30.983 1.00 38.60 C
ATOM 616 O VAL A 96 -0.344 -9.098 31.181 1.00 38.67 O
ATOM 617 CB VAL A 96 -2.789 -8.692 29.018 1.00 39.20 C
ATOM 618 CG1 VAL A 96 -3.408 -7.358 28.681 1.00 32.47 C
ATOM 619 CG2 VAL A 96 -1.469 -8.888 28.281 1.00 24.98 C
ATOM 620 N ASN A 97 -1.574 -10.984 31.165 1.00 35.63 N
ATOM 621 CA ASN A 97 -0.443 -11.802 31.551 1.00 30.91 C
ATOM 622 C ASN A 97 0.294 -12.300 30.321 1.00 36.07 C
ATOM 623 O ASN A 97 -0.214 -12.197 29.208 1.00 40.55 O
ATOM 624 CB ASN A 97 -0.870 -12.959 32.450 1.00 39.08 C
ATOM 625 CG ASN A 97 -1.726 -13.983 31.729 1.00 37.25 C
ATOM 626 OD1 ASN A 97 -1.228 -14.774 30.916 1.00 31.05 O
ATOM 627 ND2 ASN A 97 -3.015 -14.000 32.055 1.00 31.61 N
ATOM 628 N LEU A 98 1.490 -12.850 30.513 1.00 39.70 N
ATOM 629 CA LEU A 98 2.327 -13.191 29.373 1.00 33.20 C
ATOM 630 C LEU A 98 1.914 -14.483 28.701 1.00 35.08 C
ATOM 631 O LEU A 98 2.288 -14.716 27.555 1.00 38.14 O
ATOM 632 CB LEU A 98 3.792 -13.260 29.759 1.00 31.17 C
ATOM 633 CG LEU A 98 4.390 -12.002 30.370 1.00 30.35 C
ATOM 634 CD1 LEU A 98 5.815 -12.303 30.751 1.00 22.85 C
ATOM 635 CD2 LEU A 98 4.306 -10.865 29.389 1.00 23.31 C
ATOM 636 N ASP A 99 1.154 -15.326 29.399 1.00 36.07 N
ATOM 637 CA ASP A 99 0.676 -16.561 28.802 1.00 37.16 C
ATOM 638 C ASP A 99 -0.398 -16.191 27.778 1.00 38.14 C
ATOM 639 O ASP A 99 -0.378 -16.638 26.620 1.00 29.38 O
ATOM 640 CB ASP A 99 0.126 -17.516 29.864 1.00 39.80 C
ATOM 641 CG ASP A 99 -0.352 -18.845 29.271 1.00 52.05 C
ATOM 642 OD1 ASP A 99 -1.484 -19.275 29.593 1.00 49.08 O
ATOM 643 OD2 ASP A 99 0.404 -19.455 28.479 1.00 48.72 O
ATOM 644 N GLN A 100 -1.311 -15.345 28.231 1.00 33.32 N
ATOM 645 CA GLN A 100 -2.370 -14.790 27.421 1.00 30.85 C
ATOM 646 C GLN A 100 -1.773 -14.106 26.195 1.00 35.55 C
ATOM 647 O GLN A 100 -2.142 -14.409 25.063 1.00 39.94 O
ATOM 648 CB GLN A 100 -3.155 -13.801 28.277 1.00 31.06 C
ATOM 649 CG GLN A 100 -4.240 -13.027 27.565 1.00 36.27 C
ATOM 650 CD GLN A 100 -4.773 -11.849 28.391 1.00 36.59 C
ATOM 651 OE1 GLN A 100 -4.284 -11.552 29.496 1.00 34.43 O
ATOM 652 NE2 GLN A 100 -5.778 -11.167 27.846 1.00 26.84 N
ATOM 653 N LEU A 101 -0.824 -13.211 26.427 1.00 36.78 N
ATOM 654 CA LEU A 101 -0.169 -12.485 25.351 1.00 32.14 C
ATOM 655 C LEU A 101 0.562 -13.421 24.388 1.00 35.12 C
ATOM 656 O LEU A 101 0.565 -13.218 23.173 1.00 37.36 O
ATOM 657 CB LEU A 101 0.800 -11.481 25.942 1.00 28.75 C
ATOM 658 CG LEU A 101 1.682 -10.773 24.944 1.00 29.62 C
ATOM 659 CD1 LEU A 101 0.799 -9.949 24.033 1.00 37.63 C
ATOM 660 CD2 LEU A 101 2.688 -9.893 25.675 1.00 33.05 C
ATOM 661 N MET A 102 1.177 -14.463 24.928 1.00 39.61 N
ATOM 662 CA MET A 102 1.909 -15.408 24.100 1.00 38.22 C
ATOM 663 C MET A 102 0.987 -16.096 23.091 1.00 42.15 C
ATOM 664 O MET A 102 1.321 -16.284 21.920 1.00 35.75 O
ATOM 665 CB MET A 102 2.545 -16.457 24.990 1.00 33.51 C
ATOM 666 CG MET A 102 3.562 -17.305 24.280 1.00 45.61 C
ATOM 667 SD MET A 102 3.838 -18.854 25.120 1.00 64.95 S
ATOM 668 CE MET A 102 2.187 -19.548 24.987 1.00 72.76 C
ATOM 669 N LYS A 103 -0.185 -16.469 23.578 1.00 36.60 N
ATOM 670 CA LYS A 103 -1.133 -17.227 22.809 1.00 38.20 C
ATOM 671 C LYS A 103 -1.829 -16.333 21.767 1.00 43.21 C
ATOM 672 O LYS A 103 -2.090 -16.757 20.636 1.00 43.27 O
ATOM 673 CB LYS A 103 -2.121 -17.893 23.769 1.00 33.92 C
ATOM 674 CG LYS A 103 -1.499 -19.058 24.527 1.00 45.42 C
ATOM 675 CD LYS A 103 -2.408 -19.587 25.629 1.00 52.75 C
ATOM 676 CE LYS A 103 -1.844 -20.865 26.271 1.00 66.97 C
ATOM 677 NZ LYS A 103 -2.607 -21.274 27.508 1.00 61.25 N
ATOM 678 N ALA A 104 -2.102 -15.088 22.129 1.00 34.08 N
ATOM 679 CA ALA A 104 -2.678 -14.165 21.172 1.00 32.11 C
ATOM 680 C ALA A 104 -1.689 -13.777 20.072 1.00 34.93 C
ATOM 681 O ALA A 104 -2.108 -13.467 18.962 1.00 37.62 O
ATOM 682 CB ALA A 104 -3.231 -12.926 21.864 1.00 30.07 C
ATOM 683 N ALA A 105 -0.389 -13.815 20.353 1.00 32.97 N
ATOM 684 CA ALA A 105 0.573 -13.236 19.418 1.00 27.91 C
ATOM 685 C ALA A 105 1.255 -14.226 18.491 1.00 32.88 C
ATOM 686 O ALA A 105 1.825 -13.817 17.466 1.00 36.93 O
ATOM 687 CB ALA A 105 1.611 -12.418 20.158 1.00 32.91 C
ATOM 688 N LEU A 106 1.225 -15.513 18.840 1.00 32.18 N
ATOM 689 CA LEU A 106 1.765 -16.544 17.948 1.00 33.02 C
ATOM 690 C LEU A 106 1.169 -16.495 16.537 1.00 36.91 C
ATOM 691 O LEU A 106 1.917 -16.492 15.553 1.00 37.28 O
ATOM 692 CB LEU A 106 1.605 -17.948 18.529 1.00 36.82 C
ATOM 693 CG LEU A 106 2.751 -18.489 19.370 1.00 38.48 C
ATOM 694 CD1 LEU A 106 2.369 -19.811 20.000 1.00 46.39 C
ATOM 695 CD2 LEU A 106 4.007 -18.611 18.524 1.00 37.14 C
ATOM 696 N PRO A 107 -0.173 -16.441 16.425 1.00 37.82 N
ATOM 697 CA PRO A 107 -0.755 -16.409 15.080 1.00 33.03 C
ATOM 698 C PRO A 107 -0.171 -15.319 14.171 1.00 37.69 C
ATOM 699 O PRO A 107 -0.292 -15.405 12.950 1.00 36.89 O
ATOM 700 CB PRO A 107 -2.233 -16.132 15.364 1.00 31.93 C
ATOM 701 CG PRO A 107 -2.482 -16.785 16.704 1.00 35.89 C
ATOM 702 CD PRO A 107 -1.219 -16.539 17.475 1.00 37.92 C
ATOM 703 N PHE A 108 0.479 -14.323 14.749 1.00 29.56 N
ATOM 704 CA PHE A 108 1.034 -13.250 13.945 1.00 28.59 C
ATOM 705 C PHE A 108 2.514 -13.518 13.657 1.00 28.67 C
ATOM 706 O PHE A 108 3.199 -12.699 13.065 1.00 31.76 O
ATOM 707 CB PHE A 108 0.860 -11.904 14.653 1.00 29.63 C
ATOM 708 CG PHE A 108 -0.566 -11.579 15.021 1.00 26.24 C
ATOM 709 CD1 PHE A 108 -1.216 -10.522 14.434 1.00 35.08 C
ATOM 710 CD2 PHE A 108 -1.247 -12.319 15.956 1.00 28.53 C
ATOM 711 CE1 PHE A 108 -2.522 -10.216 14.789 1.00 36.10 C
ATOM 712 CE2 PHE A 108 -2.541 -12.016 16.302 1.00 27.46 C
ATOM 713 CZ PHE A 108 -3.176 -10.970 15.731 1.00 25.19 C
ATOM 714 N GLY A 109 3.015 -14.670 14.077 1.00 27.77 N
ATOM 715 CA GLY A 109 4.447 -14.915 13.995 1.00 31.53 C
ATOM 716 C GLY A 109 5.244 -14.006 14.920 1.00 34.09 C
ATOM 717 O GLY A 109 6.363 -13.602 14.596 1.00 31.59 O
ATOM 718 N LEU A 110 4.655 -13.675 16.066 1.00 28.77 N
ATOM 719 CA LEU A 110 5.311 -12.818 17.062 1.00 39.27 C
ATOM 720 C LEU A 110 5.620 -13.576 18.366 1.00 34.43 C
ATOM 721 O LEU A 110 4.776 -14.308 18.887 1.00 32.05 O
ATOM 722 CB LEU A 110 4.450 -11.579 17.347 1.00 31.34 C
ATOM 723 CG LEU A 110 4.313 -10.567 16.207 1.00 32.89 C
ATOM 724 CD1 LEU A 110 3.445 -9.381 16.640 1.00 25.29 C
ATOM 725 CD2 LEU A 110 5.684 -10.085 15.718 1.00 28.49 C
ATOM 726 N TRP A 111 6.831 -13.392 18.883 1.00 36.04 N
ATOM 727 CA TRP A 111 7.275 -14.065 20.116 1.00 35.60 C
ATOM 728 C TRP A 111 7.514 -13.030 21.233 1.00 33.78 C
ATOM 729 O TRP A 111 8.130 -11.988 20.977 1.00 30.75 O
ATOM 730 CB TRP A 111 8.547 -14.883 19.822 1.00 31.09 C
ATOM 731 CG TRP A 111 8.936 -15.853 20.887 1.00 39.26 C
ATOM 732 CD1 TRP A 111 9.910 -15.684 21.828 1.00 33.74 C
ATOM 733 CD2 TRP A 111 8.371 -17.152 21.128 1.00 43.59 C
ATOM 734 NE1 TRP A 111 9.980 -16.788 22.646 1.00 37.45 N
ATOM 735 CE2 TRP A 111 9.043 -17.705 22.239 1.00 41.57 C
ATOM 736 CE3 TRP A 111 7.378 -17.911 20.503 1.00 40.08 C
ATOM 737 CZ2 TRP A 111 8.755 -18.972 22.736 1.00 43.68 C
ATOM 738 CZ3 TRP A 111 7.077 -19.162 21.009 1.00 42.07 C
ATOM 739 CH2 TRP A 111 7.768 -19.684 22.109 1.00 42.18 C
ATOM 740 N VAL A 112 6.993 -13.305 22.435 1.00 30.24 N
ATOM 741 CA VAL A 112 7.232 -12.481 23.621 1.00 32.84 C
ATOM 742 C VAL A 112 8.747 -12.425 23.859 1.00 33.70 C
ATOM 743 O VAL A 112 9.402 -13.472 24.035 1.00 30.72 O
ATOM 744 CB VAL A 112 6.545 -13.069 24.887 1.00 36.42 C
ATOM 745 CG1 VAL A 112 7.009 -12.339 26.132 1.00 31.54 C
ATOM 746 CG2 VAL A 112 5.039 -12.994 24.798 1.00 30.20 C
ATOM 747 N PRO A 113 9.315 -11.208 23.859 1.00 30.68 N
ATOM 748 CA PRO A 113 10.774 -11.050 23.731 1.00 33.44 C
ATOM 749 C PRO A 113 11.570 -11.496 24.953 1.00 29.15 C
ATOM 750 O PRO A 113 12.766 -11.749 24.838 1.00 31.13 O
ATOM 751 CB PRO A 113 10.950 -9.557 23.457 1.00 27.99 C
ATOM 752 CG PRO A 113 9.661 -8.916 23.924 1.00 29.91 C
ATOM 753 CD PRO A 113 8.589 -9.930 23.805 1.00 28.14 C
ATOM 754 N VAL A 114 10.900 -11.598 26.098 1.00 29.43 N
ATOM 755 CA VAL A 114 11.522 -12.025 27.349 1.00 29.59 C
ATOM 756 C VAL A 114 10.504 -12.851 28.125 1.00 32.50 C
ATOM 757 O VAL A 114 9.517 -12.311 28.623 1.00 30.45 O
ATOM 758 CB VAL A 114 11.930 -10.814 28.232 1.00 23.96 C
ATOM 759 CG1 VAL A 114 12.234 -11.265 29.671 1.00 27.66 C
ATOM 760 CG2 VAL A 114 13.113 -10.118 27.640 1.00 21.46 C
ATOM 761 N LEU A 115 10.727 -14.159 28.218 1.00 34.98 N
ATOM 762 CA LEU A 115 9.863 -15.001 29.040 1.00 34.91 C
ATOM 763 C LEU A 115 10.569 -15.447 30.330 1.00 42.65 C
ATOM 764 O LEU A 115 11.690 -15.983 30.298 1.00 43.83 O
ATOM 765 CB LEU A 115 9.340 -16.201 28.233 1.00 29.90 C
ATOM 766 CG LEU A 115 8.447 -15.837 27.024 1.00 34.43 C
ATOM 767 CD1 LEU A 115 8.534 -16.877 25.911 1.00 32.63 C
ATOM 768 CD2 LEU A 115 6.984 -15.627 27.424 1.00 24.69 C
ATOM 769 N PRO A 116 9.907 -15.212 31.474 1.00 38.31 N
ATOM 770 CA PRO A 116 10.370 -15.673 32.783 1.00 38.32 C
ATOM 771 C PRO A 116 9.944 -17.137 32.960 1.00 46.64 C
ATOM 772 O PRO A 116 9.315 -17.691 32.059 1.00 44.19 O
ATOM 773 CB PRO A 116 9.615 -14.757 33.737 1.00 34.76 C
ATOM 774 CG PRO A 116 8.276 -14.516 32.995 1.00 29.46 C
ATOM 775 CD PRO A 116 8.597 -14.530 31.543 1.00 33.15 C
ATOM 776 N GLY A 117 10.267 -17.752 34.093 1.00 46.34 N
ATOM 777 CA GLY A 117 9.991 -19.170 34.286 1.00 47.09 C
ATOM 778 C GLY A 117 8.528 -19.554 34.452 1.00 44.38 C
ATOM 779 O GLY A 117 8.157 -20.710 34.306 1.00 52.51 O
ATOM 780 N THR A 118 7.692 -18.591 34.789 1.00 40.47 N
ATOM 781 CA THR A 118 6.265 -18.832 34.841 1.00 43.79 C
ATOM 782 C THR A 118 5.618 -17.760 33.971 1.00 47.77 C
ATOM 783 O THR A 118 6.041 -16.602 33.986 1.00 48.34 O
ATOM 784 CB THR A 118 5.724 -18.754 36.283 1.00 42.96 C
ATOM 785 OG1 THR A 118 4.314 -19.029 36.295 1.00 53.68 O
ATOM 786 CG2 THR A 118 5.960 -17.377 36.866 1.00 37.30 C
ATOM 787 N ARG A 119 4.613 -18.128 33.186 1.00 48.46 N
ATOM 788 CA ARG A 119 4.011 -17.144 32.288 1.00 43.75 C
ATOM 789 C ARG A 119 2.863 -16.439 32.981 1.00 46.59 C
ATOM 790 O ARG A 119 2.220 -15.566 32.406 1.00 46.12 O
ATOM 791 CB ARG A 119 3.517 -17.790 31.009 1.00 44.25 C
ATOM 792 CG ARG A 119 4.592 -18.427 30.149 1.00 51.77 C
ATOM 793 CD ARG A 119 3.965 -18.891 28.835 1.00 55.59 C
ATOM 794 NE ARG A 119 3.910 -20.346 28.684 1.00 68.25 N
ATOM 795 CZ ARG A 119 3.078 -21.152 29.343 1.00 75.87 C
ATOM 796 NH1 ARG A 119 2.226 -20.661 30.241 1.00 75.61 N
ATOM 797 NH2 ARG A 119 3.111 -22.460 29.111 1.00 76.61 N
ATOM 798 N GLN A 120 2.620 -16.814 34.229 1.00 46.05 N
ATOM 799 CA GLN A 120 1.566 -16.204 35.014 1.00 45.64 C
ATOM 800 C GLN A 120 2.052 -14.933 35.682 1.00 43.79 C
ATOM 801 O GLN A 120 1.962 -14.792 36.897 1.00 42.81 O
ATOM 802 CB GLN A 120 1.060 -17.193 36.057 1.00 46.08 C
ATOM 803 CG GLN A 120 0.390 -18.384 35.410 1.00 43.53 C
ATOM 804 CD GLN A 120 -0.733 -17.953 34.512 1.00 45.12 C
ATOM 805 OE1 GLN A 120 -1.667 -17.262 34.946 1.00 40.71 O
ATOM 806 NE2 GLN A 120 -0.654 -18.344 33.243 1.00 56.51 N
ATOM 807 N VAL A 121 2.589 -14.019 34.881 1.00 41.96 N
ATOM 808 CA VAL A 121 2.963 -12.701 35.372 1.00 41.56 C
ATOM 809 C VAL A 121 2.345 -11.636 34.470 1.00 39.52 C
ATOM 810 O VAL A 121 2.232 -11.835 33.265 1.00 38.89 O
ATOM 811 CB VAL A 121 4.508 -12.547 35.519 1.00 36.50 C
ATOM 812 CG1 VAL A 121 5.135 -13.877 35.882 1.00 35.33 C
ATOM 813 CG2 VAL A 121 5.141 -12.037 34.269 1.00 32.17 C
ATOM 814 N THR A 122 1.907 -10.523 35.052 1.00 38.66 N
ATOM 815 CA THR A 122 1.271 -9.489 34.255 1.00 38.16 C
ATOM 816 C THR A 122 2.317 -8.664 33.524 1.00 36.58 C
ATOM 817 O THR A 122 3.507 -8.798 33.774 1.00 38.05 O
ATOM 818 CB THR A 122 0.451 -8.546 35.112 1.00 35.90 C
ATOM 819 OG1 THR A 122 1.329 -7.857 35.998 1.00 32.24 O
ATOM 820 CG2 THR A 122 -0.620 -9.301 35.887 1.00 31.91 C
ATOM 821 N VAL A 123 1.872 -7.805 32.618 1.00 33.89 N
ATOM 822 CA VAL A 123 2.795 -6.952 31.913 1.00 30.12 C
ATOM 823 C VAL A 123 3.292 -5.886 32.879 1.00 33.87 C
ATOM 824 O VAL A 123 4.477 -5.512 32.871 1.00 40.26 O
ATOM 825 CB VAL A 123 2.129 -6.347 30.669 1.00 36.83 C
ATOM 826 CG1 VAL A 123 2.924 -5.156 30.153 1.00 19.79 C
ATOM 827 CG2 VAL A 123 1.943 -7.441 29.585 1.00 24.81 C
ATOM 828 N GLY A 124 2.399 -5.413 33.741 1.00 32.54 N
ATOM 829 CA GLY A 124 2.794 -4.434 34.743 1.00 36.27 C
ATOM 830 C GLY A 124 3.908 -4.974 35.625 1.00 34.19 C
ATOM 831 O GLY A 124 4.908 -4.291 35.838 1.00 35.22 O
ATOM 832 N GLY A 125 3.723 -6.198 36.127 1.00 29.49 N
ATOM 833 CA GLY A 125 4.709 -6.886 36.933 1.00 30.75 C
ATOM 834 C GLY A 125 6.001 -7.184 36.194 1.00 35.13 C
ATOM 835 O GLY A 125 7.086 -7.182 36.789 1.00 35.35 O
ATOM 836 N ALA A 126 5.897 -7.428 34.895 1.00 28.18 N
ATOM 837 CA ALA A 126 7.079 -7.707 34.100 1.00 30.54 C
ATOM 838 C ALA A 126 7.904 -6.447 33.960 1.00 31.12 C
ATOM 839 O ALA A 126 9.140 -6.489 33.980 1.00 30.18 O
ATOM 840 CB ALA A 126 6.691 -8.233 32.721 1.00 30.34 C
ATOM 841 N ILE A 127 7.225 -5.318 33.795 1.00 29.87 N
ATOM 842 CA ILE A 127 7.939 -4.048 33.678 1.00 35.47 C
ATOM 843 C ILE A 127 8.510 -3.541 35.008 1.00 34.65 C
ATOM 844 O ILE A 127 9.651 -3.089 35.068 1.00 30.04 O
ATOM 845 CB ILE A 127 7.055 -2.948 33.090 1.00 32.63 C
ATOM 846 CG1 ILE A 127 6.621 -3.325 31.691 1.00 23.21 C
ATOM 847 CG2 ILE A 127 7.803 -1.583 33.088 1.00 27.86 C
ATOM 848 CD1 ILE A 127 5.560 -2.391 31.180 1.00 26.20 C
ATOM 849 N ALA A 128 7.696 -3.613 36.060 1.00 32.59 N
ATOM 850 CA ALA A 128 8.051 -3.055 37.354 1.00 32.26 C
ATOM 851 C ALA A 128 9.169 -3.834 38.035 1.00 39.41 C
ATOM 852 O ALA A 128 9.868 -3.288 38.876 1.00 35.80 O
ATOM 853 CB ALA A 128 6.838 -3.000 38.251 1.00 35.34 C
ATOM 854 N CYS A 129 9.331 -5.113 37.700 1.00 37.49 N
ATOM 855 CA CYS A 129 10.498 -5.838 38.199 1.00 28.71 C
ATOM 856 C CYS A 129 11.550 -5.998 37.107 1.00 31.74 C
ATOM 857 O CYS A 129 12.591 -6.616 37.346 1.00 27.41 O
ATOM 858 CB CYS A 129 10.145 -7.207 38.770 1.00 33.94 C
ATOM 859 SG CYS A 129 9.186 -7.213 40.264 1.00 39.34 S
ATOM 860 N ASP A 130 11.277 -5.446 35.922 1.00 28.96 N
ATOM 861 CA ASP A 130 12.210 -5.527 34.788 1.00 32.13 C
ATOM 862 C ASP A 130 12.769 -6.960 34.615 1.00 33.43 C
ATOM 863 O ASP A 130 13.991 -7.190 34.607 1.00 27.31 O
ATOM 864 CB ASP A 130 13.324 -4.476 34.934 1.00 24.05 C
ATOM 865 CG ASP A 130 14.152 -4.320 33.678 1.00 30.21 C
ATOM 866 OD1 ASP A 130 13.781 -4.894 32.628 1.00 38.00 O
ATOM 867 OD2 ASP A 130 15.172 -3.611 33.723 1.00 25.72 O
ATOM 868 N ILE A 131 11.846 -7.912 34.501 1.00 28.08 N
ATOM 869 CA ILE A 131 12.167 -9.329 34.567 1.00 25.32 C
ATOM 870 C ILE A 131 13.146 -9.763 33.487 1.00 31.43 C
ATOM 871 O ILE A 131 13.265 -9.130 32.423 1.00 30.16 O
ATOM 872 CB ILE A 131 10.893 -10.191 34.461 1.00 29.84 C
ATOM 873 CG1 ILE A 131 10.247 -10.028 33.077 1.00 30.03 C
ATOM 874 CG2 ILE A 131 9.905 -9.850 35.577 1.00 25.26 C
ATOM 875 CD1 ILE A 131 9.038 -10.918 32.874 1.00 29.92 C
ATOM 876 N HIS A 132 13.846 -10.861 33.751 1.00 28.11 N
ATOM 877 CA HIS A 132 14.797 -11.388 32.778 1.00 28.14 C
ATOM 878 C HIS A 132 14.375 -12.810 32.485 1.00 31.64 C
ATOM 879 O HIS A 132 13.532 -13.377 33.177 1.00 30.91 O
ATOM 880 CB HIS A 132 16.181 -11.418 33.394 1.00 29.36 C
ATOM 881 CG HIS A 132 16.197 -12.098 34.723 1.00 30.45 C
ATOM 882 ND1 HIS A 132 15.949 -11.429 35.899 1.00 28.44 N
ATOM 883 CD2 HIS A 132 16.340 -13.405 35.053 1.00 30.27 C
ATOM 884 CE1 HIS A 132 15.973 -12.289 36.904 1.00 35.90 C
ATOM 885 NE2 HIS A 132 16.211 -13.494 36.415 1.00 37.42 N
ATOM 886 N GLY A 133 14.976 -13.404 31.475 1.00 31.90 N
ATOM 887 CA GLY A 133 14.746 -14.802 31.221 1.00 33.22 C
ATOM 888 C GLY A 133 15.980 -15.467 30.659 1.00 36.10 C
ATOM 889 O GLY A 133 17.089 -14.924 30.676 1.00 37.45 O
ATOM 890 N LYS A 134 15.753 -16.649 30.125 1.00 35.19 N
ATOM 891 CA LYS A 134 16.781 -17.521 29.599 1.00 37.65 C
ATOM 892 C LYS A 134 17.588 -16.873 28.478 1.00 34.52 C
ATOM 893 O LYS A 134 18.684 -17.331 28.133 1.00 38.07 O
ATOM 894 CB LYS A 134 16.070 -18.777 29.087 1.00 39.00 C
ATOM 895 CG LYS A 134 16.879 -20.010 28.982 1.00 34.66 C
ATOM 896 CD LYS A 134 15.973 -21.219 29.168 1.00 46.14 C
ATOM 897 CE LYS A 134 16.401 -22.394 28.274 1.00 46.58 C
ATOM 898 NZ LYS A 134 17.793 -22.867 28.466 1.00 47.88 N
ATOM 899 N ASN A 135 17.057 -15.808 27.894 1.00 33.98 N
ATOM 900 CA ASN A 135 17.757 -15.151 26.791 1.00 33.79 C
ATOM 901 C ASN A 135 18.316 -13.769 27.123 1.00 34.17 C
ATOM 902 O ASN A 135 18.563 -12.960 26.206 1.00 34.31 O
ATOM 903 CB ASN A 135 16.838 -15.027 25.584 1.00 32.41 C
ATOM 904 CG ASN A 135 15.671 -14.114 25.858 1.00 36.77 C
ATOM 905 OD1 ASN A 135 15.352 -13.845 27.013 1.00 35.02 O
ATOM 906 ND2 ASN A 135 15.038 -13.621 24.807 1.00 33.49 N
ATOM 907 N HIS A 136 18.533 -13.497 28.409 1.00 30.35 N
ATOM 908 CA HIS A 136 19.005 -12.183 28.810 1.00 30.03 C
ATOM 909 C HIS A 136 20.287 -11.729 28.124 1.00 30.56 C
ATOM 910 O HIS A 136 20.449 -10.552 27.821 1.00 36.82 O
ATOM 911 CB HIS A 136 19.220 -12.070 30.315 1.00 35.55 C
ATOM 912 CG HIS A 136 19.633 -10.695 30.728 1.00 30.36 C
ATOM 913 ND1 HIS A 136 20.946 -10.277 30.706 1.00 33.91 N
ATOM 914 CD2 HIS A 136 18.898 -9.609 31.076 1.00 26.92 C
ATOM 915 CE1 HIS A 136 21.008 -9.008 31.064 1.00 28.75 C
ATOM 916 NE2 HIS A 136 19.777 -8.578 31.290 1.00 28.97 N
ATOM 917 N HIS A 137 21.205 -12.650 27.887 1.00 29.69 N
ATOM 918 CA HIS A 137 22.507 -12.274 27.351 1.00 33.87 C
ATOM 919 C HIS A 137 22.400 -11.883 25.892 1.00 38.06 C
ATOM 920 O HIS A 137 23.331 -11.300 25.343 1.00 40.65 O
ATOM 921 CB HIS A 137 23.490 -13.424 27.458 1.00 30.91 C
ATOM 922 CG HIS A 137 23.044 -14.634 26.714 1.00 34.52 C
ATOM 923 ND1 HIS A 137 22.065 -15.477 27.196 1.00 37.26 N
ATOM 924 CD2 HIS A 137 23.403 -15.122 25.505 1.00 40.33 C
ATOM 925 CE1 HIS A 137 21.856 -16.448 26.325 1.00 37.15 C
ATOM 926 NE2 HIS A 137 22.654 -16.255 25.289 1.00 44.57 N
ATOM 927 N SER A 138 21.281 -12.220 25.251 1.00 41.34 N
ATOM 928 CA SER A 138 21.068 -11.839 23.848 1.00 33.77 C
ATOM 929 C SER A 138 19.951 -10.805 23.653 1.00 39.13 C
ATOM 930 O SER A 138 19.977 -10.054 22.664 1.00 36.47 O
ATOM 931 CB SER A 138 20.843 -13.061 22.933 1.00 34.98 C
ATOM 932 OG SER A 138 19.523 -13.588 23.014 1.00 38.92 O
ATOM 933 N ALA A 139 18.991 -10.744 24.588 1.00 35.33 N
ATOM 934 CA ALA A 139 17.835 -9.839 24.424 1.00 35.96 C
ATOM 935 C ALA A 139 17.653 -8.769 25.508 1.00 31.36 C
ATOM 936 O ALA A 139 16.818 -7.883 25.365 1.00 30.46 O
ATOM 937 CB ALA A 139 16.541 -10.639 24.265 1.00 29.17 C
ATOM 938 N GLY A 140 18.418 -8.855 26.589 1.00 31.90 N
ATOM 939 CA GLY A 140 18.235 -7.949 27.708 1.00 32.29 C
ATOM 940 C GLY A 140 17.032 -8.372 28.532 1.00 34.56 C
ATOM 941 O GLY A 140 16.581 -9.524 28.454 1.00 30.54 O
ATOM 942 N SER A 141 16.509 -7.442 29.324 1.00 29.26 N
ATOM 943 CA SER A 141 15.372 -7.726 30.192 1.00 25.92 C
ATOM 944 C SER A 141 14.128 -7.057 29.626 1.00 29.99 C
ATOM 945 O SER A 141 14.186 -6.440 28.575 1.00 29.25 O
ATOM 946 CB SER A 141 15.646 -7.227 31.605 1.00 28.60 C
ATOM 947 OG SER A 141 16.281 -5.962 31.575 1.00 25.61 O
ATOM 948 N PHE A 142 13.007 -7.163 30.330 1.00 30.38 N
ATOM 949 CA PHE A 142 11.729 -6.777 29.764 1.00 26.94 C
ATOM 950 C PHE A 142 11.692 -5.307 29.363 1.00 34.82 C
ATOM 951 O PHE A 142 11.169 -4.952 28.303 1.00 31.11 O
ATOM 952 CB PHE A 142 10.577 -7.112 30.711 1.00 29.48 C
ATOM 953 CG PHE A 142 9.233 -7.276 30.015 1.00 30.27 C
ATOM 954 CD1 PHE A 142 8.313 -6.236 29.986 1.00 28.26 C
ATOM 955 CD2 PHE A 142 8.888 -8.483 29.409 1.00 37.18 C
ATOM 956 CE1 PHE A 142 7.074 -6.398 29.350 1.00 33.13 C
ATOM 957 CE2 PHE A 142 7.655 -8.656 28.765 1.00 29.26 C
ATOM 958 CZ PHE A 142 6.747 -7.612 28.735 1.00 28.43 C
ATOM 959 N GLY A 143 12.265 -4.446 30.195 1.00 33.11 N
ATOM 960 CA GLY A 143 12.274 -3.028 29.898 1.00 22.51 C
ATOM 961 C GLY A 143 12.894 -2.667 28.552 1.00 26.16 C
ATOM 962 O GLY A 143 12.482 -1.686 27.944 1.00 29.93 O
ATOM 963 N ASN A 144 13.877 -3.427 28.069 1.00 27.19 N
ATOM 964 CA ASN A 144 14.466 -3.118 26.750 1.00 29.24 C
ATOM 965 C ASN A 144 13.490 -3.162 25.584 1.00 32.68 C
ATOM 966 O ASN A 144 13.802 -2.667 24.505 1.00 36.72 O
ATOM 967 CB ASN A 144 15.607 -4.063 26.376 1.00 36.14 C
ATOM 968 CG ASN A 144 16.676 -4.108 27.408 1.00 32.37 C
ATOM 969 OD1 ASN A 144 16.389 -4.020 28.585 1.00 36.07 O
ATOM 970 ND2 ASN A 144 17.918 -4.267 26.980 1.00 31.78 N
ATOM 971 N HIS A 145 12.331 -3.781 25.781 1.00 33.86 N
ATOM 972 CA HIS A 145 11.396 -4.015 24.681 1.00 32.20 C
ATOM 973 C HIS A 145 10.142 -3.178 24.787 1.00 30.99 C
ATOM 974 O HIS A 145 9.281 -3.263 23.939 1.00 35.45 O
ATOM 975 CB HIS A 145 11.047 -5.510 24.601 1.00 27.11 C
ATOM 976 CG HIS A 145 12.267 -6.377 24.578 1.00 31.98 C
ATOM 977 ND1 HIS A 145 12.955 -6.655 23.420 1.00 32.24 N
ATOM 978 CD2 HIS A 145 12.972 -6.943 25.586 1.00 30.92 C
ATOM 979 CE1 HIS A 145 14.016 -7.393 23.709 1.00 32.15 C
ATOM 980 NE2 HIS A 145 14.048 -7.579 25.015 1.00 34.85 N
ATOM 981 N VAL A 146 10.043 -2.369 25.832 1.00 28.36 N
ATOM 982 CA VAL A 146 8.894 -1.507 26.017 1.00 26.24 C
ATOM 983 C VAL A 146 9.150 -0.267 25.183 1.00 35.93 C
ATOM 984 O VAL A 146 10.198 0.372 25.335 1.00 39.95 O
ATOM 985 CB VAL A 146 8.730 -1.160 27.512 1.00 29.61 C
ATOM 986 CG1 VAL A 146 7.653 -0.093 27.736 1.00 25.72 C
ATOM 987 CG2 VAL A 146 8.426 -2.428 28.301 1.00 20.59 C
ATOM 988 N ARG A 147 8.228 0.049 24.276 1.00 32.58 N
ATOM 989 CA ARG A 147 8.381 1.215 23.403 1.00 33.68 C
ATOM 990 C ARG A 147 7.580 2.406 23.915 1.00 30.82 C
ATOM 991 O ARG A 147 7.831 3.542 23.538 1.00 40.35 O
ATOM 992 CB ARG A 147 7.966 0.896 21.957 1.00 37.59 C
ATOM 993 CG ARG A 147 8.816 -0.159 21.289 1.00 35.31 C
ATOM 994 CD ARG A 147 10.236 0.311 21.020 1.00 32.23 C
ATOM 995 NE ARG A 147 11.088 -0.854 20.770 1.00 36.62 N
ATOM 996 CZ ARG A 147 11.908 -1.408 21.667 1.00 42.05 C
ATOM 997 NH1 ARG A 147 12.019 -0.895 22.895 1.00 36.40 N
ATOM 998 NH2 ARG A 147 12.622 -2.483 21.332 1.00 36.26 N
ATOM 999 N SER A 148 6.609 2.144 24.773 1.00 30.53 N
ATOM 1000 CA SER A 148 5.862 3.219 25.403 1.00 35.25 C
ATOM 1001 C SER A 148 5.101 2.650 26.579 1.00 35.39 C
ATOM 1002 O SER A 148 4.879 1.445 26.645 1.00 39.65 O
ATOM 1003 CB SER A 148 4.875 3.865 24.414 1.00 40.53 C
ATOM 1004 OG SER A 148 3.617 3.200 24.433 1.00 38.00 O
ATOM 1005 N MET A 149 4.715 3.511 27.514 1.00 38.36 N
ATOM 1006 CA MET A 149 3.745 3.125 28.528 1.00 36.49 C
ATOM 1007 C MET A 149 2.964 4.323 29.048 1.00 39.34 C
ATOM 1008 O MET A 149 3.398 5.459 28.936 1.00 44.12 O
ATOM 1009 CB MET A 149 4.387 2.336 29.666 1.00 33.99 C
ATOM 1010 CG MET A 149 5.589 2.991 30.317 1.00 46.44 C
ATOM 1011 SD MET A 149 6.295 1.852 31.522 1.00 38.03 S
ATOM 1012 CE MET A 149 7.981 2.436 31.609 1.00 37.50 C
ATOM 1013 N ASP A 150 1.784 4.050 29.577 1.00 38.13 N
ATOM 1014 CA ASP A 150 0.956 5.072 30.161 1.00 40.13 C
ATOM 1015 C ASP A 150 0.995 4.876 31.666 1.00 44.23 C
ATOM 1016 O ASP A 150 0.570 3.842 32.187 1.00 42.34 O
ATOM 1017 CB ASP A 150 -0.483 4.961 29.668 1.00 43.35 C
ATOM 1018 CG ASP A 150 -0.607 5.159 28.175 1.00 48.94 C
ATOM 1019 OD1 ASP A 150 0.275 5.809 27.565 1.00 51.97 O
ATOM 1020 OD2 ASP A 150 -1.602 4.660 27.616 1.00 50.00 O
ATOM 1021 N LEU A 151 1.505 5.883 32.355 1.00 39.25 N
ATOM 1022 CA LEU A 151 1.698 5.801 33.782 1.00 49.00 C
ATOM 1023 C LEU A 151 0.763 6.758 34.529 1.00 51.27 C
ATOM 1024 O LEU A 151 0.789 7.976 34.324 1.00 49.08 O
ATOM 1025 CB LEU A 151 3.162 6.102 34.109 1.00 51.96 C
ATOM 1026 CG LEU A 151 3.568 6.255 35.574 1.00 48.38 C
ATOM 1027 CD1 LEU A 151 3.637 4.903 36.263 1.00 51.64 C
ATOM 1028 CD2 LEU A 151 4.901 6.987 35.674 1.00 44.92 C
ATOM 1029 N LEU A 152 -0.069 6.183 35.386 1.00 46.19 N
ATOM 1030 CA LEU A 152 -0.933 6.943 36.264 1.00 49.05 C
ATOM 1031 C LEU A 152 -0.120 7.493 37.451 1.00 59.83 C
ATOM 1032 O LEU A 152 0.208 6.762 38.397 1.00 48.53 O
ATOM 1033 CB LEU A 152 -2.075 6.054 36.767 1.00 43.41 C
ATOM 1034 CG LEU A 152 -2.987 6.691 37.824 1.00 59.18 C
ATOM 1035 CD1 LEU A 152 -3.465 8.087 37.365 1.00 57.61 C
ATOM 1036 CD2 LEU A 152 -4.159 5.782 38.136 1.00 45.45 C
ATOM 1037 N THR A 153 0.204 8.783 37.401 1.00 59.53 N
ATOM 1038 CA THR A 153 1.011 9.394 38.450 1.00 58.12 C
ATOM 1039 C THR A 153 0.192 9.889 39.660 1.00 59.81 C
ATOM 1040 O THR A 153 -1.036 9.813 39.670 1.00 57.51 O
ATOM 1041 CB THR A 153 1.928 10.513 37.888 1.00 64.90 C
ATOM 1042 OG1 THR A 153 1.148 11.479 37.176 1.00 62.35 O
ATOM 1043 CG2 THR A 153 2.965 9.923 36.945 1.00 48.92 C
ATOM 1044 N ALA A 154 0.890 10.370 40.687 1.00 67.17 N
ATOM 1045 CA ALA A 154 0.254 10.831 41.932 1.00 69.82 C
ATOM 1046 C ALA A 154 -0.759 11.965 41.733 1.00 67.00 C
ATOM 1047 O ALA A 154 -1.802 12.006 42.392 1.00 58.20 O
ATOM 1048 CB ALA A 154 1.318 11.254 42.932 1.00 67.98 C
ATOM 1049 N ASP A 155 -0.436 12.872 40.815 1.00 63.56 N
ATOM 1050 CA ASP A 155 -1.306 13.987 40.444 1.00 62.78 C
ATOM 1051 C ASP A 155 -2.574 13.603 39.650 1.00 67.38 C
ATOM 1052 O ASP A 155 -3.222 14.473 39.067 1.00 73.36 O
ATOM 1053 CB ASP A 155 -0.497 15.034 39.651 1.00 60.24 C
ATOM 1054 CG ASP A 155 0.116 14.467 38.360 1.00 72.58 C
ATOM 1055 OD1 ASP A 155 -0.421 13.477 37.819 1.00 74.52 O
ATOM 1056 OD2 ASP A 155 1.138 15.011 37.876 1.00 70.98 O
ATOM 1057 N GLY A 156 -2.911 12.317 39.598 1.00 57.05 N
ATOM 1058 CA GLY A 156 -4.086 11.870 38.871 1.00 56.28 C
ATOM 1059 C GLY A 156 -3.967 11.891 37.347 1.00 63.13 C
ATOM 1060 O GLY A 156 -4.869 11.437 36.648 1.00 64.39 O
ATOM 1061 N GLU A 157 -2.858 12.409 36.828 1.00 57.99 N
ATOM 1062 CA GLU A 157 -2.617 12.444 35.388 1.00 60.84 C
ATOM 1063 C GLU A 157 -2.023 11.138 34.831 1.00 65.98 C
ATOM 1064 O GLU A 157 -1.317 10.410 35.537 1.00 63.81 O
ATOM 1065 CB GLU A 157 -1.693 13.609 35.035 1.00 65.49 C
ATOM 1066 CG GLU A 157 -2.275 14.973 35.348 1.00 80.13 C
ATOM 1067 CD GLU A 157 -2.850 15.660 34.121 1.00 96.87 C
ATOM 1068 OE1 GLU A 157 -3.239 16.844 34.239 1.00 97.30 O
ATOM 1069 OE2 GLU A 157 -2.904 15.019 33.042 1.00 90.50 O
ATOM 1070 N ILE A 158 -2.321 10.856 33.564 1.00 54.59 N
ATOM 1071 CA ILE A 158 -1.727 9.738 32.848 1.00 50.18 C
ATOM 1072 C ILE A 158 -0.629 10.236 31.909 1.00 55.97 C
ATOM 1073 O ILE A 158 -0.895 10.971 30.964 1.00 56.11 O
ATOM 1074 CB ILE A 158 -2.788 8.937 32.067 1.00 52.50 C
ATOM 1075 CG1 ILE A 158 -3.736 8.255 33.053 1.00 52.68 C
ATOM 1076 CG2 ILE A 158 -2.131 7.886 31.158 1.00 43.23 C
ATOM 1077 CD1 ILE A 158 -4.825 7.453 32.388 1.00 51.77 C
ATOM 1078 N ARG A 159 0.610 9.845 32.191 1.00 54.85 N
ATOM 1079 CA ARG A 159 1.751 10.271 31.386 1.00 49.32 C
ATOM 1080 C ARG A 159 2.183 9.204 30.399 1.00 51.94 C
ATOM 1081 O ARG A 159 2.309 8.031 30.737 1.00 52.95 O
ATOM 1082 CB ARG A 159 2.923 10.666 32.277 1.00 52.86 C
ATOM 1083 CG ARG A 159 2.859 12.113 32.747 1.00 64.24 C
ATOM 1084 CD ARG A 159 2.842 12.208 34.259 1.00 60.56 C
ATOM 1085 NE ARG A 159 3.994 12.819 34.950 1.00 66.26 N
ATOM 1086 CZ ARG A 159 5.200 13.120 34.452 1.00 67.66 C
ATOM 1087 NH1 ARG A 159 5.551 12.893 33.186 1.00 61.55 N
ATOM 1088 NH2 ARG A 159 6.092 13.665 35.268 1.00 51.11 N
ATOM 1089 N HIS A 160 2.401 9.623 29.165 1.00 53.57 N
ATOM 1090 CA HIS A 160 2.789 8.707 28.116 1.00 52.34 C
ATOM 1091 C HIS A 160 4.307 8.724 28.009 1.00 53.21 C
ATOM 1092 O HIS A 160 4.887 9.662 27.467 1.00 53.22 O
ATOM 1093 CB HIS A 160 2.129 9.121 26.808 1.00 47.25 C
ATOM 1094 CG HIS A 160 2.525 8.285 25.632 1.00 49.97 C
ATOM 1095 ND1 HIS A 160 2.039 7.010 25.426 1.00 47.04 N
ATOM 1096 CD2 HIS A 160 3.341 8.551 24.583 1.00 47.37 C
ATOM 1097 CE1 HIS A 160 2.543 6.525 24.305 1.00 49.79 C
ATOM 1098 NE2 HIS A 160 3.337 7.441 23.773 1.00 59.55 N
ATOM 1099 N LEU A 161 4.945 7.684 28.543 1.00 47.12 N
ATOM 1100 CA LEU A 161 6.393 7.625 28.584 1.00 41.92 C
ATOM 1101 C LEU A 161 6.958 6.810 27.421 1.00 43.35 C
ATOM 1102 O LEU A 161 6.397 5.778 27.039 1.00 45.17 O
ATOM 1103 CB LEU A 161 6.862 7.048 29.926 1.00 43.68 C
ATOM 1104 CG LEU A 161 6.123 7.512 31.189 1.00 43.27 C
ATOM 1105 CD1 LEU A 161 6.345 6.545 32.339 1.00 45.71 C
ATOM 1106 CD2 LEU A 161 6.549 8.907 31.590 1.00 45.18 C
ATOM 1107 N THR A 162 8.074 7.284 26.870 1.00 38.78 N
ATOM 1108 CA THR A 162 8.864 6.538 25.898 1.00 41.84 C
ATOM 1109 C THR A 162 10.325 6.400 26.374 1.00 44.33 C
ATOM 1110 O THR A 162 10.785 7.182 27.203 1.00 51.28 O
ATOM 1111 CB THR A 162 8.841 7.240 24.526 1.00 48.93 C
ATOM 1112 OG1 THR A 162 9.406 8.544 24.664 1.00 54.18 O
ATOM 1113 CG2 THR A 162 7.418 7.352 23.987 1.00 38.37 C
ATOM 1114 N PRO A 163 11.062 5.404 25.853 1.00 38.30 N
ATOM 1115 CA PRO A 163 12.463 5.177 26.231 1.00 43.14 C
ATOM 1116 C PRO A 163 13.388 6.350 25.936 1.00 49.15 C
ATOM 1117 O PRO A 163 14.335 6.593 26.700 1.00 46.36 O
ATOM 1118 CB PRO A 163 12.893 4.039 25.294 1.00 39.21 C
ATOM 1119 CG PRO A 163 11.670 3.365 24.893 1.00 33.99 C
ATOM 1120 CD PRO A 163 10.599 4.411 24.866 1.00 38.18 C
ATOM 1121 N THR A 164 13.152 7.033 24.814 1.00 45.28 N
ATOM 1122 CA THR A 164 14.042 8.111 24.373 1.00 44.06 C
ATOM 1123 C THR A 164 13.378 9.466 24.305 1.00 46.14 C
ATOM 1124 O THR A 164 13.984 10.416 23.827 1.00 54.52 O
ATOM 1125 CB THR A 164 14.580 7.857 22.982 1.00 49.17 C
ATOM 1126 OG1 THR A 164 13.482 7.871 22.057 1.00 52.21 O
ATOM 1127 CG2 THR A 164 15.306 6.519 22.930 1.00 42.83 C
ATOM 1128 N GLY A 165 12.138 9.561 24.774 1.00 50.56 N
ATOM 1129 CA GLY A 165 11.431 10.830 24.794 1.00 49.56 C
ATOM 1130 C GLY A 165 12.016 11.826 25.779 1.00 57.59 C
ATOM 1131 O GLY A 165 13.137 11.664 26.264 1.00 55.94 O
ATOM 1132 N GLU A 166 11.257 12.874 26.076 1.00 60.83 N
ATOM 1133 CA GLU A 166 11.716 13.877 27.021 1.00 67.24 C
ATOM 1134 C GLU A 166 11.287 13.448 28.411 1.00 66.29 C
ATOM 1135 O GLU A 166 11.544 14.132 29.399 1.00 62.10 O
ATOM 1136 CB GLU A 166 11.140 15.254 26.685 1.00 60.18 C
ATOM 1137 N ASP A 167 10.610 12.310 28.476 1.00 66.12 N
ATOM 1138 CA ASP A 167 10.213 11.745 29.753 1.00 63.11 C
ATOM 1139 C ASP A 167 10.992 10.445 30.027 1.00 55.85 C
ATOM 1140 O ASP A 167 10.631 9.664 30.915 1.00 52.59 O
ATOM 1141 CB ASP A 167 8.701 11.520 29.778 1.00 62.17 C
ATOM 1142 CG ASP A 167 7.997 12.350 30.850 1.00 69.02 C
ATOM 1143 OD1 ASP A 167 8.605 12.626 31.917 1.00 65.97 O
ATOM 1144 OD2 ASP A 167 6.820 12.710 30.627 1.00 63.47 O
ATOM 1145 N ALA A 168 12.075 10.250 29.269 1.00 46.25 N
ATOM 1146 CA ALA A 168 12.947 9.077 29.384 1.00 49.80 C
ATOM 1147 C ALA A 168 13.294 8.698 30.816 1.00 45.40 C
ATOM 1148 O ALA A 168 13.339 7.514 31.163 1.00 48.64 O
ATOM 1149 CB ALA A 168 14.236 9.284 28.588 1.00 42.23 C
ATOM 1150 N GLU A 169 13.532 9.704 31.645 1.00 45.09 N
ATOM 1151 CA GLU A 169 14.039 9.480 32.999 1.00 44.19 C
ATOM 1152 C GLU A 169 12.999 8.796 33.870 1.00 36.67 C
ATOM 1153 O GLU A 169 13.309 7.868 34.610 1.00 43.25 O
ATOM 1154 CB GLU A 169 14.462 10.812 33.608 1.00 42.01 C
ATOM 1155 CG GLU A 169 15.337 10.745 34.815 1.00 46.70 C
ATOM 1156 CD GLU A 169 15.418 12.096 35.503 1.00 60.56 C
ATOM 1157 OE1 GLU A 169 14.343 12.717 35.715 1.00 51.79 O
ATOM 1158 OE2 GLU A 169 16.552 12.538 35.813 1.00 55.95 O
ATOM 1159 N LEU A 170 11.760 9.246 33.777 1.00 37.67 N
ATOM 1160 CA LEU A 170 10.681 8.627 34.530 1.00 39.39 C
ATOM 1161 C LEU A 170 10.303 7.261 33.936 1.00 46.56 C
ATOM 1162 O LEU A 170 9.813 6.383 34.657 1.00 43.08 O
ATOM 1163 CB LEU A 170 9.468 9.555 34.565 1.00 39.82 C
ATOM 1164 CG LEU A 170 8.165 9.000 35.138 1.00 45.08 C
ATOM 1165 CD1 LEU A 170 8.352 8.536 36.565 1.00 32.06 C
ATOM 1166 CD2 LEU A 170 7.060 10.045 35.047 1.00 48.98 C
ATOM 1167 N PHE A 171 10.533 7.087 32.629 1.00 36.81 N
ATOM 1168 CA PHE A 171 10.324 5.801 31.971 1.00 39.95 C
ATOM 1169 C PHE A 171 11.274 4.777 32.578 1.00 39.44 C
ATOM 1170 O PHE A 171 10.873 3.683 32.993 1.00 33.21 O
ATOM 1171 CB PHE A 171 10.587 5.930 30.461 1.00 42.51 C
ATOM 1172 CG PHE A 171 10.574 4.624 29.720 1.00 34.70 C
ATOM 1173 CD1 PHE A 171 9.429 4.190 29.083 1.00 40.38 C
ATOM 1174 CD2 PHE A 171 11.717 3.844 29.633 1.00 41.15 C
ATOM 1175 CE1 PHE A 171 9.413 2.992 28.397 1.00 39.25 C
ATOM 1176 CE2 PHE A 171 11.705 2.635 28.954 1.00 38.68 C
ATOM 1177 CZ PHE A 171 10.549 2.213 28.338 1.00 38.97 C
ATOM 1178 N TRP A 172 12.548 5.144 32.619 1.00 36.19 N
ATOM 1179 CA TRP A 172 13.566 4.245 33.127 1.00 33.91 C
ATOM 1180 C TRP A 172 13.610 4.154 34.652 1.00 35.06 C
ATOM 1181 O TRP A 172 14.368 3.373 35.221 1.00 43.03 O
ATOM 1182 CB TRP A 172 14.929 4.594 32.553 1.00 35.56 C
ATOM 1183 CG TRP A 172 14.997 4.291 31.085 1.00 43.37 C
ATOM 1184 CD1 TRP A 172 14.984 5.190 30.066 1.00 30.68 C
ATOM 1185 CD2 TRP A 172 15.064 2.988 30.476 1.00 41.15 C
ATOM 1186 NE1 TRP A 172 15.055 4.541 28.859 1.00 37.92 N
ATOM 1187 CE2 TRP A 172 15.094 3.188 29.073 1.00 43.53 C
ATOM 1188 CE3 TRP A 172 15.115 1.676 30.978 1.00 26.79 C
ATOM 1189 CZ2 TRP A 172 15.173 2.128 28.154 1.00 30.73 C
ATOM 1190 CZ3 TRP A 172 15.192 0.619 30.070 1.00 35.13 C
ATOM 1191 CH2 TRP A 172 15.221 0.856 28.663 1.00 29.87 C
ATOM 1192 N ALA A 173 12.783 4.932 35.320 1.00 35.58 N
ATOM 1193 CA ALA A 173 12.661 4.810 36.760 1.00 40.13 C
ATOM 1194 C ALA A 173 11.522 3.866 37.036 1.00 35.84 C
ATOM 1195 O ALA A 173 11.486 3.181 38.042 1.00 42.51 O
ATOM 1196 CB ALA A 173 12.374 6.153 37.372 1.00 38.61 C
ATOM 1197 N THR A 174 10.574 3.847 36.121 1.00 42.47 N
ATOM 1198 CA THR A 174 9.411 2.995 36.247 1.00 40.69 C
ATOM 1199 C THR A 174 9.811 1.560 35.974 1.00 38.50 C
ATOM 1200 O THR A 174 9.408 0.665 36.712 1.00 39.75 O
ATOM 1201 CB THR A 174 8.297 3.480 35.322 1.00 34.91 C
ATOM 1202 OG1 THR A 174 7.844 4.742 35.823 1.00 33.52 O
ATOM 1203 CG2 THR A 174 7.124 2.498 35.307 1.00 31.52 C
ATOM 1204 N VAL A 175 10.620 1.358 34.933 1.00 35.50 N
ATOM 1205 CA VAL A 175 11.248 0.072 34.669 1.00 31.24 C
ATOM 1206 C VAL A 175 12.023 -0.344 35.883 1.00 36.38 C
ATOM 1207 O VAL A 175 12.971 0.332 36.271 1.00 44.38 O
ATOM 1208 CB VAL A 175 12.237 0.164 33.506 1.00 32.96 C
ATOM 1209 CG1 VAL A 175 13.146 -1.065 33.477 1.00 23.86 C
ATOM 1210 CG2 VAL A 175 11.476 0.332 32.187 1.00 29.77 C
ATOM 1211 N GLY A 176 11.617 -1.446 36.502 1.00 37.20 N
ATOM 1212 CA GLY A 176 12.321 -1.954 37.667 1.00 34.61 C
ATOM 1213 C GLY A 176 12.000 -1.160 38.915 1.00 40.05 C
ATOM 1214 O GLY A 176 12.633 -1.343 39.955 1.00 38.36 O
ATOM 1215 N GLY A 177 10.995 -0.295 38.816 1.00 37.88 N
ATOM 1216 CA GLY A 177 10.630 0.600 39.895 1.00 33.45 C
ATOM 1217 C GLY A 177 9.682 0.030 40.924 1.00 35.40 C
ATOM 1218 O GLY A 177 9.263 0.749 41.823 1.00 42.72 O
ATOM 1219 N ASN A 178 9.358 -1.258 40.809 1.00 36.55 N
ATOM 1220 CA ASN A 178 8.459 -1.944 41.750 1.00 34.52 C
ATOM 1221 C ASN A 178 7.192 -1.162 42.068 1.00 39.49 C
ATOM 1222 O ASN A 178 6.716 -1.169 43.199 1.00 45.02 O
ATOM 1223 CB ASN A 178 9.195 -2.313 43.045 1.00 38.24 C
ATOM 1224 CG ASN A 178 10.268 -3.363 42.821 1.00 42.22 C
ATOM 1225 OD1 ASN A 178 10.017 -4.559 42.961 1.00 46.06 O
ATOM 1226 ND2 ASN A 178 11.461 -2.924 42.433 1.00 33.02 N
ATOM 1227 N GLY A 179 6.676 -0.467 41.059 1.00 38.49 N
ATOM 1228 CA GLY A 179 5.405 0.220 41.144 1.00 39.77 C
ATOM 1229 C GLY A 179 5.427 1.545 41.875 1.00 42.67 C
ATOM 1230 O GLY A 179 4.380 2.149 42.075 1.00 43.73 O
ATOM 1231 N LEU A 180 6.613 2.014 42.246 1.00 39.04 N
ATOM 1232 CA LEU A 180 6.732 3.198 43.093 1.00 44.14 C
ATOM 1233 C LEU A 180 6.794 4.529 42.329 1.00 44.02 C
ATOM 1234 O LEU A 180 7.133 5.577 42.898 1.00 41.45 O
ATOM 1235 CB LEU A 180 7.916 3.043 44.079 1.00 33.69 C
ATOM 1236 CG LEU A 180 7.790 1.834 45.022 1.00 41.88 C
ATOM 1237 CD1 LEU A 180 9.117 1.431 45.711 1.00 34.39 C
ATOM 1238 CD2 LEU A 180 6.701 2.071 46.050 1.00 35.82 C
ATOM 1239 N THR A 181 6.461 4.499 41.045 1.00 43.91 N
ATOM 1240 CA THR A 181 6.344 5.740 40.284 1.00 33.98 C
ATOM 1241 C THR A 181 4.894 5.969 39.900 1.00 41.64 C
ATOM 1242 O THR A 181 4.550 6.981 39.295 1.00 48.90 O
ATOM 1243 CB THR A 181 7.230 5.738 39.044 1.00 32.57 C
ATOM 1244 OG1 THR A 181 6.846 4.664 38.173 1.00 37.34 O
ATOM 1245 CG2 THR A 181 8.680 5.581 39.440 1.00 30.40 C
ATOM 1246 N GLY A 182 4.040 5.023 40.271 1.00 41.18 N
ATOM 1247 CA GLY A 182 2.646 5.068 39.884 1.00 50.18 C
ATOM 1248 C GLY A 182 2.174 3.811 39.170 1.00 50.43 C
ATOM 1249 O GLY A 182 2.897 2.809 39.116 1.00 45.49 O
ATOM 1250 N ILE A 183 0.959 3.861 38.625 1.00 42.96 N
ATOM 1251 CA ILE A 183 0.363 2.670 38.032 1.00 47.13 C
ATOM 1252 C ILE A 183 0.517 2.646 36.519 1.00 45.44 C
ATOM 1253 O ILE A 183 0.112 3.570 35.825 1.00 48.74 O
ATOM 1254 CB ILE A 183 -1.124 2.522 38.378 1.00 41.04 C
ATOM 1255 CG1 ILE A 183 -1.364 2.873 39.833 1.00 43.29 C
ATOM 1256 CG2 ILE A 183 -1.573 1.121 38.108 1.00 34.15 C
ATOM 1257 CD1 ILE A 183 -2.564 2.208 40.389 1.00 50.55 C
ATOM 1258 N ILE A 184 1.135 1.592 36.014 1.00 44.80 N
ATOM 1259 CA ILE A 184 1.214 1.399 34.579 1.00 46.64 C
ATOM 1260 C ILE A 184 -0.145 0.895 34.128 1.00 45.65 C
ATOM 1261 O ILE A 184 -0.598 -0.154 34.576 1.00 47.39 O
ATOM 1262 CB ILE A 184 2.288 0.363 34.226 1.00 47.03 C
ATOM 1263 CG1 ILE A 184 3.614 0.754 34.887 1.00 36.99 C
ATOM 1264 CG2 ILE A 184 2.400 0.210 32.709 1.00 41.45 C
ATOM 1265 CD1 ILE A 184 4.648 -0.363 34.947 1.00 35.83 C
ATOM 1266 N MET A 185 -0.816 1.650 33.273 1.00 39.94 N
ATOM 1267 CA MET A 185 -2.172 1.290 32.884 1.00 42.26 C
ATOM 1268 C MET A 185 -2.136 0.437 31.630 1.00 43.96 C
ATOM 1269 O MET A 185 -2.942 -0.465 31.438 1.00 38.76 O
ATOM 1270 CB MET A 185 -2.984 2.558 32.639 1.00 41.68 C
ATOM 1271 CG MET A 185 -3.007 3.508 33.833 1.00 39.47 C
ATOM 1272 SD MET A 185 -3.884 2.808 35.245 1.00 59.57 S
ATOM 1273 CE MET A 185 -5.560 2.746 34.595 1.00 54.99 C
ATOM 1274 N ARG A 186 -1.153 0.712 30.793 1.00 39.08 N
ATOM 1275 CA ARG A 186 -1.172 0.236 29.439 1.00 40.99 C
ATOM 1276 C ARG A 186 0.225 0.448 28.867 1.00 43.10 C
ATOM 1277 O ARG A 186 0.910 1.410 29.225 1.00 37.77 O
ATOM 1278 CB ARG A 186 -2.223 1.045 28.672 1.00 39.73 C
ATOM 1279 CG ARG A 186 -2.230 0.885 27.165 1.00 41.93 C
ATOM 1280 CD ARG A 186 -3.485 1.521 26.593 1.00 45.08 C
ATOM 1281 NE ARG A 186 -3.644 1.255 25.171 1.00 45.28 N
ATOM 1282 CZ ARG A 186 -4.785 1.417 24.511 1.00 47.93 C
ATOM 1283 NH1 ARG A 186 -5.864 1.839 25.152 1.00 43.31 N
ATOM 1284 NH2 ARG A 186 -4.852 1.144 23.215 1.00 45.19 N
ATOM 1285 N ALA A 187 0.656 -0.447 27.987 1.00 36.78 N
ATOM 1286 CA ALA A 187 1.971 -0.297 27.390 1.00 35.56 C
ATOM 1287 C ALA A 187 1.991 -0.776 25.940 1.00 40.45 C
ATOM 1288 O ALA A 187 1.052 -1.438 25.463 1.00 37.52 O
ATOM 1289 CB ALA A 187 3.004 -1.042 28.211 1.00 29.15 C
ATOM 1290 N THR A 188 3.068 -0.438 25.242 1.00 37.57 N
ATOM 1291 CA THR A 188 3.302 -0.962 23.910 1.00 34.84 C
ATOM 1292 C THR A 188 4.627 -1.691 23.925 1.00 32.85 C
ATOM 1293 O THR A 188 5.655 -1.097 24.239 1.00 40.49 O
ATOM 1294 CB THR A 188 3.326 0.166 22.859 1.00 39.84 C
ATOM 1295 OG1 THR A 188 1.985 0.616 22.612 1.00 42.79 O
ATOM 1296 CG2 THR A 188 3.910 -0.333 21.566 1.00 35.07 C
ATOM 1297 N ILE A 189 4.592 -2.982 23.616 1.00 30.88 N
ATOM 1298 CA ILE A 189 5.789 -3.818 23.570 1.00 27.93 C
ATOM 1299 C ILE A 189 6.145 -4.108 22.107 1.00 36.50 C
ATOM 1300 O ILE A 189 5.244 -4.390 21.286 1.00 35.45 O
ATOM 1301 CB ILE A 189 5.549 -5.185 24.267 1.00 22.63 C
ATOM 1302 CG1 ILE A 189 4.944 -5.021 25.662 1.00 29.80 C
ATOM 1303 CG2 ILE A 189 6.795 -6.006 24.299 1.00 26.01 C
ATOM 1304 CD1 ILE A 189 5.629 -4.003 26.514 1.00 35.93 C
ATOM 1305 N GLU A 190 7.439 -4.060 21.775 1.00 30.75 N
ATOM 1306 CA GLU A 190 7.900 -4.592 20.491 1.00 34.71 C
ATOM 1307 C GLU A 190 8.303 -6.056 20.643 1.00 37.06 C
ATOM 1308 O GLU A 190 9.198 -6.381 21.432 1.00 33.10 O
ATOM 1309 CB GLU A 190 9.055 -3.783 19.897 1.00 34.94 C
ATOM 1310 CG GLU A 190 9.675 -4.451 18.676 1.00 34.01 C
ATOM 1311 CD GLU A 190 10.755 -3.614 18.018 1.00 46.10 C
ATOM 1312 OE1 GLU A 190 11.378 -4.108 17.049 1.00 43.46 O
ATOM 1313 OE2 GLU A 190 10.996 -2.470 18.470 1.00 45.92 O
ATOM 1314 N MET A 191 7.631 -6.923 19.882 1.00 33.27 N
ATOM 1315 CA MET A 191 7.795 -8.368 19.995 1.00 31.66 C
ATOM 1316 C MET A 191 8.951 -8.851 19.131 1.00 30.79 C
ATOM 1317 O MET A 191 9.551 -8.068 18.394 1.00 33.55 O
ATOM 1318 CB MET A 191 6.504 -9.073 19.580 1.00 30.63 C
ATOM 1319 CG MET A 191 5.277 -8.569 20.316 1.00 31.66 C
ATOM 1320 SD MET A 191 5.183 -9.220 21.989 1.00 36.71 S
ATOM 1321 CE MET A 191 4.340 -10.787 21.685 1.00 24.86 C
ATOM 1322 N THR A 192 9.263 -10.142 19.231 1.00 28.63 N
ATOM 1323 CA THR A 192 10.325 -10.731 18.442 1.00 32.17 C
ATOM 1324 C THR A 192 9.716 -11.603 17.347 1.00 35.14 C
ATOM 1325 O THR A 192 8.886 -12.462 17.630 1.00 39.00 O
ATOM 1326 CB THR A 192 11.252 -11.561 19.334 1.00 34.16 C
ATOM 1327 OG1 THR A 192 11.846 -10.702 20.316 1.00 33.15 O
ATOM 1328 CG2 THR A 192 12.355 -12.261 18.512 1.00 20.80 C
ATOM 1329 N PRO A 193 10.113 -11.387 16.087 1.00 30.72 N
ATOM 1330 CA PRO A 193 9.492 -12.215 15.042 1.00 39.12 C
ATOM 1331 C PRO A 193 9.981 -13.643 15.132 1.00 36.07 C
ATOM 1332 O PRO A 193 11.158 -13.873 15.386 1.00 38.18 O
ATOM 1333 CB PRO A 193 9.979 -11.576 13.727 1.00 26.66 C
ATOM 1334 CG PRO A 193 11.284 -10.940 14.092 1.00 38.27 C
ATOM 1335 CD PRO A 193 11.146 -10.487 15.544 1.00 33.46 C
ATOM 1336 N THR A 194 9.064 -14.584 14.945 1.00 36.08 N
ATOM 1337 CA THR A 194 9.379 -15.999 14.897 1.00 36.46 C
ATOM 1338 C THR A 194 8.524 -16.651 13.797 1.00 45.72 C
ATOM 1339 O THR A 194 7.411 -16.193 13.492 1.00 36.62 O
ATOM 1340 CB THR A 194 9.073 -16.689 16.242 1.00 34.51 C
ATOM 1341 OG1 THR A 194 9.533 -18.049 16.210 1.00 35.34 O
ATOM 1342 CG2 THR A 194 7.570 -16.676 16.523 1.00 29.80 C
ATOM 1343 N SER A 195 9.053 -17.713 13.201 1.00 41.94 N
ATOM 1344 CA SER A 195 8.305 -18.473 12.225 1.00 41.46 C
ATOM 1345 C SER A 195 7.767 -19.771 12.829 1.00 45.96 C
ATOM 1346 O SER A 195 6.978 -20.465 12.187 1.00 47.73 O
ATOM 1347 CB SER A 195 9.160 -18.771 11.001 1.00 35.51 C
ATOM 1348 OG SER A 195 10.215 -19.664 11.322 1.00 49.42 O
ATOM 1349 N THR A 196 8.201 -20.108 14.047 1.00 42.48 N
ATOM 1350 CA THR A 196 7.667 -21.282 14.759 1.00 46.32 C
ATOM 1351 C THR A 196 7.479 -21.032 16.255 1.00 41.08 C
ATOM 1352 O THR A 196 7.910 -20.005 16.778 1.00 44.98 O
ATOM 1353 CB THR A 196 8.562 -22.544 14.610 1.00 43.95 C
ATOM 1354 OG1 THR A 196 9.701 -22.438 15.473 1.00 45.68 O
ATOM 1355 CG2 THR A 196 9.033 -22.733 13.173 1.00 47.79 C
ATOM 1356 N ALA A 197 6.831 -21.981 16.930 1.00 40.12 N
ATOM 1357 CA ALA A 197 6.690 -21.980 18.389 1.00 42.29 C
ATOM 1358 C ALA A 197 7.682 -22.965 19.028 1.00 47.66 C
ATOM 1359 O ALA A 197 7.470 -23.455 20.147 1.00 45.12 O
ATOM 1360 CB ALA A 197 5.275 -22.359 18.778 1.00 37.52 C
ATOM 1361 N TYR A 198 8.771 -23.248 18.318 1.00 40.49 N
ATOM 1362 CA TYR A 198 9.658 -24.331 18.695 1.00 44.73 C
ATOM 1363 C TYR A 198 11.074 -23.870 18.879 1.00 43.38 C
ATOM 1364 O TYR A 198 11.508 -22.879 18.281 1.00 43.26 O
ATOM 1365 CB TYR A 198 9.648 -25.441 17.620 1.00 48.29 C
ATOM 1366 CG TYR A 198 8.385 -26.251 17.643 1.00 48.86 C
ATOM 1367 CD1 TYR A 198 8.244 -27.328 18.514 1.00 46.96 C
ATOM 1368 CD2 TYR A 198 7.312 -25.910 16.829 1.00 47.19 C
ATOM 1369 CE1 TYR A 198 7.064 -28.055 18.560 1.00 59.00 C
ATOM 1370 CE2 TYR A 198 6.133 -26.627 16.863 1.00 51.91 C
ATOM 1371 CZ TYR A 198 6.010 -27.699 17.726 1.00 63.72 C
ATOM 1372 OH TYR A 198 4.828 -28.409 17.744 1.00 66.27 O
ATOM 1373 N PHE A 199 11.809 -24.632 19.682 1.00 44.31 N
ATOM 1374 CA PHE A 199 13.220 -24.370 19.898 1.00 41.10 C
ATOM 1375 C PHE A 199 14.066 -25.489 19.332 1.00 44.33 C
ATOM 1376 O PHE A 199 13.680 -26.667 19.367 1.00 42.97 O
ATOM 1377 CB PHE A 199 13.504 -24.256 21.392 1.00 39.27 C
ATOM 1378 CG PHE A 199 13.122 -22.934 21.986 1.00 38.88 C
ATOM 1379 CD1 PHE A 199 13.999 -21.856 21.934 1.00 35.83 C
ATOM 1380 CD2 PHE A 199 11.898 -22.777 22.619 1.00 38.36 C
ATOM 1381 CE1 PHE A 199 13.659 -20.646 22.508 1.00 36.43 C
ATOM 1382 CE2 PHE A 199 11.553 -21.578 23.196 1.00 42.69 C
ATOM 1383 CZ PHE A 199 12.428 -20.507 23.142 1.00 38.14 C
ATOM 1384 N ILE A 200 15.228 -25.129 18.815 1.00 40.38 N
ATOM 1385 CA ILE A 200 16.222 -26.142 18.550 1.00 49.13 C
ATOM 1386 C ILE A 200 17.325 -26.047 19.616 1.00 51.02 C
ATOM 1387 O ILE A 200 18.079 -25.069 19.677 1.00 45.97 O
ATOM 1388 CB ILE A 200 16.706 -26.133 17.072 1.00 52.31 C
ATOM 1389 CG1 ILE A 200 18.019 -26.898 16.927 1.00 43.79 C
ATOM 1390 CG2 ILE A 200 16.815 -24.717 16.536 1.00 56.52 C
ATOM 1391 CD1 ILE A 200 18.282 -27.381 15.518 1.00 63.06 C
ATOM 1392 N ALA A 201 17.374 -27.062 20.480 1.00 47.02 N
ATOM 1393 CA ALA A 201 18.231 -27.026 21.670 1.00 51.13 C
ATOM 1394 C ALA A 201 19.451 -27.965 21.637 1.00 51.44 C
ATOM 1395 O ALA A 201 19.364 -29.105 21.181 1.00 49.70 O
ATOM 1396 CB ALA A 201 17.403 -27.280 22.915 1.00 40.52 C
ATOM 1397 N ASP A 202 20.587 -27.460 22.116 1.00 50.43 N
ATOM 1398 CA ASP A 202 21.789 -28.270 22.365 1.00 47.85 C
ATOM 1399 C ASP A 202 21.929 -28.492 23.856 1.00 45.97 C
ATOM 1400 O ASP A 202 21.741 -27.570 24.636 1.00 48.85 O
ATOM 1401 CB ASP A 202 23.062 -27.553 21.903 1.00 45.68 C
ATOM 1402 CG ASP A 202 23.220 -27.522 20.392 1.00 51.97 C
ATOM 1403 OD1 ASP A 202 22.425 -28.163 19.665 1.00 49.93 O
ATOM 1404 OD2 ASP A 202 24.173 -26.857 19.933 1.00 49.44 O
ATOM 1405 N GLY A 203 22.286 -29.708 24.248 1.00 57.98 N
ATOM 1406 CA GLY A 203 22.432 -30.066 25.654 1.00 47.02 C
ATOM 1407 C GLY A 203 23.871 -30.411 25.981 1.00 53.75 C
ATOM 1408 O GLY A 203 24.600 -30.965 25.162 1.00 59.45 O
ATOM 1409 N ASP A 204 24.294 -30.069 27.186 1.00 53.29 N
ATOM 1410 CA ASP A 204 25.668 -30.292 27.599 1.00 53.47 C
ATOM 1411 C ASP A 204 25.694 -30.568 29.092 1.00 52.02 C
ATOM 1412 O ASP A 204 24.866 -30.059 29.841 1.00 53.69 O
ATOM 1413 CB ASP A 204 26.517 -29.066 27.265 1.00 42.93 C
ATOM 1414 CG ASP A 204 26.981 -29.053 25.824 1.00 50.23 C
ATOM 1415 OD1 ASP A 204 27.424 -30.119 25.357 1.00 56.47 O
ATOM 1416 OD2 ASP A 204 26.910 -27.989 25.153 1.00 57.53 O
ATOM 1417 N VAL A 205 26.632 -31.389 29.527 1.00 52.56 N
ATOM 1418 CA VAL A 205 26.765 -31.674 30.946 1.00 54.56 C
ATOM 1419 C VAL A 205 28.222 -31.399 31.362 1.00 61.45 C
ATOM 1420 O VAL A 205 29.150 -31.540 30.555 1.00 56.67 O
ATOM 1421 CB VAL A 205 26.236 -33.104 31.254 1.00 50.77 C
ATOM 1422 CG1 VAL A 205 26.898 -33.706 32.445 1.00 56.01 C
ATOM 1423 CG2 VAL A 205 24.718 -33.084 31.447 1.00 42.74 C
ATOM 1424 N THR A 206 28.405 -30.919 32.588 1.00 59.14 N
ATOM 1425 CA THR A 206 29.727 -30.650 33.127 1.00 55.39 C
ATOM 1426 C THR A 206 29.893 -31.495 34.379 1.00 56.79 C
ATOM 1427 O THR A 206 28.906 -32.006 34.917 1.00 49.31 O
ATOM 1428 CB THR A 206 29.895 -29.159 33.475 1.00 57.12 C
ATOM 1429 OG1 THR A 206 28.761 -28.715 34.237 1.00 56.61 O
ATOM 1430 CG2 THR A 206 30.023 -28.318 32.208 1.00 47.64 C
ATOM 1431 N ALA A 207 31.134 -31.660 34.833 1.00 65.65 N
ATOM 1432 CA ALA A 207 31.404 -32.472 36.025 1.00 66.44 C
ATOM 1433 C ALA A 207 31.893 -31.636 37.210 1.00 67.54 C
ATOM 1434 O ALA A 207 31.998 -32.142 38.327 1.00 67.89 O
ATOM 1435 CB ALA A 207 32.388 -33.610 35.710 1.00 62.83 C
ATOM 1436 N SER A 208 32.161 -30.355 36.972 1.00 64.36 N
ATOM 1437 CA SER A 208 32.728 -29.500 38.005 1.00 59.47 C
ATOM 1438 C SER A 208 32.306 -28.049 37.807 1.00 64.17 C
ATOM 1439 O SER A 208 31.984 -27.632 36.681 1.00 57.51 O
ATOM 1440 CB SER A 208 34.251 -29.576 37.939 1.00 57.59 C
ATOM 1441 OG SER A 208 34.751 -28.569 37.069 1.00 63.99 O
ATOM 1442 N LEU A 209 32.335 -27.279 38.894 1.00 57.74 N
ATOM 1443 CA LEU A 209 32.089 -25.849 38.812 1.00 53.01 C
ATOM 1444 C LEU A 209 33.048 -25.180 37.847 1.00 54.02 C
ATOM 1445 O LEU A 209 32.674 -24.240 37.149 1.00 59.26 O
ATOM 1446 CB LEU A 209 32.235 -25.207 40.185 1.00 56.95 C
ATOM 1447 CG LEU A 209 32.102 -23.689 40.219 1.00 51.17 C
ATOM 1448 CD1 LEU A 209 30.702 -23.270 39.792 1.00 56.43 C
ATOM 1449 CD2 LEU A 209 32.401 -23.195 41.603 1.00 55.10 C
ATOM 1450 N ASP A 210 34.290 -25.658 37.801 1.00 61.52 N
ATOM 1451 CA ASP A 210 35.278 -25.053 36.911 1.00 59.39 C
ATOM 1452 C ASP A 210 34.927 -25.319 35.467 1.00 53.37 C
ATOM 1453 O ASP A 210 35.157 -24.468 34.617 1.00 59.85 O
ATOM 1454 CB ASP A 210 36.684 -25.560 37.219 1.00 68.82 C
ATOM 1455 CG ASP A 210 37.053 -25.392 38.679 1.00 68.87 C
ATOM 1456 OD1 ASP A 210 37.501 -24.280 39.054 1.00 65.83 O
ATOM 1457 OD2 ASP A 210 36.884 -26.375 39.442 1.00 58.26 O
ATOM 1458 N GLU A 211 34.368 -26.497 35.194 1.00 53.16 N
ATOM 1459 CA GLU A 211 33.943 -26.844 33.828 1.00 61.46 C
ATOM 1460 C GLU A 211 32.799 -25.943 33.369 1.00 58.58 C
ATOM 1461 O GLU A 211 32.835 -25.377 32.266 1.00 53.36 O
ATOM 1462 CB GLU A 211 33.494 -28.306 33.729 1.00 68.77 C
ATOM 1463 CG GLU A 211 34.618 -29.322 33.622 1.00 69.83 C
ATOM 1464 CD GLU A 211 34.112 -30.716 33.283 1.00 76.45 C
ATOM 1465 OE1 GLU A 211 32.884 -30.877 33.087 1.00 64.11 O
ATOM 1466 OE2 GLU A 211 34.948 -31.646 33.203 1.00 77.51 O
ATOM 1467 N THR A 212 31.790 -25.825 34.233 1.00 48.36 N
ATOM 1468 CA THR A 212 30.674 -24.910 34.036 1.00 50.05 C
ATOM 1469 C THR A 212 31.109 -23.482 33.660 1.00 56.27 C
ATOM 1470 O THR A 212 30.652 -22.942 32.648 1.00 55.95 O
ATOM 1471 CB THR A 212 29.746 -24.895 35.268 1.00 53.78 C
ATOM 1472 OG1 THR A 212 29.156 -26.190 35.428 1.00 53.82 O
ATOM 1473 CG2 THR A 212 28.642 -23.878 35.095 1.00 56.17 C
ATOM 1474 N ILE A 213 31.997 -22.883 34.452 1.00 51.57 N
ATOM 1475 CA ILE A 213 32.505 -21.543 34.147 1.00 52.96 C
ATOM 1476 C ILE A 213 33.214 -21.497 32.795 1.00 55.15 C
ATOM 1477 O ILE A 213 33.067 -20.529 32.039 1.00 57.09 O
ATOM 1478 CB ILE A 213 33.458 -20.999 35.254 1.00 49.98 C
ATOM 1479 CG1 ILE A 213 32.668 -20.302 36.357 1.00 49.11 C
ATOM 1480 CG2 ILE A 213 34.410 -19.958 34.684 1.00 50.05 C
ATOM 1481 CD1 ILE A 213 31.842 -21.218 37.213 1.00 53.18 C
ATOM 1482 N ALA A 214 33.979 -22.550 32.498 1.00 59.65 N
ATOM 1483 CA ALA A 214 34.723 -22.668 31.238 1.00 60.55 C
ATOM 1484 C ALA A 214 33.786 -22.617 30.043 1.00 57.03 C
ATOM 1485 O ALA A 214 33.985 -21.842 29.102 1.00 57.07 O
ATOM 1486 CB ALA A 214 35.492 -23.981 31.224 1.00 59.91 C
ATOM 1487 N LEU A 215 32.762 -23.465 30.111 1.00 57.11 N
ATOM 1488 CA LEU A 215 31.734 -23.582 29.079 1.00 55.88 C
ATOM 1489 C LEU A 215 31.059 -22.247 28.800 1.00 57.33 C
ATOM 1490 O LEU A 215 30.686 -21.946 27.657 1.00 48.75 O
ATOM 1491 CB LEU A 215 30.694 -24.619 29.513 1.00 48.36 C
ATOM 1492 CG LEU A 215 29.623 -25.022 28.502 1.00 53.28 C
ATOM 1493 CD1 LEU A 215 30.238 -25.317 27.146 1.00 59.96 C
ATOM 1494 CD2 LEU A 215 28.879 -26.239 29.003 1.00 52.92 C
ATOM 1495 N HIS A 216 30.922 -21.440 29.848 1.00 52.63 N
ATOM 1496 CA HIS A 216 30.223 -20.172 29.726 1.00 53.26 C
ATOM 1497 C HIS A 216 31.144 -19.025 29.351 1.00 53.55 C
ATOM 1498 O HIS A 216 30.686 -17.920 29.069 1.00 59.66 O
ATOM 1499 CB HIS A 216 29.464 -19.855 31.004 1.00 45.23 C
ATOM 1500 CG HIS A 216 28.241 -20.697 31.209 1.00 44.95 C
ATOM 1501 ND1 HIS A 216 28.282 -21.950 31.785 1.00 47.36 N
ATOM 1502 CD2 HIS A 216 26.935 -20.452 30.943 1.00 40.71 C
ATOM 1503 CE1 HIS A 216 27.058 -22.441 31.865 1.00 37.16 C
ATOM 1504 NE2 HIS A 216 26.220 -21.548 31.369 1.00 41.02 N
ATOM 1505 N SER A 217 32.444 -19.284 29.328 1.00 57.14 N
ATOM 1506 CA SER A 217 33.388 -18.238 28.943 1.00 62.52 C
ATOM 1507 C SER A 217 34.247 -18.623 27.739 1.00 62.45 C
ATOM 1508 O SER A 217 35.228 -17.939 27.439 1.00 65.41 O
ATOM 1509 CB SER A 217 34.261 -17.817 30.132 1.00 51.86 C
ATOM 1510 OG SER A 217 34.234 -18.822 31.126 1.00 55.42 O
ATOM 1511 N ASP A 218 33.866 -19.696 27.041 1.00 62.00 N
ATOM 1512 CA ASP A 218 34.627 -20.144 25.866 1.00 62.22 C
ATOM 1513 C ASP A 218 34.164 -19.545 24.546 1.00 61.93 C
ATOM 1514 O ASP A 218 34.729 -19.852 23.501 1.00 68.73 O
ATOM 1515 CB ASP A 218 34.670 -21.675 25.751 1.00 58.79 C
ATOM 1516 CG ASP A 218 33.328 -22.284 25.385 1.00 67.77 C
ATOM 1517 OD1 ASP A 218 32.346 -21.527 25.203 1.00 70.13 O
ATOM 1518 OD2 ASP A 218 33.258 -23.535 25.274 1.00 64.96 O
ATOM 1519 N GLY A 219 33.127 -18.713 24.597 1.00 68.01 N
ATOM 1520 CA GLY A 219 32.576 -18.101 23.399 1.00 59.96 C
ATOM 1521 C GLY A 219 31.399 -18.840 22.784 1.00 59.44 C
ATOM 1522 O GLY A 219 30.773 -18.327 21.859 1.00 60.82 O
ATOM 1523 N SER A 220 31.095 -20.038 23.285 1.00 52.24 N
ATOM 1524 CA SER A 220 29.994 -20.818 22.739 1.00 56.29 C
ATOM 1525 C SER A 220 28.654 -20.141 23.006 1.00 57.67 C
ATOM 1526 O SER A 220 27.730 -20.206 22.197 1.00 54.38 O
ATOM 1527 CB SER A 220 29.998 -22.236 23.292 1.00 50.77 C
ATOM 1528 OG SER A 220 29.807 -22.240 24.681 1.00 54.82 O
ATOM 1529 N GLU A 221 28.570 -19.473 24.144 1.00 58.45 N
ATOM 1530 CA GLU A 221 27.383 -18.722 24.532 1.00 56.80 C
ATOM 1531 C GLU A 221 26.848 -17.767 23.417 1.00 55.59 C
ATOM 1532 O GLU A 221 25.639 -17.556 23.292 1.00 51.61 O
ATOM 1533 CB GLU A 221 27.691 -17.986 25.846 1.00 43.22 C
ATOM 1534 CG GLU A 221 26.492 -17.477 26.581 1.00 46.88 C
ATOM 1535 CD GLU A 221 25.826 -18.499 27.495 1.00 48.37 C
ATOM 1536 OE1 GLU A 221 25.995 -19.726 27.280 1.00 40.56 O
ATOM 1537 OE2 GLU A 221 25.107 -18.049 28.428 1.00 47.07 O
ATOM 1538 N ALA A 222 27.738 -17.230 22.585 1.00 53.42 N
ATOM 1539 CA ALA A 222 27.333 -16.313 21.511 1.00 48.67 C
ATOM 1540 C ALA A 222 26.620 -17.005 20.345 1.00 54.86 C
ATOM 1541 O ALA A 222 26.123 -16.340 19.432 1.00 48.65 O
ATOM 1542 CB ALA A 222 28.531 -15.524 20.996 1.00 39.34 C
ATOM 1543 N ARG A 223 26.582 -18.333 20.374 1.00 52.42 N
ATOM 1544 CA ARG A 223 25.934 -19.110 19.325 1.00 54.47 C
ATOM 1545 C ARG A 223 24.482 -19.397 19.688 1.00 57.64 C
ATOM 1546 O ARG A 223 23.683 -19.810 18.843 1.00 53.43 O
ATOM 1547 CB ARG A 223 26.688 -20.420 19.081 1.00 44.69 C
ATOM 1548 CG ARG A 223 28.086 -20.222 18.519 1.00 51.00 C
ATOM 1549 CD ARG A 223 28.653 -21.521 17.930 1.00 66.66 C
ATOM 1550 NE ARG A 223 28.842 -22.608 18.901 1.00 61.94 N
ATOM 1551 CZ ARG A 223 29.933 -22.765 19.654 1.00 64.27 C
ATOM 1552 NH1 ARG A 223 30.936 -21.890 19.578 1.00 61.84 N
ATOM 1553 NH2 ARG A 223 30.016 -23.795 20.495 1.00 49.29 N
ATOM 1554 N TYR A 224 24.148 -19.175 20.954 1.00 52.47 N
ATOM 1555 CA TYR A 224 22.810 -19.443 21.432 1.00 45.50 C
ATOM 1556 C TYR A 224 22.132 -18.167 21.888 1.00 46.46 C
ATOM 1557 O TYR A 224 22.758 -17.340 22.537 1.00 50.76 O
ATOM 1558 CB TYR A 224 22.892 -20.403 22.591 1.00 44.78 C
ATOM 1559 CG TYR A 224 23.562 -21.709 22.267 1.00 52.43 C
ATOM 1560 CD1 TYR A 224 22.857 -22.737 21.659 1.00 53.16 C
ATOM 1561 CD2 TYR A 224 24.892 -21.934 22.601 1.00 55.35 C
ATOM 1562 CE1 TYR A 224 23.467 -23.949 21.380 1.00 55.73 C
ATOM 1563 CE2 TYR A 224 25.506 -23.146 22.328 1.00 52.13 C
ATOM 1564 CZ TYR A 224 24.790 -24.147 21.717 1.00 47.04 C
ATOM 1565 OH TYR A 224 25.386 -25.351 21.437 1.00 50.23 O
ATOM 1566 N THR A 225 20.855 -18.005 21.560 1.00 39.47 N
ATOM 1567 CA THR A 225 20.097 -16.857 22.044 1.00 40.57 C
ATOM 1568 C THR A 225 19.536 -17.130 23.440 1.00 40.52 C
ATOM 1569 O THR A 225 19.326 -16.206 24.214 1.00 42.52 O
ATOM 1570 CB THR A 225 18.927 -16.525 21.119 1.00 42.49 C
ATOM 1571 OG1 THR A 225 18.183 -17.723 20.872 1.00 45.39 O
ATOM 1572 CG2 THR A 225 19.421 -15.936 19.778 1.00 31.57 C
ATOM 1573 N TYR A 226 19.290 -18.400 23.744 1.00 37.47 N
ATOM 1574 CA TYR A 226 18.720 -18.822 25.023 1.00 35.92 C
ATOM 1575 C TYR A 226 19.716 -19.754 25.695 1.00 39.58 C
ATOM 1576 O TYR A 226 20.321 -20.583 25.033 1.00 39.10 O
ATOM 1577 CB TYR A 226 17.403 -19.585 24.809 1.00 36.22 C
ATOM 1578 CG TYR A 226 16.250 -18.717 24.374 1.00 37.35 C
ATOM 1579 CD1 TYR A 226 15.174 -18.494 25.215 1.00 36.69 C
ATOM 1580 CD2 TYR A 226 16.242 -18.107 23.120 1.00 31.55 C
ATOM 1581 CE1 TYR A 226 14.121 -17.686 24.823 1.00 38.55 C
ATOM 1582 CE2 TYR A 226 15.201 -17.300 22.724 1.00 31.24 C
ATOM 1583 CZ TYR A 226 14.139 -17.091 23.579 1.00 32.81 C
ATOM 1584 OH TYR A 226 13.077 -16.295 23.192 1.00 29.37 O
ATOM 1585 N SER A 227 19.881 -19.624 27.005 1.00 37.96 N
ATOM 1586 CA SER A 227 20.854 -20.442 27.725 1.00 37.33 C
ATOM 1587 C SER A 227 20.637 -20.377 29.230 1.00 36.02 C
ATOM 1588 O SER A 227 20.477 -19.290 29.781 1.00 35.92 O
ATOM 1589 CB SER A 227 22.279 -20.004 27.381 1.00 35.36 C
ATOM 1590 OG SER A 227 23.235 -20.743 28.129 1.00 41.74 O
ATOM 1591 N SER A 228 20.609 -21.541 29.876 1.00 34.24 N
ATOM 1592 CA SER A 228 20.546 -21.635 31.331 1.00 35.19 C
ATOM 1593 C SER A 228 20.951 -23.040 31.763 1.00 41.36 C
ATOM 1594 O SER A 228 21.055 -23.930 30.925 1.00 40.25 O
ATOM 1595 CB SER A 228 19.147 -21.318 31.823 1.00 36.59 C
ATOM 1596 OG SER A 228 18.218 -22.221 31.280 1.00 38.69 O
ATOM 1597 N ALA A 229 21.192 -23.249 33.056 1.00 38.09 N
ATOM 1598 CA ALA A 229 21.650 -24.561 33.511 1.00 34.58 C
ATOM 1599 C ALA A 229 21.078 -24.982 34.858 1.00 36.93 C
ATOM 1600 O ALA A 229 20.811 -24.144 35.706 1.00 44.90 O
ATOM 1601 CB ALA A 229 23.132 -24.598 33.526 1.00 32.21 C
ATOM 1602 N TRP A 230 20.834 -26.274 35.039 1.00 35.58 N
ATOM 1603 CA TRP A 230 20.613 -26.803 36.386 1.00 51.04 C
ATOM 1604 C TRP A 230 21.985 -27.066 36.991 1.00 46.72 C
ATOM 1605 O TRP A 230 22.895 -27.504 36.311 1.00 49.78 O
ATOM 1606 CB TRP A 230 19.837 -28.106 36.355 1.00 55.18 C
ATOM 1607 CG TRP A 230 18.540 -28.006 35.641 1.00 73.69 C
ATOM 1608 CD1 TRP A 230 18.238 -28.499 34.395 1.00 73.09 C
ATOM 1609 CD2 TRP A 230 17.352 -27.377 36.123 1.00 79.71 C
ATOM 1610 NE1 TRP A 230 16.931 -28.216 34.080 1.00 79.65 N
ATOM 1611 CE2 TRP A 230 16.364 -27.526 35.125 1.00 78.01 C
ATOM 1612 CE3 TRP A 230 17.020 -26.706 37.309 1.00 78.04 C
ATOM 1613 CZ2 TRP A 230 15.077 -27.030 35.271 1.00 81.08 C
ATOM 1614 CZ3 TRP A 230 15.742 -26.213 37.451 1.00 85.73 C
ATOM 1615 CH2 TRP A 230 14.787 -26.376 36.435 1.00 82.29 C
ATOM 1616 N PHE A 231 22.125 -26.849 38.280 1.00 49.81 N
ATOM 1617 CA PHE A 231 23.434 -26.635 38.861 1.00 53.32 C
ATOM 1618 C PHE A 231 23.514 -27.329 40.210 1.00 42.16 C
ATOM 1619 O PHE A 231 22.656 -27.079 41.045 1.00 44.23 O
ATOM 1620 CB PHE A 231 23.472 -25.114 39.035 1.00 52.98 C
ATOM 1621 CG PHE A 231 24.678 -24.578 39.704 1.00 51.26 C
ATOM 1622 CD1 PHE A 231 25.715 -24.048 38.950 1.00 50.40 C
ATOM 1623 CD2 PHE A 231 24.741 -24.507 41.081 1.00 44.20 C
ATOM 1624 CE1 PHE A 231 26.832 -23.524 39.560 1.00 52.29 C
ATOM 1625 CE2 PHE A 231 25.849 -23.982 41.704 1.00 50.05 C
ATOM 1626 CZ PHE A 231 26.901 -23.489 40.943 1.00 51.84 C
ATOM 1627 N ASP A 232 24.515 -28.194 40.427 1.00 49.11 N
ATOM 1628 CA ASP A 232 24.658 -28.920 41.707 1.00 54.46 C
ATOM 1629 C ASP A 232 25.250 -28.020 42.810 1.00 48.42 C
ATOM 1630 O ASP A 232 26.390 -27.548 42.701 1.00 44.27 O
ATOM 1631 CB ASP A 232 25.482 -30.209 41.530 1.00 59.68 C
ATOM 1632 CG ASP A 232 25.314 -31.200 42.700 1.00 61.05 C
ATOM 1633 OD1 ASP A 232 24.891 -30.788 43.802 1.00 52.03 O
ATOM 1634 OD2 ASP A 232 25.608 -32.404 42.515 1.00 57.96 O
ATOM 1635 N ALA A 233 24.453 -27.779 43.852 1.00 44.25 N
ATOM 1636 CA ALA A 233 24.868 -26.951 44.990 1.00 56.91 C
ATOM 1637 C ALA A 233 24.981 -27.743 46.308 1.00 62.54 C
ATOM 1638 O ALA A 233 25.006 -27.156 47.406 1.00 50.91 O
ATOM 1639 CB ALA A 233 23.904 -25.768 45.164 1.00 39.88 C
ATOM 1640 N ILE A 234 25.039 -29.070 46.192 1.00 62.54 N
ATOM 1641 CA ILE A 234 25.085 -29.942 47.359 1.00 62.93 C
ATOM 1642 C ILE A 234 26.349 -30.828 47.419 1.00 63.25 C
ATOM 1643 O ILE A 234 26.991 -30.919 48.468 1.00 67.18 O
ATOM 1644 CB ILE A 234 23.796 -30.756 47.482 1.00 53.22 C
ATOM 1645 CG1 ILE A 234 22.599 -29.812 47.504 1.00 55.95 C
ATOM 1646 CG2 ILE A 234 23.795 -31.576 48.764 1.00 65.75 C
ATOM 1647 CD1 ILE A 234 21.268 -30.503 47.768 1.00 53.81 C
ATOM 1648 N SER A 235 26.711 -31.447 46.299 1.00 54.16 N
ATOM 1649 CA SER A 235 27.923 -32.253 46.220 1.00 61.45 C
ATOM 1650 C SER A 235 29.186 -31.458 46.536 1.00 69.98 C
ATOM 1651 O SER A 235 29.340 -30.328 46.076 1.00 70.36 O
ATOM 1652 CB SER A 235 28.047 -32.907 44.842 1.00 60.50 C
ATOM 1653 OG SER A 235 27.208 -34.048 44.749 1.00 58.69 O
ATOM 1654 N ALA A 236 30.087 -32.058 47.317 1.00 65.23 N
ATOM 1655 CA ALA A 236 31.341 -31.398 47.677 1.00 66.38 C
ATOM 1656 C ALA A 236 32.261 -31.302 46.464 1.00 63.62 C
ATOM 1657 O ALA A 236 32.133 -32.085 45.530 1.00 65.61 O
ATOM 1658 CB ALA A 236 32.020 -32.141 48.809 1.00 68.68 C
ATOM 1659 N PRO A 237 33.189 -30.336 46.477 1.00 62.37 N
ATOM 1660 CA PRO A 237 34.125 -30.164 45.368 1.00 64.31 C
ATOM 1661 C PRO A 237 34.924 -31.425 45.079 1.00 69.91 C
ATOM 1662 O PRO A 237 35.039 -32.278 45.969 1.00 72.38 O
ATOM 1663 CB PRO A 237 35.059 -29.072 45.876 1.00 54.94 C
ATOM 1664 CG PRO A 237 34.239 -28.282 46.796 1.00 50.41 C
ATOM 1665 CD PRO A 237 33.312 -29.257 47.468 1.00 53.90 C
ATOM 1666 N PRO A 238 35.450 -31.557 43.836 1.00 72.81 N
ATOM 1667 CA PRO A 238 35.188 -30.633 42.716 1.00 76.87 C
ATOM 1668 C PRO A 238 33.937 -30.984 41.908 1.00 69.58 C
ATOM 1669 O PRO A 238 33.791 -30.481 40.807 1.00 59.81 O
ATOM 1670 CB PRO A 238 36.448 -30.763 41.857 1.00 53.71 C
ATOM 1671 CG PRO A 238 36.899 -32.139 42.083 1.00 66.61 C
ATOM 1672 CD PRO A 238 36.607 -32.432 43.542 1.00 83.21 C
ATOM 1673 N LYS A 239 33.066 -31.819 42.466 1.00 68.14 N
ATOM 1674 CA LYS A 239 31.791 -32.145 41.842 1.00 63.68 C
ATOM 1675 C LYS A 239 30.782 -30.992 42.032 1.00 69.77 C
ATOM 1676 O LYS A 239 29.828 -30.839 41.254 1.00 66.80 O
ATOM 1677 CB LYS A 239 31.268 -33.461 42.425 1.00 55.68 C
ATOM 1678 CG LYS A 239 29.910 -33.919 41.949 1.00 68.10 C
ATOM 1679 CD LYS A 239 29.653 -35.382 42.355 1.00 72.10 C
ATOM 1680 CE LYS A 239 30.384 -36.361 41.425 1.00 79.24 C
ATOM 1681 NZ LYS A 239 29.734 -37.709 41.354 1.00 74.11 N
ATOM 1682 N LEU A 240 31.004 -30.172 43.057 1.00 65.79 N
ATOM 1683 CA LEU A 240 30.181 -28.988 43.276 1.00 60.67 C
ATOM 1684 C LEU A 240 30.189 -28.100 42.037 1.00 62.00 C
ATOM 1685 O LEU A 240 31.245 -27.775 41.499 1.00 56.06 O
ATOM 1686 CB LEU A 240 30.675 -28.178 44.486 1.00 65.26 C
ATOM 1687 CG LEU A 240 30.036 -26.799 44.743 1.00 58.00 C
ATOM 1688 CD1 LEU A 240 28.560 -26.909 45.096 1.00 46.11 C
ATOM 1689 CD2 LEU A 240 30.789 -25.995 45.817 1.00 53.58 C
ATOM 1690 N GLY A 241 29.002 -27.714 41.583 1.00 58.27 N
ATOM 1691 CA GLY A 241 28.893 -26.767 40.488 1.00 57.94 C
ATOM 1692 C GLY A 241 28.858 -27.397 39.110 1.00 52.95 C
ATOM 1693 O GLY A 241 28.937 -26.707 38.101 1.00 48.36 O
ATOM 1694 N ARG A 242 28.764 -28.719 39.070 1.00 60.87 N
ATOM 1695 CA ARG A 242 28.558 -29.413 37.816 1.00 54.72 C
ATOM 1696 C ARG A 242 27.158 -29.056 37.401 1.00 56.71 C
ATOM 1697 O ARG A 242 26.297 -28.821 38.253 1.00 53.57 O
ATOM 1698 CB ARG A 242 28.650 -30.920 38.006 1.00 53.49 C
ATOM 1699 CG ARG A 242 27.594 -31.479 38.916 1.00 50.23 C
ATOM 1700 CD ARG A 242 27.685 -32.978 39.002 1.00 51.36 C
ATOM 1701 NE ARG A 242 26.824 -33.481 40.064 1.00 59.21 N
ATOM 1702 CZ ARG A 242 26.694 -34.769 40.371 1.00 66.70 C
ATOM 1703 NH1 ARG A 242 27.377 -35.684 39.685 1.00 72.53 N
ATOM 1704 NH2 ARG A 242 25.884 -35.143 41.362 1.00 57.24 N
ATOM 1705 N ALA A 243 26.922 -29.015 36.097 1.00 51.45 N
ATOM 1706 CA ALA A 243 25.653 -28.514 35.609 1.00 52.34 C
ATOM 1707 C ALA A 243 25.112 -29.277 34.407 1.00 50.94 C
ATOM 1708 O ALA A 243 25.878 -29.784 33.578 1.00 54.46 O
ATOM 1709 CB ALA A 243 25.779 -27.030 35.268 1.00 55.52 C
ATOM 1710 N ALA A 244 23.784 -29.344 34.315 1.00 47.65 N
ATOM 1711 CA ALA A 244 23.111 -29.733 33.073 1.00 46.94 C
ATOM 1712 C ALA A 244 22.741 -28.475 32.292 1.00 39.84 C
ATOM 1713 O ALA A 244 21.745 -27.820 32.600 1.00 43.40 O
ATOM 1714 CB ALA A 244 21.865 -30.549 33.365 1.00 43.03 C
ATOM 1715 N VAL A 245 23.550 -28.141 31.290 1.00 34.73 N
ATOM 1716 CA VAL A 245 23.344 -26.942 30.468 1.00 40.54 C
ATOM 1717 C VAL A 245 22.414 -27.122 29.252 1.00 48.81 C
ATOM 1718 O VAL A 245 22.702 -27.900 28.344 1.00 48.65 O
ATOM 1719 CB VAL A 245 24.676 -26.438 29.910 1.00 35.85 C
ATOM 1720 CG1 VAL A 245 24.500 -25.069 29.293 1.00 33.05 C
ATOM 1721 CG2 VAL A 245 25.732 -26.415 31.000 1.00 43.49 C
ATOM 1722 N SER A 246 21.319 -26.369 29.214 1.00 51.61 N
ATOM 1723 CA SER A 246 20.383 -26.408 28.091 1.00 39.16 C
ATOM 1724 C SER A 246 20.423 -25.103 27.295 1.00 39.40 C
ATOM 1725 O SER A 246 20.001 -24.067 27.791 1.00 44.47 O
ATOM 1726 CB SER A 246 18.970 -26.654 28.626 1.00 40.35 C
ATOM 1727 OG SER A 246 17.976 -26.414 27.630 1.00 56.31 O
ATOM 1728 N ARG A 247 20.923 -25.132 26.065 1.00 41.84 N
ATOM 1729 CA ARG A 247 21.004 -23.901 25.269 1.00 39.63 C
ATOM 1730 C ARG A 247 20.334 -24.045 23.912 1.00 51.06 C
ATOM 1731 O ARG A 247 20.206 -25.146 23.394 1.00 54.20 O
ATOM 1732 CB ARG A 247 22.451 -23.476 25.069 1.00 38.02 C
ATOM 1733 CG ARG A 247 23.283 -23.630 26.326 1.00 43.12 C
ATOM 1734 CD ARG A 247 24.661 -23.009 26.171 1.00 48.87 C
ATOM 1735 NE ARG A 247 25.662 -23.927 25.637 1.00 47.23 N
ATOM 1736 CZ ARG A 247 26.934 -23.590 25.445 1.00 53.93 C
ATOM 1737 NH1 ARG A 247 27.338 -22.361 25.748 1.00 50.01 N
ATOM 1738 NH2 ARG A 247 27.799 -24.471 24.956 1.00 54.98 N
ATOM 1739 N GLY A 248 19.913 -22.935 23.318 1.00 47.52 N
ATOM 1740 CA GLY A 248 19.192 -23.041 22.077 1.00 44.78 C
ATOM 1741 C GLY A 248 18.783 -21.762 21.399 1.00 45.91 C
ATOM 1742 O GLY A 248 19.315 -20.692 21.679 1.00 47.56 O
ATOM 1743 N ARG A 249 17.829 -21.904 20.486 1.00 42.90 N
ATOM 1744 CA ARG A 249 17.340 -20.810 19.679 1.00 44.72 C
ATOM 1745 C ARG A 249 16.002 -21.217 19.068 1.00 44.23 C
ATOM 1746 O ARG A 249 15.703 -22.407 18.946 1.00 43.07 O
ATOM 1747 CB ARG A 249 18.356 -20.417 18.611 1.00 48.36 C
ATOM 1748 CG ARG A 249 18.320 -21.276 17.360 1.00 59.83 C
ATOM 1749 CD ARG A 249 19.475 -20.919 16.432 1.00 59.52 C
ATOM 1750 NE ARG A 249 20.740 -20.858 17.168 1.00 78.15 N
ATOM 1751 CZ ARG A 249 21.478 -21.917 17.516 1.00 68.64 C
ATOM 1752 NH1 ARG A 249 21.103 -23.156 17.201 1.00 51.18 N
ATOM 1753 NH2 ARG A 249 22.605 -21.730 18.188 1.00 67.12 N
ATOM 1754 N LEU A 250 15.182 -20.225 18.726 1.00 45.16 N
ATOM 1755 CA LEU A 250 13.904 -20.490 18.070 1.00 43.35 C
ATOM 1756 C LEU A 250 14.161 -21.159 16.729 1.00 44.05 C
ATOM 1757 O LEU A 250 15.073 -20.773 15.987 1.00 40.80 O
ATOM 1758 CB LEU A 250 13.115 -19.199 17.854 1.00 37.30 C
ATOM 1759 CG LEU A 250 12.484 -18.576 19.090 1.00 35.09 C
ATOM 1760 CD1 LEU A 250 12.006 -17.183 18.760 1.00 30.61 C
ATOM 1761 CD2 LEU A 250 11.352 -19.435 19.596 1.00 31.16 C
ATOM 1762 N ALA A 251 13.360 -22.171 16.425 1.00 43.84 N
ATOM 1763 CA ALA A 251 13.531 -22.901 15.181 1.00 49.36 C
ATOM 1764 C ALA A 251 12.768 -22.222 14.042 1.00 48.92 C
ATOM 1765 O ALA A 251 11.708 -21.626 14.261 1.00 42.20 O
ATOM 1766 CB ALA A 251 13.090 -24.338 15.353 1.00 40.54 C
ATOM 1767 N THR A 252 13.336 -22.288 12.841 1.00 46.76 N
ATOM 1768 CA THR A 252 12.639 -21.864 11.634 1.00 46.05 C
ATOM 1769 C THR A 252 11.799 -23.042 11.138 1.00 51.29 C
ATOM 1770 O THR A 252 11.958 -24.168 11.620 1.00 46.91 O
ATOM 1771 CB THR A 252 13.610 -21.442 10.525 1.00 45.11 C
ATOM 1772 OG1 THR A 252 14.362 -22.585 10.108 1.00 50.71 O
ATOM 1773 CG2 THR A 252 14.573 -20.357 11.013 1.00 42.60 C
ATOM 1774 N VAL A 253 10.906 -22.782 10.184 1.00 53.84 N
ATOM 1775 CA VAL A 253 10.025 -23.821 9.666 1.00 52.11 C
ATOM 1776 C VAL A 253 10.795 -24.947 8.960 1.00 53.94 C
ATOM 1777 O VAL A 253 10.501 -26.132 9.145 1.00 54.98 O
ATOM 1778 CB VAL A 253 8.957 -23.224 8.727 1.00 55.21 C
ATOM 1779 CG1 VAL A 253 8.149 -24.329 8.067 1.00 50.99 C
ATOM 1780 CG2 VAL A 253 8.041 -22.307 9.505 1.00 46.47 C
ATOM 1781 N GLU A 254 11.802 -24.573 8.178 1.00 49.84 N
ATOM 1782 CA GLU A 254 12.624 -25.550 7.472 1.00 58.30 C
ATOM 1783 C GLU A 254 13.431 -26.495 8.398 1.00 62.18 C
ATOM 1784 O GLU A 254 14.131 -27.381 7.916 1.00 67.62 O
ATOM 1785 CB GLU A 254 13.555 -24.826 6.488 1.00 48.40 C
ATOM 1786 N GLN A 255 13.333 -26.313 9.715 1.00 60.84 N
ATOM 1787 CA GLN A 255 14.073 -27.151 10.665 1.00 59.80 C
ATOM 1788 C GLN A 255 13.159 -28.048 11.476 1.00 61.75 C
ATOM 1789 O GLN A 255 13.617 -28.843 12.304 1.00 56.89 O
ATOM 1790 CB GLN A 255 14.894 -26.300 11.618 1.00 46.82 C
ATOM 1791 CG GLN A 255 15.863 -25.384 10.933 1.00 49.31 C
ATOM 1792 CD GLN A 255 16.747 -24.669 11.931 1.00 56.33 C
ATOM 1793 OE1 GLN A 255 16.375 -23.627 12.481 1.00 56.13 O
ATOM 1794 NE2 GLN A 255 17.918 -25.241 12.193 1.00 61.25 N
ATOM 1795 N LEU A 256 11.864 -27.912 11.233 1.00 59.83 N
ATOM 1796 CA LEU A 256 10.876 -28.730 11.907 1.00 59.25 C
ATOM 1797 C LEU A 256 10.754 -30.078 11.222 1.00 66.06 C
ATOM 1798 O LEU A 256 10.967 -30.194 10.018 1.00 63.89 O
ATOM 1799 CB LEU A 256 9.520 -28.023 11.893 1.00 63.82 C
ATOM 1800 CG LEU A 256 9.207 -27.115 13.084 1.00 62.07 C
ATOM 1801 CD1 LEU A 256 10.453 -26.378 13.549 1.00 45.91 C
ATOM 1802 CD2 LEU A 256 8.075 -26.141 12.732 1.00 45.81 C
ATOM 1803 N PRO A 257 10.434 -31.114 11.997 1.00 72.63 N
ATOM 1804 CA PRO A 257 10.008 -32.365 11.366 1.00 73.14 C
ATOM 1805 C PRO A 257 8.745 -32.115 10.550 1.00 74.57 C
ATOM 1806 O PRO A 257 7.904 -31.317 10.957 1.00 76.45 O
ATOM 1807 CB PRO A 257 9.736 -33.298 12.554 1.00 65.69 C
ATOM 1808 CG PRO A 257 9.816 -32.432 13.797 1.00 66.57 C
ATOM 1809 CD PRO A 257 10.660 -31.255 13.443 1.00 62.48 C
ATOM 1810 N ALA A 258 8.626 -32.785 9.410 1.00 79.18 N
ATOM 1811 CA ALA A 258 7.548 -32.528 8.459 1.00 79.06 C
ATOM 1812 C ALA A 258 6.126 -32.669 9.029 1.00 81.69 C
ATOM 1813 O ALA A 258 5.165 -32.155 8.450 1.00 86.34 O
ATOM 1814 CB ALA A 258 7.724 -33.421 7.236 1.00 85.66 C
ATOM 1815 N LYS A 259 5.995 -33.366 10.154 1.00 79.15 N
ATOM 1816 CA LYS A 259 4.700 -33.522 10.808 1.00 76.92 C
ATOM 1817 C LYS A 259 4.229 -32.206 11.407 1.00 81.61 C
ATOM 1818 O LYS A 259 3.039 -32.027 11.678 1.00 78.45 O
ATOM 1819 CB LYS A 259 4.790 -34.568 11.928 1.00 61.66 C
ATOM 1820 N LEU A 260 5.175 -31.292 11.622 1.00 76.83 N
ATOM 1821 CA LEU A 260 4.926 -30.060 12.375 1.00 71.57 C
ATOM 1822 C LEU A 260 4.951 -28.818 11.494 1.00 72.68 C
ATOM 1823 O LEU A 260 4.419 -27.771 11.866 1.00 73.22 O
ATOM 1824 CB LEU A 260 5.977 -29.912 13.470 1.00 67.78 C
ATOM 1825 CG LEU A 260 5.748 -30.587 14.821 1.00 71.55 C
ATOM 1826 CD1 LEU A 260 4.828 -31.792 14.712 1.00 64.83 C
ATOM 1827 CD2 LEU A 260 7.082 -30.980 15.432 1.00 64.75 C
ATOM 1828 N ARG A 261 5.616 -28.955 10.350 1.00 66.56 N
ATOM 1829 CA ARG A 261 5.766 -27.907 9.348 1.00 61.79 C
ATOM 1830 C ARG A 261 4.426 -27.418 8.788 1.00 69.54 C
ATOM 1831 O ARG A 261 4.338 -26.326 8.212 1.00 66.54 O
ATOM 1832 CB ARG A 261 6.617 -28.459 8.207 1.00 64.23 C
ATOM 1833 CG ARG A 261 7.930 -27.748 7.998 1.00 68.27 C
ATOM 1834 CD ARG A 261 8.670 -28.344 6.831 1.00 68.44 C
ATOM 1835 NE ARG A 261 9.037 -29.722 7.129 1.00 81.09 N
ATOM 1836 CZ ARG A 261 10.189 -30.284 6.785 1.00 81.14 C
ATOM 1837 NH1 ARG A 261 11.111 -29.600 6.111 1.00 78.83 N
ATOM 1838 NH2 ARG A 261 10.415 -31.540 7.119 1.00 82.33 N
ATOM 1839 N SER A 262 3.398 -28.248 8.931 1.00 70.16 N
ATOM 1840 CA SER A 262 2.039 -27.872 8.567 1.00 74.94 C
ATOM 1841 C SER A 262 1.497 -26.810 9.534 1.00 74.36 C
ATOM 1842 O SER A 262 0.806 -25.866 9.128 1.00 67.86 O
ATOM 1843 CB SER A 262 1.132 -29.106 8.594 1.00 70.03 C
ATOM 1844 OG SER A 262 1.149 -29.711 9.880 1.00 78.51 O
ATOM 1845 N GLU A 263 1.840 -26.973 10.810 1.00 69.42 N
ATOM 1846 CA GLU A 263 1.330 -26.139 11.897 1.00 69.12 C
ATOM 1847 C GLU A 263 2.484 -25.648 12.773 1.00 60.13 C
ATOM 1848 O GLU A 263 2.643 -26.102 13.919 1.00 55.98 O
ATOM 1849 CB GLU A 263 0.401 -26.985 12.756 1.00 71.85 C
ATOM 1850 CG GLU A 263 -0.979 -26.430 12.952 1.00 84.55 C
ATOM 1851 CD GLU A 263 -1.732 -27.211 14.004 1.00 91.05 C
ATOM 1852 OE1 GLU A 263 -1.780 -26.751 15.169 1.00 85.93 O
ATOM 1853 OE2 GLU A 263 -2.255 -28.297 13.670 1.00 95.14 O
ATOM 1854 N PRO A 264 3.304 -24.728 12.242 1.00 54.87 N
ATOM 1855 CA PRO A 264 4.569 -24.410 12.929 1.00 53.48 C
ATOM 1856 C PRO A 264 4.415 -23.516 14.178 1.00 45.70 C
ATOM 1857 O PRO A 264 5.284 -23.535 15.043 1.00 49.39 O
ATOM 1858 CB PRO A 264 5.400 -23.721 11.834 1.00 51.83 C
ATOM 1859 CG PRO A 264 4.365 -23.108 10.899 1.00 49.58 C
ATOM 1860 CD PRO A 264 3.083 -23.904 11.038 1.00 47.84 C
ATOM 1861 N LEU A 265 3.313 -22.776 14.271 1.00 45.33 N
ATOM 1862 CA LEU A 265 3.100 -21.805 15.332 1.00 37.27 C
ATOM 1863 C LEU A 265 2.089 -22.295 16.352 1.00 43.64 C
ATOM 1864 O LEU A 265 1.554 -21.509 17.139 1.00 56.47 O
ATOM 1865 CB LEU A 265 2.635 -20.474 14.742 1.00 39.12 C
ATOM 1866 CG LEU A 265 3.666 -19.759 13.873 1.00 39.75 C
ATOM 1867 CD1 LEU A 265 3.018 -18.681 13.051 1.00 33.18 C
ATOM 1868 CD2 LEU A 265 4.738 -19.162 14.740 1.00 35.34 C
ATOM 1869 N LYS A 266 1.851 -23.601 16.355 1.00 46.27 N
ATOM 1870 CA LYS A 266 0.946 -24.231 17.309 1.00 55.16 C
ATOM 1871 C LYS A 266 1.532 -24.291 18.709 1.00 57.37 C
ATOM 1872 O LYS A 266 2.727 -24.530 18.881 1.00 65.79 O
ATOM 1873 CB LYS A 266 0.633 -25.658 16.860 1.00 67.76 C
ATOM 1874 N PHE A 267 0.688 -24.099 19.717 1.00 64.69 N
ATOM 1875 CA PHE A 267 1.120 -24.308 21.094 1.00 70.95 C
ATOM 1876 C PHE A 267 0.290 -25.343 21.875 1.00 82.39 C
ATOM 1877 O PHE A 267 -0.881 -25.103 22.177 1.00 79.36 O
ATOM 1878 CB PHE A 267 1.171 -22.989 21.871 1.00 73.86 C
ATOM 1879 CG PHE A 267 1.569 -23.164 23.308 1.00 88.39 C
ATOM 1880 CD1 PHE A 267 2.808 -23.717 23.634 1.00 90.78 C
ATOM 1881 CD2 PHE A 267 0.704 -22.800 24.337 1.00 93.31 C
ATOM 1882 CE1 PHE A 267 3.189 -23.898 24.961 1.00 90.33 C
ATOM 1883 CE2 PHE A 267 1.072 -22.977 25.672 1.00 95.45 C
ATOM 1884 CZ PHE A 267 2.321 -23.527 25.984 1.00 97.34 C
ATOM 1885 N ASP A 268 0.928 -26.483 22.171 1.00 87.55 N
ATOM 1886 CA ASP A 268 0.494 -27.499 23.148 1.00 81.73 C
ATOM 1887 C ASP A 268 1.311 -28.777 22.936 1.00 79.08 C
ATOM 1888 O ASP A 268 1.665 -29.128 21.803 1.00 65.35 O
ATOM 1889 CB ASP A 268 -1.008 -27.819 23.080 1.00 70.34 C
ATOM 1890 N ALA A 284 13.838 -42.707 40.760 1.00 92.47 N
ATOM 1891 CA ALA A 284 14.992 -42.883 41.638 1.00 93.09 C
ATOM 1892 C ALA A 284 15.135 -44.334 42.103 1.00 82.78 C
ATOM 1893 O ALA A 284 14.533 -44.742 43.097 1.00 84.69 O
ATOM 1894 CB ALA A 284 14.912 -41.931 42.832 1.00 86.03 C
ATOM 1895 N ASN A 285 15.935 -45.104 41.369 1.00 81.19 N
ATOM 1896 CA ASN A 285 16.190 -46.508 41.692 1.00 75.33 C
ATOM 1897 C ASN A 285 17.619 -46.746 42.175 1.00 79.02 C
ATOM 1898 O ASN A 285 18.377 -45.791 42.396 1.00 75.98 O
ATOM 1899 CB ASN A 285 15.885 -47.410 40.490 1.00 66.54 C
ATOM 1900 CG ASN A 285 16.737 -47.081 39.269 1.00 77.41 C
ATOM 1901 OD1 ASN A 285 17.384 -46.035 39.202 1.00 76.26 O
ATOM 1902 ND2 ASN A 285 16.722 -47.973 38.287 1.00 80.25 N
ATOM 1903 N LYS A 286 17.978 -48.024 42.316 1.00 78.10 N
ATOM 1904 CA LYS A 286 19.269 -48.438 42.876 1.00 72.52 C
ATOM 1905 C LYS A 286 20.485 -47.940 42.094 1.00 70.92 C
ATOM 1906 O LYS A 286 21.588 -47.854 42.638 1.00 71.38 O
ATOM 1907 CB LYS A 286 19.333 -49.964 43.005 1.00 63.99 C
ATOM 1908 CG LYS A 286 19.182 -50.716 41.693 1.00 60.15 C
ATOM 1909 CD LYS A 286 19.407 -52.217 41.911 1.00 62.09 C
ATOM 1910 CE LYS A 286 19.748 -52.923 40.592 1.00 60.44 C
ATOM 1911 NZ LYS A 286 20.039 -54.377 40.766 1.00 50.32 N
ATOM 1912 N TYR A 287 20.275 -47.608 40.825 1.00 71.44 N
ATOM 1913 CA TYR A 287 21.361 -47.188 39.956 1.00 63.34 C
ATOM 1914 C TYR A 287 21.590 -45.695 40.012 1.00 59.24 C
ATOM 1915 O TYR A 287 22.670 -45.224 39.660 1.00 57.90 O
ATOM 1916 CB TYR A 287 21.043 -47.520 38.504 1.00 57.78 C
ATOM 1917 CG TYR A 287 20.890 -48.978 38.186 1.00 53.57 C
ATOM 1918 CD1 TYR A 287 21.995 -49.777 37.996 1.00 49.26 C
ATOM 1919 CD2 TYR A 287 19.634 -49.544 38.024 1.00 61.83 C
ATOM 1920 CE1 TYR A 287 21.859 -51.109 37.685 1.00 62.19 C
ATOM 1921 CE2 TYR A 287 19.485 -50.875 37.707 1.00 57.14 C
ATOM 1922 CZ TYR A 287 20.602 -51.654 37.535 1.00 60.52 C
ATOM 1923 OH TYR A 287 20.472 -52.987 37.219 1.00 59.97 O
ATOM 1924 N THR A 288 20.559 -44.958 40.416 1.00 63.83 N
ATOM 1925 CA THR A 288 20.507 -43.506 40.223 1.00 62.75 C
ATOM 1926 C THR A 288 21.758 -42.804 40.726 1.00 59.71 C
ATOM 1927 O THR A 288 22.213 -41.823 40.144 1.00 58.95 O
ATOM 1928 CB THR A 288 19.268 -42.881 40.917 1.00 72.58 C
ATOM 1929 OG1 THR A 288 18.093 -43.634 40.590 1.00 76.54 O
ATOM 1930 CG2 THR A 288 19.074 -41.438 40.484 1.00 57.35 C
ATOM 1931 N PHE A 289 22.331 -43.326 41.800 1.00 60.07 N
ATOM 1932 CA PHE A 289 23.479 -42.671 42.406 1.00 67.08 C
ATOM 1933 C PHE A 289 24.807 -43.400 42.124 1.00 64.61 C
ATOM 1934 O PHE A 289 25.884 -42.953 42.514 1.00 51.38 O
ATOM 1935 CB PHE A 289 23.198 -42.432 43.894 1.00 69.23 C
ATOM 1936 CG PHE A 289 21.910 -41.675 44.133 1.00 74.74 C
ATOM 1937 CD1 PHE A 289 21.834 -40.311 43.862 1.00 70.15 C
ATOM 1938 CD2 PHE A 289 20.767 -42.329 44.581 1.00 77.40 C
ATOM 1939 CE1 PHE A 289 20.656 -39.610 44.053 1.00 67.20 C
ATOM 1940 CE2 PHE A 289 19.576 -41.628 44.772 1.00 78.69 C
ATOM 1941 CZ PHE A 289 19.525 -40.267 44.510 1.00 74.40 C
ATOM 1942 N GLY A 290 24.721 -44.502 41.393 1.00 64.73 N
ATOM 1943 CA GLY A 290 25.909 -45.237 41.010 1.00 56.76 C
ATOM 1944 C GLY A 290 26.488 -44.775 39.684 1.00 51.51 C
ATOM 1945 O GLY A 290 25.955 -43.871 39.047 1.00 51.79 O
ATOM 1946 N PRO A 291 27.604 -45.392 39.275 1.00 50.70 N
ATOM 1947 CA PRO A 291 28.280 -45.102 38.003 1.00 41.28 C
ATOM 1948 C PRO A 291 27.383 -45.248 36.770 1.00 41.25 C
ATOM 1949 O PRO A 291 27.612 -44.524 35.797 1.00 39.09 O
ATOM 1950 CB PRO A 291 29.430 -46.117 37.975 1.00 45.16 C
ATOM 1951 CG PRO A 291 29.717 -46.387 39.452 1.00 40.31 C
ATOM 1952 CD PRO A 291 28.387 -46.301 40.145 1.00 38.33 C
ATOM 1953 N ILE A 292 26.392 -46.143 36.800 1.00 49.13 N
ATOM 1954 CA ILE A 292 25.445 -46.272 35.686 1.00 36.58 C
ATOM 1955 C ILE A 292 24.471 -45.085 35.659 1.00 47.44 C
ATOM 1956 O ILE A 292 24.064 -44.618 34.580 1.00 50.57 O
ATOM 1957 CB ILE A 292 24.636 -47.587 35.737 1.00 46.62 C
ATOM 1958 CG1 ILE A 292 25.555 -48.810 35.667 1.00 48.10 C
ATOM 1959 CG2 ILE A 292 23.627 -47.647 34.585 1.00 43.61 C
ATOM 1960 CD1 ILE A 292 24.811 -50.138 35.406 1.00 37.17 C
ATOM 1961 N GLY A 293 24.099 -44.604 36.845 1.00 42.17 N
ATOM 1962 CA GLY A 293 23.280 -43.413 36.974 1.00 39.11 C
ATOM 1963 C GLY A 293 23.990 -42.194 36.417 1.00 44.60 C
ATOM 1964 O GLY A 293 23.413 -41.412 35.668 1.00 55.33 O
ATOM 1965 N GLU A 294 25.255 -42.030 36.777 1.00 47.61 N
ATOM 1966 CA GLU A 294 26.046 -40.904 36.293 1.00 45.02 C
ATOM 1967 C GLU A 294 26.148 -40.961 34.770 1.00 46.27 C
ATOM 1968 O GLU A 294 26.051 -39.939 34.086 1.00 47.45 O
ATOM 1969 CB GLU A 294 27.441 -40.892 36.960 1.00 44.49 C
ATOM 1970 CG GLU A 294 27.587 -39.918 38.164 1.00 41.02 C
ATOM 1971 N LEU A 295 26.321 -42.170 34.242 1.00 49.38 N
ATOM 1972 CA LEU A 295 26.376 -42.389 32.793 1.00 49.83 C
ATOM 1973 C LEU A 295 25.065 -42.010 32.092 1.00 49.97 C
ATOM 1974 O LEU A 295 25.083 -41.337 31.062 1.00 52.60 O
ATOM 1975 CB LEU A 295 26.723 -43.851 32.486 1.00 40.26 C
ATOM 1976 CG LEU A 295 28.207 -44.174 32.348 1.00 46.08 C
ATOM 1977 CD1 LEU A 295 28.396 -45.651 32.097 1.00 45.84 C
ATOM 1978 CD2 LEU A 295 28.825 -43.354 31.229 1.00 48.08 C
ATOM 1979 N TRP A 296 23.938 -42.459 32.644 1.00 50.71 N
ATOM 1980 CA TRP A 296 22.624 -42.137 32.088 1.00 57.41 C
ATOM 1981 C TRP A 296 22.443 -40.629 32.028 1.00 55.11 C
ATOM 1982 O TRP A 296 22.157 -40.069 30.974 1.00 55.48 O
ATOM 1983 CB TRP A 296 21.503 -42.769 32.923 1.00 54.10 C
ATOM 1984 CG TRP A 296 20.117 -42.487 32.391 1.00 71.56 C
ATOM 1985 CD1 TRP A 296 19.428 -43.215 31.451 1.00 81.22 C
ATOM 1986 CD2 TRP A 296 19.255 -41.401 32.762 1.00 77.73 C
ATOM 1987 NE1 TRP A 296 18.199 -42.645 31.216 1.00 82.24 N
ATOM 1988 CE2 TRP A 296 18.066 -41.533 32.010 1.00 83.77 C
ATOM 1989 CE3 TRP A 296 19.374 -40.326 33.653 1.00 83.38 C
ATOM 1990 CZ2 TRP A 296 17.005 -40.632 32.122 1.00 91.95 C
ATOM 1991 CZ3 TRP A 296 18.319 -39.431 33.765 1.00 87.35 C
ATOM 1992 CH2 TRP A 296 17.150 -39.590 33.002 1.00 97.40 C
ATOM 1993 N TYR A 297 22.640 -39.984 33.171 1.00 52.51 N
ATOM 1994 CA TYR A 297 22.496 -38.540 33.303 1.00 62.88 C
ATOM 1995 C TYR A 297 23.382 -37.730 32.326 1.00 52.25 C
ATOM 1996 O TYR A 297 22.969 -36.687 31.844 1.00 53.59 O
ATOM 1997 CB TYR A 297 22.747 -38.147 34.768 1.00 69.44 C
ATOM 1998 CG TYR A 297 22.539 -36.684 35.095 1.00 81.17 C
ATOM 1999 CD1 TYR A 297 21.263 -36.186 35.357 1.00 81.50 C
ATOM 2000 CD2 TYR A 297 23.625 -35.800 35.167 1.00 78.40 C
ATOM 2001 CE1 TYR A 297 21.067 -34.844 35.666 1.00 78.89 C
ATOM 2002 CE2 TYR A 297 23.441 -34.454 35.475 1.00 73.22 C
ATOM 2003 CZ TYR A 297 22.160 -33.986 35.724 1.00 87.34 C
ATOM 2004 OH TYR A 297 21.961 -32.658 36.035 1.00 98.08 O
ATOM 2005 N ARG A 298 24.588 -38.213 32.034 1.00 54.08 N
ATOM 2006 CA ARG A 298 25.452 -37.606 31.008 1.00 54.67 C
ATOM 2007 C ARG A 298 24.891 -37.853 29.597 1.00 55.59 C
ATOM 2008 O ARG A 298 24.837 -36.940 28.756 1.00 48.50 O
ATOM 2009 CB ARG A 298 26.872 -38.190 31.098 1.00 59.29 C
ATOM 2010 CG ARG A 298 27.999 -37.196 31.392 1.00 70.94 C
ATOM 2011 N LYS A 299 24.484 -39.093 29.329 1.00 48.45 N
ATOM 2012 CA LYS A 299 23.937 -39.431 28.015 1.00 58.11 C
ATOM 2013 C LYS A 299 22.667 -38.597 27.802 1.00 60.36 C
ATOM 2014 O LYS A 299 22.623 -37.718 26.934 1.00 57.19 O
ATOM 2015 CB LYS A 299 23.652 -40.939 27.896 1.00 50.85 C
ATOM 2016 CG LYS A 299 23.236 -41.391 26.485 1.00 68.22 C
ATOM 2017 CD LYS A 299 22.150 -42.476 26.506 1.00 63.96 C
ATOM 2018 N SER A 300 21.659 -38.863 28.625 1.00 52.42 N
ATOM 2019 CA SER A 300 20.436 -38.084 28.642 1.00 49.83 C
ATOM 2020 C SER A 300 20.636 -36.551 28.516 1.00 51.42 C
ATOM 2021 O SER A 300 19.925 -35.885 27.771 1.00 53.98 O
ATOM 2022 CB SER A 300 19.642 -38.445 29.898 1.00 58.40 C
ATOM 2023 OG SER A 300 18.956 -37.322 30.413 1.00 64.72 O
ATOM 2024 N GLY A 301 21.612 -35.988 29.215 1.00 51.28 N
ATOM 2025 CA GLY A 301 21.786 -34.543 29.210 1.00 41.41 C
ATOM 2026 C GLY A 301 22.702 -33.991 28.132 1.00 44.51 C
ATOM 2027 O GLY A 301 22.942 -32.780 28.093 1.00 45.93 O
ATOM 2028 N THR A 302 23.233 -34.871 27.279 1.00 44.22 N
ATOM 2029 CA THR A 302 24.075 -34.464 26.141 1.00 47.99 C
ATOM 2030 C THR A 302 23.385 -34.710 24.787 1.00 47.11 C
ATOM 2031 O THR A 302 22.946 -35.821 24.505 1.00 46.18 O
ATOM 2032 CB THR A 302 25.400 -35.243 26.118 1.00 42.34 C
ATOM 2033 OG1 THR A 302 26.094 -35.037 27.344 1.00 39.51 O
ATOM 2034 CG2 THR A 302 26.275 -34.792 24.950 1.00 37.08 C
ATOM 2035 N TYR A 303 23.313 -33.684 23.946 1.00 49.18 N
ATOM 2036 CA TYR A 303 22.599 -33.779 22.676 1.00 51.90 C
ATOM 2037 C TYR A 303 22.813 -32.561 21.802 1.00 51.79 C
ATOM 2038 O TYR A 303 23.362 -31.556 22.239 1.00 52.36 O
ATOM 2039 CB TYR A 303 21.094 -34.008 22.876 1.00 44.04 C
ATOM 2040 CG TYR A 303 20.410 -33.019 23.795 1.00 48.99 C
ATOM 2041 CD1 TYR A 303 20.133 -31.729 23.376 1.00 42.43 C
ATOM 2042 CD2 TYR A 303 20.023 -33.384 25.082 1.00 48.81 C
ATOM 2043 CE1 TYR A 303 19.481 -30.827 24.204 1.00 41.55 C
ATOM 2044 CE2 TYR A 303 19.382 -32.483 25.922 1.00 50.38 C
ATOM 2045 CZ TYR A 303 19.116 -31.202 25.475 1.00 46.12 C
ATOM 2046 OH TYR A 303 18.481 -30.291 26.298 1.00 49.80 O
ATOM 2047 N ARG A 304 22.377 -32.672 20.554 1.00 49.74 N
ATOM 2048 CA ARG A 304 22.523 -31.597 19.585 1.00 49.79 C
ATOM 2049 C ARG A 304 21.256 -31.485 18.753 1.00 50.10 C
ATOM 2050 O ARG A 304 20.581 -32.488 18.497 1.00 48.95 O
ATOM 2051 CB ARG A 304 23.732 -31.849 18.690 1.00 43.95 C
ATOM 2052 CG ARG A 304 25.066 -31.691 19.400 1.00 45.23 C
ATOM 2053 CD ARG A 304 25.214 -30.250 19.833 1.00 55.47 C
ATOM 2054 NE ARG A 304 26.538 -29.932 20.347 1.00 58.38 N
ATOM 2055 CZ ARG A 304 26.876 -30.035 21.626 1.00 53.73 C
ATOM 2056 NH1 ARG A 304 25.984 -30.462 22.511 1.00 51.08 N
ATOM 2057 NH2 ARG A 304 28.103 -29.720 22.012 1.00 46.43 N
ATOM 2058 N GLY A 305 20.933 -30.258 18.352 1.00 50.81 N
ATOM 2059 CA GLY A 305 19.783 -29.980 17.510 1.00 41.26 C
ATOM 2060 C GLY A 305 18.466 -30.642 17.897 1.00 46.05 C
ATOM 2061 O GLY A 305 17.668 -30.988 17.031 1.00 50.15 O
ATOM 2062 N LYS A 306 18.220 -30.847 19.185 1.00 46.53 N
ATOM 2063 CA LYS A 306 16.941 -31.422 19.573 1.00 43.14 C
ATOM 2064 C LYS A 306 15.831 -30.385 19.444 1.00 51.99 C
ATOM 2065 O LYS A 306 15.938 -29.270 19.966 1.00 52.51 O
ATOM 2066 CB LYS A 306 16.986 -31.993 20.983 1.00 41.73 C
ATOM 2067 CG LYS A 306 15.641 -32.534 21.452 1.00 47.81 C
ATOM 2068 CD LYS A 306 15.537 -32.586 22.990 1.00 52.68 C
ATOM 2069 CE LYS A 306 15.965 -33.931 23.564 1.00 48.54 C
ATOM 2070 NZ LYS A 306 15.828 -33.961 25.047 1.00 57.21 N
ATOM 2071 N VAL A 307 14.767 -30.733 18.728 1.00 55.01 N
ATOM 2072 CA VAL A 307 13.647 -29.808 18.633 1.00 45.60 C
ATOM 2073 C VAL A 307 12.679 -29.995 19.798 1.00 49.20 C
ATOM 2074 O VAL A 307 12.257 -31.109 20.129 1.00 49.81 O
ATOM 2075 CB VAL A 307 12.944 -29.766 17.232 1.00 51.27 C
ATOM 2076 CG1 VAL A 307 13.756 -30.512 16.171 1.00 53.61 C
ATOM 2077 CG2 VAL A 307 11.502 -30.253 17.309 1.00 48.22 C
ATOM 2078 N GLN A 308 12.372 -28.882 20.452 1.00 47.38 N
ATOM 2079 CA GLN A 308 11.481 -28.893 21.605 1.00 54.16 C
ATOM 2080 C GLN A 308 10.529 -27.708 21.522 1.00 52.11 C
ATOM 2081 O GLN A 308 10.921 -26.617 21.086 1.00 49.12 O
ATOM 2082 CB GLN A 308 12.277 -28.795 22.927 1.00 57.20 C
ATOM 2083 CG GLN A 308 13.512 -29.672 23.005 1.00 49.54 C
ATOM 2084 CD GLN A 308 14.272 -29.501 24.304 1.00 63.89 C
ATOM 2085 OE1 GLN A 308 15.020 -28.536 24.475 1.00 67.41 O
ATOM 2086 NE2 GLN A 308 14.084 -30.440 25.235 1.00 59.06 N
ATOM 2087 N ASN A 309 9.286 -27.923 21.948 1.00 57.56 N
ATOM 2088 CA ASN A 309 8.332 -26.838 22.079 1.00 57.00 C
ATOM 2089 C ASN A 309 8.695 -26.050 23.325 1.00 61.61 C
ATOM 2090 O ASN A 309 9.712 -26.324 23.958 1.00 64.62 O
ATOM 2091 CB ASN A 309 6.892 -27.367 22.160 1.00 52.69 C
ATOM 2092 CG ASN A 309 6.659 -28.279 23.368 1.00 70.57 C
ATOM 2093 OD1 ASN A 309 6.733 -27.844 24.528 1.00 74.38 O
ATOM 2094 ND2 ASN A 309 6.350 -29.543 23.099 1.00 68.35 N
ATOM 2095 N LEU A 310 7.857 -25.089 23.690 1.00 64.45 N
ATOM 2096 CA LEU A 310 8.157 -24.207 24.804 1.00 61.70 C
ATOM 2097 C LEU A 310 8.227 -24.961 26.131 1.00 67.23 C
ATOM 2098 O LEU A 310 9.179 -24.780 26.904 1.00 69.25 O
ATOM 2099 CB LEU A 310 7.140 -23.061 24.861 1.00 66.15 C
ATOM 2100 CG LEU A 310 7.433 -21.915 25.837 1.00 61.17 C
ATOM 2101 CD1 LEU A 310 8.907 -21.554 25.864 1.00 60.79 C
ATOM 2102 CD2 LEU A 310 6.634 -20.706 25.455 1.00 65.22 C
ATOM 2103 N THR A 311 7.236 -25.816 26.380 1.00 72.94 N
ATOM 2104 CA THR A 311 7.174 -26.595 27.626 1.00 70.20 C
ATOM 2105 C THR A 311 8.406 -27.476 27.869 1.00 69.27 C
ATOM 2106 O THR A 311 8.961 -27.492 28.976 1.00 67.96 O
ATOM 2107 CB THR A 311 5.930 -27.493 27.677 1.00 74.53 C
ATOM 2108 OG1 THR A 311 4.769 -26.743 27.286 1.00 82.62 O
ATOM 2109 CG2 THR A 311 5.751 -28.030 29.083 1.00 60.75 C
ATOM 2110 N GLN A 312 8.826 -28.201 26.833 1.00 66.77 N
ATOM 2111 CA GLN A 312 9.992 -29.084 26.922 1.00 67.87 C
ATOM 2112 C GLN A 312 11.282 -28.323 27.229 1.00 64.99 C
ATOM 2113 O GLN A 312 12.102 -28.767 28.032 1.00 66.19 O
ATOM 2114 CB GLN A 312 10.159 -29.895 25.627 1.00 60.36 C
ATOM 2115 CG GLN A 312 8.964 -30.772 25.299 1.00 68.51 C
ATOM 2116 CD GLN A 312 9.022 -31.349 23.894 1.00 77.64 C
ATOM 2117 OE1 GLN A 312 9.006 -30.617 22.899 1.00 71.85 O
ATOM 2118 NE2 GLN A 312 9.085 -32.672 23.806 1.00 83.89 N
ATOM 2119 N PHE A 313 11.442 -27.172 26.591 1.00 63.35 N
ATOM 2120 CA PHE A 313 12.676 -26.411 26.652 1.00 54.25 C
ATOM 2121 C PHE A 313 12.716 -25.516 27.881 1.00 61.22 C
ATOM 2122 O PHE A 313 13.775 -25.000 28.236 1.00 61.08 O
ATOM 2123 CB PHE A 313 12.778 -25.591 25.382 1.00 50.10 C
ATOM 2124 CG PHE A 313 14.008 -24.735 25.272 1.00 44.84 C
ATOM 2125 CD1 PHE A 313 15.214 -25.271 24.874 1.00 41.79 C
ATOM 2126 CD2 PHE A 313 13.930 -23.367 25.484 1.00 46.25 C
ATOM 2127 CE1 PHE A 313 16.331 -24.461 24.716 1.00 44.83 C
ATOM 2128 CE2 PHE A 313 15.029 -22.562 25.323 1.00 41.98 C
ATOM 2129 CZ PHE A 313 16.235 -23.105 24.939 1.00 43.78 C
ATOM 2130 N TYR A 314 11.567 -25.345 28.536 1.00 71.66 N
ATOM 2131 CA TYR A 314 11.500 -24.561 29.780 1.00 82.47 C
ATOM 2132 C TYR A 314 11.219 -25.384 31.067 1.00 92.25 C
ATOM 2133 O TYR A 314 11.332 -24.850 32.176 1.00101.78 O
ATOM 2134 CB TYR A 314 10.485 -23.421 29.645 1.00 71.63 C
ATOM 2135 CG TYR A 314 11.081 -22.073 29.266 1.00 76.04 C
ATOM 2136 CD1 TYR A 314 11.201 -21.056 30.213 1.00 66.28 C
ATOM 2137 CD2 TYR A 314 11.508 -21.809 27.962 1.00 67.17 C
ATOM 2138 CE1 TYR A 314 11.735 -19.807 29.876 1.00 65.63 C
ATOM 2139 CE2 TYR A 314 12.039 -20.563 27.611 1.00 59.18 C
ATOM 2140 CZ TYR A 314 12.153 -19.564 28.573 1.00 65.03 C
ATOM 2141 OH TYR A 314 12.693 -18.327 28.248 1.00 48.99 O
ATOM 2142 N HIS A 315 10.831 -26.655 30.898 1.00 98.95 N
ATOM 2143 CA HIS A 315 10.500 -27.602 31.991 1.00 98.16 C
ATOM 2144 C HIS A 315 9.858 -27.008 33.255 1.00107.72 C
ATOM 2145 O HIS A 315 9.518 -27.733 34.198 1.00114.50 O
ATOM 2146 CB HIS A 315 11.719 -28.462 32.363 1.00 92.14 C
ATOM 2147 N GLY A 331 7.701 -22.323 53.575 1.00 48.18 N
ATOM 2148 CA GLY A 331 8.282 -23.599 53.199 1.00 60.11 C
ATOM 2149 C GLY A 331 9.747 -23.490 52.805 1.00 66.46 C
ATOM 2150 O GLY A 331 10.613 -24.174 53.356 1.00 61.29 O
ATOM 2151 N PHE A 332 10.014 -22.618 51.841 1.00 65.36 N
ATOM 2152 CA PHE A 332 11.344 -22.427 51.278 1.00 57.27 C
ATOM 2153 C PHE A 332 11.701 -20.957 51.216 1.00 59.41 C
ATOM 2154 O PHE A 332 10.834 -20.083 51.246 1.00 55.82 O
ATOM 2155 CB PHE A 332 11.422 -22.980 49.860 1.00 58.50 C
ATOM 2156 CG PHE A 332 11.625 -24.458 49.793 1.00 65.28 C
ATOM 2157 CD1 PHE A 332 12.844 -24.982 49.390 1.00 60.20 C
ATOM 2158 CD2 PHE A 332 10.598 -25.329 50.125 1.00 65.96 C
ATOM 2159 CE1 PHE A 332 13.036 -26.356 49.316 1.00 61.27 C
ATOM 2160 CE2 PHE A 332 10.785 -26.696 50.061 1.00 51.00 C
ATOM 2161 CZ PHE A 332 12.002 -27.210 49.654 1.00 53.03 C
ATOM 2162 N LEU A 333 12.994 -20.685 51.121 1.00 61.15 N
ATOM 2163 CA LEU A 333 13.454 -19.325 50.934 1.00 51.14 C
ATOM 2164 C LEU A 333 14.187 -19.274 49.620 1.00 53.85 C
ATOM 2165 O LEU A 333 15.218 -19.908 49.430 1.00 52.08 O
ATOM 2166 CB LEU A 333 14.349 -18.833 52.078 1.00 50.44 C
ATOM 2167 CG LEU A 333 14.550 -17.311 52.063 1.00 50.39 C
ATOM 2168 CD1 LEU A 333 13.199 -16.606 52.238 1.00 63.68 C
ATOM 2169 CD2 LEU A 333 15.530 -16.822 53.116 1.00 48.11 C
ATOM 2170 N GLN A 334 13.616 -18.512 48.707 1.00 52.48 N
ATOM 2171 CA GLN A 334 14.128 -18.349 47.372 1.00 52.20 C
ATOM 2172 C GLN A 334 15.123 -17.202 47.419 1.00 53.05 C
ATOM 2173 O GLN A 334 14.802 -16.101 47.870 1.00 51.30 O
ATOM 2174 CB GLN A 334 12.958 -18.050 46.446 1.00 56.15 C
ATOM 2175 CG GLN A 334 11.899 -17.123 47.090 1.00 68.94 C
ATOM 2176 CD GLN A 334 10.986 -17.772 48.182 1.00 67.83 C
ATOM 2177 OE1 GLN A 334 10.633 -18.974 48.130 1.00 62.68 O
ATOM 2178 NE2 GLN A 334 10.602 -16.952 49.169 1.00 48.43 N
ATOM 2179 N TYR A 335 16.343 -17.480 46.986 1.00 48.67 N
ATOM 2180 CA TYR A 335 17.420 -16.521 47.092 1.00 47.07 C
ATOM 2181 C TYR A 335 18.096 -16.425 45.745 1.00 44.82 C
ATOM 2182 O TYR A 335 18.535 -17.431 45.198 1.00 43.32 O
ATOM 2183 CB TYR A 335 18.432 -16.991 48.138 1.00 37.45 C
ATOM 2184 CG TYR A 335 19.481 -15.962 48.485 1.00 33.53 C
ATOM 2185 CD1 TYR A 335 19.163 -14.877 49.289 1.00 39.24 C
ATOM 2186 CD2 TYR A 335 20.793 -16.080 48.030 1.00 32.55 C
ATOM 2187 CE1 TYR A 335 20.116 -13.920 49.632 1.00 43.16 C
ATOM 2188 CE2 TYR A 335 21.753 -15.138 48.379 1.00 39.22 C
ATOM 2189 CZ TYR A 335 21.399 -14.059 49.184 1.00 38.28 C
ATOM 2190 OH TYR A 335 22.304 -13.092 49.525 1.00 33.74 O
ATOM 2191 N GLN A 336 18.186 -15.214 45.210 1.00 43.18 N
ATOM 2192 CA GLN A 336 18.789 -15.001 43.898 1.00 40.20 C
ATOM 2193 C GLN A 336 19.743 -13.800 43.935 1.00 39.61 C
ATOM 2194 O GLN A 336 19.408 -12.746 44.479 1.00 40.23 O
ATOM 2195 CB GLN A 336 17.699 -14.816 42.813 1.00 27.52 C
ATOM 2196 CG GLN A 336 18.262 -14.520 41.398 1.00 34.66 C
ATOM 2197 CD GLN A 336 17.189 -14.353 40.302 1.00 35.26 C
ATOM 2198 OE1 GLN A 336 15.997 -14.463 40.559 1.00 37.06 O
ATOM 2199 NE2 GLN A 336 17.628 -14.071 39.078 1.00 31.91 N
ATOM 2200 N PHE A 337 20.931 -13.967 43.361 1.00 31.21 N
ATOM 2201 CA PHE A 337 21.898 -12.886 43.274 1.00 33.31 C
ATOM 2202 C PHE A 337 22.650 -13.005 41.975 1.00 32.64 C
ATOM 2203 O PHE A 337 22.575 -14.037 41.319 1.00 34.80 O
ATOM 2204 CB PHE A 337 22.905 -12.932 44.433 1.00 33.08 C
ATOM 2205 CG PHE A 337 23.717 -14.214 44.501 1.00 30.69 C
ATOM 2206 CD1 PHE A 337 24.915 -14.340 43.807 1.00 28.26 C
ATOM 2207 CD2 PHE A 337 23.287 -15.282 45.280 1.00 29.01 C
ATOM 2208 CE1 PHE A 337 25.663 -15.518 43.874 1.00 29.05 C
ATOM 2209 CE2 PHE A 337 24.030 -16.462 45.346 1.00 33.32 C
ATOM 2210 CZ PHE A 337 25.221 -16.573 44.650 1.00 26.62 C
ATOM 2211 N VAL A 338 23.376 -11.946 41.614 1.00 30.90 N
ATOM 2212 CA VAL A 338 24.286 -11.961 40.475 1.00 30.76 C
ATOM 2213 C VAL A 338 25.602 -11.330 40.896 1.00 34.07 C
ATOM 2214 O VAL A 338 25.608 -10.367 41.653 1.00 33.84 O
ATOM 2215 CB VAL A 338 23.718 -11.210 39.243 1.00 29.11 C
ATOM 2216 CG1 VAL A 338 23.262 -9.817 39.614 1.00 27.16 C
ATOM 2217 CG2 VAL A 338 24.746 -11.143 38.124 1.00 24.48 C
ATOM 2218 N ILE A 339 26.707 -11.902 40.423 1.00 34.91 N
ATOM 2219 CA ILE A 339 28.047 -11.442 40.743 1.00 35.36 C
ATOM 2220 C ILE A 339 28.693 -10.976 39.455 1.00 38.93 C
ATOM 2221 O ILE A 339 28.624 -11.680 38.448 1.00 43.76 O
ATOM 2222 CB ILE A 339 28.868 -12.599 41.305 1.00 38.24 C
ATOM 2223 CG1 ILE A 339 28.251 -13.101 42.618 1.00 34.50 C
ATOM 2224 CG2 ILE A 339 30.309 -12.177 41.510 1.00 43.35 C
ATOM 2225 CD1 ILE A 339 28.367 -12.119 43.750 1.00 27.51 C
ATOM 2226 N PRO A 340 29.302 -9.784 39.460 1.00 36.91 N
ATOM 2227 CA PRO A 340 29.833 -9.266 38.197 1.00 37.90 C
ATOM 2228 C PRO A 340 30.769 -10.262 37.525 1.00 42.52 C
ATOM 2229 O PRO A 340 31.452 -11.030 38.210 1.00 47.55 O
ATOM 2230 CB PRO A 340 30.560 -7.977 38.613 1.00 36.06 C
ATOM 2231 CG PRO A 340 30.562 -7.971 40.080 1.00 37.99 C
ATOM 2232 CD PRO A 340 29.416 -8.796 40.536 1.00 35.97 C
ATOM 2233 N THR A 341 30.752 -10.265 36.199 1.00 40.87 N
ATOM 2234 CA THR A 341 31.473 -11.236 35.375 1.00 45.13 C
ATOM 2235 C THR A 341 32.919 -11.456 35.780 1.00 47.65 C
ATOM 2236 O THR A 341 33.346 -12.597 35.929 1.00 48.11 O
ATOM 2237 CB THR A 341 31.466 -10.786 33.894 1.00 50.61 C
ATOM 2238 OG1 THR A 341 30.209 -10.183 33.589 1.00 47.84 O
ATOM 2239 CG2 THR A 341 31.692 -11.954 32.956 1.00 34.89 C
ATOM 2240 N GLU A 342 33.660 -10.360 35.945 1.00 48.72 N
ATOM 2241 CA GLU A 342 35.089 -10.409 36.273 1.00 51.23 C
ATOM 2242 C GLU A 342 35.385 -11.043 37.631 1.00 50.12 C
ATOM 2243 O GLU A 342 36.414 -11.695 37.798 1.00 54.25 O
ATOM 2244 CB GLU A 342 35.723 -9.010 36.198 1.00 47.84 C
ATOM 2245 CG GLU A 342 35.117 -7.971 37.154 1.00 46.33 C
ATOM 2246 CD GLU A 342 33.913 -7.240 36.565 1.00 51.12 C
ATOM 2247 OE1 GLU A 342 33.248 -7.808 35.665 1.00 49.76 O
ATOM 2248 OE2 GLU A 342 33.637 -6.094 36.996 1.00 40.25 O
ATOM 2249 N ALA A 343 34.490 -10.866 38.598 1.00 48.26 N
ATOM 2250 CA ALA A 343 34.701 -11.431 39.939 1.00 44.71 C
ATOM 2251 C ALA A 343 34.370 -12.916 39.972 1.00 41.69 C
ATOM 2252 O ALA A 343 33.605 -13.378 40.825 1.00 42.61 O
ATOM 2253 CB ALA A 343 33.879 -10.682 40.976 1.00 40.04 C
ATOM 2254 N VAL A 344 34.955 -13.662 39.044 1.00 42.23 N
ATOM 2255 CA VAL A 344 34.640 -15.078 38.905 1.00 49.21 C
ATOM 2256 C VAL A 344 35.102 -15.897 40.109 1.00 47.41 C
ATOM 2257 O VAL A 344 34.356 -16.746 40.606 1.00 46.89 O
ATOM 2258 CB VAL A 344 35.167 -15.651 37.555 1.00 50.84 C
ATOM 2259 CG1 VAL A 344 36.557 -15.130 37.249 1.00 45.94 C
ATOM 2260 CG2 VAL A 344 35.101 -17.189 37.525 1.00 47.07 C
ATOM 2261 N ASP A 345 36.308 -15.624 40.602 1.00 51.05 N
ATOM 2262 CA ASP A 345 36.809 -16.360 41.762 1.00 52.64 C
ATOM 2263 C ASP A 345 35.945 -16.163 43.017 1.00 53.82 C
ATOM 2264 O ASP A 345 35.797 -17.060 43.858 1.00 52.10 O
ATOM 2265 CB ASP A 345 38.265 -16.004 42.037 1.00 63.81 C
ATOM 2266 CG ASP A 345 39.217 -16.729 41.111 1.00 69.84 C
ATOM 2267 OD1 ASP A 345 38.903 -17.883 40.739 1.00 66.47 O
ATOM 2268 OD2 ASP A 345 40.268 -16.150 40.753 1.00 65.50 O
ATOM 2269 N GLU A 346 35.354 -14.984 43.115 1.00 52.55 N
ATOM 2270 CA GLU A 346 34.473 -14.648 44.213 1.00 50.17 C
ATOM 2271 C GLU A 346 33.175 -15.422 44.074 1.00 53.23 C
ATOM 2272 O GLU A 346 32.612 -15.918 45.066 1.00 49.09 O
ATOM 2273 CB GLU A 346 34.211 -13.154 44.162 1.00 40.33 C
ATOM 2274 CG GLU A 346 35.455 -12.312 44.414 1.00 50.78 C
ATOM 2275 CD GLU A 346 36.453 -12.282 43.264 1.00 50.99 C
ATOM 2276 OE1 GLU A 346 36.353 -13.117 42.334 1.00 51.35 O
ATOM 2277 OE2 GLU A 346 37.358 -11.416 43.301 1.00 56.86 O
ATOM 2278 N PHE A 347 32.704 -15.527 42.833 1.00 48.12 N
ATOM 2279 CA PHE A 347 31.523 -16.324 42.553 1.00 46.83 C
ATOM 2280 C PHE A 347 31.733 -17.770 42.989 1.00 37.76 C
ATOM 2281 O PHE A 347 30.879 -18.350 43.649 1.00 37.95 O
ATOM 2282 CB PHE A 347 31.134 -16.242 41.070 1.00 49.73 C
ATOM 2283 CG PHE A 347 30.019 -17.178 40.689 1.00 34.60 C
ATOM 2284 CD1 PHE A 347 28.762 -17.029 41.234 1.00 34.68 C
ATOM 2285 CD2 PHE A 347 30.236 -18.199 39.790 1.00 37.60 C
ATOM 2286 CE1 PHE A 347 27.744 -17.886 40.898 1.00 44.22 C
ATOM 2287 CE2 PHE A 347 29.221 -19.057 39.444 1.00 43.90 C
ATOM 2288 CZ PHE A 347 27.973 -18.906 40.003 1.00 41.19 C
ATOM 2289 N LYS A 348 32.874 -18.347 42.632 1.00 41.84 N
ATOM 2290 CA LYS A 348 33.196 -19.707 43.056 1.00 44.65 C
ATOM 2291 C LYS A 348 33.170 -19.830 44.580 1.00 48.04 C
ATOM 2292 O LYS A 348 32.609 -20.785 45.137 1.00 46.96 O
ATOM 2293 CB LYS A 348 34.572 -20.127 42.517 1.00 49.80 C
ATOM 2294 CG LYS A 348 34.623 -20.368 41.007 1.00 51.23 C
ATOM 2295 CD LYS A 348 35.998 -20.844 40.535 1.00 52.87 C
ATOM 2296 CE LYS A 348 36.134 -20.644 39.022 1.00 62.51 C
ATOM 2297 NZ LYS A 348 37.305 -21.341 38.392 1.00 61.90 N
ATOM 2298 N LYS A 349 33.777 -18.850 45.246 1.00 41.30 N
ATOM 2299 CA LYS A 349 33.839 -18.813 46.698 1.00 44.66 C
ATOM 2300 C LYS A 349 32.452 -18.888 47.342 1.00 47.65 C
ATOM 2301 O LYS A 349 32.227 -19.675 48.282 1.00 47.87 O
ATOM 2302 CB LYS A 349 34.559 -17.528 47.132 1.00 54.27 C
ATOM 2303 CG LYS A 349 34.764 -17.357 48.629 1.00 42.26 C
ATOM 2304 CD LYS A 349 35.694 -18.431 49.171 1.00 64.94 C
ATOM 2305 CE LYS A 349 36.335 -18.022 50.507 1.00 58.16 C
ATOM 2306 NZ LYS A 349 35.380 -18.104 51.641 1.00 55.78 N
ATOM 2307 N ILE A 350 31.528 -18.065 46.841 1.00 38.71 N
ATOM 2308 CA ILE A 350 30.157 -18.054 47.351 1.00 42.72 C
ATOM 2309 C ILE A 350 29.459 -19.401 47.194 1.00 43.79 C
ATOM 2310 O ILE A 350 28.748 -19.853 48.095 1.00 47.83 O
ATOM 2311 CB ILE A 350 29.290 -16.974 46.688 1.00 43.89 C
ATOM 2312 CG1 ILE A 350 29.788 -15.582 47.066 1.00 54.83 C
ATOM 2313 CG2 ILE A 350 27.856 -17.093 47.155 1.00 39.59 C
ATOM 2314 CD1 ILE A 350 28.907 -14.463 46.527 1.00 42.67 C
ATOM 2315 N ILE A 351 29.674 -20.050 46.059 1.00 40.05 N
ATOM 2316 CA ILE A 351 29.107 -21.374 45.843 1.00 44.72 C
ATOM 2317 C ILE A 351 29.643 -22.358 46.875 1.00 42.65 C
ATOM 2318 O ILE A 351 28.876 -23.093 47.498 1.00 42.37 O
ATOM 2319 CB ILE A 351 29.351 -21.880 44.398 1.00 46.34 C
ATOM 2320 CG1 ILE A 351 28.749 -20.903 43.396 1.00 43.89 C
ATOM 2321 CG2 ILE A 351 28.725 -23.236 44.195 1.00 38.73 C
ATOM 2322 CD1 ILE A 351 27.281 -20.634 43.646 1.00 38.32 C
ATOM 2323 N GLY A 352 30.959 -22.352 47.067 1.00 43.81 N
ATOM 2324 CA GLY A 352 31.575 -23.142 48.124 1.00 46.51 C
ATOM 2325 C GLY A 352 31.004 -22.887 49.523 1.00 45.38 C
ATOM 2326 O GLY A 352 30.762 -23.822 50.310 1.00 43.80 O
ATOM 2327 N VAL A 353 30.773 -21.620 49.841 1.00 39.76 N
ATOM 2328 CA VAL A 353 30.166 -21.279 51.124 1.00 43.54 C
ATOM 2329 C VAL A 353 28.791 -21.902 51.237 1.00 49.59 C
ATOM 2330 O VAL A 353 28.447 -22.477 52.265 1.00 49.84 O
ATOM 2331 CB VAL A 353 30.033 -19.748 51.313 1.00 50.51 C
ATOM 2332 CG1 VAL A 353 29.045 -19.431 52.418 1.00 45.09 C
ATOM 2333 CG2 VAL A 353 31.398 -19.101 51.598 1.00 39.07 C
ATOM 2334 N ILE A 354 28.008 -21.792 50.162 1.00 56.40 N
ATOM 2335 CA ILE A 354 26.666 -22.368 50.121 1.00 47.52 C
ATOM 2336 C ILE A 354 26.623 -23.867 50.402 1.00 46.88 C
ATOM 2337 O ILE A 354 25.883 -24.294 51.283 1.00 48.93 O
ATOM 2338 CB ILE A 354 25.925 -22.016 48.821 1.00 44.39 C
ATOM 2339 CG1 ILE A 354 25.250 -20.655 48.978 1.00 44.60 C
ATOM 2340 CG2 ILE A 354 24.857 -23.053 48.487 1.00 37.60 C
ATOM 2341 CD1 ILE A 354 24.959 -19.965 47.669 1.00 37.96 C
ATOM 2342 N GLN A 355 27.412 -24.672 49.693 1.00 49.59 N
ATOM 2343 CA GLN A 355 27.293 -26.126 49.888 1.00 60.36 C
ATOM 2344 C GLN A 355 27.774 -26.585 51.273 1.00 56.13 C
ATOM 2345 O GLN A 355 27.177 -27.476 51.883 1.00 53.94 O
ATOM 2346 CB GLN A 355 27.887 -26.953 48.724 1.00 53.06 C
ATOM 2347 CG GLN A 355 29.389 -27.126 48.692 1.00 56.79 C
ATOM 2348 CD GLN A 355 29.942 -28.027 49.806 1.00 64.36 C
ATOM 2349 OE1 GLN A 355 30.955 -27.684 50.418 1.00 59.35 O
ATOM 2350 NE2 GLN A 355 29.276 -29.169 50.076 1.00 45.95 N
ATOM 2351 N ALA A 356 28.825 -25.938 51.767 1.00 54.95 N
ATOM 2352 CA ALA A 356 29.380 -26.233 53.094 1.00 62.48 C
ATOM 2353 C ALA A 356 28.540 -25.680 54.251 1.00 62.71 C
ATOM 2354 O ALA A 356 28.814 -25.971 55.417 1.00 63.95 O
ATOM 2355 CB ALA A 356 30.821 -25.704 53.200 1.00 56.75 C
ATOM 2356 N SER A 357 27.523 -24.890 53.930 1.00 56.77 N
ATOM 2357 CA SER A 357 26.682 -24.273 54.947 1.00 52.68 C
ATOM 2358 C SER A 357 25.726 -25.241 55.622 1.00 59.51 C
ATOM 2359 O SER A 357 25.106 -24.886 56.618 1.00 54.98 O
ATOM 2360 CB SER A 357 25.845 -23.157 54.331 1.00 61.96 C
ATOM 2361 OG SER A 357 24.796 -23.681 53.517 1.00 59.23 O
ATOM 2362 N GLY A 358 25.566 -26.438 55.064 1.00 61.99 N
ATOM 2363 CA GLY A 358 24.610 -27.391 55.600 1.00 63.28 C
ATOM 2364 C GLY A 358 23.177 -27.106 55.175 1.00 71.25 C
ATOM 2365 O GLY A 358 22.238 -27.781 55.607 1.00 69.48 O
ATOM 2366 N HIS A 359 23.005 -26.089 54.339 1.00 64.63 N
ATOM 2367 CA HIS A 359 21.702 -25.782 53.777 1.00 65.44 C
ATOM 2368 C HIS A 359 21.678 -26.307 52.351 1.00 58.64 C
ATOM 2369 O HIS A 359 22.447 -25.853 51.507 1.00 54.96 O
ATOM 2370 CB HIS A 359 21.450 -24.276 53.802 1.00 57.40 C
ATOM 2371 CG HIS A 359 21.347 -23.703 55.180 1.00 45.55 C
ATOM 2372 ND1 HIS A 359 20.208 -23.814 55.944 1.00 43.07 N
ATOM 2373 CD2 HIS A 359 22.235 -23.001 55.926 1.00 46.38 C
ATOM 2374 CE1 HIS A 359 20.398 -23.205 57.104 1.00 46.25 C
ATOM 2375 NE2 HIS A 359 21.621 -22.702 57.116 1.00 36.35 N
ATOM 2376 N TYR A 360 20.804 -27.274 52.096 1.00 61.06 N
ATOM 2377 CA TYR A 360 20.819 -27.990 50.827 1.00 67.75 C
ATOM 2378 C TYR A 360 19.766 -27.470 49.845 1.00 63.83 C
ATOM 2379 O TYR A 360 18.589 -27.321 50.187 1.00 55.27 O
ATOM 2380 CB TYR A 360 20.691 -29.490 51.096 1.00 65.25 C
ATOM 2381 CG TYR A 360 21.564 -29.905 52.257 1.00 68.98 C
ATOM 2382 CD1 TYR A 360 22.955 -29.924 52.140 1.00 66.70 C
ATOM 2383 CD2 TYR A 360 21.002 -30.231 53.486 1.00 73.84 C
ATOM 2384 CE1 TYR A 360 23.762 -30.278 53.213 1.00 73.93 C
ATOM 2385 CE2 TYR A 360 21.795 -30.590 54.569 1.00 70.92 C
ATOM 2386 CZ TYR A 360 23.176 -30.611 54.434 1.00 84.26 C
ATOM 2387 OH TYR A 360 23.960 -30.966 55.527 1.00 66.67 O
ATOM 2388 N SER A 361 20.211 -27.156 48.633 1.00 60.76 N
ATOM 2389 CA SER A 361 19.310 -26.679 47.587 1.00 60.94 C
ATOM 2390 C SER A 361 19.359 -27.591 46.355 1.00 57.70 C
ATOM 2391 O SER A 361 20.420 -27.783 45.746 1.00 55.06 O
ATOM 2392 CB SER A 361 19.670 -25.241 47.220 1.00 55.40 C
ATOM 2393 OG SER A 361 18.856 -24.754 46.174 1.00 59.08 O
ATOM 2394 N PHE A 362 18.216 -28.168 45.996 1.00 59.87 N
ATOM 2395 CA PHE A 362 18.173 -29.077 44.847 1.00 68.83 C
ATOM 2396 C PHE A 362 17.845 -28.330 43.542 1.00 68.53 C
ATOM 2397 O PHE A 362 18.440 -28.597 42.489 1.00 66.51 O
ATOM 2398 CB PHE A 362 17.213 -30.251 45.098 1.00 54.63 C
ATOM 2399 N LEU A 363 16.923 -27.373 43.620 1.00 63.51 N
ATOM 2400 CA LEU A 363 16.533 -26.590 42.447 1.00 62.50 C
ATOM 2401 C LEU A 363 17.397 -25.345 42.275 1.00 60.13 C
ATOM 2402 O LEU A 363 17.113 -24.313 42.877 1.00 64.95 O
ATOM 2403 CB LEU A 363 15.064 -26.179 42.550 1.00 60.22 C
ATOM 2404 CG LEU A 363 14.070 -27.343 42.575 1.00 79.26 C
ATOM 2405 CD1 LEU A 363 12.654 -26.831 42.820 1.00 82.42 C
ATOM 2406 CD2 LEU A 363 14.147 -28.158 41.282 1.00 73.26 C
ATOM 2407 N ASN A 364 18.442 -25.438 41.454 1.00 53.81 N
ATOM 2408 CA ASN A 364 19.367 -24.320 41.264 1.00 46.57 C
ATOM 2409 C ASN A 364 19.546 -23.937 39.809 1.00 57.77 C
ATOM 2410 O ASN A 364 20.128 -24.695 39.028 1.00 61.06 O
ATOM 2411 CB ASN A 364 20.745 -24.622 41.856 1.00 52.00 C
ATOM 2412 CG ASN A 364 20.666 -25.217 43.237 1.00 50.47 C
ATOM 2413 OD1 ASN A 364 20.288 -24.545 44.194 1.00 52.17 O
ATOM 2414 ND2 ASN A 364 21.021 -26.488 43.351 1.00 53.92 N
ATOM 2415 N VAL A 365 19.068 -22.750 39.450 1.00 48.38 N
ATOM 2416 CA VAL A 365 19.214 -22.266 38.091 1.00 44.17 C
ATOM 2417 C VAL A 365 20.370 -21.275 37.925 1.00 41.64 C
ATOM 2418 O VAL A 365 20.394 -20.215 38.536 1.00 50.79 O
ATOM 2419 CB VAL A 365 17.920 -21.623 37.581 1.00 48.53 C
ATOM 2420 CG1 VAL A 365 18.011 -21.430 36.088 1.00 41.09 C
ATOM 2421 CG2 VAL A 365 16.715 -22.487 37.942 1.00 50.61 C
ATOM 2422 N PHE A 366 21.315 -21.633 37.070 1.00 41.41 N
ATOM 2423 CA PHE A 366 22.461 -20.800 36.749 1.00 37.36 C
ATOM 2424 C PHE A 366 22.358 -20.201 35.327 1.00 36.38 C
ATOM 2425 O PHE A 366 21.886 -20.850 34.403 1.00 34.44 O
ATOM 2426 CB PHE A 366 23.691 -21.678 36.865 1.00 27.37 C
ATOM 2427 CG PHE A 366 24.948 -21.068 36.335 1.00 37.74 C
ATOM 2428 CD1 PHE A 366 25.368 -21.326 35.048 1.00 34.39 C
ATOM 2429 CD2 PHE A 366 25.748 -20.285 37.144 1.00 41.31 C
ATOM 2430 CE1 PHE A 366 26.547 -20.784 34.567 1.00 41.63 C
ATOM 2431 CE2 PHE A 366 26.921 -19.744 36.660 1.00 38.79 C
ATOM 2432 CZ PHE A 366 27.323 -20.001 35.370 1.00 38.85 C
ATOM 2433 N LYS A 367 22.793 -18.959 35.159 1.00 32.58 N
ATOM 2434 CA LYS A 367 22.923 -18.369 33.831 1.00 41.85 C
ATOM 2435 C LYS A 367 23.877 -17.170 33.880 1.00 39.82 C
ATOM 2436 O LYS A 367 24.032 -16.534 34.913 1.00 37.11 O
ATOM 2437 CB LYS A 367 21.547 -18.017 33.198 1.00 37.71 C
ATOM 2438 CG LYS A 367 21.418 -16.584 32.699 1.00 33.63 C
ATOM 2439 CD LYS A 367 20.252 -16.395 31.769 1.00 39.27 C
ATOM 2440 CE LYS A 367 20.720 -15.865 30.403 1.00 33.73 C
ATOM 2441 NZ LYS A 367 21.605 -16.835 29.687 1.00 29.58 N
ATOM 2442 N LEU A 368 24.533 -16.890 32.761 1.00 40.03 N
ATOM 2443 CA LEU A 368 25.377 -15.716 32.641 1.00 36.80 C
ATOM 2444 C LEU A 368 24.599 -14.585 31.966 1.00 39.78 C
ATOM 2445 O LEU A 368 24.260 -14.679 30.791 1.00 43.85 O
ATOM 2446 CB LEU A 368 26.631 -16.062 31.836 1.00 34.50 C
ATOM 2447 CG LEU A 368 27.594 -14.958 31.384 1.00 35.62 C
ATOM 2448 CD1 LEU A 368 28.250 -14.263 32.582 1.00 47.35 C
ATOM 2449 CD2 LEU A 368 28.662 -15.549 30.480 1.00 35.81 C
ATOM 2450 N PHE A 369 24.305 -13.526 32.716 1.00 37.57 N
ATOM 2451 CA PHE A 369 23.649 -12.344 32.173 1.00 31.32 C
ATOM 2452 C PHE A 369 24.536 -11.617 31.172 1.00 34.48 C
ATOM 2453 O PHE A 369 25.755 -11.760 31.202 1.00 36.73 O
ATOM 2454 CB PHE A 369 23.304 -11.386 33.298 1.00 31.02 C
ATOM 2455 CG PHE A 369 22.115 -11.806 34.106 1.00 28.84 C
ATOM 2456 CD1 PHE A 369 21.204 -12.711 33.592 1.00 29.64 C
ATOM 2457 CD2 PHE A 369 21.904 -11.284 35.377 1.00 27.32 C
ATOM 2458 CE1 PHE A 369 20.098 -13.085 34.318 1.00 30.55 C
ATOM 2459 CE2 PHE A 369 20.806 -11.660 36.120 1.00 30.84 C
ATOM 2460 CZ PHE A 369 19.891 -12.565 35.581 1.00 33.55 C
ATOM 2461 N GLY A 370 23.919 -10.839 30.283 1.00 34.68 N
ATOM 2462 CA GLY A 370 24.653 -9.997 29.350 1.00 25.47 C
ATOM 2463 C GLY A 370 24.550 -8.540 29.772 1.00 32.77 C
ATOM 2464 O GLY A 370 24.254 -8.240 30.929 1.00 36.03 O
ATOM 2465 N PRO A 371 24.786 -7.620 28.836 1.00 33.54 N
ATOM 2466 CA PRO A 371 24.754 -6.180 29.125 1.00 33.25 C
ATOM 2467 C PRO A 371 23.500 -5.763 29.901 1.00 34.87 C
ATOM 2468 O PRO A 371 22.457 -6.375 29.702 1.00 35.71 O
ATOM 2469 CB PRO A 371 24.740 -5.551 27.722 1.00 28.13 C
ATOM 2470 CG PRO A 371 25.465 -6.548 26.861 1.00 23.19 C
ATOM 2471 CD PRO A 371 25.116 -7.909 27.425 1.00 27.65 C
ATOM 2472 N ARG A 372 23.614 -4.754 30.765 1.00 38.72 N
ATOM 2473 CA ARG A 372 22.482 -4.225 31.516 1.00 31.32 C
ATOM 2474 C ARG A 372 21.823 -3.094 30.743 1.00 34.19 C
ATOM 2475 O ARG A 372 22.260 -2.741 29.645 1.00 33.36 O
ATOM 2476 CB ARG A 372 22.963 -3.698 32.863 1.00 37.59 C
ATOM 2477 CG ARG A 372 24.014 -2.574 32.759 1.00 33.25 C
ATOM 2478 CD ARG A 372 24.080 -1.790 34.076 1.00 29.50 C
ATOM 2479 NE ARG A 372 22.769 -1.230 34.402 1.00 36.15 N
ATOM 2480 CZ ARG A 372 22.337 -0.994 35.634 1.00 31.93 C
ATOM 2481 NH1 ARG A 372 23.115 -1.272 36.667 1.00 31.79 N
ATOM 2482 NH2 ARG A 372 21.121 -0.490 35.825 1.00 33.62 N
ATOM 2483 N ASN A 373 20.768 -2.524 31.314 1.00 34.04 N
ATOM 2484 CA ASN A 373 20.036 -1.438 30.657 1.00 36.52 C
ATOM 2485 C ASN A 373 20.132 -0.162 31.509 1.00 42.47 C
ATOM 2486 O ASN A 373 20.786 -0.166 32.557 1.00 44.76 O
ATOM 2487 CB ASN A 373 18.572 -1.841 30.349 1.00 27.76 C
ATOM 2488 CG ASN A 373 17.730 -2.067 31.608 1.00 34.66 C
ATOM 2489 OD1 ASN A 373 18.023 -1.515 32.683 1.00 32.65 O
ATOM 2490 ND2 ASN A 373 16.672 -2.880 31.481 1.00 25.94 N
ATOM 2491 N GLN A 374 19.476 0.917 31.095 1.00 42.32 N
ATOM 2492 CA GLN A 374 19.669 2.185 31.787 1.00 36.13 C
ATOM 2493 C GLN A 374 18.734 2.407 32.967 1.00 37.01 C
ATOM 2494 O GLN A 374 18.685 3.511 33.508 1.00 44.48 O
ATOM 2495 CB GLN A 374 19.642 3.383 30.814 1.00 36.27 C
ATOM 2496 CG GLN A 374 18.367 3.542 30.022 1.00 43.55 C
ATOM 2497 CD GLN A 374 18.498 4.522 28.838 1.00 56.47 C
ATOM 2498 OE1 GLN A 374 18.344 5.750 28.990 1.00 50.34 O
ATOM 2499 NE2 GLN A 374 18.769 3.975 27.654 1.00 39.64 N
ATOM 2500 N ALA A 375 18.007 1.371 33.384 1.00 35.75 N
ATOM 2501 CA ALA A 375 17.130 1.504 34.556 1.00 38.93 C
ATOM 2502 C ALA A 375 17.942 1.460 35.856 1.00 40.96 C
ATOM 2503 O ALA A 375 18.565 0.438 36.166 1.00 35.56 O
ATOM 2504 CB ALA A 375 16.095 0.428 34.566 1.00 35.06 C
ATOM 2505 N PRO A 376 17.943 2.569 36.614 1.00 40.99 N
ATOM 2506 CA PRO A 376 18.731 2.615 37.843 1.00 37.79 C
ATOM 2507 C PRO A 376 18.493 1.431 38.781 1.00 33.99 C
ATOM 2508 O PRO A 376 19.479 0.895 39.279 1.00 34.97 O
ATOM 2509 CB PRO A 376 18.339 3.960 38.485 1.00 38.79 C
ATOM 2510 CG PRO A 376 17.198 4.482 37.695 1.00 41.21 C
ATOM 2511 CD PRO A 376 17.327 3.874 36.323 1.00 44.71 C
ATOM 2512 N LEU A 377 17.254 0.994 38.980 1.00 34.92 N
ATOM 2513 CA LEU A 377 16.999 -0.143 39.879 1.00 36.05 C
ATOM 2514 C LEU A 377 16.854 -1.511 39.189 1.00 34.46 C
ATOM 2515 O LEU A 377 16.377 -2.479 39.801 1.00 35.93 O
ATOM 2516 CB LEU A 377 15.759 0.097 40.754 1.00 35.52 C
ATOM 2517 CG LEU A 377 15.753 1.066 41.939 1.00 38.50 C
ATOM 2518 CD1 LEU A 377 14.530 0.787 42.836 1.00 33.62 C
ATOM 2519 CD2 LEU A 377 17.059 1.007 42.735 1.00 38.00 C
ATOM 2520 N SER A 378 17.257 -1.599 37.931 1.00 35.42 N
ATOM 2521 CA SER A 378 17.197 -2.864 37.215 1.00 33.15 C
ATOM 2522 C SER A 378 18.140 -3.872 37.876 1.00 32.37 C
ATOM 2523 O SER A 378 19.307 -3.585 38.101 1.00 30.59 O
ATOM 2524 CB SER A 378 17.571 -2.644 35.755 1.00 30.14 C
ATOM 2525 OG SER A 378 17.712 -3.876 35.076 1.00 37.62 O
ATOM 2526 N PHE A 379 17.626 -5.054 38.185 1.00 31.07 N
ATOM 2527 CA PHE A 379 18.453 -6.105 38.778 1.00 27.14 C
ATOM 2528 C PHE A 379 19.618 -6.623 37.906 1.00 32.55 C
ATOM 2529 O PHE A 379 20.758 -6.664 38.369 1.00 30.97 O
ATOM 2530 CB PHE A 379 17.587 -7.250 39.309 1.00 26.35 C
ATOM 2531 CG PHE A 379 18.343 -8.532 39.553 1.00 31.54 C
ATOM 2532 CD1 PHE A 379 19.246 -8.636 40.605 1.00 27.38 C
ATOM 2533 CD2 PHE A 379 18.126 -9.648 38.740 1.00 27.72 C
ATOM 2534 CE1 PHE A 379 19.947 -9.817 40.834 1.00 24.14 C
ATOM 2535 CE2 PHE A 379 18.810 -10.835 38.946 1.00 27.18 C
ATOM 2536 CZ PHE A 379 19.728 -10.921 40.013 1.00 35.38 C
ATOM 2537 N PRO A 380 19.351 -7.001 36.642 1.00 31.95 N
ATOM 2538 CA PRO A 380 20.432 -7.691 35.935 1.00 28.33 C
ATOM 2539 C PRO A 380 21.659 -6.838 35.606 1.00 31.55 C
ATOM 2540 O PRO A 380 21.519 -5.693 35.194 1.00 32.03 O
ATOM 2541 CB PRO A 380 19.751 -8.176 34.652 1.00 23.59 C
ATOM 2542 CG PRO A 380 18.293 -8.231 34.984 1.00 27.09 C
ATOM 2543 CD PRO A 380 18.084 -7.059 35.887 1.00 27.67 C
ATOM 2544 N ILE A 381 22.848 -7.411 35.811 1.00 31.01 N
ATOM 2545 CA ILE A 381 24.102 -6.849 35.306 1.00 27.52 C
ATOM 2546 C ILE A 381 24.903 -7.994 34.689 1.00 28.28 C
ATOM 2547 O ILE A 381 24.674 -9.153 35.048 1.00 33.15 O
ATOM 2548 CB ILE A 381 24.906 -6.172 36.419 1.00 26.49 C
ATOM 2549 CG1 ILE A 381 25.381 -7.202 37.439 1.00 25.94 C
ATOM 2550 CG2 ILE A 381 24.086 -5.061 37.069 1.00 28.82 C
ATOM 2551 CD1 ILE A 381 26.276 -6.599 38.499 1.00 35.47 C
ATOM 2552 N PRO A 382 25.823 -7.698 33.750 1.00 25.17 N
ATOM 2553 CA PRO A 382 26.562 -8.832 33.176 1.00 28.30 C
ATOM 2554 C PRO A 382 27.330 -9.602 34.247 1.00 37.86 C
ATOM 2555 O PRO A 382 28.067 -8.998 35.015 1.00 37.77 O
ATOM 2556 CB PRO A 382 27.535 -8.179 32.196 1.00 20.02 C
ATOM 2557 CG PRO A 382 27.535 -6.697 32.545 1.00 21.77 C
ATOM 2558 CD PRO A 382 26.192 -6.413 33.129 1.00 28.07 C
ATOM 2559 N GLY A 383 27.137 -10.917 34.299 1.00 40.31 N
ATOM 2560 CA GLY A 383 27.816 -11.737 35.273 1.00 37.06 C
ATOM 2561 C GLY A 383 27.050 -12.987 35.648 1.00 38.69 C
ATOM 2562 O GLY A 383 26.093 -13.373 34.973 1.00 38.58 O
ATOM 2563 N TRP A 384 27.457 -13.587 36.759 1.00 33.36 N
ATOM 2564 CA TRP A 384 27.037 -14.921 37.133 1.00 31.36 C
ATOM 2565 C TRP A 384 25.775 -14.880 37.976 1.00 34.45 C
ATOM 2566 O TRP A 384 25.787 -14.456 39.122 1.00 35.43 O
ATOM 2567 CB TRP A 384 28.207 -15.606 37.861 1.00 45.03 C
ATOM 2568 CG TRP A 384 29.525 -15.454 37.089 1.00 38.35 C
ATOM 2569 CD1 TRP A 384 30.518 -14.546 37.320 1.00 42.82 C
ATOM 2570 CD2 TRP A 384 29.933 -16.201 35.937 1.00 46.48 C
ATOM 2571 NE1 TRP A 384 31.527 -14.687 36.392 1.00 41.90 N
ATOM 2572 CE2 TRP A 384 31.198 -15.707 35.538 1.00 39.87 C
ATOM 2573 CE3 TRP A 384 29.346 -17.244 35.194 1.00 41.60 C
ATOM 2574 CZ2 TRP A 384 31.892 -16.216 34.440 1.00 43.40 C
ATOM 2575 CZ3 TRP A 384 30.040 -17.753 34.105 1.00 48.52 C
ATOM 2576 CH2 TRP A 384 31.302 -17.236 33.738 1.00 48.55 C
ATOM 2577 N ASN A 385 24.670 -15.304 37.389 1.00 35.37 N
ATOM 2578 CA ASN A 385 23.380 -15.268 38.071 1.00 35.15 C
ATOM 2579 C ASN A 385 22.979 -16.636 38.590 1.00 36.85 C
ATOM 2580 O ASN A 385 23.115 -17.643 37.884 1.00 36.07 O
ATOM 2581 CB ASN A 385 22.285 -14.708 37.145 1.00 26.12 C
ATOM 2582 CG ASN A 385 20.887 -14.888 37.716 1.00 33.78 C
ATOM 2583 OD1 ASN A 385 20.444 -14.122 38.587 1.00 32.33 O
ATOM 2584 ND2 ASN A 385 20.179 -15.912 37.234 1.00 39.92 N
ATOM 2585 N ILE A 386 22.481 -16.685 39.821 1.00 36.27 N
ATOM 2586 CA ILE A 386 22.034 -17.961 40.337 1.00 38.74 C
ATOM 2587 C ILE A 386 20.801 -17.850 41.213 1.00 36.42 C
ATOM 2588 O ILE A 386 20.592 -16.847 41.874 1.00 37.78 O
ATOM 2589 CB ILE A 386 23.208 -18.768 40.986 1.00 42.26 C
ATOM 2590 CG1 ILE A 386 23.019 -20.267 40.729 1.00 42.95 C
ATOM 2591 CG2 ILE A 386 23.394 -18.454 42.473 1.00 36.37 C
ATOM 2592 CD1 ILE A 386 23.626 -21.157 41.777 1.00 46.93 C
ATOM 2593 N CYS A 387 19.965 -18.881 41.157 1.00 37.88 N
ATOM 2594 CA CYS A 387 18.810 -19.025 42.035 1.00 46.30 C
ATOM 2595 C CYS A 387 18.941 -20.243 42.920 1.00 46.20 C
ATOM 2596 O CYS A 387 19.199 -21.332 42.427 1.00 47.26 O
ATOM 2597 CB CYS A 387 17.583 -19.268 41.198 1.00 47.85 C
ATOM 2598 SG CYS A 387 16.434 -17.932 41.236 1.00 69.95 S
ATOM 2599 N VAL A 388 18.716 -20.085 44.215 1.00 47.55 N
ATOM 2600 CA VAL A 388 18.738 -21.237 45.105 1.00 45.42 C
ATOM 2601 C VAL A 388 17.491 -21.285 45.962 1.00 45.95 C
ATOM 2602 O VAL A 388 16.955 -20.260 46.354 1.00 50.87 O
ATOM 2603 CB VAL A 388 19.971 -21.226 46.017 1.00 42.74 C
ATOM 2604 CG1 VAL A 388 21.253 -21.475 45.216 1.00 29.53 C
ATOM 2605 CG2 VAL A 388 20.042 -19.909 46.776 1.00 48.20 C
ATOM 2606 N ASP A 389 17.034 -22.492 46.243 1.00 51.15 N
ATOM 2607 CA ASP A 389 15.846 -22.689 47.048 1.00 57.57 C
ATOM 2608 C ASP A 389 16.237 -23.376 48.353 1.00 55.28 C
ATOM 2609 O ASP A 389 16.685 -24.526 48.346 1.00 57.61 O
ATOM 2610 CB ASP A 389 14.854 -23.552 46.268 1.00 66.08 C
ATOM 2611 CG ASP A 389 13.456 -22.985 46.281 1.00 70.17 C
ATOM 2612 OD1 ASP A 389 13.312 -21.745 46.376 1.00 72.59 O
ATOM 2613 OD2 ASP A 389 12.500 -23.785 46.190 1.00 79.86 O
ATOM 2614 N PHE A 390 16.061 -22.672 49.468 1.00 57.10 N
ATOM 2615 CA PHE A 390 16.518 -23.142 50.777 1.00 49.70 C
ATOM 2616 C PHE A 390 15.360 -23.578 51.625 1.00 50.76 C
ATOM 2617 O PHE A 390 14.447 -22.796 51.858 1.00 51.17 O
ATOM 2618 CB PHE A 390 17.202 -22.012 51.528 1.00 39.29 C
ATOM 2619 CG PHE A 390 18.571 -21.708 51.042 1.00 36.33 C
ATOM 2620 CD1 PHE A 390 19.435 -22.728 50.681 1.00 42.41 C
ATOM 2621 CD2 PHE A 390 19.002 -20.404 50.951 1.00 34.09 C
ATOM 2622 CE1 PHE A 390 20.708 -22.449 50.244 1.00 40.20 C
ATOM 2623 CE2 PHE A 390 20.284 -20.115 50.518 1.00 37.34 C
ATOM 2624 CZ PHE A 390 21.136 -21.139 50.165 1.00 36.66 C
ATOM 2625 N PRO A 391 15.394 -24.826 52.106 1.00 46.85 N
ATOM 2626 CA PRO A 391 14.336 -25.267 53.017 1.00 42.20 C
ATOM 2627 C PRO A 391 14.429 -24.458 54.278 1.00 47.97 C
ATOM 2628 O PRO A 391 15.507 -24.385 54.873 1.00 56.49 O
ATOM 2629 CB PRO A 391 14.703 -26.720 53.314 1.00 45.79 C
ATOM 2630 CG PRO A 391 15.601 -27.140 52.199 1.00 51.05 C
ATOM 2631 CD PRO A 391 16.314 -25.911 51.733 1.00 43.76 C
ATOM 2632 N ILE A 392 13.336 -23.833 54.678 1.00 47.49 N
ATOM 2633 CA ILE A 392 13.342 -23.086 55.924 1.00 50.83 C
ATOM 2634 C ILE A 392 13.699 -23.986 57.121 1.00 57.30 C
ATOM 2635 O ILE A 392 13.051 -25.005 57.385 1.00 56.17 O
ATOM 2636 CB ILE A 392 12.047 -22.300 56.130 1.00 48.83 C
ATOM 2637 CG1 ILE A 392 12.027 -21.110 55.170 1.00 47.89 C
ATOM 2638 CG2 ILE A 392 11.947 -21.829 57.576 1.00 48.94 C
ATOM 2639 CD1 ILE A 392 10.846 -20.165 55.348 1.00 49.64 C
ATOM 2640 N LYS A 393 14.752 -23.583 57.826 1.00 60.42 N
ATOM 2641 CA LYS A 393 15.487 -24.436 58.758 1.00 57.84 C
ATOM 2642 C LYS A 393 16.229 -23.524 59.753 1.00 62.72 C
ATOM 2643 O LYS A 393 16.395 -22.329 59.497 1.00 54.93 O
ATOM 2644 CB LYS A 393 16.483 -25.284 57.962 1.00 42.94 C
ATOM 2645 CG LYS A 393 17.060 -26.456 58.687 1.00 46.93 C
ATOM 2646 CD LYS A 393 17.963 -27.290 57.769 1.00 38.67 C
ATOM 2647 CE LYS A 393 19.169 -26.513 57.312 1.00 38.82 C
ATOM 2648 NZ LYS A 393 20.289 -27.427 56.896 1.00 53.72 N
ATOM 2649 N ASP A 394 16.671 -24.069 60.885 1.00 66.10 N
ATOM 2650 CA ASP A 394 17.317 -23.242 61.915 1.00 61.11 C
ATOM 2651 C ASP A 394 18.632 -22.605 61.452 1.00 54.34 C
ATOM 2652 O ASP A 394 19.487 -23.263 60.856 1.00 50.57 O
ATOM 2653 CB ASP A 394 17.572 -24.029 63.213 1.00 56.14 C
ATOM 2654 CG ASP A 394 16.385 -24.014 64.167 1.00 56.59 C
ATOM 2655 OD1 ASP A 394 15.548 -23.081 64.107 1.00 50.95 O
ATOM 2656 OD2 ASP A 394 16.303 -24.955 64.990 1.00 57.18 O
ATOM 2657 N GLY A 395 18.779 -21.319 61.747 1.00 49.66 N
ATOM 2658 CA GLY A 395 19.987 -20.584 61.438 1.00 50.87 C
ATOM 2659 C GLY A 395 20.123 -20.239 59.973 1.00 51.95 C
ATOM 2660 O GLY A 395 21.204 -19.871 59.513 1.00 45.61 O
ATOM 2661 N LEU A 396 19.026 -20.360 59.238 1.00 47.24 N
ATOM 2662 CA LEU A 396 19.043 -20.103 57.803 1.00 54.43 C
ATOM 2663 C LEU A 396 18.944 -18.599 57.581 1.00 50.22 C
ATOM 2664 O LEU A 396 19.674 -18.022 56.773 1.00 44.07 O
ATOM 2665 CB LEU A 396 17.893 -20.852 57.141 1.00 52.19 C
ATOM 2666 CG LEU A 396 17.576 -20.821 55.650 1.00 38.21 C
ATOM 2667 CD1 LEU A 396 16.457 -19.854 55.414 1.00 39.59 C
ATOM 2668 CD2 LEU A 396 18.790 -20.519 54.788 1.00 39.02 C
ATOM 2669 N GLY A 397 18.053 -17.969 58.336 1.00 50.16 N
ATOM 2670 CA GLY A 397 17.929 -16.526 58.330 1.00 47.04 C
ATOM 2671 C GLY A 397 19.257 -15.841 58.577 1.00 50.32 C
ATOM 2672 O GLY A 397 19.604 -14.873 57.900 1.00 46.05 O
ATOM 2673 N LYS A 398 20.023 -16.348 59.538 1.00 57.12 N
ATOM 2674 CA LYS A 398 21.302 -15.715 59.822 1.00 47.31 C
ATOM 2675 C LYS A 398 22.348 -16.066 58.775 1.00 43.97 C
ATOM 2676 O LYS A 398 23.202 -15.239 58.470 1.00 46.95 O
ATOM 2677 CB LYS A 398 21.774 -15.957 61.259 1.00 42.51 C
ATOM 2678 CG LYS A 398 21.184 -14.958 62.248 1.00 42.25 C
ATOM 2679 CD LYS A 398 21.874 -15.047 63.606 1.00 44.84 C
ATOM 2680 CE LYS A 398 21.391 -13.979 64.571 1.00 42.64 C
ATOM 2681 NZ LYS A 398 20.013 -14.239 65.043 1.00 41.44 N
ATOM 2682 N PHE A 399 22.267 -17.263 58.195 1.00 43.58 N
ATOM 2683 CA PHE A 399 23.212 -17.629 57.142 1.00 41.20 C
ATOM 2684 C PHE A 399 23.041 -16.779 55.892 1.00 47.90 C
ATOM 2685 O PHE A 399 24.038 -16.448 55.255 1.00 43.95 O
ATOM 2686 CB PHE A 399 23.138 -19.106 56.781 1.00 38.64 C
ATOM 2687 CG PHE A 399 23.835 -19.448 55.495 1.00 40.09 C
ATOM 2688 CD1 PHE A 399 25.215 -19.486 55.429 1.00 28.15 C
ATOM 2689 CD2 PHE A 399 23.101 -19.731 54.342 1.00 43.98 C
ATOM 2690 CE1 PHE A 399 25.860 -19.793 54.247 1.00 37.65 C
ATOM 2691 CE2 PHE A 399 23.740 -20.041 53.146 1.00 35.91 C
ATOM 2692 CZ PHE A 399 25.123 -20.073 53.102 1.00 46.83 C
ATOM 2693 N VAL A 400 21.800 -16.421 55.534 1.00 45.07 N
ATOM 2694 CA VAL A 400 21.603 -15.646 54.309 1.00 45.34 C
ATOM 2695 C VAL A 400 22.016 -14.196 54.507 1.00 48.36 C
ATOM 2696 O VAL A 400 22.426 -13.522 53.551 1.00 46.79 O
ATOM 2697 CB VAL A 400 20.176 -15.734 53.678 1.00 42.32 C
ATOM 2698 CG1 VAL A 400 19.791 -17.180 53.365 1.00 40.25 C
ATOM 2699 CG2 VAL A 400 19.149 -15.069 54.543 1.00 41.95 C
ATOM 2700 N SER A 401 21.929 -13.709 55.738 1.00 45.54 N
ATOM 2701 CA SER A 401 22.463 -12.384 56.019 1.00 46.61 C
ATOM 2702 C SER A 401 23.948 -12.327 55.712 1.00 45.25 C
ATOM 2703 O SER A 401 24.448 -11.310 55.244 1.00 40.52 O
ATOM 2704 CB SER A 401 22.217 -11.979 57.460 1.00 39.41 C
ATOM 2705 OG SER A 401 21.056 -11.193 57.547 1.00 47.41 O
ATOM 2706 N GLU A 402 24.647 -13.425 55.966 1.00 39.03 N
ATOM 2707 CA GLU A 402 26.054 -13.490 55.653 1.00 44.53 C
ATOM 2708 C GLU A 402 26.271 -13.541 54.150 1.00 48.45 C
ATOM 2709 O GLU A 402 27.201 -12.913 53.629 1.00 47.56 O
ATOM 2710 CB GLU A 402 26.662 -14.685 56.384 1.00 48.67 C
ATOM 2711 CG GLU A 402 26.356 -14.612 57.891 1.00 49.15 C
ATOM 2712 CD GLU A 402 26.844 -13.269 58.465 1.00 50.06 C
ATOM 2713 OE1 GLU A 402 26.109 -12.548 59.161 1.00 44.13 O
ATOM 2714 OE2 GLU A 402 27.987 -13.017 58.184 1.00 44.63 O
ATOM 2715 N LEU A 403 25.381 -14.253 53.464 1.00 41.28 N
ATOM 2716 CA LEU A 403 25.404 -14.316 52.025 1.00 38.03 C
ATOM 2717 C LEU A 403 25.230 -12.937 51.416 1.00 39.51 C
ATOM 2718 O LEU A 403 25.976 -12.567 50.493 1.00 31.04 O
ATOM 2719 CB LEU A 403 24.303 -15.229 51.531 1.00 38.19 C
ATOM 2720 CG LEU A 403 24.727 -16.682 51.447 1.00 42.49 C
ATOM 2721 CD1 LEU A 403 23.719 -17.451 50.619 1.00 48.32 C
ATOM 2722 CD2 LEU A 403 26.121 -16.744 50.843 1.00 42.14 C
ATOM 2723 N ASP A 404 24.227 -12.197 51.904 1.00 34.36 N
ATOM 2724 CA ASP A 404 24.063 -10.793 51.525 1.00 35.40 C
ATOM 2725 C ASP A 404 25.377 -10.058 51.630 1.00 38.21 C
ATOM 2726 O ASP A 404 25.754 -9.350 50.710 1.00 46.12 O
ATOM 2727 CB ASP A 404 23.070 -10.047 52.413 1.00 27.77 C
ATOM 2728 CG ASP A 404 21.649 -10.490 52.201 1.00 39.24 C
ATOM 2729 OD1 ASP A 404 21.411 -11.302 51.281 1.00 47.86 O
ATOM 2730 OD2 ASP A 404 20.761 -10.012 52.942 1.00 34.02 O
ATOM 2731 N ARG A 405 26.078 -10.228 52.743 1.00 38.77 N
ATOM 2732 CA ARG A 405 27.325 -9.502 52.972 1.00 43.73 C
ATOM 2733 C ARG A 405 28.317 -9.866 51.896 1.00 37.80 C
ATOM 2734 O ARG A 405 28.979 -9.010 51.340 1.00 40.43 O
ATOM 2735 CB ARG A 405 27.900 -9.833 54.360 1.00 42.63 C
ATOM 2736 CG ARG A 405 29.242 -9.188 54.753 1.00 44.10 C
ATOM 2737 CD ARG A 405 29.777 -9.827 56.045 1.00 57.10 C
ATOM 2738 NE ARG A 405 30.618 -10.954 55.756 1.00 63.02 N
ATOM 2739 CZ ARG A 405 30.361 -12.188 56.201 1.00 65.47 C
ATOM 2740 NH1 ARG A 405 29.314 -12.415 57.000 1.00 57.44 N
ATOM 2741 NH2 ARG A 405 31.149 -13.232 55.870 1.00 59.69 N
ATOM 2742 N ARG A 406 28.416 -11.146 51.601 1.00 36.60 N
ATOM 2743 CA ARG A 406 29.336 -11.620 50.585 1.00 37.29 C
ATOM 2744 C ARG A 406 28.967 -11.104 49.180 1.00 42.27 C
ATOM 2745 O ARG A 406 29.821 -10.639 48.422 1.00 40.04 O
ATOM 2746 CB ARG A 406 29.288 -13.133 50.584 1.00 41.33 C
ATOM 2747 CG ARG A 406 30.555 -13.783 50.985 1.00 46.38 C
ATOM 2748 CD ARG A 406 30.697 -13.895 52.484 1.00 62.60 C
ATOM 2749 NE ARG A 406 31.553 -15.033 52.795 1.00 66.75 N
ATOM 2750 CZ ARG A 406 32.865 -15.063 52.571 1.00 66.51 C
ATOM 2751 NH1 ARG A 406 33.494 -14.011 52.043 1.00 52.50 N
ATOM 2752 NH2 ARG A 406 33.551 -16.151 52.884 1.00 68.97 N
ATOM 2753 N VAL A 407 27.688 -11.205 48.829 1.00 39.03 N
ATOM 2754 CA VAL A 407 27.208 -10.716 47.544 1.00 37.31 C
ATOM 2755 C VAL A 407 27.537 -9.247 47.414 1.00 37.48 C
ATOM 2756 O VAL A 407 28.000 -8.796 46.373 1.00 37.95 O
ATOM 2757 CB VAL A 407 25.683 -10.884 47.414 1.00 28.99 C
ATOM 2758 CG1 VAL A 407 25.178 -10.143 46.227 1.00 25.27 C
ATOM 2759 CG2 VAL A 407 25.315 -12.344 47.297 1.00 30.59 C
ATOM 2760 N LEU A 408 27.296 -8.497 48.485 1.00 35.95 N
ATOM 2761 CA LEU A 408 27.598 -7.072 48.499 1.00 34.07 C
ATOM 2762 C LEU A 408 29.085 -6.825 48.397 1.00 33.80 C
ATOM 2763 O LEU A 408 29.512 -6.021 47.601 1.00 38.72 O
ATOM 2764 CB LEU A 408 27.026 -6.396 49.738 1.00 30.20 C
ATOM 2765 CG LEU A 408 27.502 -4.959 49.989 1.00 35.53 C
ATOM 2766 CD1 LEU A 408 27.264 -4.095 48.762 1.00 42.18 C
ATOM 2767 CD2 LEU A 408 26.806 -4.338 51.210 1.00 30.66 C
ATOM 2768 N GLU A 409 29.876 -7.532 49.192 1.00 39.86 N
ATOM 2769 CA GLU A 409 31.323 -7.327 49.217 1.00 43.19 C
ATOM 2770 C GLU A 409 31.893 -7.550 47.813 1.00 44.95 C
ATOM 2771 O GLU A 409 32.819 -6.871 47.375 1.00 45.23 O
ATOM 2772 CB GLU A 409 31.953 -8.281 50.235 1.00 48.09 C
ATOM 2773 CG GLU A 409 33.416 -8.044 50.533 1.00 55.45 C
ATOM 2774 CD GLU A 409 34.139 -9.325 50.944 1.00 63.19 C
ATOM 2775 OE1 GLU A 409 35.361 -9.408 50.660 1.00 59.38 O
ATOM 2776 OE2 GLU A 409 33.486 -10.236 51.533 1.00 52.41 O
ATOM 2777 N PHE A 410 31.292 -8.487 47.092 1.00 45.33 N
ATOM 2778 CA PHE A 410 31.770 -8.869 45.765 1.00 45.17 C
ATOM 2779 C PHE A 410 31.108 -8.106 44.606 1.00 43.77 C
ATOM 2780 O PHE A 410 31.272 -8.478 43.445 1.00 43.93 O
ATOM 2781 CB PHE A 410 31.577 -10.380 45.544 1.00 39.24 C
ATOM 2782 CG PHE A 410 32.379 -11.253 46.481 1.00 46.23 C
ATOM 2783 CD1 PHE A 410 33.627 -10.854 46.950 1.00 41.60 C
ATOM 2784 CD2 PHE A 410 31.888 -12.491 46.889 1.00 57.71 C
ATOM 2785 CE1 PHE A 410 34.360 -11.670 47.808 1.00 36.43 C
ATOM 2786 CE2 PHE A 410 32.631 -13.311 47.758 1.00 50.62 C
ATOM 2787 CZ PHE A 410 33.864 -12.894 48.207 1.00 36.81 C
ATOM 2788 N GLY A 411 30.348 -7.057 44.904 1.00 39.54 N
ATOM 2789 CA GLY A 411 29.898 -6.164 43.852 1.00 35.63 C
ATOM 2790 C GLY A 411 28.610 -6.596 43.157 1.00 43.52 C
ATOM 2791 O GLY A 411 28.202 -6.007 42.167 1.00 40.77 O
ATOM 2792 N GLY A 412 27.964 -7.621 43.687 1.00 36.69 N
ATOM 2793 CA GLY A 412 26.746 -8.128 43.114 1.00 32.39 C
ATOM 2794 C GLY A 412 25.526 -7.554 43.793 1.00 35.99 C
ATOM 2795 O GLY A 412 25.640 -6.575 44.515 1.00 34.48 O
ATOM 2796 N ARG A 413 24.357 -8.152 43.567 1.00 33.47 N
ATOM 2797 CA ARG A 413 23.142 -7.657 44.204 1.00 36.09 C
ATOM 2798 C ARG A 413 22.085 -8.741 44.294 1.00 32.40 C
ATOM 2799 O ARG A 413 22.197 -9.760 43.632 1.00 34.68 O
ATOM 2800 CB ARG A 413 22.585 -6.444 43.441 1.00 32.68 C
ATOM 2801 CG ARG A 413 22.195 -6.755 42.001 1.00 30.86 C
ATOM 2802 CD ARG A 413 23.298 -6.397 41.004 1.00 26.36 C
ATOM 2803 NE ARG A 413 23.511 -4.962 41.005 1.00 27.68 N
ATOM 2804 CZ ARG A 413 22.663 -4.090 40.475 1.00 33.71 C
ATOM 2805 NH1 ARG A 413 21.558 -4.517 39.885 1.00 36.09 N
ATOM 2806 NH2 ARG A 413 22.912 -2.789 40.536 1.00 32.50 N
ATOM 2807 N LEU A 414 21.076 -8.512 45.129 1.00 34.27 N
ATOM 2808 CA LEU A 414 19.878 -9.353 45.201 1.00 39.41 C
ATOM 2809 C LEU A 414 18.790 -8.786 44.310 1.00 35.15 C
ATOM 2810 O LEU A 414 18.925 -7.683 43.788 1.00 33.25 O
ATOM 2811 CB LEU A 414 19.305 -9.371 46.616 1.00 35.58 C
ATOM 2812 CG LEU A 414 20.234 -9.798 47.730 1.00 45.51 C
ATOM 2813 CD1 LEU A 414 19.533 -9.707 49.095 1.00 38.19 C
ATOM 2814 CD2 LEU A 414 20.717 -11.198 47.418 1.00 38.41 C
ATOM 2815 N TYR A 415 17.686 -9.524 44.222 1.00 38.43 N
ATOM 2816 CA TYR A 415 16.563 -9.237 43.332 1.00 35.02 C
ATOM 2817 C TYR A 415 15.338 -9.007 44.194 1.00 38.87 C
ATOM 2818 O TYR A 415 14.967 -9.886 44.976 1.00 37.95 O
ATOM 2819 CB TYR A 415 16.319 -10.473 42.449 1.00 36.14 C
ATOM 2820 CG TYR A 415 15.366 -10.321 41.265 1.00 32.47 C
ATOM 2821 CD1 TYR A 415 15.002 -9.076 40.784 1.00 31.43 C
ATOM 2822 CD2 TYR A 415 14.836 -11.450 40.629 1.00 35.01 C
ATOM 2823 CE1 TYR A 415 14.137 -8.942 39.706 1.00 28.60 C
ATOM 2824 CE2 TYR A 415 13.980 -11.335 39.550 1.00 30.06 C
ATOM 2825 CZ TYR A 415 13.633 -10.077 39.089 1.00 35.37 C
ATOM 2826 OH TYR A 415 12.787 -9.949 38.008 1.00 31.38 O
ATOM 2827 N THR A 416 14.701 -7.846 44.046 1.00 38.79 N
ATOM 2828 CA THR A 416 13.511 -7.496 44.835 1.00 44.73 C
ATOM 2829 C THR A 416 12.326 -8.415 44.598 1.00 45.53 C
ATOM 2830 O THR A 416 11.466 -8.585 45.469 1.00 51.21 O
ATOM 2831 CB THR A 416 12.995 -6.093 44.505 1.00 48.84 C
ATOM 2832 OG1 THR A 416 12.554 -6.045 43.135 1.00 46.22 O
ATOM 2833 CG2 THR A 416 14.081 -5.057 44.747 1.00 45.93 C
ATOM 2834 N ALA A 417 12.258 -8.981 43.399 1.00 44.58 N
ATOM 2835 CA ALA A 417 11.194 -9.915 43.059 1.00 44.86 C
ATOM 2836 C ALA A 417 11.321 -11.218 43.845 1.00 46.68 C
ATOM 2837 O ALA A 417 10.387 -12.009 43.878 1.00 47.47 O
ATOM 2838 CB ALA A 417 11.178 -10.194 41.554 1.00 42.30 C
ATOM 2839 N LYS A 418 12.479 -11.424 44.473 1.00 44.17 N
ATOM 2840 CA LYS A 418 12.757 -12.609 45.293 1.00 46.83 C
ATOM 2841 C LYS A 418 12.843 -12.313 46.791 1.00 48.44 C
ATOM 2842 O LYS A 418 12.732 -13.220 47.620 1.00 55.97 O
ATOM 2843 CB LYS A 418 14.108 -13.215 44.896 1.00 38.63 C
ATOM 2844 CG LYS A 418 14.142 -13.920 43.583 1.00 37.89 C
ATOM 2845 CD LYS A 418 13.006 -14.901 43.513 1.00 53.50 C
ATOM 2846 CE LYS A 418 12.864 -15.459 42.133 1.00 42.99 C
ATOM 2847 NZ LYS A 418 13.590 -16.752 42.030 1.00 44.73 N
ATOM 2848 N ASP A 419 13.061 -11.050 47.135 1.00 53.69 N
ATOM 2849 CA ASP A 419 13.515 -10.702 48.475 1.00 53.51 C
ATOM 2850 C ASP A 419 12.475 -10.106 49.406 1.00 57.56 C
ATOM 2851 O ASP A 419 11.664 -9.286 49.003 1.00 54.29 O
ATOM 2852 CB ASP A 419 14.677 -9.719 48.390 1.00 51.32 C
ATOM 2853 CG ASP A 419 14.975 -9.080 49.716 1.00 45.68 C
ATOM 2854 OD1 ASP A 419 15.606 -9.766 50.537 1.00 49.47 O
ATOM 2855 OD2 ASP A 419 14.551 -7.925 49.943 1.00 46.28 O
ATOM 2856 N SER A 420 12.552 -10.483 50.677 1.00 61.70 N
ATOM 2857 CA SER A 420 11.714 -9.878 51.705 1.00 62.75 C
ATOM 2858 C SER A 420 12.465 -9.566 52.998 1.00 63.01 C
ATOM 2859 O SER A 420 11.959 -8.826 53.832 1.00 62.77 O
ATOM 2860 CB SER A 420 10.547 -10.802 52.028 1.00 55.64 C
ATOM 2861 OG SER A 420 11.008 -12.145 52.047 1.00 62.37 O
ATOM 2862 N ARG A 421 13.660 -10.123 53.164 1.00 53.88 N
ATOM 2863 CA ARG A 421 14.362 -10.009 54.433 1.00 59.76 C
ATOM 2864 C ARG A 421 15.622 -9.113 54.500 1.00 58.08 C
ATOM 2865 O ARG A 421 16.038 -8.731 55.598 1.00 57.95 O
ATOM 2866 CB ARG A 421 14.611 -11.401 55.041 1.00 59.20 C
ATOM 2867 CG ARG A 421 14.830 -12.521 54.050 1.00 53.85 C
ATOM 2868 CD ARG A 421 16.098 -12.265 53.246 1.00 60.65 C
ATOM 2869 NE ARG A 421 17.235 -12.010 54.125 1.00 64.94 N
ATOM 2870 CZ ARG A 421 18.490 -11.841 53.714 1.00 60.79 C
ATOM 2871 NH1 ARG A 421 18.795 -11.906 52.412 1.00 44.72 N
ATOM 2872 NH2 ARG A 421 19.441 -11.621 54.616 1.00 49.83 N
ATOM 2873 N THR A 422 16.207 -8.753 53.359 1.00 50.08 N
ATOM 2874 CA THR A 422 17.403 -7.902 53.372 1.00 48.84 C
ATOM 2875 C THR A 422 17.143 -6.479 53.920 1.00 50.16 C
ATOM 2876 O THR A 422 16.000 -6.056 54.066 1.00 52.43 O
ATOM 2877 CB THR A 422 18.129 -7.888 52.000 1.00 46.60 C
ATOM 2878 OG1 THR A 422 19.533 -7.689 52.192 1.00 46.62 O
ATOM 2879 CG2 THR A 422 17.585 -6.799 51.087 1.00 46.29 C
ATOM 2880 N THR A 423 18.214 -5.763 54.242 1.00 47.63 N
ATOM 2881 CA THR A 423 18.113 -4.446 54.876 1.00 47.83 C
ATOM 2882 C THR A 423 18.260 -3.275 53.897 1.00 47.74 C
ATOM 2883 O THR A 423 18.868 -3.410 52.835 1.00 48.78 O
ATOM 2884 CB THR A 423 19.198 -4.303 55.959 1.00 40.25 C
ATOM 2885 OG1 THR A 423 20.494 -4.433 55.356 1.00 43.26 O
ATOM 2886 CG2 THR A 423 19.050 -5.400 57.007 1.00 29.14 C
ATOM 2887 N ALA A 424 17.704 -2.127 54.267 1.00 46.61 N
ATOM 2888 CA ALA A 424 17.824 -0.917 53.472 1.00 39.98 C
ATOM 2889 C ALA A 424 19.290 -0.605 53.154 1.00 48.68 C
ATOM 2890 O ALA A 424 19.629 -0.269 52.025 1.00 46.47 O
ATOM 2891 CB ALA A 424 17.166 0.242 54.191 1.00 37.01 C
ATOM 2892 N GLU A 425 20.161 -0.742 54.149 1.00 49.52 N
ATOM 2893 CA GLU A 425 21.564 -0.395 53.969 1.00 50.12 C
ATOM 2894 C GLU A 425 22.281 -1.291 52.962 1.00 41.47 C
ATOM 2895 O GLU A 425 23.049 -0.810 52.130 1.00 45.76 O
ATOM 2896 CB GLU A 425 22.302 -0.427 55.304 1.00 43.90 C
ATOM 2897 CG GLU A 425 23.797 -0.161 55.139 1.00 53.52 C
ATOM 2898 CD GLU A 425 24.570 -0.191 56.438 1.00 63.12 C
ATOM 2899 OE1 GLU A 425 24.098 -0.817 57.425 1.00 53.04 O
ATOM 2900 OE2 GLU A 425 25.661 0.423 56.453 1.00 66.46 O
ATOM 2901 N THR A 426 22.049 -2.593 53.066 1.00 35.08 N
ATOM 2902 CA THR A 426 22.523 -3.553 52.088 1.00 34.91 C
ATOM 2903 C THR A 426 22.000 -3.245 50.657 1.00 42.50 C
ATOM 2904 O THR A 426 22.760 -3.196 49.687 1.00 38.44 O
ATOM 2905 CB THR A 426 22.081 -4.955 52.504 1.00 39.25 C
ATOM 2906 OG1 THR A 426 22.600 -5.247 53.806 1.00 37.21 O
ATOM 2907 CG2 THR A 426 22.593 -6.012 51.517 1.00 40.66 C
ATOM 2908 N PHE A 427 20.702 -3.021 50.537 1.00 39.22 N
ATOM 2909 CA PHE A 427 20.117 -2.764 49.247 1.00 41.59 C
ATOM 2910 C PHE A 427 20.678 -1.494 48.621 1.00 45.22 C
ATOM 2911 O PHE A 427 20.992 -1.474 47.419 1.00 43.88 O
ATOM 2912 CB PHE A 427 18.599 -2.691 49.358 1.00 42.68 C
ATOM 2913 CG PHE A 427 17.917 -2.632 48.040 1.00 39.80 C
ATOM 2914 CD1 PHE A 427 17.552 -3.795 47.390 1.00 39.71 C
ATOM 2915 CD2 PHE A 427 17.660 -1.414 47.429 1.00 43.03 C
ATOM 2916 CE1 PHE A 427 16.926 -3.741 46.158 1.00 45.84 C
ATOM 2917 CE2 PHE A 427 17.028 -1.350 46.190 1.00 39.02 C
ATOM 2918 CZ PHE A 427 16.667 -2.511 45.555 1.00 34.59 C
ATOM 2919 N HIS A 428 20.820 -0.447 49.429 1.00 42.21 N
ATOM 2920 CA HIS A 428 21.290 0.837 48.919 1.00 40.15 C
ATOM 2921 C HIS A 428 22.724 0.737 48.442 1.00 37.61 C
ATOM 2922 O HIS A 428 23.130 1.426 47.499 1.00 36.26 O
ATOM 2923 CB HIS A 428 21.113 1.946 49.954 1.00 35.20 C
ATOM 2924 CG HIS A 428 19.703 2.441 50.065 1.00 37.60 C
ATOM 2925 ND1 HIS A 428 19.354 3.758 49.851 1.00 40.81 N
ATOM 2926 CD2 HIS A 428 18.547 1.791 50.359 1.00 31.87 C
ATOM 2927 CE1 HIS A 428 18.050 3.899 50.013 1.00 36.71 C
ATOM 2928 NE2 HIS A 428 17.540 2.718 50.331 1.00 38.52 N
ATOM 2929 N ALA A 429 23.484 -0.152 49.065 1.00 33.29 N
ATOM 2930 CA ALA A 429 24.875 -0.321 48.668 1.00 39.96 C
ATOM 2931 C ALA A 429 24.993 -1.195 47.428 1.00 38.06 C
ATOM 2932 O ALA A 429 25.900 -1.020 46.625 1.00 40.68 O
ATOM 2933 CB ALA A 429 25.712 -0.880 49.819 1.00 34.57 C
ATOM 2934 N MET A 430 24.066 -2.135 47.275 1.00 41.34 N
ATOM 2935 CA MET A 430 24.032 -3.004 46.107 1.00 34.84 C
ATOM 2936 C MET A 430 23.630 -2.261 44.835 1.00 34.91 C
ATOM 2937 O MET A 430 24.064 -2.623 43.746 1.00 39.38 O
ATOM 2938 CB MET A 430 23.073 -4.161 46.366 1.00 33.52 C
ATOM 2939 CG MET A 430 23.635 -5.297 47.185 1.00 23.31 C
ATOM 2940 SD MET A 430 22.279 -6.336 47.746 1.00 30.22 S
ATOM 2941 CE MET A 430 23.177 -7.787 48.277 1.00 25.05 C
ATOM 2942 N TYR A 431 22.798 -1.233 44.982 1.00 35.48 N
ATOM 2943 CA TYR A 431 22.303 -0.442 43.864 1.00 35.70 C
ATOM 2944 C TYR A 431 22.796 1.015 43.963 1.00 40.33 C
ATOM 2945 O TYR A 431 22.060 1.905 44.396 1.00 38.17 O
ATOM 2946 CB TYR A 431 20.764 -0.501 43.853 1.00 29.97 C
ATOM 2947 CG TYR A 431 20.155 -1.852 43.453 1.00 34.35 C
ATOM 2948 CD1 TYR A 431 20.040 -2.899 44.360 1.00 29.26 C
ATOM 2949 CD2 TYR A 431 19.674 -2.064 42.165 1.00 36.35 C
ATOM 2950 CE1 TYR A 431 19.480 -4.113 43.992 1.00 32.32 C
ATOM 2951 CE2 TYR A 431 19.115 -3.271 41.785 1.00 24.03 C
ATOM 2952 CZ TYR A 431 19.013 -4.289 42.690 1.00 34.15 C
ATOM 2953 OH TYR A 431 18.456 -5.483 42.279 1.00 26.84 O
ATOM 2954 N PRO A 432 24.052 1.271 43.572 1.00 43.06 N
ATOM 2955 CA PRO A 432 24.622 2.618 43.748 1.00 42.88 C
ATOM 2956 C PRO A 432 23.837 3.791 43.092 1.00 49.18 C
ATOM 2957 O PRO A 432 23.960 4.940 43.550 1.00 44.41 O
ATOM 2958 CB PRO A 432 26.057 2.473 43.217 1.00 37.41 C
ATOM 2959 CG PRO A 432 26.080 1.181 42.457 1.00 47.39 C
ATOM 2960 CD PRO A 432 25.060 0.303 43.117 1.00 45.04 C
ATOM 2961 N ARG A 433 23.020 3.501 42.084 1.00 42.86 N
ATOM 2962 CA ARG A 433 22.173 4.522 41.478 1.00 39.54 C
ATOM 2963 C ARG A 433 20.826 4.708 42.185 1.00 37.70 C
ATOM 2964 O ARG A 433 19.967 5.431 41.686 1.00 43.51 O
ATOM 2965 CB ARG A 433 21.976 4.237 39.986 1.00 40.43 C
ATOM 2966 CG ARG A 433 23.293 4.149 39.225 1.00 36.21 C
ATOM 2967 CD ARG A 433 23.088 3.626 37.849 1.00 33.96 C
ATOM 2968 NE ARG A 433 22.105 4.448 37.147 1.00 50.26 N
ATOM 2969 CZ ARG A 433 21.709 4.237 35.896 1.00 48.20 C
ATOM 2970 NH1 ARG A 433 22.216 3.220 35.198 1.00 41.70 N
ATOM 2971 NH2 ARG A 433 20.808 5.044 35.345 1.00 52.02 N
ATOM 2972 N VAL A 434 20.648 4.081 43.348 1.00 34.54 N
ATOM 2973 CA VAL A 434 19.394 4.226 44.101 1.00 34.18 C
ATOM 2974 C VAL A 434 19.052 5.688 44.397 1.00 46.03 C
ATOM 2975 O VAL A 434 17.894 6.090 44.278 1.00 55.72 O
ATOM 2976 CB VAL A 434 19.368 3.392 45.434 1.00 39.54 C
ATOM 2977 CG1 VAL A 434 20.507 3.787 46.377 1.00 39.77 C
ATOM 2978 CG2 VAL A 434 18.022 3.534 46.149 1.00 29.09 C
ATOM 2979 N ASP A 435 20.057 6.479 44.776 1.00 49.14 N
ATOM 2980 CA ASP A 435 19.868 7.900 45.067 1.00 46.95 C
ATOM 2981 C ASP A 435 19.366 8.643 43.836 1.00 50.79 C
ATOM 2982 O ASP A 435 18.506 9.517 43.928 1.00 55.60 O
ATOM 2983 CB ASP A 435 21.184 8.551 45.498 1.00 39.29 C
ATOM 2984 CG ASP A 435 21.626 8.146 46.908 1.00 55.10 C
ATOM 2985 OD1 ASP A 435 20.760 7.857 47.772 1.00 47.61 O
ATOM 2986 OD2 ASP A 435 22.856 8.138 47.155 1.00 51.76 O
ATOM 2987 N GLU A 436 19.930 8.306 42.686 1.00 44.38 N
ATOM 2988 CA GLU A 436 19.488 8.866 41.429 1.00 48.33 C
ATOM 2989 C GLU A 436 18.000 8.567 41.222 1.00 51.63 C
ATOM 2990 O GLU A 436 17.208 9.446 40.867 1.00 52.47 O
ATOM 2991 CB GLU A 436 20.335 8.261 40.320 1.00 37.68 C
ATOM 2992 CG GLU A 436 19.801 8.470 38.946 1.00 47.77 C
ATOM 2993 CD GLU A 436 20.571 7.676 37.930 1.00 48.43 C
ATOM 2994 OE1 GLU A 436 21.671 7.181 38.282 1.00 45.98 O
ATOM 2995 OE2 GLU A 436 20.066 7.535 36.792 1.00 49.29 O
ATOM 2996 N TRP A 437 17.636 7.318 41.493 1.00 48.33 N
ATOM 2997 CA TRP A 437 16.269 6.829 41.343 1.00 47.72 C
ATOM 2998 C TRP A 437 15.285 7.519 42.286 1.00 48.62 C
ATOM 2999 O TRP A 437 14.201 7.950 41.878 1.00 53.95 O
ATOM 3000 CB TRP A 437 16.228 5.310 41.571 1.00 42.68 C
ATOM 3001 CG TRP A 437 14.877 4.732 41.382 1.00 41.03 C
ATOM 3002 CD1 TRP A 437 14.313 4.340 40.201 1.00 41.74 C
ATOM 3003 CD2 TRP A 437 13.887 4.508 42.394 1.00 42.93 C
ATOM 3004 NE1 TRP A 437 13.034 3.882 40.416 1.00 41.68 N
ATOM 3005 CE2 TRP A 437 12.746 3.975 41.758 1.00 40.86 C
ATOM 3006 CE3 TRP A 437 13.849 4.706 43.778 1.00 37.60 C
ATOM 3007 CZ2 TRP A 437 11.588 3.626 42.456 1.00 39.45 C
ATOM 3008 CZ3 TRP A 437 12.696 4.357 44.473 1.00 37.24 C
ATOM 3009 CH2 TRP A 437 11.583 3.825 43.812 1.00 37.98 C
ATOM 3010 N ILE A 438 15.667 7.603 43.551 1.00 47.58 N
ATOM 3011 CA ILE A 438 14.841 8.235 44.563 1.00 52.26 C
ATOM 3012 C ILE A 438 14.494 9.678 44.178 1.00 50.99 C
ATOM 3013 O ILE A 438 13.354 10.112 44.334 1.00 51.14 O
ATOM 3014 CB ILE A 438 15.539 8.134 45.937 1.00 54.67 C
ATOM 3015 CG1 ILE A 438 15.545 6.671 46.387 1.00 46.80 C
ATOM 3016 CG2 ILE A 438 14.850 9.005 46.967 1.00 54.62 C
ATOM 3017 CD1 ILE A 438 16.082 6.446 47.757 1.00 35.43 C
ATOM 3018 N SER A 439 15.472 10.394 43.632 1.00 48.55 N
ATOM 3019 CA SER A 439 15.267 11.769 43.185 1.00 55.00 C
ATOM 3020 C SER A 439 14.128 11.866 42.187 1.00 60.20 C
ATOM 3021 O SER A 439 13.203 12.662 42.373 1.00 65.86 O
ATOM 3022 CB SER A 439 16.533 12.322 42.552 1.00 50.20 C
ATOM 3023 OG SER A 439 17.552 12.423 43.521 1.00 51.39 O
ATOM 3024 N VAL A 440 14.209 11.052 41.134 1.00 57.18 N
ATOM 3025 CA VAL A 440 13.150 10.931 40.134 1.00 52.15 C
ATOM 3026 C VAL A 440 11.812 10.623 40.795 1.00 52.63 C
ATOM 3027 O VAL A 440 10.801 11.270 40.523 1.00 53.34 O
ATOM 3028 CB VAL A 440 13.460 9.787 39.139 1.00 49.58 C
ATOM 3029 CG1 VAL A 440 12.303 9.594 38.165 1.00 43.85 C
ATOM 3030 CG2 VAL A 440 14.768 10.046 38.393 1.00 42.41 C
ATOM 3031 N ARG A 441 11.818 9.626 41.673 1.00 53.47 N
ATOM 3032 CA ARG A 441 10.609 9.217 42.378 1.00 49.38 C
ATOM 3033 C ARG A 441 10.011 10.354 43.193 1.00 56.19 C
ATOM 3034 O ARG A 441 8.796 10.442 43.344 1.00 55.34 O
ATOM 3035 CB ARG A 441 10.896 8.017 43.280 1.00 49.72 C
ATOM 3036 CG ARG A 441 10.123 8.022 44.582 1.00 47.03 C
ATOM 3037 CD ARG A 441 9.584 6.661 44.906 1.00 39.60 C
ATOM 3038 NE ARG A 441 8.890 6.659 46.184 1.00 47.77 N
ATOM 3039 CZ ARG A 441 7.570 6.741 46.335 1.00 53.93 C
ATOM 3040 NH1 ARG A 441 6.776 6.823 45.280 1.00 55.80 N
ATOM 3041 NH2 ARG A 441 7.040 6.730 47.554 1.00 60.20 N
ATOM 3042 N ARG A 442 10.872 11.221 43.716 1.00 57.13 N
ATOM 3043 CA ARG A 442 10.440 12.350 44.531 1.00 57.29 C
ATOM 3044 C ARG A 442 9.796 13.440 43.688 1.00 59.73 C
ATOM 3045 O ARG A 442 8.856 14.103 44.130 1.00 65.65 O
ATOM 3046 CB ARG A 442 11.638 12.962 45.260 1.00 59.84 C
ATOM 3047 CG ARG A 442 12.186 12.126 46.400 1.00 66.72 C
ATOM 3048 CD ARG A 442 11.203 12.057 47.547 1.00 70.29 C
ATOM 3049 NE ARG A 442 11.295 10.801 48.289 1.00 74.55 N
ATOM 3050 CZ ARG A 442 12.284 10.489 49.124 1.00 82.87 C
ATOM 3051 NH1 ARG A 442 13.287 11.342 49.314 1.00 83.33 N
ATOM 3052 NH2 ARG A 442 12.278 9.321 49.762 1.00 69.04 N
ATOM 3053 N LYS A 443 10.324 13.645 42.485 1.00 51.70 N
ATOM 3054 CA LYS A 443 9.768 14.641 41.576 1.00 52.97 C
ATOM 3055 C LYS A 443 8.353 14.275 41.168 1.00 59.41 C
ATOM 3056 O LYS A 443 7.550 15.157 40.862 1.00 57.34 O
ATOM 3057 CB LYS A 443 10.626 14.819 40.313 1.00 43.63 C
ATOM 3058 CG LYS A 443 11.976 15.466 40.569 1.00 50.25 C
ATOM 3059 CD LYS A 443 12.611 15.994 39.288 1.00 53.91 C
ATOM 3060 CE LYS A 443 12.954 14.864 38.316 1.00 66.53 C
ATOM 3061 NZ LYS A 443 13.924 15.281 37.256 1.00 49.60 N
ATOM 3062 N VAL A 444 8.050 12.978 41.173 1.00 54.94 N
ATOM 3063 CA VAL A 444 6.820 12.482 40.558 1.00 57.85 C
ATOM 3064 C VAL A 444 5.763 12.104 41.586 1.00 51.36 C
ATOM 3065 O VAL A 444 4.571 12.071 41.291 1.00 61.54 O
ATOM 3066 CB VAL A 444 7.089 11.284 39.587 1.00 60.20 C
ATOM 3067 CG1 VAL A 444 7.176 9.951 40.341 1.00 42.88 C
ATOM 3068 CG2 VAL A 444 6.004 11.204 38.511 1.00 58.57 C
ATOM 3069 N ASP A 445 6.205 11.814 42.795 1.00 56.38 N
ATOM 3070 CA ASP A 445 5.292 11.520 43.888 1.00 57.58 C
ATOM 3071 C ASP A 445 5.812 12.221 45.147 1.00 62.68 C
ATOM 3072 O ASP A 445 6.352 11.577 46.040 1.00 62.40 O
ATOM 3073 CB ASP A 445 5.208 10.011 44.098 1.00 44.54 C
ATOM 3074 CG ASP A 445 4.265 9.625 45.215 1.00 56.75 C
ATOM 3075 OD1 ASP A 445 3.428 10.468 45.614 1.00 65.67 O
ATOM 3076 OD2 ASP A 445 4.365 8.473 45.699 1.00 54.74 O
ATOM 3077 N PRO A 446 5.666 13.555 45.209 1.00 65.31 N
ATOM 3078 CA PRO A 446 6.226 14.337 46.318 1.00 62.43 C
ATOM 3079 C PRO A 446 5.542 14.001 47.637 1.00 64.62 C
ATOM 3080 O PRO A 446 6.191 14.005 48.680 1.00 66.63 O
ATOM 3081 CB PRO A 446 5.896 15.784 45.929 1.00 67.60 C
ATOM 3082 CG PRO A 446 5.550 15.742 44.458 1.00 62.16 C
ATOM 3083 CD PRO A 446 4.921 14.402 44.263 1.00 65.49 C
ATOM 3084 N LEU A 447 4.250 13.686 47.573 1.00 65.38 N
ATOM 3085 CA LEU A 447 3.436 13.430 48.761 1.00 59.64 C
ATOM 3086 C LEU A 447 3.380 11.977 49.217 1.00 59.45 C
ATOM 3087 O LEU A 447 2.563 11.632 50.068 1.00 57.22 O
ATOM 3088 CB LEU A 447 2.004 13.885 48.499 1.00 52.55 C
ATOM 3089 CG LEU A 447 1.874 15.386 48.303 1.00 62.81 C
ATOM 3090 CD1 LEU A 447 0.446 15.723 47.899 1.00 68.00 C
ATOM 3091 CD2 LEU A 447 2.302 16.108 49.591 1.00 57.53 C
ATOM 3092 N ARG A 448 4.226 11.132 48.638 1.00 65.15 N
ATOM 3093 CA ARG A 448 4.249 9.690 48.929 1.00 63.37 C
ATOM 3094 C ARG A 448 2.891 8.979 48.777 1.00 62.50 C
ATOM 3095 O ARG A 448 2.454 8.213 49.648 1.00 64.98 O
ATOM 3096 CB ARG A 448 4.915 9.412 50.281 1.00 67.47 C
ATOM 3097 CG ARG A 448 6.413 9.693 50.270 1.00 68.77 C
ATOM 3098 CD ARG A 448 6.843 10.565 51.436 1.00 75.49 C
ATOM 3099 NE ARG A 448 8.096 10.076 52.014 1.00 88.83 N
ATOM 3100 CZ ARG A 448 9.294 10.627 51.819 1.00 86.99 C
ATOM 3101 NH1 ARG A 448 9.422 11.720 51.064 1.00 77.40 N
ATOM 3102 NH2 ARG A 448 10.366 10.084 52.396 1.00 71.51 N
ATOM 3103 N VAL A 449 2.250 9.231 47.640 1.00 59.17 N
ATOM 3104 CA VAL A 449 0.974 8.624 47.299 1.00 55.22 C
ATOM 3105 C VAL A 449 1.127 7.120 47.030 1.00 56.82 C
ATOM 3106 O VAL A 449 0.266 6.321 47.392 1.00 53.98 O
ATOM 3107 CB VAL A 449 0.374 9.346 46.085 1.00 61.38 C
ATOM 3108 CG1 VAL A 449 -0.930 8.696 45.655 1.00 55.08 C
ATOM 3109 CG2 VAL A 449 0.189 10.831 46.412 1.00 54.84 C
ATOM 3110 N PHE A 450 2.241 6.732 46.411 1.00 55.19 N
ATOM 3111 CA PHE A 450 2.525 5.314 46.165 1.00 54.29 C
ATOM 3112 C PHE A 450 3.520 4.748 47.170 1.00 49.45 C
ATOM 3113 O PHE A 450 4.589 5.316 47.389 1.00 49.70 O
ATOM 3114 CB PHE A 450 3.014 5.095 44.724 1.00 51.16 C
ATOM 3115 CG PHE A 450 2.056 5.604 43.700 1.00 50.16 C
ATOM 3116 CD1 PHE A 450 0.925 4.871 43.372 1.00 46.20 C
ATOM 3117 CD2 PHE A 450 2.254 6.833 43.101 1.00 49.06 C
ATOM 3118 CE1 PHE A 450 0.020 5.354 42.463 1.00 44.67 C
ATOM 3119 CE2 PHE A 450 1.346 7.320 42.179 1.00 50.04 C
ATOM 3120 CZ PHE A 450 0.228 6.582 41.869 1.00 46.90 C
ATOM 3121 N ALA A 451 3.161 3.616 47.762 1.00 42.78 N
ATOM 3122 CA ALA A 451 3.901 3.074 48.882 1.00 45.82 C
ATOM 3123 C ALA A 451 3.628 1.590 49.024 1.00 50.26 C
ATOM 3124 O ALA A 451 2.566 1.115 48.634 1.00 50.10 O
ATOM 3125 CB ALA A 451 3.489 3.787 50.151 1.00 44.59 C
ATOM 3126 N SER A 452 4.583 0.865 49.604 1.00 47.79 N
ATOM 3127 CA SER A 452 4.427 -0.560 49.863 1.00 50.15 C
ATOM 3128 C SER A 452 5.292 -1.010 51.043 1.00 51.57 C
ATOM 3129 O SER A 452 6.153 -0.266 51.517 1.00 49.45 O
ATOM 3130 CB SER A 452 4.823 -1.365 48.630 1.00 46.29 C
ATOM 3131 OG SER A 452 6.232 -1.428 48.503 1.00 49.41 O
ATOM 3132 N ASP A 453 5.054 -2.233 51.503 1.00 44.33 N
ATOM 3133 CA ASP A 453 5.891 -2.849 52.510 1.00 47.89 C
ATOM 3134 C ASP A 453 7.363 -2.694 52.145 1.00 50.12 C
ATOM 3135 O ASP A 453 8.165 -2.181 52.930 1.00 53.96 O
ATOM 3136 CB ASP A 453 5.535 -4.329 52.654 1.00 37.17 C
ATOM 3137 CG ASP A 453 4.263 -4.543 53.454 1.00 48.10 C
ATOM 3138 OD1 ASP A 453 3.542 -3.542 53.681 1.00 44.93 O
ATOM 3139 OD2 ASP A 453 3.995 -5.704 53.863 1.00 41.03 O
ATOM 3140 N MET A 454 7.709 -3.106 50.934 1.00 52.52 N
ATOM 3141 CA MET A 454 9.097 -3.044 50.509 1.00 49.77 C
ATOM 3142 C MET A 454 9.673 -1.626 50.514 1.00 48.94 C
ATOM 3143 O MET A 454 10.790 -1.417 50.978 1.00 48.26 O
ATOM 3144 CB MET A 454 9.296 -3.678 49.138 1.00 43.77 C
ATOM 3145 CG MET A 454 10.639 -3.308 48.552 1.00 43.96 C
ATOM 3146 SD MET A 454 10.998 -3.990 46.945 1.00 62.78 S
ATOM 3147 CE MET A 454 10.658 -5.737 47.229 1.00 51.74 C
ATOM 3148 N ALA A 455 8.918 -0.659 49.998 1.00 49.60 N
ATOM 3149 CA ALA A 455 9.381 0.722 49.968 1.00 46.86 C
ATOM 3150 C ALA A 455 9.771 1.220 51.376 1.00 51.32 C
ATOM 3151 O ALA A 455 10.746 1.960 51.563 1.00 45.02 O
ATOM 3152 CB ALA A 455 8.307 1.601 49.381 1.00 44.37 C
ATOM 3153 N ARG A 456 8.996 0.808 52.366 1.00 46.79 N
ATOM 3154 CA ARG A 456 9.256 1.240 53.724 1.00 52.03 C
ATOM 3155 C ARG A 456 10.457 0.482 54.305 1.00 54.03 C
ATOM 3156 O ARG A 456 11.354 1.091 54.892 1.00 50.43 O
ATOM 3157 CB ARG A 456 7.985 1.120 54.578 1.00 42.34 C
ATOM 3158 CG ARG A 456 6.968 2.236 54.238 1.00 53.54 C
ATOM 3159 CD ARG A 456 5.673 2.141 55.031 1.00 50.89 C
ATOM 3160 NE ARG A 456 4.963 0.891 54.780 1.00 50.20 N
ATOM 3161 CZ ARG A 456 3.864 0.784 54.037 1.00 56.01 C
ATOM 3162 NH1 ARG A 456 3.320 1.863 53.480 1.00 46.62 N
ATOM 3163 NH2 ARG A 456 3.301 -0.409 53.866 1.00 54.38 N
ATOM 3164 N ARG A 457 10.480 -0.834 54.093 1.00 49.06 N
ATOM 3165 CA ARG A 457 11.585 -1.690 54.511 1.00 40.42 C
ATOM 3166 C ARG A 457 12.927 -1.290 53.893 1.00 46.50 C
ATOM 3167 O ARG A 457 13.944 -1.237 54.590 1.00 54.51 O
ATOM 3168 CB ARG A 457 11.265 -3.166 54.218 1.00 36.85 C
ATOM 3169 CG ARG A 457 12.369 -4.159 54.602 1.00 34.13 C
ATOM 3170 CD ARG A 457 11.928 -5.618 54.428 1.00 37.63 C
ATOM 3171 NE ARG A 457 11.529 -5.939 53.051 1.00 45.93 N
ATOM 3172 CZ ARG A 457 12.378 -6.308 52.094 1.00 52.17 C
ATOM 3173 NH1 ARG A 457 13.671 -6.401 52.369 1.00 53.82 N
ATOM 3174 NH2 ARG A 457 11.949 -6.573 50.859 1.00 52.26 N
ATOM 3175 N LEU A 458 12.937 -1.000 52.597 1.00 47.44 N
ATOM 3176 CA LEU A 458 14.183 -0.677 51.910 1.00 42.40 C
ATOM 3177 C LEU A 458 14.429 0.822 51.846 1.00 47.96 C
ATOM 3178 O LEU A 458 15.404 1.281 51.231 1.00 44.24 O
ATOM 3179 CB LEU A 458 14.201 -1.280 50.509 1.00 35.77 C
ATOM 3180 CG LEU A 458 14.066 -2.804 50.441 1.00 39.72 C
ATOM 3181 CD1 LEU A 458 14.209 -3.285 49.010 1.00 33.98 C
ATOM 3182 CD2 LEU A 458 15.080 -3.492 51.342 1.00 38.17 C
ATOM 3183 N GLU A 459 13.556 1.577 52.502 1.00 44.78 N
ATOM 3184 CA GLU A 459 13.668 3.029 52.520 1.00 55.04 C
ATOM 3185 C GLU A 459 13.781 3.580 51.111 1.00 52.56 C
ATOM 3186 O GLU A 459 14.758 4.250 50.769 1.00 51.55 O
ATOM 3187 CB GLU A 459 14.837 3.477 53.400 1.00 54.90 C
ATOM 3188 CG GLU A 459 14.448 3.609 54.872 1.00 60.93 C
ATOM 3189 CD GLU A 459 15.584 3.303 55.822 1.00 58.98 C
ATOM 3190 OE1 GLU A 459 16.598 4.033 55.795 1.00 58.48 O
ATOM 3191 OE2 GLU A 459 15.453 2.328 56.593 1.00 55.25 O
ATOM 3192 N LEU A 460 12.761 3.267 50.310 1.00 57.06 N
ATOM 3193 CA LEU A 460 12.648 3.695 48.924 1.00 57.02 C
ATOM 3194 C LEU A 460 11.486 4.677 48.843 1.00 61.40 C
ATOM 3195 O LEU A 460 11.314 5.401 47.853 1.00 58.24 O
ATOM 3196 CB LEU A 460 12.395 2.480 48.029 1.00 41.98 C
ATOM 3197 CG LEU A 460 13.545 1.466 47.943 1.00 41.02 C
ATOM 3198 CD1 LEU A 460 13.201 0.322 47.016 1.00 43.58 C
ATOM 3199 CD2 LEU A 460 14.829 2.129 47.463 1.00 39.23 C
ATOM 3200 N LEU A 461 10.703 4.686 49.918 1.00 55.32 N
ATOM 3201 CA LEU A 461 9.590 5.598 50.101 1.00 59.74 C
ATOM 3202 C LEU A 461 10.006 7.052 49.905 1.00 69.03 C
ATOM 3203 O LEU A 461 9.361 7.821 49.176 1.00 67.02 O
ATOM 3204 CB LEU A 461 9.090 5.418 51.519 1.00 53.59 C
ATOM 3205 CG LEU A 461 7.675 5.852 51.855 1.00 67.23 C
ATOM 3206 CD1 LEU A 461 6.698 4.980 51.096 1.00 52.71 C
ATOM 3207 CD2 LEU A 461 7.461 5.764 53.374 1.00 71.68 C
ATOM 3208 OXT LEU A 461 11.001 7.472 50.508 1.00 64.80 O
TER 3209 LEU A 461
ATOM 3210 N THR B 7 7.759 -21.767 -12.841 1.00 92.02 N
ATOM 3211 CA THR B 7 7.106 -21.411 -11.587 1.00 96.33 C
ATOM 3212 C THR B 7 5.713 -22.044 -11.483 1.00 95.51 C
ATOM 3213 O THR B 7 5.232 -22.333 -10.382 1.00 93.05 O
ATOM 3214 CB THR B 7 6.993 -19.876 -11.430 1.00 81.53 C
ATOM 3215 N THR B 8 5.072 -22.260 -12.633 1.00 99.09 N
ATOM 3216 CA THR B 8 3.727 -22.852 -12.676 1.00 91.91 C
ATOM 3217 C THR B 8 3.768 -24.367 -12.892 1.00 87.75 C
ATOM 3218 O THR B 8 4.727 -24.898 -13.451 1.00 89.42 O
ATOM 3219 CB THR B 8 2.805 -22.218 -13.772 1.00 88.02 C
ATOM 3220 OG1 THR B 8 2.987 -22.897 -15.024 1.00 89.32 O
ATOM 3221 CG2 THR B 8 3.061 -20.707 -13.937 1.00 77.87 C
ATOM 3222 N THR B 9 2.715 -25.048 -12.449 1.00 86.86 N
ATOM 3223 CA THR B 9 2.597 -26.497 -12.598 1.00 86.67 C
ATOM 3224 C THR B 9 1.249 -26.869 -13.212 1.00 91.26 C
ATOM 3225 O THR B 9 0.200 -26.551 -12.650 1.00 89.66 O
ATOM 3226 CB THR B 9 2.725 -27.220 -11.236 1.00 83.93 C
ATOM 3227 OG1 THR B 9 4.059 -27.077 -10.738 1.00 80.19 O
ATOM 3228 CG2 THR B 9 2.390 -28.702 -11.368 1.00 79.93 C
ATOM 3229 N ALA B 10 1.280 -27.533 -14.366 1.00 93.16 N
ATOM 3230 CA ALA B 10 0.062 -28.055 -14.983 1.00 94.24 C
ATOM 3231 C ALA B 10 -0.657 -29.027 -14.029 1.00 94.68 C
ATOM 3232 O ALA B 10 -0.152 -30.117 -13.738 1.00 85.76 O
ATOM 3233 CB ALA B 10 0.388 -28.734 -16.320 1.00 95.87 C
ATOM 3234 N THR B 11 -1.827 -28.619 -13.535 1.00 92.18 N
ATOM 3235 CA THR B 11 -2.579 -29.415 -12.561 1.00 91.89 C
ATOM 3236 C THR B 11 -4.003 -29.673 -13.058 1.00 84.17 C
ATOM 3237 O THR B 11 -4.570 -28.868 -13.801 1.00 81.13 O
ATOM 3238 CB THR B 11 -2.619 -28.724 -11.151 1.00 95.48 C
ATOM 3239 OG1 THR B 11 -1.289 -28.409 -10.710 1.00 85.24 O
ATOM 3240 CG2 THR B 11 -3.300 -29.605 -10.099 1.00 88.27 C
ATOM 3241 N ARG B 12 -4.563 -30.809 -12.654 1.00 82.57 N
ATOM 3242 CA ARG B 12 -5.941 -31.168 -12.968 1.00 94.09 C
ATOM 3243 C ARG B 12 -6.852 -30.720 -11.830 1.00 95.55 C
ATOM 3244 O ARG B 12 -6.746 -31.228 -10.708 1.00 97.16 O
ATOM 3245 CB ARG B 12 -6.048 -32.685 -13.138 1.00 97.71 C
ATOM 3246 CG ARG B 12 -7.459 -33.206 -13.338 1.00100.36 C
ATOM 3247 CD ARG B 12 -7.536 -34.671 -12.932 1.00110.70 C
ATOM 3248 NE ARG B 12 -8.611 -35.400 -13.604 1.00114.87 N
ATOM 3249 CZ ARG B 12 -9.848 -35.519 -13.133 1.00107.71 C
ATOM 3250 NH1 ARG B 12 -10.180 -34.944 -11.984 1.00100.56 N
ATOM 3251 NH2 ARG B 12 -10.757 -36.208 -13.812 1.00101.11 N
ATOM 3252 N LEU B 13 -7.752 -29.781 -12.120 1.00 88.89 N
ATOM 3253 CA LEU B 13 -8.565 -29.155 -11.078 1.00 87.43 C
ATOM 3254 C LEU B 13 -10.057 -29.492 -11.177 1.00 86.83 C
ATOM 3255 O LEU B 13 -10.607 -29.625 -12.274 1.00 86.77 O
ATOM 3256 CB LEU B 13 -8.373 -27.630 -11.089 1.00 80.48 C
ATOM 3257 CG LEU B 13 -6.937 -27.087 -11.033 1.00 83.58 C
ATOM 3258 CD1 LEU B 13 -6.431 -26.772 -12.424 1.00 77.93 C
ATOM 3259 CD2 LEU B 13 -6.820 -25.853 -10.134 1.00 79.40 C
ATOM 3260 N THR B 14 -10.700 -29.648 -10.019 1.00 83.48 N
ATOM 3261 CA THR B 14 -12.160 -29.728 -9.936 1.00 81.81 C
ATOM 3262 C THR B 14 -12.624 -28.883 -8.756 1.00 82.04 C
ATOM 3263 O THR B 14 -11.814 -28.498 -7.905 1.00 84.78 O
ATOM 3264 CB THR B 14 -12.659 -31.157 -9.684 1.00 85.35 C
ATOM 3265 OG1 THR B 14 -12.439 -31.500 -8.305 1.00 79.38 O
ATOM 3266 CG2 THR B 14 -11.950 -32.153 -10.592 1.00 83.60 C
ATOM 3267 N GLY B 15 -13.922 -28.601 -8.695 1.00 77.57 N
ATOM 3268 CA GLY B 15 -14.493 -28.004 -7.504 1.00 62.76 C
ATOM 3269 C GLY B 15 -14.585 -29.072 -6.423 1.00 71.00 C
ATOM 3270 O GLY B 15 -13.974 -30.142 -6.531 1.00 76.06 O
ATOM 3271 N TRP B 16 -15.364 -28.798 -5.381 1.00 64.99 N
ATOM 3272 CA TRP B 16 -15.552 -29.759 -4.300 1.00 66.93 C
ATOM 3273 C TRP B 16 -16.467 -30.911 -4.726 1.00 71.83 C
ATOM 3274 O TRP B 16 -16.564 -31.935 -4.038 1.00 75.49 O
ATOM 3275 CB TRP B 16 -16.129 -29.055 -3.068 1.00 68.39 C
ATOM 3276 CG TRP B 16 -15.880 -29.787 -1.778 1.00 70.68 C
ATOM 3277 CD1 TRP B 16 -16.808 -30.426 -0.992 1.00 76.01 C
ATOM 3278 CD2 TRP B 16 -14.617 -29.960 -1.127 1.00 67.80 C
ATOM 3279 NE1 TRP B 16 -16.195 -30.976 0.114 1.00 74.53 N
ATOM 3280 CE2 TRP B 16 -14.849 -30.709 0.052 1.00 80.87 C
ATOM 3281 CE3 TRP B 16 -13.309 -29.557 -1.426 1.00 65.61 C
ATOM 3282 CZ2 TRP B 16 -13.818 -31.064 0.932 1.00 79.73 C
ATOM 3283 CZ3 TRP B 16 -12.284 -29.911 -0.551 1.00 67.51 C
ATOM 3284 CH2 TRP B 16 -12.547 -30.655 0.614 1.00 70.27 C
ATOM 3285 N GLY B 17 -17.143 -30.734 -5.858 1.00 78.26 N
ATOM 3286 CA GLY B 17 -18.062 -31.734 -6.372 1.00 80.27 C
ATOM 3287 C GLY B 17 -17.317 -32.837 -7.096 1.00 87.50 C
ATOM 3288 O GLY B 17 -17.920 -33.827 -7.524 1.00 91.10 O
ATOM 3289 N ARG B 18 -15.999 -32.663 -7.220 1.00 84.65 N
ATOM 3290 CA ARG B 18 -15.122 -33.627 -7.888 1.00 86.45 C
ATOM 3291 C ARG B 18 -15.578 -33.880 -9.325 1.00 91.83 C
ATOM 3292 O ARG B 18 -15.457 -34.997 -9.831 1.00 92.00 O
ATOM 3293 CB ARG B 18 -15.068 -34.969 -7.128 1.00 86.66 C
ATOM 3294 CG ARG B 18 -15.143 -34.884 -5.606 1.00 85.67 C
ATOM 3295 CD ARG B 18 -13.780 -35.058 -4.938 1.00 95.32 C
ATOM 3296 NE ARG B 18 -13.870 -34.979 -3.476 1.00103.29 N
ATOM 3297 CZ ARG B 18 -13.864 -33.841 -2.781 1.00 93.02 C
ATOM 3298 NH1 ARG B 18 -13.774 -32.677 -3.413 1.00 85.81 N
ATOM 3299 NH2 ARG B 18 -13.948 -33.862 -1.454 1.00 88.71 N
ATOM 3300 N THR B 19 -16.113 -32.851 -9.975 1.00 92.74 N
ATOM 3301 CA THR B 19 -16.640 -33.018 -11.324 1.00 88.44 C
ATOM 3302 C THR B 19 -16.260 -31.859 -12.247 1.00 89.92 C
ATOM 3303 O THR B 19 -15.771 -30.822 -11.792 1.00 91.45 O
ATOM 3304 CB THR B 19 -18.167 -33.213 -11.309 1.00 96.23 C
ATOM 3305 OG1 THR B 19 -18.567 -33.966 -12.464 1.00107.10 O
ATOM 3306 CG2 THR B 19 -18.883 -31.862 -11.283 1.00 87.96 C
ATOM 3307 N ALA B 20 -16.495 -32.058 -13.543 1.00 89.45 N
ATOM 3308 CA ALA B 20 -16.111 -31.108 -14.591 1.00 88.41 C
ATOM 3309 C ALA B 20 -14.626 -30.723 -14.580 1.00 90.78 C
ATOM 3310 O ALA B 20 -14.299 -29.530 -14.652 1.00 89.69 O
ATOM 3311 CB ALA B 20 -16.985 -29.860 -14.523 1.00 90.04 C
ATOM 3312 N PRO B 21 -13.724 -31.726 -14.528 1.00 87.83 N
ATOM 3313 CA PRO B 21 -12.294 -31.441 -14.343 1.00 84.44 C
ATOM 3314 C PRO B 21 -11.673 -30.736 -15.543 1.00 86.28 C
ATOM 3315 O PRO B 21 -12.096 -30.964 -16.675 1.00 87.49 O
ATOM 3316 CB PRO B 21 -11.685 -32.833 -14.211 1.00 89.79 C
ATOM 3317 CG PRO B 21 -12.574 -33.692 -15.034 1.00 83.36 C
ATOM 3318 CD PRO B 21 -13.958 -33.152 -14.827 1.00 78.46 C
ATOM 3319 N SER B 22 -10.678 -29.891 -15.290 1.00 86.55 N
ATOM 3320 CA SER B 22 -9.990 -29.161 -16.354 1.00 84.71 C
ATOM 3321 C SER B 22 -8.515 -28.975 -15.984 1.00 89.07 C
ATOM 3322 O SER B 22 -8.162 -28.961 -14.798 1.00 91.83 O
ATOM 3323 CB SER B 22 -10.655 -27.802 -16.621 1.00 77.00 C
ATOM 3324 OG SER B 22 -10.229 -26.819 -15.686 1.00 86.76 O
ATOM 3325 N VAL B 23 -7.655 -28.848 -16.995 1.00 85.99 N
ATOM 3326 CA VAL B 23 -6.214 -28.702 -16.762 1.00 88.20 C
ATOM 3327 C VAL B 23 -5.776 -27.245 -16.879 1.00 85.11 C
ATOM 3328 O VAL B 23 -6.028 -26.586 -17.908 1.00 70.54 O
ATOM 3329 CB VAL B 23 -5.359 -29.560 -17.746 1.00 86.66 C
ATOM 3330 CG1 VAL B 23 -3.872 -29.318 -17.518 1.00 84.64 C
ATOM 3331 CG2 VAL B 23 -5.667 -31.035 -17.584 1.00 89.28 C
ATOM 3332 N ALA B 24 -5.124 -26.749 -15.824 1.00 80.86 N
ATOM 3333 CA ALA B 24 -4.571 -25.399 -15.839 1.00 78.14 C
ATOM 3334 C ALA B 24 -3.157 -25.322 -15.250 1.00 77.45 C
ATOM 3335 O ALA B 24 -2.685 -26.254 -14.594 1.00 71.55 O
ATOM 3336 CB ALA B 24 -5.509 -24.429 -15.139 1.00 64.53 C
ATOM 3337 N ASN B 25 -2.489 -24.203 -15.509 1.00 77.04 N
ATOM 3338 CA ASN B 25 -1.168 -23.944 -14.955 1.00 81.82 C
ATOM 3339 C ASN B 25 -1.282 -23.233 -13.610 1.00 80.95 C
ATOM 3340 O ASN B 25 -1.628 -22.053 -13.540 1.00 74.43 O
ATOM 3341 CB ASN B 25 -0.326 -23.126 -15.936 1.00 88.24 C
ATOM 3342 CG ASN B 25 0.002 -23.897 -17.213 1.00 97.20 C
ATOM 3343 OD1 ASN B 25 0.301 -25.097 -17.176 1.00 92.11 O
ATOM 3344 ND2 ASN B 25 -0.057 -23.206 -18.351 1.00 87.51 N
ATOM 3345 N VAL B 26 -0.983 -23.969 -12.548 1.00 75.60 N
ATOM 3346 CA VAL B 26 -1.213 -23.498 -11.193 1.00 74.00 C
ATOM 3347 C VAL B 26 0.013 -22.852 -10.534 1.00 74.39 C
ATOM 3348 O VAL B 26 0.898 -23.546 -10.028 1.00 74.94 O
ATOM 3349 CB VAL B 26 -1.726 -24.651 -10.321 1.00 76.30 C
ATOM 3350 CG1 VAL B 26 -1.968 -24.173 -8.909 1.00 71.64 C
ATOM 3351 CG2 VAL B 26 -3.003 -25.216 -10.929 1.00 78.02 C
ATOM 3352 N LEU B 27 0.053 -21.520 -10.551 1.00 72.58 N
ATOM 3353 CA LEU B 27 1.078 -20.754 -9.839 1.00 67.64 C
ATOM 3354 C LEU B 27 0.814 -20.807 -8.334 1.00 72.98 C
ATOM 3355 O LEU B 27 -0.317 -20.585 -7.898 1.00 71.97 O
ATOM 3356 CB LEU B 27 1.083 -19.295 -10.310 1.00 63.36 C
ATOM 3357 CG LEU B 27 1.967 -18.340 -9.501 1.00 67.13 C
ATOM 3358 CD1 LEU B 27 3.382 -18.856 -9.506 1.00 75.71 C
ATOM 3359 CD2 LEU B 27 1.929 -16.916 -10.042 1.00 62.05 C
ATOM 3360 N ARG B 28 1.847 -21.111 -7.547 1.00 69.63 N
ATOM 3361 CA ARG B 28 1.733 -21.124 -6.089 1.00 68.34 C
ATOM 3362 C ARG B 28 2.901 -20.386 -5.460 1.00 67.97 C
ATOM 3363 O ARG B 28 3.959 -20.978 -5.252 1.00 73.01 O
ATOM 3364 CB ARG B 28 1.729 -22.567 -5.554 1.00 68.61 C
ATOM 3365 CG ARG B 28 0.368 -23.099 -5.138 1.00 73.32 C
ATOM 3366 CD ARG B 28 0.440 -24.485 -4.491 1.00 78.88 C
ATOM 3367 NE ARG B 28 0.919 -24.462 -3.104 1.00 89.29 N
ATOM 3368 CZ ARG B 28 0.149 -24.635 -2.025 1.00 89.39 C
ATOM 3369 NH1 ARG B 28 -1.159 -24.840 -2.151 1.00 78.44 N
ATOM 3370 NH2 ARG B 28 0.686 -24.602 -0.808 1.00 80.11 N
ATOM 3371 N THR B 29 2.728 -19.105 -5.152 1.00 60.46 N
ATOM 3372 CA THR B 29 3.802 -18.357 -4.489 1.00 70.10 C
ATOM 3373 C THR B 29 3.303 -17.461 -3.352 1.00 71.75 C
ATOM 3374 O THR B 29 2.291 -16.766 -3.513 1.00 73.46 O
ATOM 3375 CB THR B 29 4.628 -17.513 -5.497 1.00 73.10 C
ATOM 3376 OG1 THR B 29 5.630 -16.760 -4.798 1.00 69.53 O
ATOM 3377 CG2 THR B 29 3.731 -16.557 -6.268 1.00 74.42 C
ATOM 3378 N PRO B 30 3.997 -17.492 -2.192 1.00 67.81 N
ATOM 3379 CA PRO B 30 3.744 -16.541 -1.101 1.00 62.59 C
ATOM 3380 C PRO B 30 4.186 -15.131 -1.455 1.00 59.61 C
ATOM 3381 O PRO B 30 3.981 -14.195 -0.677 1.00 53.02 O
ATOM 3382 CB PRO B 30 4.609 -17.067 0.044 1.00 63.40 C
ATOM 3383 CG PRO B 30 4.768 -18.525 -0.233 1.00 71.71 C
ATOM 3384 CD PRO B 30 4.817 -18.626 -1.743 1.00 77.98 C
ATOM 3385 N ASP B 31 4.780 -14.978 -2.630 1.00 57.46 N
ATOM 3386 CA ASP B 31 5.385 -13.719 -3.021 1.00 58.95 C
ATOM 3387 C ASP B 31 4.447 -12.907 -3.928 1.00 67.07 C
ATOM 3388 O ASP B 31 4.241 -13.244 -5.099 1.00 65.00 O
ATOM 3389 CB ASP B 31 6.735 -14.021 -3.685 1.00 61.21 C
ATOM 3390 CG ASP B 31 7.464 -12.779 -4.138 1.00 78.46 C
ATOM 3391 OD1 ASP B 31 7.180 -11.685 -3.595 1.00 83.13 O
ATOM 3392 OD2 ASP B 31 8.332 -12.904 -5.039 1.00 80.82 O
ATOM 3393 N ALA B 32 3.882 -11.837 -3.369 1.00 58.86 N
ATOM 3394 CA ALA B 32 2.973 -10.960 -4.109 1.00 61.08 C
ATOM 3395 C ALA B 32 3.591 -10.415 -5.383 1.00 67.67 C
ATOM 3396 O ALA B 32 2.887 -10.022 -6.305 1.00 80.60 O
ATOM 3397 CB ALA B 32 2.509 -9.808 -3.232 1.00 57.02 C
ATOM 3398 N GLU B 33 4.912 -10.381 -5.432 1.00 70.92 N
ATOM 3399 CA GLU B 33 5.605 -9.868 -6.602 1.00 74.09 C
ATOM 3400 C GLU B 33 5.520 -10.827 -7.772 1.00 68.80 C
ATOM 3401 O GLU B 33 5.281 -10.417 -8.895 1.00 73.82 O
ATOM 3402 CB GLU B 33 7.068 -9.576 -6.267 1.00 82.87 C
ATOM 3403 CG GLU B 33 7.222 -8.337 -5.420 1.00 89.88 C
ATOM 3404 CD GLU B 33 6.266 -7.236 -5.864 1.00100.22 C
ATOM 3405 OE1 GLU B 33 6.331 -6.829 -7.052 1.00 95.84 O
ATOM 3406 OE2 GLU B 33 5.439 -6.796 -5.030 1.00 94.10 O
ATOM 3407 N MET B 34 5.728 -12.108 -7.505 1.00 70.46 N
ATOM 3408 CA MET B 34 5.617 -13.116 -8.547 1.00 74.87 C
ATOM 3409 C MET B 34 4.192 -13.134 -9.096 1.00 76.07 C
ATOM 3410 O MET B 34 3.970 -13.352 -10.292 1.00 71.02 O
ATOM 3411 CB MET B 34 6.034 -14.501 -8.030 1.00 73.50 C
ATOM 3412 CG MET B 34 7.506 -14.622 -7.599 1.00 76.86 C
ATOM 3413 SD MET B 34 8.714 -14.220 -8.885 1.00 97.64 S
ATOM 3414 CE MET B 34 9.039 -12.472 -8.590 1.00 81.59 C
ATOM 3415 N ILE B 35 3.234 -12.873 -8.214 1.00 74.64 N
ATOM 3416 CA ILE B 35 1.828 -12.835 -8.585 1.00 66.38 C
ATOM 3417 C ILE B 35 1.492 -11.658 -9.501 1.00 64.78 C
ATOM 3418 O ILE B 35 0.935 -11.867 -10.573 1.00 70.57 O
ATOM 3419 CB ILE B 35 0.931 -12.882 -7.333 1.00 67.14 C
ATOM 3420 CG1 ILE B 35 0.923 -14.320 -6.784 1.00 64.46 C
ATOM 3421 CG2 ILE B 35 -0.470 -12.388 -7.664 1.00 66.16 C
ATOM 3422 CD1 ILE B 35 0.357 -14.487 -5.402 1.00 60.22 C
ATOM 3423 N VAL B 36 1.851 -10.438 -9.105 1.00 62.65 N
ATOM 3424 CA VAL B 36 1.580 -9.266 -9.940 1.00 65.26 C
ATOM 3425 C VAL B 36 2.214 -9.389 -11.326 1.00 76.26 C
ATOM 3426 O VAL B 36 1.631 -8.970 -12.334 1.00 77.91 O
ATOM 3427 CB VAL B 36 2.022 -7.941 -9.273 1.00 63.31 C
ATOM 3428 CG1 VAL B 36 3.489 -7.960 -8.971 1.00 83.39 C
ATOM 3429 CG2 VAL B 36 1.700 -6.749 -10.165 1.00 68.93 C
ATOM 3430 N LYS B 37 3.393 -9.996 -11.381 1.00 77.19 N
ATOM 3431 CA LYS B 37 4.117 -10.099 -12.638 1.00 78.65 C
ATOM 3432 C LYS B 37 3.651 -11.288 -13.486 1.00 74.10 C
ATOM 3433 O LYS B 37 3.866 -11.303 -14.694 1.00 79.28 O
ATOM 3434 CB LYS B 37 5.641 -10.077 -12.400 1.00 79.96 C
ATOM 3435 CG LYS B 37 6.424 -11.251 -12.982 1.00 89.43 C
ATOM 3436 CD LYS B 37 6.548 -12.394 -11.983 1.00 83.14 C
ATOM 3437 N ALA B 38 2.994 -12.267 -12.865 1.00 70.91 N
ATOM 3438 CA ALA B 38 2.409 -13.374 -13.625 1.00 66.54 C
ATOM 3439 C ALA B 38 1.115 -12.915 -14.290 1.00 73.19 C
ATOM 3440 O ALA B 38 0.698 -13.461 -15.311 1.00 70.72 O
ATOM 3441 CB ALA B 38 2.165 -14.583 -12.742 1.00 49.76 C
ATOM 3442 N VAL B 39 0.499 -11.901 -13.696 1.00 69.28 N
ATOM 3443 CA VAL B 39 -0.686 -11.262 -14.241 1.00 72.37 C
ATOM 3444 C VAL B 39 -0.311 -10.384 -15.425 1.00 76.39 C
ATOM 3445 O VAL B 39 -0.983 -10.381 -16.461 1.00 79.98 O
ATOM 3446 CB VAL B 39 -1.356 -10.399 -13.166 1.00 64.28 C
ATOM 3447 CG1 VAL B 39 -2.308 -9.386 -13.790 1.00 55.74 C
ATOM 3448 CG2 VAL B 39 -2.061 -11.294 -12.152 1.00 61.06 C
ATOM 3449 N ALA B 40 0.773 -9.636 -15.263 1.00 79.80 N
ATOM 3450 CA ALA B 40 1.297 -8.818 -16.346 1.00 80.79 C
ATOM 3451 C ALA B 40 1.756 -9.698 -17.503 1.00 82.74 C
ATOM 3452 O ALA B 40 1.740 -9.265 -18.654 1.00 82.56 O
ATOM 3453 CB ALA B 40 2.437 -7.949 -15.855 1.00 76.15 C
ATOM 3454 N ARG B 41 2.153 -10.932 -17.188 1.00 77.69 N
ATOM 3455 CA ARG B 41 2.600 -11.900 -18.195 1.00 79.49 C
ATOM 3456 C ARG B 41 1.431 -12.605 -18.917 1.00 87.31 C
ATOM 3457 O ARG B 41 1.620 -13.293 -19.930 1.00 90.37 O
ATOM 3458 CB ARG B 41 3.615 -12.889 -17.593 1.00 75.55 C
ATOM 3459 CG ARG B 41 3.310 -14.371 -17.789 1.00 76.53 C
ATOM 3460 CD ARG B 41 4.561 -15.141 -18.202 1.00 67.55 C
ATOM 3461 N VAL B 42 0.217 -12.397 -18.421 1.00 88.21 N
ATOM 3462 CA VAL B 42 -0.964 -12.884 -19.123 1.00 86.10 C
ATOM 3463 C VAL B 42 -1.603 -11.737 -19.911 1.00 86.22 C
ATOM 3464 O VAL B 42 -2.279 -11.961 -20.912 1.00 91.98 O
ATOM 3465 CB VAL B 42 -1.980 -13.563 -18.168 1.00 82.97 C
ATOM 3466 CG1 VAL B 42 -3.256 -13.941 -18.907 1.00 78.09 C
ATOM 3467 CG2 VAL B 42 -1.369 -14.807 -17.535 1.00 74.57 C
ATOM 3468 N ALA B 43 -1.335 -10.506 -19.482 1.00 79.91 N
ATOM 3469 CA ALA B 43 -1.946 -9.317 -20.080 1.00 88.31 C
ATOM 3470 C ALA B 43 -1.327 -8.851 -21.405 1.00104.92 C
ATOM 3471 O ALA B 43 -1.967 -8.118 -22.164 1.00103.56 O
ATOM 3472 CB ALA B 43 -1.947 -8.168 -19.079 1.00 80.18 C
ATOM 3473 N GLU B 44 -0.086 -9.250 -21.678 1.00108.02 N
ATOM 3474 CA GLU B 44 0.578 -8.841 -22.918 1.00110.51 C
ATOM 3475 C GLU B 44 0.442 -9.919 -23.995 1.00112.56 C
ATOM 3476 O GLU B 44 0.688 -9.667 -25.174 1.00116.04 O
ATOM 3477 CB GLU B 44 2.055 -8.494 -22.671 1.00113.13 C
ATOM 3478 CG GLU B 44 3.034 -9.654 -22.854 1.00112.44 C
ATOM 3479 CD GLU B 44 2.670 -10.866 -22.019 1.00111.76 C
ATOM 3480 OE1 GLU B 44 2.013 -10.688 -20.975 1.00108.36 O
ATOM 3481 OE2 GLU B 44 3.019 -11.998 -22.418 1.00118.04 O
ATOM 3482 N SER B 45 0.063 -11.124 -23.581 1.00106.73 N
ATOM 3483 CA SER B 45 -0.308 -12.160 -24.533 1.00106.19 C
ATOM 3484 C SER B 45 -1.797 -12.025 -24.852 1.00 99.18 C
ATOM 3485 O SER B 45 -2.403 -12.912 -25.448 1.00 99.38 O
ATOM 3486 CB SER B 45 0.009 -13.551 -23.984 1.00107.15 C
ATOM 3487 OG SER B 45 -0.595 -14.558 -24.780 1.00103.05 O
ATOM 3488 N GLY B 48 -5.475 -14.732 -24.000 1.00 83.08 N
ATOM 3489 CA GLY B 48 -5.420 -16.154 -24.292 1.00 88.28 C
ATOM 3490 C GLY B 48 -5.814 -17.010 -23.099 1.00 88.67 C
ATOM 3491 O GLY B 48 -4.951 -17.539 -22.393 1.00 90.00 O
ATOM 3492 N ARG B 49 -7.121 -17.134 -22.874 1.00 77.52 N
ATOM 3493 CA ARG B 49 -7.679 -17.918 -21.758 1.00 80.73 C
ATOM 3494 C ARG B 49 -7.420 -17.348 -20.347 1.00 66.33 C
ATOM 3495 O ARG B 49 -7.858 -17.925 -19.346 1.00 59.30 O
ATOM 3496 CB ARG B 49 -7.264 -19.396 -21.840 1.00 79.08 C
ATOM 3497 CG ARG B 49 -7.734 -20.081 -23.107 1.00 85.67 C
ATOM 3498 CD ARG B 49 -7.759 -21.592 -22.958 1.00 84.05 C
ATOM 3499 NE ARG B 49 -8.874 -22.066 -22.135 1.00 87.77 N
ATOM 3500 CZ ARG B 49 -9.983 -22.626 -22.622 1.00 95.92 C
ATOM 3501 NH1 ARG B 49 -10.130 -22.777 -23.936 1.00102.20 N
ATOM 3502 NH2 ARG B 49 -10.946 -23.041 -21.800 1.00 84.09 N
ATOM 3503 N GLY B 50 -6.713 -16.221 -20.287 1.00 66.81 N
ATOM 3504 CA GLY B 50 -6.511 -15.474 -19.059 1.00 64.37 C
ATOM 3505 C GLY B 50 -6.141 -16.196 -17.768 1.00 61.72 C
ATOM 3506 O GLY B 50 -5.453 -17.230 -17.768 1.00 60.09 O
ATOM 3507 N ALA B 51 -6.609 -15.635 -16.653 1.00 58.87 N
ATOM 3508 CA ALA B 51 -6.217 -16.117 -15.323 1.00 62.69 C
ATOM 3509 C ALA B 51 -7.344 -16.063 -14.285 1.00 54.39 C
ATOM 3510 O ALA B 51 -8.176 -15.144 -14.291 1.00 55.02 O
ATOM 3511 CB ALA B 51 -5.017 -15.331 -14.824 1.00 54.80 C
ATOM 3512 N ILE B 52 -7.366 -17.044 -13.389 1.00 46.58 N
ATOM 3513 CA ILE B 52 -8.298 -16.999 -12.267 1.00 50.82 C
ATOM 3514 C ILE B 52 -7.613 -17.272 -10.918 1.00 56.60 C
ATOM 3515 O ILE B 52 -6.705 -18.115 -10.813 1.00 54.34 O
ATOM 3516 CB ILE B 52 -9.496 -17.968 -12.465 1.00 44.78 C
ATOM 3517 CG1 ILE B 52 -10.764 -17.382 -11.838 1.00 38.94 C
ATOM 3518 CG2 ILE B 52 -9.197 -19.354 -11.909 1.00 49.00 C
ATOM 3519 CD1 ILE B 52 -11.064 -15.967 -12.315 1.00 36.46 C
ATOM 3520 N ALA B 53 -8.046 -16.552 -9.886 1.00 51.60 N
ATOM 3521 CA ALA B 53 -7.595 -16.839 -8.530 1.00 40.52 C
ATOM 3522 C ALA B 53 -8.319 -18.076 -8.009 1.00 41.35 C
ATOM 3523 O ALA B 53 -9.475 -18.317 -8.356 1.00 45.21 O
ATOM 3524 CB ALA B 53 -7.861 -15.640 -7.638 1.00 40.69 C
ATOM 3525 N ARG B 54 -7.636 -18.867 -7.192 1.00 41.95 N
ATOM 3526 CA ARG B 54 -8.250 -20.000 -6.502 1.00 35.31 C
ATOM 3527 C ARG B 54 -7.933 -19.914 -5.007 1.00 49.88 C
ATOM 3528 O ARG B 54 -6.844 -19.486 -4.618 1.00 48.12 O
ATOM 3529 CB ARG B 54 -7.705 -21.295 -7.075 1.00 36.95 C
ATOM 3530 CG ARG B 54 -8.169 -22.556 -6.389 1.00 42.74 C
ATOM 3531 CD ARG B 54 -7.606 -23.763 -7.133 1.00 55.10 C
ATOM 3532 NE ARG B 54 -8.049 -25.052 -6.596 1.00 69.30 N
ATOM 3533 CZ ARG B 54 -9.046 -25.782 -7.099 1.00 71.69 C
ATOM 3534 NH1 ARG B 54 -9.729 -25.352 -8.156 1.00 64.72 N
ATOM 3535 NH2 ARG B 54 -9.362 -26.945 -6.539 1.00 70.25 N
ATOM 3536 N GLY B 55 -8.878 -20.306 -4.163 1.00 45.56 N
ATOM 3537 CA GLY B 55 -8.636 -20.311 -2.730 1.00 30.17 C
ATOM 3538 C GLY B 55 -8.424 -21.724 -2.262 1.00 35.49 C
ATOM 3539 O GLY B 55 -7.552 -22.417 -2.778 1.00 42.17 O
ATOM 3540 N LEU B 56 -9.230 -22.159 -1.298 1.00 36.23 N
ATOM 3541 CA LEU B 56 -9.181 -23.529 -0.805 1.00 32.48 C
ATOM 3542 C LEU B 56 -10.044 -24.524 -1.602 1.00 41.97 C
ATOM 3543 O LEU B 56 -10.201 -25.683 -1.192 1.00 44.56 O
ATOM 3544 CB LEU B 56 -9.576 -23.556 0.674 1.00 44.18 C
ATOM 3545 CG LEU B 56 -8.446 -23.157 1.639 1.00 48.47 C
ATOM 3546 CD1 LEU B 56 -8.937 -23.061 3.078 1.00 39.75 C
ATOM 3547 CD2 LEU B 56 -7.295 -24.145 1.535 1.00 34.56 C
ATOM 3548 N GLY B 57 -10.631 -24.065 -2.712 1.00 46.13 N
ATOM 3549 CA GLY B 57 -11.382 -24.920 -3.625 1.00 37.86 C
ATOM 3550 C GLY B 57 -12.615 -25.569 -3.033 1.00 44.25 C
ATOM 3551 O GLY B 57 -13.009 -26.659 -3.436 1.00 46.94 O
ATOM 3552 N ARG B 58 -13.241 -24.896 -2.080 1.00 43.51 N
ATOM 3553 CA ARG B 58 -14.414 -25.458 -1.428 1.00 46.19 C
ATOM 3554 C ARG B 58 -15.656 -25.224 -2.271 1.00 46.24 C
ATOM 3555 O ARG B 58 -16.710 -25.819 -2.029 1.00 49.79 O
ATOM 3556 CB ARG B 58 -14.590 -24.881 -0.016 1.00 42.41 C
ATOM 3557 CG ARG B 58 -14.187 -25.844 1.098 1.00 48.01 C
ATOM 3558 CD ARG B 58 -12.785 -26.403 0.894 1.00 42.61 C
ATOM 3559 NE ARG B 58 -12.403 -27.333 1.951 1.00 53.25 N
ATOM 3560 CZ ARG B 58 -11.143 -27.708 2.189 1.00 65.65 C
ATOM 3561 NH1 ARG B 58 -10.163 -27.225 1.426 1.00 54.85 N
ATOM 3562 NH2 ARG B 58 -10.856 -28.557 3.186 1.00 45.47 N
ATOM 3563 N SER B 59 -15.540 -24.341 -3.255 1.00 42.54 N
ATOM 3564 CA SER B 59 -16.661 -24.064 -4.141 1.00 45.65 C
ATOM 3565 C SER B 59 -16.890 -25.296 -5.019 1.00 48.23 C
ATOM 3566 O SER B 59 -15.950 -25.806 -5.619 1.00 53.31 O
ATOM 3567 CB SER B 59 -16.364 -22.823 -4.983 1.00 40.87 C
ATOM 3568 OG SER B 59 -17.517 -22.381 -5.675 1.00 56.84 O
ATOM 3569 N TYR B 60 -18.126 -25.789 -5.056 1.00 47.69 N
ATOM 3570 CA TYR B 60 -18.488 -26.990 -5.828 1.00 56.01 C
ATOM 3571 C TYR B 60 -18.394 -26.788 -7.342 1.00 58.74 C
ATOM 3572 O TYR B 60 -18.093 -27.722 -8.098 1.00 56.77 O
ATOM 3573 CB TYR B 60 -19.911 -27.448 -5.481 1.00 52.42 C
ATOM 3574 CG TYR B 60 -20.047 -28.057 -4.101 1.00 66.43 C
ATOM 3575 CD1 TYR B 60 -20.017 -29.438 -3.926 1.00 74.72 C
ATOM 3576 CD2 TYR B 60 -20.207 -27.252 -2.971 1.00 61.81 C
ATOM 3577 CE1 TYR B 60 -20.137 -30.006 -2.661 1.00 76.25 C
ATOM 3578 CE2 TYR B 60 -20.332 -27.806 -1.706 1.00 64.02 C
ATOM 3579 CZ TYR B 60 -20.294 -29.189 -1.550 1.00 75.41 C
ATOM 3580 OH TYR B 60 -20.413 -29.762 -0.288 1.00 60.46 O
ATOM 3581 N GLY B 61 -18.651 -25.560 -7.773 1.00 53.94 N
ATOM 3582 CA GLY B 61 -18.694 -25.247 -9.178 1.00 55.19 C
ATOM 3583 C GLY B 61 -17.352 -25.185 -9.871 1.00 54.90 C
ATOM 3584 O GLY B 61 -16.355 -25.755 -9.425 1.00 54.21 O
ATOM 3585 N ASP B 62 -17.346 -24.470 -10.988 1.00 54.14 N
ATOM 3586 CA ASP B 62 -16.182 -24.383 -11.839 1.00 51.90 C
ATOM 3587 C ASP B 62 -15.660 -22.946 -11.892 1.00 48.89 C
ATOM 3588 O ASP B 62 -15.040 -22.534 -12.886 1.00 44.13 O
ATOM 3589 CB ASP B 62 -16.516 -24.921 -13.243 1.00 57.14 C
ATOM 3590 CG ASP B 62 -17.581 -24.090 -13.971 1.00 62.13 C
ATOM 3591 OD1 ASP B 62 -18.297 -23.297 -13.323 1.00 55.54 O
ATOM 3592 OD2 ASP B 62 -17.702 -24.237 -15.209 1.00 73.85 O
ATOM 3593 N ASN B 63 -15.897 -22.186 -10.820 1.00 46.34 N
ATOM 3594 CA ASN B 63 -15.427 -20.796 -10.772 1.00 42.23 C
ATOM 3595 C ASN B 63 -13.941 -20.615 -10.421 1.00 45.64 C
ATOM 3596 O ASN B 63 -13.359 -19.543 -10.681 1.00 39.35 O
ATOM 3597 CB ASN B 63 -16.315 -19.913 -9.891 1.00 33.67 C
ATOM 3598 CG ASN B 63 -16.782 -20.607 -8.614 1.00 44.75 C
ATOM 3599 OD1 ASN B 63 -16.459 -21.771 -8.348 1.00 45.32 O
ATOM 3600 ND2 ASN B 63 -17.555 -19.881 -7.813 1.00 36.95 N
ATOM 3601 N ALA B 64 -13.339 -21.674 -9.867 1.00 42.98 N
ATOM 3602 CA ALA B 64 -11.963 -21.645 -9.369 1.00 50.78 C
ATOM 3603 C ALA B 64 -11.036 -22.486 -10.241 1.00 60.00 C
ATOM 3604 O ALA B 64 -10.028 -23.025 -9.765 1.00 59.45 O
ATOM 3605 CB ALA B 64 -11.927 -22.168 -7.933 1.00 40.99 C
ATOM 3606 N GLN B 65 -11.405 -22.636 -11.505 1.00 58.43 N
ATOM 3607 CA GLN B 65 -10.574 -23.349 -12.464 1.00 58.18 C
ATOM 3608 C GLN B 65 -10.655 -22.662 -13.814 1.00 56.88 C
ATOM 3609 O GLN B 65 -11.622 -21.956 -14.118 1.00 52.39 O
ATOM 3610 CB GLN B 65 -10.956 -24.819 -12.564 1.00 57.26 C
ATOM 3611 CG GLN B 65 -12.424 -25.071 -12.704 1.00 55.05 C
ATOM 3612 CD GLN B 65 -12.772 -26.520 -12.422 1.00 74.67 C
ATOM 3613 OE1 GLN B 65 -13.453 -26.830 -11.445 1.00 77.87 O
ATOM 3614 NE2 GLN B 65 -12.294 -27.419 -13.274 1.00 78.51 N
ATOM 3615 N ASN B 66 -9.618 -22.834 -14.614 1.00 56.52 N
ATOM 3616 CA ASN B 66 -9.550 -22.112 -15.868 1.00 60.95 C
ATOM 3617 C ASN B 66 -8.830 -22.969 -16.905 1.00 66.30 C
ATOM 3618 O ASN B 66 -7.630 -22.799 -17.118 1.00 71.34 O
ATOM 3619 CB ASN B 66 -8.858 -20.759 -15.646 1.00 52.21 C
ATOM 3620 CG ASN B 66 -8.837 -19.897 -16.885 1.00 58.29 C
ATOM 3621 OD1 ASN B 66 -9.512 -20.186 -17.871 1.00 64.79 O
ATOM 3622 ND2 ASN B 66 -8.071 -18.817 -16.836 1.00 58.81 N
ATOM 3623 N GLY B 67 -9.573 -23.894 -17.524 1.00 64.56 N
ATOM 3624 CA GLY B 67 -9.030 -24.828 -18.500 1.00 67.70 C
ATOM 3625 C GLY B 67 -8.046 -24.218 -19.484 1.00 64.97 C
ATOM 3626 O GLY B 67 -8.346 -23.218 -20.136 1.00 63.22 O
ATOM 3627 N GLY B 68 -6.857 -24.808 -19.569 1.00 64.83 N
ATOM 3628 CA GLY B 68 -5.816 -24.301 -20.444 1.00 63.64 C
ATOM 3629 C GLY B 68 -5.503 -22.834 -20.227 1.00 62.80 C
ATOM 3630 O GLY B 68 -5.222 -22.101 -21.166 1.00 65.47 O
ATOM 3631 N GLY B 69 -5.573 -22.399 -18.977 1.00 72.24 N
ATOM 3632 CA GLY B 69 -5.199 -21.043 -18.612 1.00 64.99 C
ATOM 3633 C GLY B 69 -4.397 -21.016 -17.319 1.00 66.26 C
ATOM 3634 O GLY B 69 -3.950 -22.057 -16.816 1.00 63.49 O
ATOM 3635 N LEU B 70 -4.214 -19.820 -16.772 1.00 63.49 N
ATOM 3636 CA LEU B 70 -3.537 -19.687 -15.486 1.00 64.78 C
ATOM 3637 C LEU B 70 -4.523 -19.728 -14.310 1.00 62.23 C
ATOM 3638 O LEU B 70 -5.517 -18.991 -14.289 1.00 57.74 O
ATOM 3639 CB LEU B 70 -2.707 -18.397 -15.449 1.00 68.72 C
ATOM 3640 CG LEU B 70 -1.996 -18.019 -14.141 1.00 59.69 C
ATOM 3641 CD1 LEU B 70 -1.000 -19.080 -13.716 1.00 60.28 C
ATOM 3642 CD2 LEU B 70 -1.309 -16.658 -14.274 1.00 51.42 C
ATOM 3643 N VAL B 71 -4.242 -20.609 -13.350 1.00 63.40 N
ATOM 3644 CA VAL B 71 -4.924 -20.634 -12.053 1.00 56.34 C
ATOM 3645 C VAL B 71 -3.932 -20.232 -10.945 1.00 62.79 C
ATOM 3646 O VAL B 71 -2.930 -20.914 -10.725 1.00 64.77 O
ATOM 3647 CB VAL B 71 -5.503 -22.040 -11.749 1.00 57.43 C
ATOM 3648 CG1 VAL B 71 -5.870 -22.179 -10.263 1.00 57.03 C
ATOM 3649 CG2 VAL B 71 -6.706 -22.312 -12.626 1.00 60.67 C
ATOM 3650 N ILE B 72 -4.194 -19.124 -10.256 1.00 56.94 N
ATOM 3651 CA ILE B 72 -3.284 -18.660 -9.199 1.00 56.68 C
ATOM 3652 C ILE B 72 -3.733 -19.040 -7.777 1.00 54.83 C
ATOM 3653 O ILE B 72 -4.676 -18.457 -7.246 1.00 56.37 O
ATOM 3654 CB ILE B 72 -3.095 -17.138 -9.259 1.00 55.05 C
ATOM 3655 CG1 ILE B 72 -2.780 -16.697 -10.689 1.00 47.01 C
ATOM 3656 CG2 ILE B 72 -2.010 -16.711 -8.313 1.00 49.72 C
ATOM 3657 CD1 ILE B 72 -2.185 -15.324 -10.754 1.00 50.01 C
ATOM 3658 N ASP B 73 -3.064 -20.016 -7.167 1.00 56.02 N
ATOM 3659 CA ASP B 73 -3.398 -20.440 -5.809 1.00 49.73 C
ATOM 3660 C ASP B 73 -2.964 -19.351 -4.828 1.00 55.36 C
ATOM 3661 O ASP B 73 -1.802 -18.946 -4.806 1.00 60.47 O
ATOM 3662 CB ASP B 73 -2.733 -21.783 -5.483 1.00 55.55 C
ATOM 3663 CG ASP B 73 -3.209 -22.385 -4.156 1.00 60.56 C
ATOM 3664 OD1 ASP B 73 -3.623 -21.626 -3.257 1.00 55.63 O
ATOM 3665 OD2 ASP B 73 -3.162 -23.627 -4.001 1.00 60.38 O
ATOM 3666 N MET B 74 -3.915 -18.883 -4.023 1.00 56.26 N
ATOM 3667 CA MET B 74 -3.701 -17.746 -3.133 1.00 53.37 C
ATOM 3668 C MET B 74 -3.452 -18.145 -1.672 1.00 51.78 C
ATOM 3669 O MET B 74 -3.079 -17.295 -0.845 1.00 48.47 O
ATOM 3670 CB MET B 74 -4.882 -16.774 -3.207 1.00 46.71 C
ATOM 3671 CG MET B 74 -5.026 -16.068 -4.522 1.00 47.48 C
ATOM 3672 SD MET B 74 -3.549 -15.130 -4.946 1.00 56.82 S
ATOM 3673 CE MET B 74 -3.625 -13.718 -3.824 1.00 45.57 C
ATOM 3674 N THR B 75 -3.659 -19.420 -1.350 1.00 43.82 N
ATOM 3675 CA THR B 75 -3.402 -19.902 0.014 1.00 53.58 C
ATOM 3676 C THR B 75 -1.997 -19.610 0.617 1.00 57.45 C
ATOM 3677 O THR B 75 -1.879 -19.402 1.830 1.00 52.92 O
ATOM 3678 CB THR B 75 -3.755 -21.396 0.182 1.00 51.84 C
ATOM 3679 OG1 THR B 75 -2.706 -22.212 -0.355 1.00 50.09 O
ATOM 3680 CG2 THR B 75 -5.083 -21.707 -0.512 1.00 46.07 C
ATOM 3681 N PRO B 76 -0.930 -19.592 -0.210 1.00 63.90 N
ATOM 3682 CA PRO B 76 0.354 -19.186 0.385 1.00 56.81 C
ATOM 3683 C PRO B 76 0.361 -17.762 0.940 1.00 55.24 C
ATOM 3684 O PRO B 76 1.132 -17.491 1.864 1.00 57.38 O
ATOM 3685 CB PRO B 76 1.333 -19.269 -0.799 1.00 66.47 C
ATOM 3686 CG PRO B 76 0.463 -19.248 -2.027 1.00 63.24 C
ATOM 3687 CD PRO B 76 -0.749 -20.025 -1.608 1.00 61.52 C
ATOM 3688 N LEU B 77 -0.451 -16.868 0.381 1.00 47.84 N
ATOM 3689 CA LEU B 77 -0.536 -15.500 0.892 1.00 44.54 C
ATOM 3690 C LEU B 77 -1.487 -15.450 2.066 1.00 48.95 C
ATOM 3691 O LEU B 77 -2.598 -14.957 1.923 1.00 50.07 O
ATOM 3692 CB LEU B 77 -1.092 -14.561 -0.159 1.00 45.91 C
ATOM 3693 CG LEU B 77 -0.142 -13.745 -1.007 1.00 56.32 C
ATOM 3694 CD1 LEU B 77 -0.919 -12.597 -1.606 1.00 49.21 C
ATOM 3695 CD2 LEU B 77 0.995 -13.241 -0.160 1.00 60.61 C
ATOM 3696 N ASN B 78 -1.052 -15.939 3.222 1.00 44.29 N
ATOM 3697 CA ASN B 78 -1.930 -16.109 4.369 1.00 41.40 C
ATOM 3698 C ASN B 78 -1.451 -15.355 5.599 1.00 45.63 C
ATOM 3699 O ASN B 78 -1.538 -15.880 6.714 1.00 36.79 O
ATOM 3700 CB ASN B 78 -1.983 -17.586 4.754 1.00 44.45 C
ATOM 3701 CG ASN B 78 -0.641 -18.096 5.229 1.00 40.00 C
ATOM 3702 OD1 ASN B 78 0.390 -17.514 4.915 1.00 39.35 O
ATOM 3703 ND2 ASN B 78 -0.646 -19.178 5.995 1.00 55.17 N
ATOM 3704 N THR B 79 -0.945 -14.138 5.418 1.00 43.78 N
ATOM 3705 CA THR B 79 -0.485 -13.359 6.571 1.00 38.10 C
ATOM 3706 C THR B 79 -1.594 -12.515 7.195 1.00 39.18 C
ATOM 3707 O THR B 79 -2.243 -11.717 6.512 1.00 42.03 O
ATOM 3708 CB THR B 79 0.741 -12.469 6.218 1.00 50.42 C
ATOM 3709 OG1 THR B 79 1.902 -13.301 6.096 1.00 50.20 O
ATOM 3710 CG2 THR B 79 0.984 -11.369 7.282 1.00 31.30 C
ATOM 3711 N ILE B 80 -1.813 -12.714 8.493 1.00 38.50 N
ATOM 3712 CA ILE B 80 -2.628 -11.805 9.286 1.00 37.38 C
ATOM 3713 C ILE B 80 -1.766 -10.618 9.726 1.00 42.16 C
ATOM 3714 O ILE B 80 -0.817 -10.787 10.488 1.00 39.38 O
ATOM 3715 CB ILE B 80 -3.179 -12.472 10.546 1.00 39.68 C
ATOM 3716 CG1 ILE B 80 -4.038 -13.677 10.173 1.00 30.21 C
ATOM 3717 CG2 ILE B 80 -3.981 -11.449 11.383 1.00 33.44 C
ATOM 3718 CD1 ILE B 80 -4.596 -14.370 11.373 1.00 33.58 C
ATOM 3719 N HIS B 81 -2.110 -9.424 9.246 1.00 38.10 N
ATOM 3720 CA HIS B 81 -1.286 -8.248 9.439 1.00 31.25 C
ATOM 3721 C HIS B 81 -1.571 -7.562 10.756 1.00 38.58 C
ATOM 3722 O HIS B 81 -0.651 -7.129 11.460 1.00 36.10 O
ATOM 3723 CB HIS B 81 -1.483 -7.268 8.294 1.00 35.41 C
ATOM 3724 CG HIS B 81 -1.005 -7.790 6.975 1.00 47.93 C
ATOM 3725 ND1 HIS B 81 0.333 -7.876 6.648 1.00 50.63 N
ATOM 3726 CD2 HIS B 81 -1.681 -8.267 5.905 1.00 44.24 C
ATOM 3727 CE1 HIS B 81 0.459 -8.376 5.433 1.00 52.27 C
ATOM 3728 NE2 HIS B 81 -0.749 -8.623 4.959 1.00 51.76 N
ATOM 3729 N SER B 82 -2.846 -7.451 11.097 1.00 36.47 N
ATOM 3730 CA SER B 82 -3.192 -6.907 12.391 1.00 32.62 C
ATOM 3731 C SER B 82 -4.635 -7.209 12.755 1.00 33.33 C
ATOM 3732 O SER B 82 -5.449 -7.492 11.897 1.00 36.54 O
ATOM 3733 CB SER B 82 -2.921 -5.399 12.428 1.00 35.63 C
ATOM 3734 OG SER B 82 -3.861 -4.677 11.671 1.00 29.00 O
ATOM 3735 N ILE B 83 -4.929 -7.167 14.044 1.00 32.43 N
ATOM 3736 CA ILE B 83 -6.280 -7.256 14.551 1.00 27.37 C
ATOM 3737 C ILE B 83 -6.326 -6.193 15.622 1.00 31.96 C
ATOM 3738 O ILE B 83 -5.338 -5.975 16.313 1.00 37.48 O
ATOM 3739 CB ILE B 83 -6.565 -8.626 15.167 1.00 26.88 C
ATOM 3740 CG1 ILE B 83 -6.501 -9.705 14.089 1.00 27.97 C
ATOM 3741 CG2 ILE B 83 -7.902 -8.643 15.860 1.00 23.58 C
ATOM 3742 CD1 ILE B 83 -6.701 -11.082 14.629 1.00 25.40 C
ATOM 3743 N ASP B 84 -7.459 -5.523 15.759 1.00 31.13 N
ATOM 3744 CA ASP B 84 -7.578 -4.428 16.692 1.00 29.24 C
ATOM 3745 C ASP B 84 -8.929 -4.563 17.397 1.00 34.60 C
ATOM 3746 O ASP B 84 -9.968 -4.510 16.769 1.00 36.84 O
ATOM 3747 CB ASP B 84 -7.451 -3.119 15.914 1.00 36.75 C
ATOM 3748 CG ASP B 84 -7.404 -1.896 16.801 1.00 37.45 C
ATOM 3749 OD1 ASP B 84 -8.297 -1.751 17.670 1.00 37.25 O
ATOM 3750 OD2 ASP B 84 -6.469 -1.077 16.608 1.00 36.72 O
ATOM 3751 N ALA B 85 -8.904 -4.764 18.707 1.00 35.34 N
ATOM 3752 CA ALA B 85 -10.123 -4.955 19.482 1.00 34.22 C
ATOM 3753 C ALA B 85 -10.962 -3.673 19.584 1.00 37.41 C
ATOM 3754 O ALA B 85 -12.150 -3.716 19.917 1.00 34.40 O
ATOM 3755 CB ALA B 85 -9.761 -5.456 20.882 1.00 31.70 C
ATOM 3756 N ASP B 86 -10.327 -2.532 19.340 1.00 34.87 N
ATOM 3757 CA ASP B 86 -10.975 -1.251 19.587 1.00 38.04 C
ATOM 3758 C ASP B 86 -11.752 -0.781 18.369 1.00 39.52 C
ATOM 3759 O ASP B 86 -12.894 -0.332 18.489 1.00 33.82 O
ATOM 3760 CB ASP B 86 -9.949 -0.201 20.007 1.00 37.39 C
ATOM 3761 CG ASP B 86 -9.269 -0.546 21.327 1.00 50.42 C
ATOM 3762 OD1 ASP B 86 -9.983 -0.930 22.292 1.00 46.75 O
ATOM 3763 OD2 ASP B 86 -8.019 -0.440 21.388 1.00 41.42 O
ATOM 3764 N THR B 87 -11.126 -0.893 17.201 1.00 30.58 N
ATOM 3765 CA THR B 87 -11.789 -0.578 15.947 1.00 36.39 C
ATOM 3766 C THR B 87 -12.594 -1.774 15.415 1.00 41.11 C
ATOM 3767 O THR B 87 -13.411 -1.639 14.507 1.00 39.75 O
ATOM 3768 CB THR B 87 -10.767 -0.143 14.891 1.00 39.19 C
ATOM 3769 OG1 THR B 87 -9.814 -1.196 14.690 1.00 40.33 O
ATOM 3770 CG2 THR B 87 -10.031 1.106 15.360 1.00 32.87 C
ATOM 3771 N LYS B 88 -12.343 -2.937 16.000 1.00 37.25 N
ATOM 3772 CA LYS B 88 -12.945 -4.185 15.578 1.00 34.57 C
ATOM 3773 C LYS B 88 -12.459 -4.620 14.204 1.00 30.21 C
ATOM 3774 O LYS B 88 -13.037 -5.520 13.611 1.00 38.75 O
ATOM 3775 CB LYS B 88 -14.477 -4.111 15.645 1.00 41.81 C
ATOM 3776 CG LYS B 88 -15.044 -3.710 17.035 1.00 39.39 C
ATOM 3777 CD LYS B 88 -16.523 -3.271 16.889 1.00 48.40 C
ATOM 3778 CE LYS B 88 -17.316 -4.271 15.995 1.00 63.63 C
ATOM 3779 NZ LYS B 88 -18.367 -3.774 14.975 1.00 41.26 N
ATOM 3780 N LEU B 89 -11.383 -4.018 13.708 1.00 32.89 N
ATOM 3781 CA LEU B 89 -10.919 -4.293 12.332 1.00 31.76 C
ATOM 3782 C LEU B 89 -9.810 -5.337 12.272 1.00 36.86 C
ATOM 3783 O LEU B 89 -8.891 -5.326 13.093 1.00 39.60 O
ATOM 3784 CB LEU B 89 -10.432 -3.006 11.624 1.00 26.36 C
ATOM 3785 CG LEU B 89 -11.444 -1.870 11.432 1.00 34.77 C
ATOM 3786 CD1 LEU B 89 -10.816 -0.627 10.821 1.00 22.06 C
ATOM 3787 CD2 LEU B 89 -12.599 -2.331 10.573 1.00 34.48 C
ATOM 3788 N VAL B 90 -9.886 -6.226 11.290 1.00 32.63 N
ATOM 3789 CA VAL B 90 -8.784 -7.138 11.027 1.00 32.22 C
ATOM 3790 C VAL B 90 -8.295 -6.890 9.604 1.00 37.50 C
ATOM 3791 O VAL B 90 -9.066 -6.544 8.713 1.00 39.62 O
ATOM 3792 CB VAL B 90 -9.149 -8.628 11.216 1.00 31.31 C
ATOM 3793 CG1 VAL B 90 -9.769 -8.879 12.599 1.00 23.20 C
ATOM 3794 CG2 VAL B 90 -10.082 -9.099 10.083 1.00 34.39 C
ATOM 3795 N ASP B 91 -7.000 -7.060 9.406 1.00 37.27 N
ATOM 3796 CA ASP B 91 -6.352 -6.699 8.163 1.00 34.12 C
ATOM 3797 C ASP B 91 -5.532 -7.908 7.763 1.00 32.65 C
ATOM 3798 O ASP B 91 -4.523 -8.212 8.373 1.00 44.12 O
ATOM 3799 CB ASP B 91 -5.475 -5.473 8.421 1.00 34.30 C
ATOM 3800 CG ASP B 91 -4.594 -5.124 7.252 1.00 38.94 C
ATOM 3801 OD1 ASP B 91 -4.608 -5.867 6.251 1.00 36.63 O
ATOM 3802 OD2 ASP B 91 -3.874 -4.103 7.346 1.00 35.97 O
ATOM 3803 N ILE B 92 -5.976 -8.620 6.746 1.00 41.74 N
ATOM 3804 CA ILE B 92 -5.379 -9.914 6.426 1.00 39.46 C
ATOM 3805 C ILE B 92 -5.180 -10.086 4.919 1.00 42.53 C
ATOM 3806 O ILE B 92 -5.760 -9.351 4.123 1.00 40.86 O
ATOM 3807 CB ILE B 92 -6.260 -11.077 6.935 1.00 31.91 C
ATOM 3808 CG1 ILE B 92 -7.483 -11.269 6.016 1.00 41.28 C
ATOM 3809 CG2 ILE B 92 -6.676 -10.845 8.371 1.00 33.62 C
ATOM 3810 CD1 ILE B 92 -8.749 -10.561 6.466 1.00 37.11 C
ATOM 3811 N ASP B 93 -4.343 -11.051 4.551 1.00 36.49 N
ATOM 3812 CA ASP B 93 -4.151 -11.408 3.163 1.00 37.48 C
ATOM 3813 C ASP B 93 -5.318 -12.275 2.716 1.00 44.64 C
ATOM 3814 O ASP B 93 -5.928 -12.990 3.531 1.00 38.63 O
ATOM 3815 CB ASP B 93 -2.831 -12.148 2.981 1.00 43.44 C
ATOM 3816 CG ASP B 93 -1.639 -11.222 3.055 1.00 51.22 C
ATOM 3817 OD1 ASP B 93 -1.816 -10.027 2.750 1.00 47.39 O
ATOM 3818 OD2 ASP B 93 -0.533 -11.678 3.414 1.00 54.14 O
ATOM 3819 N ALA B 94 -5.636 -12.220 1.420 1.00 49.08 N
ATOM 3820 CA ALA B 94 -6.778 -12.971 0.894 1.00 37.31 C
ATOM 3821 C ALA B 94 -6.656 -14.465 1.133 1.00 37.63 C
ATOM 3822 O ALA B 94 -7.664 -15.172 1.179 1.00 43.86 O
ATOM 3823 CB ALA B 94 -6.962 -12.704 -0.560 1.00 38.28 C
ATOM 3824 N GLY B 95 -5.430 -14.949 1.288 1.00 35.66 N
ATOM 3825 CA GLY B 95 -5.208 -16.370 1.460 1.00 33.46 C
ATOM 3826 C GLY B 95 -5.555 -16.898 2.837 1.00 36.81 C
ATOM 3827 O GLY B 95 -5.605 -18.127 3.003 1.00 37.68 O
ATOM 3828 N VAL B 96 -5.786 -16.023 3.827 1.00 33.67 N
ATOM 3829 CA VAL B 96 -6.074 -16.565 5.169 1.00 37.72 C
ATOM 3830 C VAL B 96 -7.474 -17.145 5.207 1.00 37.95 C
ATOM 3831 O VAL B 96 -8.418 -16.561 4.658 1.00 38.67 O
ATOM 3832 CB VAL B 96 -5.755 -15.617 6.410 1.00 38.44 C
ATOM 3833 CG1 VAL B 96 -4.994 -14.367 6.014 1.00 37.95 C
ATOM 3834 CG2 VAL B 96 -7.003 -15.284 7.222 1.00 36.29 C
ATOM 3835 N ASN B 97 -7.591 -18.332 5.792 1.00 33.20 N
ATOM 3836 CA ASN B 97 -8.876 -18.986 5.872 1.00 28.84 C
ATOM 3837 C ASN B 97 -9.609 -18.541 7.113 1.00 34.41 C
ATOM 3838 O ASN B 97 -9.018 -17.931 8.005 1.00 41.67 O
ATOM 3839 CB ASN B 97 -8.740 -20.505 5.790 1.00 35.88 C
ATOM 3840 CG ASN B 97 -8.109 -21.111 7.026 1.00 38.13 C
ATOM 3841 OD1 ASN B 97 -8.772 -21.313 8.045 1.00 36.86 O
ATOM 3842 ND2 ASN B 97 -6.827 -21.423 6.936 1.00 30.71 N
ATOM 3843 N LEU B 98 -10.904 -18.821 7.170 1.00 40.87 N
ATOM 3844 CA LEU B 98 -11.737 -18.302 8.255 1.00 36.95 C
ATOM 3845 C LEU B 98 -11.558 -19.066 9.557 1.00 34.05 C
ATOM 3846 O LEU B 98 -11.904 -18.553 10.602 1.00 38.76 O
ATOM 3847 CB LEU B 98 -13.217 -18.298 7.845 1.00 42.38 C
ATOM 3848 CG LEU B 98 -13.582 -17.508 6.591 1.00 39.53 C
ATOM 3849 CD1 LEU B 98 -15.078 -17.595 6.294 1.00 31.46 C
ATOM 3850 CD2 LEU B 98 -13.129 -16.062 6.726 1.00 20.83 C
ATOM 3851 N ASP B 99 -11.049 -20.295 9.495 1.00 37.05 N
ATOM 3852 CA ASP B 99 -10.734 -21.033 10.716 1.00 41.08 C
ATOM 3853 C ASP B 99 -9.568 -20.357 11.430 1.00 39.35 C
ATOM 3854 O ASP B 99 -9.618 -20.071 12.636 1.00 28.94 O
ATOM 3855 CB ASP B 99 -10.360 -22.469 10.400 1.00 41.16 C
ATOM 3856 CG ASP B 99 -9.969 -23.240 11.636 1.00 57.11 C
ATOM 3857 OD1 ASP B 99 -8.759 -23.540 11.819 1.00 58.64 O
ATOM 3858 OD2 ASP B 99 -10.879 -23.525 12.441 1.00 53.39 O
ATOM 3859 N GLN B 100 -8.527 -20.099 10.645 1.00 34.21 N
ATOM 3860 CA GLN B 100 -7.332 -19.408 11.100 1.00 31.92 C
ATOM 3861 C GLN B 100 -7.698 -18.055 11.677 1.00 35.15 C
ATOM 3862 O GLN B 100 -7.298 -17.701 12.781 1.00 39.41 O
ATOM 3863 CB GLN B 100 -6.388 -19.234 9.919 1.00 35.64 C
ATOM 3864 CG GLN B 100 -5.284 -18.198 10.092 1.00 32.11 C
ATOM 3865 CD GLN B 100 -4.493 -18.006 8.789 1.00 41.95 C
ATOM 3866 OE1 GLN B 100 -4.897 -18.478 7.715 1.00 36.94 O
ATOM 3867 NE2 GLN B 100 -3.360 -17.327 8.886 1.00 38.70 N
ATOM 3868 N LEU B 101 -8.484 -17.302 10.921 1.00 39.38 N
ATOM 3869 CA LEU B 101 -8.931 -15.983 11.353 1.00 36.26 C
ATOM 3870 C LEU B 101 -9.761 -16.051 12.648 1.00 35.90 C
ATOM 3871 O LEU B 101 -9.641 -15.204 13.540 1.00 36.55 O
ATOM 3872 CB LEU B 101 -9.720 -15.307 10.232 1.00 32.52 C
ATOM 3873 CG LEU B 101 -10.405 -13.993 10.588 1.00 33.03 C
ATOM 3874 CD1 LEU B 101 -9.364 -13.027 11.109 1.00 34.28 C
ATOM 3875 CD2 LEU B 101 -11.145 -13.418 9.365 1.00 29.14 C
ATOM 3876 N MET B 102 -10.588 -17.071 12.764 1.00 35.81 N
ATOM 3877 CA MET B 102 -11.438 -17.183 13.931 1.00 39.53 C
ATOM 3878 C MET B 102 -10.602 -17.403 15.197 1.00 43.22 C
ATOM 3879 O MET B 102 -10.865 -16.827 16.253 1.00 35.81 O
ATOM 3880 CB MET B 102 -12.444 -18.313 13.733 1.00 36.09 C
ATOM 3881 CG MET B 102 -12.649 -19.147 14.961 1.00 36.06 C
ATOM 3882 SD MET B 102 -14.136 -20.106 14.791 1.00 60.79 S
ATOM 3883 CE MET B 102 -14.656 -20.194 16.501 1.00 55.08 C
ATOM 3884 N LYS B 103 -9.576 -18.230 15.062 1.00 38.95 N
ATOM 3885 CA LYS B 103 -8.726 -18.583 16.174 1.00 40.60 C
ATOM 3886 C LYS B 103 -7.834 -17.404 16.575 1.00 42.27 C
ATOM 3887 O LYS B 103 -7.590 -17.166 17.765 1.00 41.03 O
ATOM 3888 CB LYS B 103 -7.920 -19.843 15.827 1.00 41.90 C
ATOM 3889 CG LYS B 103 -8.828 -21.077 15.742 1.00 47.39 C
ATOM 3890 CD LYS B 103 -8.184 -22.263 15.049 1.00 55.94 C
ATOM 3891 CE LYS B 103 -9.066 -23.500 15.207 1.00 55.74 C
ATOM 3892 NZ LYS B 103 -8.466 -24.676 14.520 1.00 67.21 N
ATOM 3893 N ALA B 104 -7.375 -16.653 15.587 1.00 33.56 N
ATOM 3894 CA ALA B 104 -6.554 -15.485 15.857 1.00 31.42 C
ATOM 3895 C ALA B 104 -7.326 -14.369 16.526 1.00 32.14 C
ATOM 3896 O ALA B 104 -6.752 -13.603 17.293 1.00 35.07 O
ATOM 3897 CB ALA B 104 -5.916 -14.974 14.572 1.00 34.30 C
ATOM 3898 N ALA B 105 -8.624 -14.265 16.253 1.00 35.34 N
ATOM 3899 CA ALA B 105 -9.372 -13.075 16.692 1.00 28.20 C
ATOM 3900 C ALA B 105 -10.205 -13.261 17.949 1.00 30.36 C
ATOM 3901 O ALA B 105 -10.643 -12.277 18.536 1.00 34.18 O
ATOM 3902 CB ALA B 105 -10.232 -12.520 15.577 1.00 27.77 C
ATOM 3903 N LEU B 106 -10.442 -14.502 18.356 1.00 30.87 N
ATOM 3904 CA LEU B 106 -11.126 -14.748 19.625 1.00 34.45 C
ATOM 3905 C LEU B 106 -10.464 -14.043 20.817 1.00 36.68 C
ATOM 3906 O LEU B 106 -11.158 -13.384 21.584 1.00 35.82 O
ATOM 3907 CB LEU B 106 -11.285 -16.247 19.913 1.00 37.25 C
ATOM 3908 CG LEU B 106 -12.561 -16.918 19.398 1.00 43.54 C
ATOM 3909 CD1 LEU B 106 -12.499 -18.447 19.443 1.00 55.29 C
ATOM 3910 CD2 LEU B 106 -13.854 -16.351 20.049 1.00 35.04 C
ATOM 3911 N PRO B 107 -9.126 -14.167 20.977 1.00 38.41 N
ATOM 3912 CA PRO B 107 -8.524 -13.525 22.158 1.00 33.85 C
ATOM 3913 C PRO B 107 -8.751 -12.006 22.221 1.00 39.82 C
ATOM 3914 O PRO B 107 -8.568 -11.410 23.278 1.00 36.59 O
ATOM 3915 CB PRO B 107 -7.035 -13.823 22.005 1.00 29.32 C
ATOM 3916 CG PRO B 107 -6.987 -15.067 21.170 1.00 36.19 C
ATOM 3917 CD PRO B 107 -8.114 -14.895 20.187 1.00 38.02 C
ATOM 3918 N PHE B 108 -9.164 -11.389 21.118 1.00 35.65 N
ATOM 3919 CA PHE B 108 -9.499 -9.968 21.137 1.00 30.26 C
ATOM 3920 C PHE B 108 -10.986 -9.740 21.419 1.00 30.48 C
ATOM 3921 O PHE B 108 -11.454 -8.611 21.366 1.00 33.83 O
ATOM 3922 CB PHE B 108 -9.149 -9.308 19.807 1.00 32.08 C
ATOM 3923 CG PHE B 108 -7.681 -9.341 19.462 1.00 33.99 C
ATOM 3924 CD1 PHE B 108 -6.883 -8.233 19.667 1.00 33.33 C
ATOM 3925 CD2 PHE B 108 -7.107 -10.465 18.894 1.00 33.53 C
ATOM 3926 CE1 PHE B 108 -5.533 -8.255 19.311 1.00 32.64 C
ATOM 3927 CE2 PHE B 108 -5.760 -10.500 18.551 1.00 28.15 C
ATOM 3928 CZ PHE B 108 -4.976 -9.401 18.757 1.00 29.45 C
ATOM 3929 N GLY B 109 -11.737 -10.797 21.713 1.00 30.29 N
ATOM 3930 CA GLY B 109 -13.181 -10.660 21.835 1.00 30.11 C
ATOM 3931 C GLY B 109 -13.850 -10.312 20.503 1.00 37.65 C
ATOM 3932 O GLY B 109 -14.876 -9.609 20.466 1.00 35.95 O
ATOM 3933 N LEU B 110 -13.288 -10.806 19.397 1.00 30.97 N
ATOM 3934 CA LEU B 110 -13.877 -10.548 18.078 1.00 37.08 C
ATOM 3935 C LEU B 110 -14.350 -11.832 17.417 1.00 34.37 C
ATOM 3936 O LEU B 110 -13.671 -12.865 17.468 1.00 34.08 O
ATOM 3937 CB LEU B 110 -12.917 -9.780 17.143 1.00 28.06 C
ATOM 3938 CG LEU B 110 -12.385 -8.414 17.602 1.00 25.54 C
ATOM 3939 CD1 LEU B 110 -11.326 -7.946 16.657 1.00 28.47 C
ATOM 3940 CD2 LEU B 110 -13.448 -7.343 17.749 1.00 22.80 C
ATOM 3941 N TRP B 111 -15.512 -11.746 16.775 1.00 38.17 N
ATOM 3942 CA TRP B 111 -16.146 -12.881 16.094 1.00 34.37 C
ATOM 3943 C TRP B 111 -16.281 -12.611 14.590 1.00 33.00 C
ATOM 3944 O TRP B 111 -16.726 -11.539 14.190 1.00 32.88 O
ATOM 3945 CB TRP B 111 -17.523 -13.141 16.714 1.00 33.99 C
ATOM 3946 CG TRP B 111 -18.134 -14.415 16.309 1.00 36.53 C
ATOM 3947 CD1 TRP B 111 -19.092 -14.577 15.388 1.00 36.07 C
ATOM 3948 CD2 TRP B 111 -17.834 -15.724 16.815 1.00 43.64 C
ATOM 3949 NE1 TRP B 111 -19.426 -15.903 15.272 1.00 38.81 N
ATOM 3950 CE2 TRP B 111 -18.652 -16.638 16.136 1.00 36.26 C
ATOM 3951 CE3 TRP B 111 -16.948 -16.219 17.783 1.00 38.69 C
ATOM 3952 CZ2 TRP B 111 -18.630 -18.009 16.374 1.00 45.13 C
ATOM 3953 CZ3 TRP B 111 -16.910 -17.590 18.019 1.00 44.90 C
ATOM 3954 CH2 TRP B 111 -17.747 -18.469 17.317 1.00 42.95 C
ATOM 3955 N VAL B 112 -15.874 -13.573 13.767 1.00 33.08 N
ATOM 3956 CA VAL B 112 -16.021 -13.515 12.320 1.00 34.28 C
ATOM 3957 C VAL B 112 -17.505 -13.351 12.023 1.00 31.20 C
ATOM 3958 O VAL B 112 -18.305 -14.187 12.444 1.00 31.76 O
ATOM 3959 CB VAL B 112 -15.446 -14.794 11.613 1.00 38.33 C
ATOM 3960 CG1 VAL B 112 -15.758 -14.795 10.122 1.00 30.05 C
ATOM 3961 CG2 VAL B 112 -13.956 -14.867 11.784 1.00 35.20 C
ATOM 3962 N PRO B 113 -17.871 -12.274 11.288 1.00 32.46 N
ATOM 3963 CA PRO B 113 -19.258 -11.788 11.245 1.00 31.97 C
ATOM 3964 C PRO B 113 -20.189 -12.677 10.465 1.00 28.12 C
ATOM 3965 O PRO B 113 -21.391 -12.580 10.661 1.00 31.96 O
ATOM 3966 CB PRO B 113 -19.148 -10.419 10.552 1.00 28.42 C
ATOM 3967 CG PRO B 113 -17.701 -10.280 10.110 1.00 30.28 C
ATOM 3968 CD PRO B 113 -17.045 -11.608 10.264 1.00 29.25 C
ATOM 3969 N VAL B 114 -19.642 -13.515 9.591 1.00 27.99 N
ATOM 3970 CA VAL B 114 -20.429 -14.449 8.797 1.00 25.99 C
ATOM 3971 C VAL B 114 -19.644 -15.725 8.652 1.00 32.88 C
ATOM 3972 O VAL B 114 -18.602 -15.741 7.982 1.00 34.21 O
ATOM 3973 CB VAL B 114 -20.707 -13.925 7.349 1.00 29.47 C
ATOM 3974 CG1 VAL B 114 -21.387 -15.002 6.517 1.00 26.69 C
ATOM 3975 CG2 VAL B 114 -21.551 -12.636 7.369 1.00 24.08 C
ATOM 3976 N LEU B 115 -20.126 -16.801 9.269 1.00 34.91 N
ATOM 3977 CA LEU B 115 -19.482 -18.097 9.083 1.00 36.24 C
ATOM 3978 C LEU B 115 -20.327 -19.044 8.216 1.00 43.37 C
ATOM 3979 O LEU B 115 -21.523 -19.251 8.480 1.00 47.07 O
ATOM 3980 CB LEU B 115 -19.164 -18.727 10.432 1.00 40.37 C
ATOM 3981 CG LEU B 115 -18.158 -17.923 11.257 1.00 45.81 C
ATOM 3982 CD1 LEU B 115 -18.238 -18.341 12.706 1.00 43.07 C
ATOM 3983 CD2 LEU B 115 -16.757 -18.146 10.712 1.00 42.07 C
ATOM 3984 N PRO B 116 -19.709 -19.619 7.174 1.00 34.05 N
ATOM 3985 CA PRO B 116 -20.364 -20.650 6.379 1.00 37.45 C
ATOM 3986 C PRO B 116 -20.213 -22.000 7.083 1.00 47.13 C
ATOM 3987 O PRO B 116 -19.607 -22.072 8.150 1.00 46.66 O
ATOM 3988 CB PRO B 116 -19.555 -20.637 5.086 1.00 36.12 C
ATOM 3989 CG PRO B 116 -18.182 -20.334 5.536 1.00 31.70 C
ATOM 3990 CD PRO B 116 -18.337 -19.373 6.701 1.00 37.89 C
ATOM 3991 N GLY B 117 -20.735 -23.061 6.484 1.00 45.76 N
ATOM 3992 CA GLY B 117 -20.748 -24.363 7.124 1.00 44.83 C
ATOM 3993 C GLY B 117 -19.403 -25.049 7.283 1.00 45.06 C
ATOM 3994 O GLY B 117 -19.275 -25.966 8.087 1.00 55.31 O
ATOM 3995 N THR B 118 -18.409 -24.645 6.501 1.00 42.98 N
ATOM 3996 CA THR B 118 -17.058 -25.143 6.693 1.00 42.63 C
ATOM 3997 C THR B 118 -16.164 -23.936 6.817 1.00 46.93 C
ATOM 3998 O THR B 118 -16.383 -22.937 6.144 1.00 49.19 O
ATOM 3999 CB THR B 118 -16.572 -26.077 5.558 1.00 43.87 C
ATOM 4000 OG1 THR B 118 -15.208 -26.441 5.811 1.00 49.73 O
ATOM 4001 CG2 THR B 118 -16.673 -25.412 4.179 1.00 35.97 C
ATOM 4002 N ARG B 119 -15.177 -23.997 7.700 1.00 49.16 N
ATOM 4003 CA ARG B 119 -14.375 -22.814 7.939 1.00 46.01 C
ATOM 4004 C ARG B 119 -13.115 -22.871 7.099 1.00 48.48 C
ATOM 4005 O ARG B 119 -12.255 -21.987 7.168 1.00 48.44 O
ATOM 4006 CB ARG B 119 -14.124 -22.626 9.428 1.00 55.53 C
ATOM 4007 CG ARG B 119 -15.432 -22.303 10.170 1.00 60.17 C
ATOM 4008 CD ARG B 119 -15.264 -22.310 11.676 1.00 67.41 C
ATOM 4009 NE ARG B 119 -15.144 -23.655 12.251 1.00 81.16 N
ATOM 4010 CZ ARG B 119 -14.036 -24.132 12.819 1.00 75.84 C
ATOM 4011 NH1 ARG B 119 -12.948 -23.371 12.878 1.00 70.48 N
ATOM 4012 NH2 ARG B 119 -14.014 -25.361 13.331 1.00 55.28 N
ATOM 4013 N GLN B 120 -13.043 -23.898 6.261 1.00 44.65 N
ATOM 4014 CA GLN B 120 -11.921 -24.041 5.357 1.00 45.93 C
ATOM 4015 C GLN B 120 -12.189 -23.284 4.064 1.00 45.86 C
ATOM 4016 O GLN B 120 -12.152 -23.867 2.979 1.00 47.95 O
ATOM 4017 CB GLN B 120 -11.627 -25.522 5.080 1.00 46.73 C
ATOM 4018 CG GLN B 120 -11.150 -26.304 6.305 1.00 51.49 C
ATOM 4019 CD GLN B 120 -9.873 -25.717 6.937 1.00 65.94 C
ATOM 4020 OE1 GLN B 120 -8.947 -25.278 6.222 1.00 52.89 O
ATOM 4021 NE2 GLN B 120 -9.827 -25.695 8.286 1.00 50.81 N
ATOM 4022 N VAL B 121 -12.483 -21.990 4.184 1.00 42.14 N
ATOM 4023 CA VAL B 121 -12.620 -21.121 3.014 1.00 42.14 C
ATOM 4024 C VAL B 121 -11.744 -19.885 3.196 1.00 39.53 C
ATOM 4025 O VAL B 121 -11.589 -19.389 4.302 1.00 40.28 O
ATOM 4026 CB VAL B 121 -14.098 -20.717 2.715 1.00 36.63 C
ATOM 4027 CG1 VAL B 121 -15.058 -21.824 3.119 1.00 39.56 C
ATOM 4028 CG2 VAL B 121 -14.458 -19.461 3.426 1.00 31.09 C
ATOM 4029 N THR B 122 -11.138 -19.393 2.124 1.00 40.52 N
ATOM 4030 CA THR B 122 -10.262 -18.251 2.277 1.00 37.85 C
ATOM 4031 C THR B 122 -11.101 -16.997 2.332 1.00 36.78 C
ATOM 4032 O THR B 122 -12.305 -17.033 2.114 1.00 37.01 O
ATOM 4033 CB THR B 122 -9.324 -18.091 1.096 1.00 42.60 C
ATOM 4034 OG1 THR B 122 -10.115 -17.797 -0.046 1.00 35.35 O
ATOM 4035 CG2 THR B 122 -8.511 -19.348 0.847 1.00 35.18 C
ATOM 4036 N VAL B 123 -10.452 -15.874 2.608 1.00 37.42 N
ATOM 4037 CA VAL B 123 -11.145 -14.607 2.665 1.00 31.52 C
ATOM 4038 C VAL B 123 -11.490 -14.193 1.240 1.00 32.77 C
ATOM 4039 O VAL B 123 -12.556 -13.644 0.987 1.00 35.90 O
ATOM 4040 CB VAL B 123 -10.290 -13.536 3.399 1.00 33.34 C
ATOM 4041 CG1 VAL B 123 -10.836 -12.117 3.186 1.00 28.97 C
ATOM 4042 CG2 VAL B 123 -10.230 -13.862 4.864 1.00 29.98 C
ATOM 4043 N GLY B 124 -10.586 -14.470 0.306 1.00 34.67 N
ATOM 4044 CA GLY B 124 -10.828 -14.148 -1.093 1.00 37.07 C
ATOM 4045 C GLY B 124 -12.068 -14.864 -1.601 1.00 33.40 C
ATOM 4046 O GLY B 124 -12.940 -14.248 -2.198 1.00 34.03 O
ATOM 4047 N GLY B 125 -12.140 -16.165 -1.332 1.00 30.28 N
ATOM 4048 CA GLY B 125 -13.296 -16.986 -1.639 1.00 32.73 C
ATOM 4049 C GLY B 125 -14.571 -16.530 -0.953 1.00 37.67 C
ATOM 4050 O GLY B 125 -15.652 -16.577 -1.547 1.00 37.63 O
ATOM 4051 N ALA B 126 -14.452 -16.085 0.293 1.00 30.56 N
ATOM 4052 CA ALA B 126 -15.604 -15.612 1.031 1.00 30.16 C
ATOM 4053 C ALA B 126 -16.154 -14.342 0.402 1.00 32.44 C
ATOM 4054 O ALA B 126 -17.362 -14.145 0.351 1.00 32.80 O
ATOM 4055 CB ALA B 126 -15.231 -15.361 2.451 1.00 30.97 C
ATOM 4056 N ILE B 127 -15.266 -13.478 -0.078 1.00 32.35 N
ATOM 4057 CA ILE B 127 -15.693 -12.228 -0.702 1.00 35.14 C
ATOM 4058 C ILE B 127 -16.242 -12.443 -2.125 1.00 36.53 C
ATOM 4059 O ILE B 127 -17.311 -11.951 -2.478 1.00 32.00 O
ATOM 4060 CB ILE B 127 -14.556 -11.181 -0.692 1.00 30.96 C
ATOM 4061 CG1 ILE B 127 -14.242 -10.754 0.748 1.00 33.92 C
ATOM 4062 CG2 ILE B 127 -14.933 -9.944 -1.501 1.00 33.11 C
ATOM 4063 CD1 ILE B 127 -12.973 -9.904 0.889 1.00 24.46 C
ATOM 4064 N ALA B 128 -15.513 -13.203 -2.927 1.00 35.50 N
ATOM 4065 CA ALA B 128 -15.864 -13.386 -4.319 1.00 31.60 C
ATOM 4066 C ALA B 128 -17.130 -14.239 -4.515 1.00 39.78 C
ATOM 4067 O ALA B 128 -17.774 -14.171 -5.564 1.00 38.00 O
ATOM 4068 CB ALA B 128 -14.682 -13.951 -5.085 1.00 30.81 C
ATOM 4069 N CYS B 129 -17.495 -15.027 -3.512 1.00 34.60 N
ATOM 4070 CA CYS B 129 -18.774 -15.711 -3.539 1.00 27.20 C
ATOM 4071 C CYS B 129 -19.788 -15.033 -2.620 1.00 31.41 C
ATOM 4072 O CYS B 129 -20.931 -15.475 -2.525 1.00 31.08 O
ATOM 4073 CB CYS B 129 -18.609 -17.172 -3.151 1.00 30.32 C
ATOM 4074 SG CYS B 129 -18.009 -18.182 -4.510 1.00 41.98 S
ATOM 4075 N ASP B 130 -19.372 -13.955 -1.954 1.00 30.67 N
ATOM 4076 CA ASP B 130 -20.259 -13.215 -1.044 1.00 31.08 C
ATOM 4077 C ASP B 130 -21.048 -14.190 -0.160 1.00 32.73 C
ATOM 4078 O ASP B 130 -22.275 -14.176 -0.135 1.00 30.70 O
ATOM 4079 CB ASP B 130 -21.191 -12.288 -1.830 1.00 24.68 C
ATOM 4080 CG ASP B 130 -21.925 -11.280 -0.941 1.00 33.74 C
ATOM 4081 OD1 ASP B 130 -21.606 -11.191 0.258 1.00 32.42 O
ATOM 4082 OD2 ASP B 130 -22.829 -10.570 -1.440 1.00 36.39 O
ATOM 4083 N ILE B 131 -20.325 -15.070 0.529 1.00 28.28 N
ATOM 4084 CA ILE B 131 -20.946 -16.173 1.243 1.00 24.22 C
ATOM 4085 C ILE B 131 -21.937 -15.712 2.311 1.00 29.46 C
ATOM 4086 O ILE B 131 -21.891 -14.579 2.786 1.00 28.98 O
ATOM 4087 CB ILE B 131 -19.893 -17.084 1.902 1.00 35.99 C
ATOM 4088 CG1 ILE B 131 -19.040 -16.313 2.935 1.00 30.39 C
ATOM 4089 CG2 ILE B 131 -19.017 -17.727 0.865 1.00 25.61 C
ATOM 4090 CD1 ILE B 131 -18.114 -17.223 3.690 1.00 27.69 C
ATOM 4091 N HIS B 132 -22.832 -16.608 2.692 1.00 28.12 N
ATOM 4092 CA HIS B 132 -23.834 -16.299 3.687 1.00 27.24 C
ATOM 4093 C HIS B 132 -23.699 -17.365 4.740 1.00 34.06 C
ATOM 4094 O HIS B 132 -23.045 -18.382 4.503 1.00 33.28 O
ATOM 4095 CB HIS B 132 -25.226 -16.370 3.077 1.00 27.16 C
ATOM 4096 CG HIS B 132 -25.530 -17.689 2.437 1.00 36.55 C
ATOM 4097 ND1 HIS B 132 -25.400 -17.911 1.077 1.00 32.28 N
ATOM 4098 CD2 HIS B 132 -25.951 -18.864 2.967 1.00 37.42 C
ATOM 4099 CE1 HIS B 132 -25.721 -19.162 0.804 1.00 35.37 C
ATOM 4100 NE2 HIS B 132 -26.056 -19.765 1.932 1.00 40.08 N
ATOM 4101 N GLY B 133 -24.310 -17.144 5.900 1.00 33.10 N
ATOM 4102 CA GLY B 133 -24.315 -18.165 6.925 1.00 34.72 C
ATOM 4103 C GLY B 133 -25.614 -18.183 7.682 1.00 36.13 C
ATOM 4104 O GLY B 133 -26.594 -17.547 7.295 1.00 37.53 O
ATOM 4105 N LYS B 134 -25.591 -18.892 8.797 1.00 39.34 N
ATOM 4106 CA LYS B 134 -26.759 -19.106 9.634 1.00 39.14 C
ATOM 4107 C LYS B 134 -27.360 -17.800 10.169 1.00 35.90 C
ATOM 4108 O LYS B 134 -28.501 -17.770 10.620 1.00 36.24 O
ATOM 4109 CB LYS B 134 -26.366 -20.048 10.773 1.00 43.93 C
ATOM 4110 CG LYS B 134 -27.527 -20.541 11.578 1.00 49.12 C
ATOM 4111 CD LYS B 134 -27.143 -21.698 12.485 1.00 51.16 C
ATOM 4112 CE LYS B 134 -28.355 -22.110 13.301 1.00 44.92 C
ATOM 4113 NZ LYS B 134 -28.157 -23.414 13.987 1.00 63.69 N
ATOM 4114 N ASN B 135 -26.596 -16.716 10.096 1.00 35.64 N
ATOM 4115 CA ASN B 135 -27.049 -15.434 10.624 1.00 35.00 C
ATOM 4116 C ASN B 135 -27.349 -14.386 9.550 1.00 33.61 C
ATOM 4117 O ASN B 135 -27.414 -13.180 9.835 1.00 34.84 O
ATOM 4118 CB ASN B 135 -26.023 -14.895 11.623 1.00 30.15 C
ATOM 4119 CG ASN B 135 -24.696 -14.570 10.976 1.00 30.22 C
ATOM 4120 OD1 ASN B 135 -24.366 -15.077 9.901 1.00 36.73 O
ATOM 4121 ND2 ASN B 135 -23.930 -13.727 11.622 1.00 24.43 N
ATOM 4122 N HIS B 136 -27.543 -14.845 8.320 1.00 31.96 N
ATOM 4123 CA HIS B 136 -27.798 -13.925 7.219 1.00 32.79 C
ATOM 4124 C HIS B 136 -28.942 -12.938 7.450 1.00 33.45 C
ATOM 4125 O HIS B 136 -28.843 -11.771 7.068 1.00 41.26 O
ATOM 4126 CB HIS B 136 -28.053 -14.653 5.899 1.00 38.77 C
ATOM 4127 CG HIS B 136 -28.291 -13.709 4.767 1.00 32.71 C
ATOM 4128 ND1 HIS B 136 -29.538 -13.205 4.475 1.00 37.52 N
ATOM 4129 CD2 HIS B 136 -27.429 -13.101 3.917 1.00 31.15 C
ATOM 4130 CE1 HIS B 136 -29.439 -12.346 3.474 1.00 42.25 C
ATOM 4131 NE2 HIS B 136 -28.171 -12.268 3.115 1.00 33.58 N
ATOM 4132 N HIS B 137 -30.028 -13.406 8.050 1.00 30.39 N
ATOM 4133 CA HIS B 137 -31.202 -12.567 8.276 1.00 34.17 C
ATOM 4134 C HIS B 137 -30.928 -11.413 9.245 1.00 36.21 C
ATOM 4135 O HIS B 137 -31.695 -10.455 9.298 1.00 40.23 O
ATOM 4136 CB HIS B 137 -32.355 -13.429 8.795 1.00 34.66 C
ATOM 4137 CG HIS B 137 -32.086 -14.043 10.135 1.00 40.83 C
ATOM 4138 ND1 HIS B 137 -31.194 -15.079 10.311 1.00 41.29 N
ATOM 4139 CD2 HIS B 137 -32.571 -13.749 11.364 1.00 39.27 C
ATOM 4140 CE1 HIS B 137 -31.149 -15.406 11.591 1.00 38.99 C
ATOM 4141 NE2 HIS B 137 -31.974 -14.615 12.251 1.00 43.49 N
ATOM 4142 N SER B 138 -29.829 -11.503 9.996 1.00 41.38 N
ATOM 4143 CA SER B 138 -29.471 -10.474 10.970 1.00 34.21 C
ATOM 4144 C SER B 138 -28.185 -9.726 10.605 1.00 37.18 C
ATOM 4145 O SER B 138 -28.019 -8.570 10.986 1.00 36.76 O
ATOM 4146 CB SER B 138 -29.350 -11.086 12.371 1.00 38.40 C
ATOM 4147 OG SER B 138 -28.189 -11.895 12.490 1.00 45.12 O
ATOM 4148 N ALA B 139 -27.300 -10.370 9.842 1.00 34.96 N
ATOM 4149 CA ALA B 139 -25.955 -9.829 9.592 1.00 36.26 C
ATOM 4150 C ALA B 139 -25.621 -9.591 8.115 1.00 33.24 C
ATOM 4151 O ALA B 139 -24.580 -9.017 7.800 1.00 32.45 O
ATOM 4152 CB ALA B 139 -24.880 -10.765 10.220 1.00 21.18 C
ATOM 4153 N GLY B 140 -26.470 -10.071 7.215 1.00 31.80 N
ATOM 4154 CA GLY B 140 -26.182 -9.997 5.798 1.00 30.33 C
ATOM 4155 C GLY B 140 -25.137 -11.028 5.413 1.00 36.43 C
ATOM 4156 O GLY B 140 -24.896 -11.993 6.154 1.00 32.99 O
ATOM 4157 N SER B 141 -24.516 -10.834 4.252 1.00 30.69 N
ATOM 4158 CA SER B 141 -23.542 -11.786 3.738 1.00 27.19 C
ATOM 4159 C SER B 141 -22.148 -11.213 3.935 1.00 29.42 C
ATOM 4160 O SER B 141 -22.028 -10.127 4.494 1.00 30.34 O
ATOM 4161 CB SER B 141 -23.842 -12.131 2.259 1.00 31.21 C
ATOM 4162 OG SER B 141 -24.032 -10.992 1.449 1.00 25.90 O
ATOM 4163 N PHE B 142 -21.109 -11.928 3.490 1.00 29.12 N
ATOM 4164 CA PHE B 142 -19.719 -11.567 3.804 1.00 29.18 C
ATOM 4165 C PHE B 142 -19.346 -10.160 3.345 1.00 33.99 C
ATOM 4166 O PHE B 142 -18.662 -9.414 4.063 1.00 32.04 O
ATOM 4167 CB PHE B 142 -18.751 -12.592 3.209 1.00 38.12 C
ATOM 4168 CG PHE B 142 -17.439 -12.723 3.965 1.00 41.47 C
ATOM 4169 CD1 PHE B 142 -16.303 -12.043 3.545 1.00 42.42 C
ATOM 4170 CD2 PHE B 142 -17.338 -13.549 5.076 1.00 36.70 C
ATOM 4171 CE1 PHE B 142 -15.100 -12.176 4.227 1.00 30.34 C
ATOM 4172 CE2 PHE B 142 -16.136 -13.685 5.766 1.00 32.99 C
ATOM 4173 CZ PHE B 142 -15.024 -12.997 5.342 1.00 34.85 C
ATOM 4174 N GLY B 143 -19.818 -9.792 2.160 1.00 31.65 N
ATOM 4175 CA GLY B 143 -19.537 -8.481 1.597 1.00 24.00 C
ATOM 4176 C GLY B 143 -19.949 -7.317 2.470 1.00 25.71 C
ATOM 4177 O GLY B 143 -19.296 -6.282 2.431 1.00 30.05 O
ATOM 4178 N ASN B 144 -21.024 -7.465 3.244 1.00 26.74 N
ATOM 4179 CA ASN B 144 -21.492 -6.380 4.121 1.00 28.03 C
ATOM 4180 C ASN B 144 -20.480 -5.944 5.156 1.00 30.43 C
ATOM 4181 O ASN B 144 -20.611 -4.874 5.737 1.00 32.91 O
ATOM 4182 CB ASN B 144 -22.777 -6.774 4.856 1.00 27.99 C
ATOM 4183 CG ASN B 144 -23.892 -7.240 3.909 1.00 38.65 C
ATOM 4184 OD1 ASN B 144 -23.633 -7.858 2.875 1.00 37.33 O
ATOM 4185 ND2 ASN B 144 -25.140 -6.948 4.276 1.00 33.61 N
ATOM 4186 N HIS B 145 -19.476 -6.782 5.413 1.00 34.93 N
ATOM 4187 CA HIS B 145 -18.536 -6.517 6.513 1.00 30.35 C
ATOM 4188 C HIS B 145 -17.136 -6.155 6.025 1.00 30.26 C
ATOM 4189 O HIS B 145 -16.244 -5.896 6.821 1.00 34.50 O
ATOM 4190 CB HIS B 145 -18.506 -7.702 7.491 1.00 26.11 C
ATOM 4191 CG HIS B 145 -19.866 -8.133 7.946 1.00 27.85 C
ATOM 4192 ND1 HIS B 145 -20.531 -7.523 8.989 1.00 27.87 N
ATOM 4193 CD2 HIS B 145 -20.709 -9.086 7.473 1.00 29.75 C
ATOM 4194 CE1 HIS B 145 -21.714 -8.093 9.150 1.00 30.29 C
ATOM 4195 NE2 HIS B 145 -21.845 -9.048 8.245 1.00 28.38 N
ATOM 4196 N VAL B 146 -16.940 -6.134 4.716 1.00 26.86 N
ATOM 4197 CA VAL B 146 -15.666 -5.719 4.160 1.00 26.80 C
ATOM 4198 C VAL B 146 -15.621 -4.198 4.131 1.00 34.32 C
ATOM 4199 O VAL B 146 -16.533 -3.555 3.631 1.00 37.20 O
ATOM 4200 CB VAL B 146 -15.458 -6.283 2.762 1.00 31.27 C
ATOM 4201 CG1 VAL B 146 -14.193 -5.739 2.159 1.00 28.27 C
ATOM 4202 CG2 VAL B 146 -15.434 -7.788 2.823 1.00 30.93 C
ATOM 4203 N ARG B 147 -14.568 -3.629 4.704 1.00 36.10 N
ATOM 4204 CA ARG B 147 -14.448 -2.184 4.826 1.00 34.35 C
ATOM 4205 C ARG B 147 -13.477 -1.641 3.786 1.00 33.63 C
ATOM 4206 O ARG B 147 -13.461 -0.444 3.499 1.00 40.12 O
ATOM 4207 CB ARG B 147 -13.990 -1.827 6.240 1.00 25.83 C
ATOM 4208 CG ARG B 147 -14.993 -2.252 7.313 1.00 32.61 C
ATOM 4209 CD ARG B 147 -16.300 -1.443 7.213 1.00 32.55 C
ATOM 4210 NE ARG B 147 -17.402 -2.020 7.998 1.00 34.14 N
ATOM 4211 CZ ARG B 147 -18.414 -2.732 7.488 1.00 36.49 C
ATOM 4212 NH1 ARG B 147 -18.490 -2.963 6.172 1.00 30.95 N
ATOM 4213 NH2 ARG B 147 -19.352 -3.224 8.298 1.00 28.70 N
ATOM 4214 N SER B 148 -12.665 -2.533 3.228 1.00 32.05 N
ATOM 4215 CA SER B 148 -11.717 -2.170 2.187 1.00 33.12 C
ATOM 4216 C SER B 148 -11.146 -3.439 1.583 1.00 34.26 C
ATOM 4217 O SER B 148 -11.163 -4.499 2.205 1.00 38.98 O
ATOM 4218 CB SER B 148 -10.564 -1.321 2.751 1.00 43.99 C
ATOM 4219 OG SER B 148 -9.393 -2.108 2.984 1.00 35.96 O
ATOM 4220 N MET B 149 -10.654 -3.336 0.359 1.00 36.70 N
ATOM 4221 CA MET B 149 -9.870 -4.413 -0.224 1.00 38.69 C
ATOM 4222 C MET B 149 -8.904 -3.895 -1.276 1.00 40.33 C
ATOM 4223 O MET B 149 -9.081 -2.818 -1.826 1.00 44.21 O
ATOM 4224 CB MET B 149 -10.727 -5.573 -0.768 1.00 38.08 C
ATOM 4225 CG MET B 149 -12.056 -5.203 -1.406 1.00 42.81 C
ATOM 4226 SD MET B 149 -12.809 -6.657 -2.192 1.00 44.60 S
ATOM 4227 CE MET B 149 -14.513 -6.146 -2.257 1.00 40.72 C
ATOM 4228 N ASP B 150 -7.850 -4.664 -1.502 1.00 42.44 N
ATOM 4229 CA ASP B 150 -6.821 -4.312 -2.446 1.00 41.21 C
ATOM 4230 C ASP B 150 -7.010 -5.282 -3.588 1.00 44.95 C
ATOM 4231 O ASP B 150 -6.864 -6.500 -3.407 1.00 43.23 O
ATOM 4232 CB ASP B 150 -5.426 -4.517 -1.831 1.00 42.75 C
ATOM 4233 CG ASP B 150 -5.155 -3.628 -0.611 1.00 49.96 C
ATOM 4234 OD1 ASP B 150 -5.841 -2.606 -0.380 1.00 51.88 O
ATOM 4235 OD2 ASP B 150 -4.205 -3.957 0.125 1.00 64.24 O
ATOM 4236 N LEU B 151 -7.342 -4.751 -4.759 1.00 44.24 N
ATOM 4237 CA LEU B 151 -7.654 -5.587 -5.908 1.00 48.58 C
ATOM 4238 C LEU B 151 -6.592 -5.427 -6.987 1.00 52.34 C
ATOM 4239 O LEU B 151 -6.366 -4.322 -7.491 1.00 55.21 O
ATOM 4240 CB LEU B 151 -9.036 -5.217 -6.448 1.00 47.71 C
ATOM 4241 CG LEU B 151 -9.515 -5.820 -7.766 1.00 44.46 C
ATOM 4242 CD1 LEU B 151 -9.765 -7.317 -7.638 1.00 44.40 C
ATOM 4243 CD2 LEU B 151 -10.765 -5.107 -8.170 1.00 40.34 C
ATOM 4244 N LEU B 152 -5.924 -6.527 -7.319 1.00 49.39 N
ATOM 4245 CA LEU B 152 -4.991 -6.533 -8.443 1.00 52.60 C
ATOM 4246 C LEU B 152 -5.757 -6.618 -9.766 1.00 57.33 C
ATOM 4247 O LEU B 152 -6.294 -7.676 -10.135 1.00 50.25 O
ATOM 4248 CB LEU B 152 -3.969 -7.675 -8.305 1.00 54.05 C
ATOM 4249 CG LEU B 152 -3.032 -7.952 -9.496 1.00 53.94 C
ATOM 4250 CD1 LEU B 152 -2.319 -6.690 -9.978 1.00 58.27 C
ATOM 4251 CD2 LEU B 152 -2.023 -9.047 -9.149 1.00 46.71 C
ATOM 4252 N THR B 153 -5.811 -5.495 -10.473 1.00 58.43 N
ATOM 4253 CA THR B 153 -6.548 -5.431 -11.735 1.00 58.76 C
ATOM 4254 C THR B 153 -5.740 -5.876 -12.983 1.00 61.73 C
ATOM 4255 O THR B 153 -4.544 -6.165 -12.894 1.00 57.70 O
ATOM 4256 CB THR B 153 -7.163 -4.041 -11.908 1.00 53.92 C
ATOM 4257 OG1 THR B 153 -6.126 -3.061 -11.964 1.00 54.59 O
ATOM 4258 CG2 THR B 153 -8.039 -3.751 -10.722 1.00 50.56 C
ATOM 4259 N ALA B 154 -6.407 -5.952 -14.137 1.00 71.06 N
ATOM 4260 CA ALA B 154 -5.762 -6.388 -15.389 1.00 68.82 C
ATOM 4261 C ALA B 154 -4.530 -5.558 -15.775 1.00 69.45 C
ATOM 4262 O ALA B 154 -3.527 -6.101 -16.261 1.00 62.28 O
ATOM 4263 CB ALA B 154 -6.759 -6.381 -16.526 1.00 67.07 C
ATOM 4264 N ASP B 155 -4.610 -4.246 -15.551 1.00 63.43 N
ATOM 4265 CA ASP B 155 -3.509 -3.344 -15.865 1.00 62.46 C
ATOM 4266 C ASP B 155 -2.317 -3.418 -14.885 1.00 70.04 C
ATOM 4267 O ASP B 155 -1.492 -2.503 -14.838 1.00 71.71 O
ATOM 4268 CB ASP B 155 -4.019 -1.903 -15.992 1.00 60.01 C
ATOM 4269 CG ASP B 155 -4.554 -1.350 -14.688 1.00 74.01 C
ATOM 4270 OD1 ASP B 155 -4.948 -0.161 -14.675 1.00 81.39 O
ATOM 4271 OD2 ASP B 155 -4.584 -2.096 -13.680 1.00 71.87 O
ATOM 4272 N GLY B 156 -2.232 -4.494 -14.104 1.00 62.59 N
ATOM 4273 CA GLY B 156 -1.121 -4.681 -13.183 1.00 59.02 C
ATOM 4274 C GLY B 156 -1.150 -3.822 -11.920 1.00 65.12 C
ATOM 4275 O GLY B 156 -0.325 -4.013 -11.028 1.00 65.44 O
ATOM 4276 N GLU B 157 -2.099 -2.889 -11.844 1.00 63.55 N
ATOM 4277 CA GLU B 157 -2.272 -1.984 -10.699 1.00 61.75 C
ATOM 4278 C GLU B 157 -3.052 -2.622 -9.527 1.00 65.89 C
ATOM 4279 O GLU B 157 -3.946 -3.459 -9.739 1.00 63.00 O
ATOM 4280 CB GLU B 157 -3.042 -0.747 -11.167 1.00 66.45 C
ATOM 4281 CG GLU B 157 -3.014 0.433 -10.239 1.00 68.95 C
ATOM 4282 CD GLU B 157 -1.977 1.453 -10.665 1.00 91.64 C
ATOM 4283 OE1 GLU B 157 -0.809 1.052 -10.893 1.00 87.25 O
ATOM 4284 OE2 GLU B 157 -2.334 2.648 -10.789 1.00 89.01 O
ATOM 4285 N ILE B 158 -2.710 -2.214 -8.301 1.00 56.20 N
ATOM 4286 CA ILE B 158 -3.461 -2.570 -7.092 1.00 50.63 C
ATOM 4287 C ILE B 158 -4.400 -1.424 -6.708 1.00 57.61 C
ATOM 4288 O ILE B 158 -3.940 -0.333 -6.366 1.00 56.84 O
ATOM 4289 CB ILE B 158 -2.534 -2.864 -5.881 1.00 54.94 C
ATOM 4290 CG1 ILE B 158 -1.946 -4.271 -5.960 1.00 52.93 C
ATOM 4291 CG2 ILE B 158 -3.292 -2.759 -4.574 1.00 56.80 C
ATOM 4292 CD1 ILE B 158 -0.726 -4.363 -6.818 1.00 66.08 C
ATOM 4293 N ARG B 159 -5.711 -1.664 -6.779 1.00 53.78 N
ATOM 4294 CA ARG B 159 -6.688 -0.634 -6.450 1.00 49.73 C
ATOM 4295 C ARG B 159 -7.246 -0.862 -5.050 1.00 55.23 C
ATOM 4296 O ARG B 159 -7.608 -1.984 -4.683 1.00 55.01 O
ATOM 4297 CB ARG B 159 -7.832 -0.623 -7.470 1.00 65.10 C
ATOM 4298 CG ARG B 159 -7.550 0.110 -8.797 1.00 64.39 C
ATOM 4299 CD ARG B 159 -8.332 -0.565 -9.908 1.00 67.61 C
ATOM 4300 NE ARG B 159 -8.641 0.282 -11.056 1.00 85.42 N
ATOM 4301 CZ ARG B 159 -9.597 1.210 -11.065 1.00 90.49 C
ATOM 4302 NH1 ARG B 159 -10.326 1.437 -9.976 1.00 85.17 N
ATOM 4303 NH2 ARG B 159 -9.816 1.931 -12.157 1.00 88.05 N
ATOM 4304 N HIS B 160 -7.304 0.207 -4.268 1.00 51.61 N
ATOM 4305 CA HIS B 160 -7.803 0.131 -2.902 1.00 53.88 C
ATOM 4306 C HIS B 160 -9.283 0.479 -2.917 1.00 52.17 C
ATOM 4307 O HIS B 160 -9.648 1.647 -3.046 1.00 54.91 O
ATOM 4308 CB HIS B 160 -7.032 1.103 -2.001 1.00 47.94 C
ATOM 4309 CG HIS B 160 -7.451 1.081 -0.559 1.00 57.46 C
ATOM 4310 ND1 HIS B 160 -6.995 0.136 0.338 1.00 56.46 N
ATOM 4311 CD2 HIS B 160 -8.253 1.916 0.149 1.00 53.87 C
ATOM 4312 CE1 HIS B 160 -7.510 0.380 1.532 1.00 56.68 C
ATOM 4313 NE2 HIS B 160 -8.279 1.453 1.444 1.00 57.72 N
ATOM 4314 N LEU B 161 -10.129 -0.539 -2.791 1.00 45.67 N
ATOM 4315 CA LEU B 161 -11.570 -0.363 -2.910 1.00 43.95 C
ATOM 4316 C LEU B 161 -12.224 -0.218 -1.552 1.00 41.01 C
ATOM 4317 O LEU B 161 -11.874 -0.939 -0.634 1.00 47.29 O
ATOM 4318 CB LEU B 161 -12.174 -1.573 -3.628 1.00 44.51 C
ATOM 4319 CG LEU B 161 -11.450 -2.090 -4.867 1.00 39.42 C
ATOM 4320 CD1 LEU B 161 -12.242 -3.232 -5.486 1.00 48.72 C
ATOM 4321 CD2 LEU B 161 -11.243 -0.969 -5.873 1.00 48.19 C
ATOM 4322 N THR B 162 -13.170 0.711 -1.431 1.00 38.70 N
ATOM 4323 CA THR B 162 -14.040 0.803 -0.257 1.00 42.45 C
ATOM 4324 C THR B 162 -15.539 0.728 -0.665 1.00 46.23 C
ATOM 4325 O THR B 162 -15.892 1.000 -1.813 1.00 44.89 O
ATOM 4326 CB THR B 162 -13.765 2.089 0.507 1.00 37.36 C
ATOM 4327 OG1 THR B 162 -14.099 3.211 -0.319 1.00 48.50 O
ATOM 4328 CG2 THR B 162 -12.298 2.174 0.842 1.00 46.63 C
ATOM 4329 N PRO B 163 -16.424 0.343 0.271 1.00 40.74 N
ATOM 4330 CA PRO B 163 -17.837 0.219 -0.083 1.00 44.69 C
ATOM 4331 C PRO B 163 -18.549 1.534 -0.404 1.00 47.26 C
ATOM 4332 O PRO B 163 -19.522 1.489 -1.156 1.00 47.99 O
ATOM 4333 CB PRO B 163 -18.461 -0.448 1.158 1.00 41.54 C
ATOM 4334 CG PRO B 163 -17.544 -0.241 2.208 1.00 33.07 C
ATOM 4335 CD PRO B 163 -16.169 -0.188 1.614 1.00 41.79 C
ATOM 4336 N THR B 164 -18.105 2.655 0.157 1.00 43.10 N
ATOM 4337 CA THR B 164 -18.721 3.951 -0.133 1.00 44.28 C
ATOM 4338 C THR B 164 -17.761 4.966 -0.741 1.00 47.55 C
ATOM 4339 O THR B 164 -18.095 6.141 -0.847 1.00 57.90 O
ATOM 4340 CB THR B 164 -19.337 4.612 1.105 1.00 50.23 C
ATOM 4341 OG1 THR B 164 -18.297 4.963 2.034 1.00 51.76 O
ATOM 4342 CG2 THR B 164 -20.351 3.686 1.757 1.00 49.43 C
ATOM 4343 N GLY B 165 -16.580 4.522 -1.150 1.00 50.05 N
ATOM 4344 CA GLY B 165 -15.652 5.401 -1.838 1.00 52.32 C
ATOM 4345 C GLY B 165 -16.089 5.732 -3.254 1.00 59.72 C
ATOM 4346 O GLY B 165 -17.242 5.518 -3.634 1.00 56.83 O
ATOM 4347 N GLU B 166 -15.160 6.260 -4.041 1.00 64.14 N
ATOM 4348 CA GLU B 166 -15.460 6.644 -5.410 1.00 69.45 C
ATOM 4349 C GLU B 166 -15.185 5.449 -6.299 1.00 66.79 C
ATOM 4350 O GLU B 166 -15.339 5.498 -7.520 1.00 63.74 O
ATOM 4351 CB GLU B 166 -14.585 7.814 -5.825 1.00 72.84 C
ATOM 4352 CG GLU B 166 -13.124 7.454 -5.899 1.00 81.82 C
ATOM 4353 CD GLU B 166 -12.291 8.614 -6.356 1.00 86.87 C
ATOM 4354 OE1 GLU B 166 -12.404 9.691 -5.718 1.00 83.49 O
ATOM 4355 OE2 GLU B 166 -11.539 8.459 -7.358 1.00 67.06 O
ATOM 4356 N ASP B 167 -14.760 4.366 -5.672 1.00 64.99 N
ATOM 4357 CA ASP B 167 -14.592 3.134 -6.404 1.00 63.84 C
ATOM 4358 C ASP B 167 -15.615 2.101 -5.958 1.00 54.07 C
ATOM 4359 O ASP B 167 -15.452 0.911 -6.222 1.00 54.86 O
ATOM 4360 CB ASP B 167 -13.166 2.622 -6.263 1.00 66.58 C
ATOM 4361 CG ASP B 167 -12.341 2.894 -7.503 1.00 85.14 C
ATOM 4362 OD1 ASP B 167 -12.913 2.809 -8.619 1.00 91.64 O
ATOM 4363 OD2 ASP B 167 -11.134 3.200 -7.369 1.00 83.23 O
ATOM 4364 N ALA B 168 -16.677 2.578 -5.311 1.00 43.23 N
ATOM 4365 CA ALA B 168 -17.717 1.713 -4.766 1.00 47.89 C
ATOM 4366 C ALA B 168 -18.244 0.691 -5.771 1.00 47.50 C
ATOM 4367 O ALA B 168 -18.514 -0.452 -5.408 1.00 53.11 O
ATOM 4368 CB ALA B 168 -18.855 2.544 -4.202 1.00 40.78 C
ATOM 4369 N GLU B 169 -18.360 1.096 -7.030 1.00 43.21 N
ATOM 4370 CA GLU B 169 -18.963 0.252 -8.052 1.00 47.12 C
ATOM 4371 C GLU B 169 -18.145 -1.000 -8.266 1.00 41.16 C
ATOM 4372 O GLU B 169 -18.685 -2.112 -8.353 1.00 42.35 O
ATOM 4373 CB GLU B 169 -19.061 1.001 -9.390 1.00 56.42 C
ATOM 4374 CG GLU B 169 -20.332 1.818 -9.604 1.00 53.73 C
ATOM 4375 CD GLU B 169 -20.642 2.017 -11.095 1.00 76.49 C
ATOM 4376 OE1 GLU B 169 -19.677 2.090 -11.907 1.00 64.44 O
ATOM 4377 OE2 GLU B 169 -21.850 2.083 -11.453 1.00 66.92 O
ATOM 4378 N LEU B 170 -16.835 -0.818 -8.377 1.00 39.63 N
ATOM 4379 CA LEU B 170 -15.962 -1.950 -8.642 1.00 40.21 C
ATOM 4380 C LEU B 170 -15.779 -2.795 -7.358 1.00 45.14 C
ATOM 4381 O LEU B 170 -15.504 -3.998 -7.421 1.00 44.12 O
ATOM 4382 CB LEU B 170 -14.641 -1.467 -9.253 1.00 35.92 C
ATOM 4383 CG LEU B 170 -13.489 -2.464 -9.376 1.00 45.13 C
ATOM 4384 CD1 LEU B 170 -13.860 -3.732 -10.165 1.00 34.98 C
ATOM 4385 CD2 LEU B 170 -12.267 -1.773 -9.950 1.00 44.94 C
ATOM 4386 N PHE B 171 -15.966 -2.164 -6.201 1.00 34.95 N
ATOM 4387 CA PHE B 171 -15.963 -2.871 -4.927 1.00 40.35 C
ATOM 4388 C PHE B 171 -17.142 -3.832 -4.888 1.00 39.99 C
ATOM 4389 O PHE B 171 -16.991 -5.041 -4.630 1.00 34.76 O
ATOM 4390 CB PHE B 171 -16.069 -1.860 -3.785 1.00 45.49 C
ATOM 4391 CG PHE B 171 -16.078 -2.472 -2.406 1.00 43.49 C
ATOM 4392 CD1 PHE B 171 -14.921 -2.523 -1.651 1.00 47.41 C
ATOM 4393 CD2 PHE B 171 -17.256 -2.951 -1.846 1.00 39.85 C
ATOM 4394 CE1 PHE B 171 -14.935 -3.064 -0.369 1.00 43.80 C
ATOM 4395 CE2 PHE B 171 -17.273 -3.496 -0.581 1.00 34.40 C
ATOM 4396 CZ PHE B 171 -16.122 -3.544 0.163 1.00 39.90 C
ATOM 4397 N TRP B 172 -18.317 -3.287 -5.175 1.00 37.23 N
ATOM 4398 CA TRP B 172 -19.533 -4.076 -5.190 1.00 33.42 C
ATOM 4399 C TRP B 172 -19.676 -5.011 -6.388 1.00 33.15 C
ATOM 4400 O TRP B 172 -20.585 -5.838 -6.425 1.00 42.39 O
ATOM 4401 CB TRP B 172 -20.720 -3.156 -5.029 1.00 27.90 C
ATOM 4402 CG TRP B 172 -20.788 -2.620 -3.634 1.00 41.58 C
ATOM 4403 CD1 TRP B 172 -20.549 -1.339 -3.229 1.00 35.95 C
ATOM 4404 CD2 TRP B 172 -21.098 -3.368 -2.447 1.00 40.67 C
ATOM 4405 NE1 TRP B 172 -20.701 -1.237 -1.868 1.00 44.09 N
ATOM 4406 CE2 TRP B 172 -21.036 -2.472 -1.359 1.00 48.83 C
ATOM 4407 CE3 TRP B 172 -21.434 -4.712 -2.198 1.00 31.12 C
ATOM 4408 CZ2 TRP B 172 -21.296 -2.875 -0.033 1.00 37.66 C
ATOM 4409 CZ3 TRP B 172 -21.692 -5.106 -0.895 1.00 30.96 C
ATOM 4410 CH2 TRP B 172 -21.616 -4.191 0.173 1.00 31.42 C
ATOM 4411 N ALA B 173 -18.769 -4.911 -7.351 1.00 32.71 N
ATOM 4412 CA ALA B 173 -18.777 -5.862 -8.461 1.00 41.89 C
ATOM 4413 C ALA B 173 -17.858 -7.002 -8.100 1.00 39.90 C
ATOM 4414 O ALA B 173 -18.033 -8.142 -8.556 1.00 42.18 O
ATOM 4415 CB ALA B 173 -18.326 -5.204 -9.756 1.00 36.75 C
ATOM 4416 N THR B 174 -16.878 -6.683 -7.258 1.00 41.46 N
ATOM 4417 CA THR B 174 -15.922 -7.680 -6.811 1.00 41.53 C
ATOM 4418 C THR B 174 -16.568 -8.606 -5.803 1.00 38.34 C
ATOM 4419 O THR B 174 -16.346 -9.820 -5.834 1.00 39.26 O
ATOM 4420 CB THR B 174 -14.707 -7.057 -6.176 1.00 40.70 C
ATOM 4421 OG1 THR B 174 -14.124 -6.128 -7.099 1.00 45.99 O
ATOM 4422 CG2 THR B 174 -13.698 -8.161 -5.843 1.00 41.73 C
ATOM 4423 N VAL B 175 -17.361 -8.023 -4.908 1.00 35.92 N
ATOM 4424 CA VAL B 175 -18.192 -8.805 -3.999 1.00 33.85 C
ATOM 4425 C VAL B 175 -19.107 -9.685 -4.843 1.00 38.55 C
ATOM 4426 O VAL B 175 -19.893 -9.180 -5.632 1.00 43.83 O
ATOM 4427 CB VAL B 175 -19.050 -7.898 -3.084 1.00 37.27 C
ATOM 4428 CG1 VAL B 175 -20.057 -8.724 -2.307 1.00 30.40 C
ATOM 4429 CG2 VAL B 175 -18.164 -7.079 -2.125 1.00 29.76 C
ATOM 4430 N GLY B 176 -18.974 -11.001 -4.705 1.00 37.27 N
ATOM 4431 CA GLY B 176 -19.831 -11.921 -5.422 1.00 32.67 C
ATOM 4432 C GLY B 176 -19.444 -12.032 -6.881 1.00 41.46 C
ATOM 4433 O GLY B 176 -20.164 -12.632 -7.676 1.00 37.24 O
ATOM 4434 N GLY B 177 -18.284 -11.480 -7.223 1.00 40.25 N
ATOM 4435 CA GLY B 177 -17.827 -11.437 -8.601 1.00 35.67 C
ATOM 4436 C GLY B 177 -17.072 -12.659 -9.085 1.00 38.72 C
ATOM 4437 O GLY B 177 -16.563 -12.667 -10.202 1.00 46.06 O
ATOM 4438 N ASN B 178 -17.004 -13.694 -8.253 1.00 39.90 N
ATOM 4439 CA ASN B 178 -16.306 -14.942 -8.589 1.00 35.77 C
ATOM 4440 C ASN B 178 -14.927 -14.742 -9.202 1.00 40.55 C
ATOM 4441 O ASN B 178 -14.522 -15.481 -10.096 1.00 48.28 O
ATOM 4442 CB ASN B 178 -17.180 -15.839 -9.458 1.00 33.68 C
ATOM 4443 CG ASN B 178 -18.499 -16.185 -8.783 1.00 45.70 C
ATOM 4444 OD1 ASN B 178 -18.667 -17.277 -8.233 1.00 45.61 O
ATOM 4445 ND2 ASN B 178 -19.437 -15.246 -8.803 1.00 48.78 N
ATOM 4446 N GLY B 179 -14.219 -13.726 -8.711 1.00 39.19 N
ATOM 4447 CA GLY B 179 -12.845 -13.462 -9.098 1.00 39.77 C
ATOM 4448 C GLY B 179 -12.647 -12.789 -10.445 1.00 44.23 C
ATOM 4449 O GLY B 179 -11.510 -12.620 -10.871 1.00 46.77 O
ATOM 4450 N LEU B 180 -13.735 -12.393 -11.105 1.00 42.51 N
ATOM 4451 CA LEU B 180 -13.662 -11.855 -12.468 1.00 44.71 C
ATOM 4452 C LEU B 180 -13.429 -10.350 -12.564 1.00 46.10 C
ATOM 4453 O LEU B 180 -13.595 -9.763 -13.634 1.00 45.69 O
ATOM 4454 CB LEU B 180 -14.922 -12.214 -13.253 1.00 45.07 C
ATOM 4455 CG LEU B 180 -15.161 -13.712 -13.382 1.00 48.03 C
ATOM 4456 CD1 LEU B 180 -16.591 -13.970 -13.834 1.00 34.77 C
ATOM 4457 CD2 LEU B 180 -14.154 -14.311 -14.345 1.00 48.20 C
ATOM 4458 N THR B 181 -13.057 -9.711 -11.460 1.00 45.24 N
ATOM 4459 CA THR B 181 -12.636 -8.307 -11.532 1.00 36.82 C
ATOM 4460 C THR B 181 -11.139 -8.190 -11.258 1.00 45.27 C
ATOM 4461 O THR B 181 -10.559 -7.104 -11.344 1.00 48.20 O
ATOM 4462 CB THR B 181 -13.386 -7.407 -10.542 1.00 40.39 C
ATOM 4463 OG1 THR B 181 -13.191 -7.891 -9.199 1.00 47.63 O
ATOM 4464 CG2 THR B 181 -14.874 -7.378 -10.877 1.00 44.49 C
ATOM 4465 N GLY B 182 -10.519 -9.319 -10.927 1.00 44.59 N
ATOM 4466 CA GLY B 182 -9.104 -9.343 -10.605 1.00 48.90 C
ATOM 4467 C GLY B 182 -8.837 -10.132 -9.341 1.00 50.87 C
ATOM 4468 O GLY B 182 -9.712 -10.847 -8.836 1.00 47.80 O
ATOM 4469 N ILE B 183 -7.624 -9.995 -8.820 1.00 46.92 N
ATOM 4470 CA ILE B 183 -7.224 -10.758 -7.644 1.00 48.32 C
ATOM 4471 C ILE B 183 -7.249 -9.916 -6.374 1.00 47.12 C
ATOM 4472 O ILE B 183 -6.589 -8.868 -6.287 1.00 47.52 O
ATOM 4473 CB ILE B 183 -5.842 -11.389 -7.862 1.00 50.41 C
ATOM 4474 CG1 ILE B 183 -5.858 -12.104 -9.214 1.00 43.87 C
ATOM 4475 CG2 ILE B 183 -5.473 -12.314 -6.687 1.00 45.31 C
ATOM 4476 CD1 ILE B 183 -4.845 -13.189 -9.395 1.00 45.13 C
ATOM 4477 N ILE B 184 -8.039 -10.364 -5.402 1.00 48.29 N
ATOM 4478 CA ILE B 184 -8.089 -9.695 -4.113 1.00 45.53 C
ATOM 4479 C ILE B 184 -6.831 -10.120 -3.394 1.00 46.90 C
ATOM 4480 O ILE B 184 -6.627 -11.308 -3.168 1.00 49.01 O
ATOM 4481 CB ILE B 184 -9.323 -10.111 -3.309 1.00 46.11 C
ATOM 4482 CG1 ILE B 184 -10.569 -10.076 -4.214 1.00 46.80 C
ATOM 4483 CG2 ILE B 184 -9.490 -9.188 -2.110 1.00 41.39 C
ATOM 4484 CD1 ILE B 184 -11.796 -10.731 -3.639 1.00 35.75 C
ATOM 4485 N MET B 185 -5.970 -9.160 -3.079 1.00 41.47 N
ATOM 4486 CA MET B 185 -4.689 -9.452 -2.439 1.00 45.49 C
ATOM 4487 C MET B 185 -4.837 -9.459 -0.911 1.00 47.33 C
ATOM 4488 O MET B 185 -4.208 -10.241 -0.184 1.00 42.41 O
ATOM 4489 CB MET B 185 -3.662 -8.378 -2.825 1.00 43.96 C
ATOM 4490 CG MET B 185 -3.392 -8.228 -4.317 1.00 38.18 C
ATOM 4491 SD MET B 185 -2.814 -9.758 -5.105 1.00 55.89 S
ATOM 4492 CE MET B 185 -1.277 -10.038 -4.219 1.00 68.17 C
ATOM 4493 N ARG B 186 -5.708 -8.587 -0.435 1.00 39.86 N
ATOM 4494 CA ARG B 186 -5.693 -8.222 0.950 1.00 41.75 C
ATOM 4495 C ARG B 186 -6.972 -7.449 1.214 1.00 42.47 C
ATOM 4496 O ARG B 186 -7.455 -6.713 0.346 1.00 42.36 O
ATOM 4497 CB ARG B 186 -4.454 -7.346 1.180 1.00 49.41 C
ATOM 4498 CG ARG B 186 -4.281 -6.770 2.563 1.00 42.71 C
ATOM 4499 CD ARG B 186 -3.011 -5.949 2.614 1.00 45.34 C
ATOM 4500 NE ARG B 186 -2.774 -5.401 3.945 1.00 56.65 N
ATOM 4501 CZ ARG B 186 -1.569 -5.180 4.461 1.00 51.58 C
ATOM 4502 NH1 ARG B 186 -0.484 -5.458 3.755 1.00 38.76 N
ATOM 4503 NH2 ARG B 186 -1.455 -4.687 5.687 1.00 52.43 N
ATOM 4504 N ALA B 187 -7.525 -7.608 2.406 1.00 35.56 N
ATOM 4505 CA ALA B 187 -8.758 -6.920 2.751 1.00 34.68 C
ATOM 4506 C ALA B 187 -8.764 -6.476 4.207 1.00 37.76 C
ATOM 4507 O ALA B 187 -7.937 -6.914 5.013 1.00 37.39 O
ATOM 4508 CB ALA B 187 -9.948 -7.832 2.477 1.00 28.85 C
ATOM 4509 N THR B 188 -9.726 -5.621 4.535 1.00 39.52 N
ATOM 4510 CA THR B 188 -9.984 -5.228 5.912 1.00 37.12 C
ATOM 4511 C THR B 188 -11.424 -5.557 6.234 1.00 33.93 C
ATOM 4512 O THR B 188 -12.329 -5.048 5.588 1.00 39.32 O
ATOM 4513 CB THR B 188 -9.763 -3.722 6.127 1.00 41.59 C
ATOM 4514 OG1 THR B 188 -8.407 -3.387 5.792 1.00 51.25 O
ATOM 4515 CG2 THR B 188 -10.019 -3.366 7.589 1.00 43.23 C
ATOM 4516 N ILE B 189 -11.623 -6.406 7.232 1.00 31.05 N
ATOM 4517 CA ILE B 189 -12.934 -6.863 7.646 1.00 26.92 C
ATOM 4518 C ILE B 189 -13.265 -6.218 8.999 1.00 34.26 C
ATOM 4519 O ILE B 189 -12.398 -6.112 9.856 1.00 41.04 O
ATOM 4520 CB ILE B 189 -12.908 -8.399 7.840 1.00 29.25 C
ATOM 4521 CG1 ILE B 189 -12.350 -9.117 6.608 1.00 32.55 C
ATOM 4522 CG2 ILE B 189 -14.269 -8.961 8.207 1.00 29.97 C
ATOM 4523 CD1 ILE B 189 -13.232 -9.087 5.414 1.00 34.49 C
ATOM 4524 N GLU B 190 -14.505 -5.779 9.194 1.00 28.27 N
ATOM 4525 CA GLU B 190 -14.967 -5.365 10.510 1.00 33.63 C
ATOM 4526 C GLU B 190 -15.633 -6.536 11.201 1.00 35.50 C
ATOM 4527 O GLU B 190 -16.621 -7.076 10.714 1.00 32.25 O
ATOM 4528 CB GLU B 190 -15.992 -4.230 10.440 1.00 34.24 C
ATOM 4529 CG GLU B 190 -16.401 -3.785 11.842 1.00 30.03 C
ATOM 4530 CD GLU B 190 -17.436 -2.700 11.859 1.00 39.63 C
ATOM 4531 OE1 GLU B 190 -17.773 -2.200 12.966 1.00 40.55 O
ATOM 4532 OE2 GLU B 190 -17.922 -2.348 10.767 1.00 52.68 O
ATOM 4533 N MET B 191 -15.104 -6.912 12.354 1.00 32.79 N
ATOM 4534 CA MET B 191 -15.557 -8.116 13.046 1.00 33.03 C
ATOM 4535 C MET B 191 -16.738 -7.819 13.957 1.00 29.73 C
ATOM 4536 O MET B 191 -17.162 -6.684 14.088 1.00 35.90 O
ATOM 4537 CB MET B 191 -14.406 -8.741 13.843 1.00 33.36 C
ATOM 4538 CG MET B 191 -13.170 -9.096 13.004 1.00 31.04 C
ATOM 4539 SD MET B 191 -13.244 -10.621 12.027 1.00 33.28 S
ATOM 4540 CE MET B 191 -12.873 -11.859 13.248 1.00 35.90 C
ATOM 4541 N THR B 192 -17.286 -8.856 14.569 1.00 30.17 N
ATOM 4542 CA THR B 192 -18.422 -8.705 15.467 1.00 34.91 C
ATOM 4543 C THR B 192 -17.945 -8.919 16.904 1.00 36.50 C
ATOM 4544 O THR B 192 -17.320 -9.924 17.197 1.00 35.98 O
ATOM 4545 CB THR B 192 -19.525 -9.725 15.119 1.00 34.15 C
ATOM 4546 OG1 THR B 192 -20.050 -9.445 13.810 1.00 35.08 O
ATOM 4547 CG2 THR B 192 -20.649 -9.660 16.136 1.00 28.07 C
ATOM 4548 N PRO B 193 -18.217 -7.962 17.797 1.00 35.09 N
ATOM 4549 CA PRO B 193 -17.676 -8.118 19.153 1.00 40.39 C
ATOM 4550 C PRO B 193 -18.423 -9.223 19.883 1.00 36.75 C
ATOM 4551 O PRO B 193 -19.641 -9.315 19.747 1.00 38.65 O
ATOM 4552 CB PRO B 193 -17.935 -6.749 19.800 1.00 37.03 C
ATOM 4553 CG PRO B 193 -19.089 -6.164 19.016 1.00 37.79 C
ATOM 4554 CD PRO B 193 -19.051 -6.754 17.637 1.00 35.79 C
ATOM 4555 N THR B 194 -17.694 -10.062 20.610 1.00 34.09 N
ATOM 4556 CA THR B 194 -18.298 -11.093 21.436 1.00 35.03 C
ATOM 4557 C THR B 194 -17.515 -11.206 22.753 1.00 45.01 C
ATOM 4558 O THR B 194 -16.315 -10.908 22.806 1.00 34.30 O
ATOM 4559 CB THR B 194 -18.301 -12.449 20.724 1.00 36.56 C
ATOM 4560 OG1 THR B 194 -19.096 -13.383 21.468 1.00 41.76 O
ATOM 4561 CG2 THR B 194 -16.858 -12.987 20.558 1.00 30.46 C
ATOM 4562 N SER B 195 -18.201 -11.616 23.817 1.00 42.72 N
ATOM 4563 CA SER B 195 -17.530 -11.845 25.097 1.00 42.28 C
ATOM 4564 C SER B 195 -17.271 -13.314 25.336 1.00 46.77 C
ATOM 4565 O SER B 195 -16.584 -13.656 26.296 1.00 49.59 O
ATOM 4566 CB SER B 195 -18.307 -11.251 26.286 1.00 37.51 C
ATOM 4567 OG SER B 195 -19.703 -11.391 26.107 1.00 41.58 O
ATOM 4568 N THR B 196 -17.836 -14.182 24.486 1.00 46.69 N
ATOM 4569 CA THR B 196 -17.595 -15.631 24.586 1.00 48.36 C
ATOM 4570 C THR B 196 -17.455 -16.287 23.224 1.00 43.08 C
ATOM 4571 O THR B 196 -17.719 -15.659 22.201 1.00 48.29 O
ATOM 4572 CB THR B 196 -18.710 -16.379 25.346 1.00 47.96 C
ATOM 4573 OG1 THR B 196 -19.879 -16.462 24.523 1.00 43.35 O
ATOM 4574 CG2 THR B 196 -19.038 -15.685 26.668 1.00 48.96 C
ATOM 4575 N ALA B 197 -17.037 -17.552 23.227 1.00 41.61 N
ATOM 4576 CA ALA B 197 -17.015 -18.388 22.027 1.00 43.14 C
ATOM 4577 C ALA B 197 -18.218 -19.335 21.981 1.00 45.08 C
ATOM 4578 O ALA B 197 -18.185 -20.356 21.301 1.00 48.97 O
ATOM 4579 CB ALA B 197 -15.721 -19.183 21.968 1.00 41.83 C
ATOM 4580 N TYR B 198 -19.284 -18.995 22.695 1.00 41.23 N
ATOM 4581 CA TYR B 198 -20.386 -19.936 22.843 1.00 45.72 C
ATOM 4582 C TYR B 198 -21.715 -19.358 22.406 1.00 43.95 C
ATOM 4583 O TYR B 198 -21.894 -18.143 22.339 1.00 39.61 O
ATOM 4584 CB TYR B 198 -20.489 -20.461 24.281 1.00 46.83 C
ATOM 4585 CG TYR B 198 -19.268 -21.218 24.745 1.00 54.06 C
ATOM 4586 CD1 TYR B 198 -19.195 -22.601 24.620 1.00 59.97 C
ATOM 4587 CD2 TYR B 198 -18.186 -20.552 25.314 1.00 55.90 C
ATOM 4588 CE1 TYR B 198 -18.074 -23.298 25.041 1.00 57.13 C
ATOM 4589 CE2 TYR B 198 -17.067 -21.239 25.740 1.00 51.61 C
ATOM 4590 CZ TYR B 198 -17.017 -22.614 25.601 1.00 58.28 C
ATOM 4591 OH TYR B 198 -15.902 -23.304 26.018 1.00 64.59 O
ATOM 4592 N PHE B 199 -22.651 -20.259 22.129 1.00 45.02 N
ATOM 4593 CA PHE B 199 -23.981 -19.876 21.718 1.00 40.94 C
ATOM 4594 C PHE B 199 -24.974 -20.311 22.777 1.00 45.21 C
ATOM 4595 O PHE B 199 -24.770 -21.328 23.460 1.00 44.38 O
ATOM 4596 CB PHE B 199 -24.333 -20.561 20.395 1.00 44.05 C
ATOM 4597 CG PHE B 199 -23.600 -20.017 19.207 1.00 39.47 C
ATOM 4598 CD1 PHE B 199 -24.183 -19.059 18.394 1.00 44.07 C
ATOM 4599 CD2 PHE B 199 -22.335 -20.477 18.886 1.00 45.50 C
ATOM 4600 CE1 PHE B 199 -23.510 -18.558 17.281 1.00 41.46 C
ATOM 4601 CE2 PHE B 199 -21.655 -19.980 17.774 1.00 49.17 C
ATOM 4602 CZ PHE B 199 -22.241 -19.023 16.975 1.00 39.36 C
ATOM 4603 N ILE B 200 -26.049 -19.542 22.905 1.00 43.76 N
ATOM 4604 CA ILE B 200 -27.216 -19.982 23.648 1.00 47.88 C
ATOM 4605 C ILE B 200 -28.305 -20.316 22.645 1.00 50.31 C
ATOM 4606 O ILE B 200 -28.870 -19.419 22.016 1.00 49.26 O
ATOM 4607 CB ILE B 200 -27.740 -18.890 24.567 1.00 41.66 C
ATOM 4608 CG1 ILE B 200 -26.691 -18.546 25.612 1.00 46.54 C
ATOM 4609 CG2 ILE B 200 -29.017 -19.353 25.233 1.00 46.66 C
ATOM 4610 CD1 ILE B 200 -26.414 -19.685 26.561 1.00 53.85 C
ATOM 4611 N ALA B 201 -28.611 -21.603 22.529 1.00 45.46 N
ATOM 4612 CA ALA B 201 -29.466 -22.130 21.470 1.00 52.43 C
ATOM 4613 C ALA B 201 -30.856 -22.571 21.939 1.00 54.96 C
ATOM 4614 O ALA B 201 -30.968 -23.250 22.958 1.00 55.76 O
ATOM 4615 CB ALA B 201 -28.763 -23.316 20.824 1.00 47.26 C
ATOM 4616 N ASP B 202 -31.899 -22.206 21.189 1.00 49.48 N
ATOM 4617 CA ASP B 202 -33.232 -22.764 21.390 1.00 46.17 C
ATOM 4618 C ASP B 202 -33.530 -23.744 20.263 1.00 49.83 C
ATOM 4619 O ASP B 202 -33.219 -23.471 19.109 1.00 55.62 O
ATOM 4620 CB ASP B 202 -34.284 -21.666 21.423 1.00 45.95 C
ATOM 4621 CG ASP B 202 -34.181 -20.817 22.654 1.00 52.38 C
ATOM 4622 OD1 ASP B 202 -33.498 -21.254 23.602 1.00 55.25 O
ATOM 4623 OD2 ASP B 202 -34.784 -19.725 22.689 1.00 54.21 O
ATOM 4624 N GLY B 203 -34.125 -24.888 20.594 1.00 57.73 N
ATOM 4625 CA GLY B 203 -34.451 -25.902 19.601 1.00 49.13 C
ATOM 4626 C GLY B 203 -35.955 -26.064 19.445 1.00 57.94 C
ATOM 4627 O GLY B 203 -36.720 -25.919 20.412 1.00 61.84 O
ATOM 4628 N ASP B 204 -36.389 -26.353 18.224 1.00 51.02 N
ATOM 4629 CA ASP B 204 -37.805 -26.584 17.956 1.00 53.66 C
ATOM 4630 C ASP B 204 -37.979 -27.601 16.845 1.00 53.51 C
ATOM 4631 O ASP B 204 -37.102 -27.769 16.000 1.00 53.02 O
ATOM 4632 CB ASP B 204 -38.522 -25.293 17.588 1.00 43.74 C
ATOM 4633 CG ASP B 204 -38.691 -24.379 18.760 1.00 49.95 C
ATOM 4634 OD1 ASP B 204 -39.625 -24.612 19.552 1.00 59.67 O
ATOM 4635 OD2 ASP B 204 -37.890 -23.433 18.895 1.00 50.29 O
ATOM 4636 N VAL B 205 -39.105 -28.302 16.860 1.00 54.65 N
ATOM 4637 CA VAL B 205 -39.409 -29.220 15.778 1.00 54.98 C
ATOM 4638 C VAL B 205 -40.776 -28.886 15.229 1.00 64.62 C
ATOM 4639 O VAL B 205 -41.635 -28.334 15.941 1.00 59.48 O
ATOM 4640 CB VAL B 205 -39.385 -30.694 16.203 1.00 61.72 C
ATOM 4641 CG1 VAL B 205 -37.981 -31.102 16.606 1.00 63.21 C
ATOM 4642 CG2 VAL B 205 -40.366 -30.926 17.319 1.00 51.29 C
ATOM 4643 N THR B 206 -40.959 -29.190 13.947 1.00 60.29 N
ATOM 4644 CA THR B 206 -42.262 -29.058 13.310 1.00 57.28 C
ATOM 4645 C THR B 206 -42.671 -30.407 12.735 1.00 57.82 C
ATOM 4646 O THR B 206 -41.842 -31.307 12.612 1.00 56.79 O
ATOM 4647 CB THR B 206 -42.265 -27.970 12.201 1.00 62.53 C
ATOM 4648 OG1 THR B 206 -41.473 -28.400 11.081 1.00 53.96 O
ATOM 4649 CG2 THR B 206 -41.730 -26.650 12.745 1.00 52.00 C
ATOM 4650 N ALA B 207 -43.948 -30.544 12.392 1.00 63.75 N
ATOM 4651 CA ALA B 207 -44.474 -31.798 11.859 1.00 63.26 C
ATOM 4652 C ALA B 207 -44.822 -31.709 10.372 1.00 66.63 C
ATOM 4653 O ALA B 207 -45.083 -32.732 9.728 1.00 69.67 O
ATOM 4654 CB ALA B 207 -45.699 -32.226 12.649 1.00 52.62 C
ATOM 4655 N SER B 208 -44.816 -30.493 9.828 1.00 64.30 N
ATOM 4656 CA SER B 208 -45.253 -30.258 8.448 1.00 59.61 C
ATOM 4657 C SER B 208 -44.558 -29.064 7.819 1.00 60.75 C
ATOM 4658 O SER B 208 -44.105 -28.156 8.521 1.00 57.11 O
ATOM 4659 CB SER B 208 -46.762 -29.999 8.412 1.00 56.75 C
ATOM 4660 OG SER B 208 -47.091 -28.833 9.155 1.00 58.92 O
ATOM 4661 N LEU B 209 -44.509 -29.046 6.488 1.00 59.24 N
ATOM 4662 CA LEU B 209 -43.972 -27.885 5.776 1.00 55.70 C
ATOM 4663 C LEU B 209 -44.717 -26.615 6.144 1.00 53.31 C
ATOM 4664 O LEU B 209 -44.128 -25.549 6.228 1.00 57.40 O
ATOM 4665 CB LEU B 209 -44.034 -28.075 4.266 1.00 53.11 C
ATOM 4666 CG LEU B 209 -43.565 -26.862 3.465 1.00 52.15 C
ATOM 4667 CD1 LEU B 209 -42.159 -26.454 3.889 1.00 46.86 C
ATOM 4668 CD2 LEU B 209 -43.603 -27.177 1.990 1.00 48.05 C
ATOM 4669 N ASP B 210 -46.021 -26.724 6.355 1.00 59.46 N
ATOM 4670 CA ASP B 210 -46.798 -25.551 6.722 1.00 56.87 C
ATOM 4671 C ASP B 210 -46.384 -25.048 8.085 1.00 55.84 C
ATOM 4672 O ASP B 210 -46.371 -23.842 8.330 1.00 59.76 O
ATOM 4673 CB ASP B 210 -48.295 -25.849 6.727 1.00 61.63 C
ATOM 4674 CG ASP B 210 -48.881 -25.926 5.330 1.00 76.91 C
ATOM 4675 OD1 ASP B 210 -48.360 -25.239 4.420 1.00 67.79 O
ATOM 4676 OD2 ASP B 210 -49.869 -26.671 5.145 1.00 80.35 O
ATOM 4677 N GLU B 211 -46.050 -25.971 8.979 1.00 54.50 N
ATOM 4678 CA GLU B 211 -45.666 -25.592 10.325 1.00 57.69 C
ATOM 4679 C GLU B 211 -44.327 -24.839 10.280 1.00 57.79 C
ATOM 4680 O GLU B 211 -44.158 -23.798 10.928 1.00 54.95 O
ATOM 4681 CB GLU B 211 -45.578 -26.850 11.183 1.00 68.30 C
ATOM 4682 CG GLU B 211 -45.880 -26.666 12.662 1.00 66.51 C
ATOM 4683 CD GLU B 211 -45.691 -27.957 13.433 1.00 64.88 C
ATOM 4684 OE1 GLU B 211 -45.921 -29.042 12.851 1.00 64.24 O
ATOM 4685 OE2 GLU B 211 -45.285 -27.885 14.611 1.00 70.07 O
ATOM 4686 N THR B 212 -43.394 -25.378 9.497 1.00 49.19 N
ATOM 4687 CA THR B 212 -42.091 -24.771 9.257 1.00 50.51 C
ATOM 4688 C THR B 212 -42.207 -23.331 8.772 1.00 55.77 C
ATOM 4689 O THR B 212 -41.561 -22.428 9.312 1.00 55.18 O
ATOM 4690 CB THR B 212 -41.312 -25.559 8.199 1.00 49.37 C
ATOM 4691 OG1 THR B 212 -41.118 -26.904 8.648 1.00 49.32 O
ATOM 4692 CG2 THR B 212 -39.970 -24.919 7.937 1.00 45.31 C
ATOM 4693 N ILE B 213 -43.030 -23.114 7.754 1.00 49.85 N
ATOM 4694 CA ILE B 213 -43.222 -21.764 7.234 1.00 53.48 C
ATOM 4695 C ILE B 213 -43.847 -20.818 8.263 1.00 55.71 C
ATOM 4696 O ILE B 213 -43.462 -19.650 8.354 1.00 60.53 O
ATOM 4697 CB ILE B 213 -44.019 -21.774 5.925 1.00 53.49 C
ATOM 4698 CG1 ILE B 213 -43.146 -22.319 4.796 1.00 52.01 C
ATOM 4699 CG2 ILE B 213 -44.513 -20.378 5.568 1.00 54.25 C
ATOM 4700 CD1 ILE B 213 -43.933 -23.095 3.781 1.00 53.32 C
ATOM 4701 N ALA B 214 -44.791 -21.320 9.051 1.00 56.11 N
ATOM 4702 CA ALA B 214 -45.418 -20.497 10.085 1.00 56.71 C
ATOM 4703 C ALA B 214 -44.413 -20.057 11.149 1.00 57.07 C
ATOM 4704 O ALA B 214 -44.393 -18.894 11.548 1.00 59.66 O
ATOM 4705 CB ALA B 214 -46.587 -21.230 10.725 1.00 55.48 C
ATOM 4706 N LEU B 215 -43.587 -20.993 11.607 1.00 53.88 N
ATOM 4707 CA LEU B 215 -42.554 -20.703 12.597 1.00 57.55 C
ATOM 4708 C LEU B 215 -41.597 -19.597 12.131 1.00 59.46 C
ATOM 4709 O LEU B 215 -41.080 -18.802 12.937 1.00 52.19 O
ATOM 4710 CB LEU B 215 -41.754 -21.974 12.919 1.00 51.19 C
ATOM 4711 CG LEU B 215 -40.731 -21.850 14.046 1.00 48.23 C
ATOM 4712 CD1 LEU B 215 -41.434 -21.502 15.362 1.00 52.96 C
ATOM 4713 CD2 LEU B 215 -39.924 -23.121 14.186 1.00 46.69 C
ATOM 4714 N HIS B 216 -41.358 -19.556 10.825 1.00 52.41 N
ATOM 4715 CA HIS B 216 -40.404 -18.611 10.278 1.00 52.50 C
ATOM 4716 C HIS B 216 -41.064 -17.298 9.878 1.00 56.41 C
ATOM 4717 O HIS B 216 -40.387 -16.339 9.521 1.00 61.83 O
ATOM 4718 CB HIS B 216 -39.651 -19.224 9.101 1.00 53.35 C
ATOM 4719 CG HIS B 216 -38.588 -20.199 9.501 1.00 54.70 C
ATOM 4720 ND1 HIS B 216 -38.844 -21.538 9.715 1.00 59.14 N
ATOM 4721 CD2 HIS B 216 -37.263 -20.035 9.719 1.00 53.58 C
ATOM 4722 CE1 HIS B 216 -37.723 -22.154 10.038 1.00 47.62 C
ATOM 4723 NE2 HIS B 216 -36.746 -21.263 10.045 1.00 55.39 N
ATOM 4724 N SER B 217 -42.388 -17.250 9.961 1.00 60.17 N
ATOM 4725 CA SER B 217 -43.121 -16.037 9.622 1.00 61.50 C
ATOM 4726 C SER B 217 -43.908 -15.475 10.802 1.00 62.13 C
ATOM 4727 O SER B 217 -44.730 -14.579 10.623 1.00 68.32 O
ATOM 4728 CB SER B 217 -44.086 -16.316 8.470 1.00 58.50 C
ATOM 4729 OG SER B 217 -43.585 -17.337 7.629 1.00 58.72 O
ATOM 4730 N ASP B 218 -43.673 -15.996 12.002 1.00 58.45 N
ATOM 4731 CA ASP B 218 -44.468 -15 |
