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*** METAL BINDING PROTEIN 28-SEP-21 7PU9 ***elNémo ID: 23040100533315666Job options:ID = 23040100533315666 JOBID = METAL BINDING PROTEIN 28-SEP-21 7PU9 USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:
HEADER METAL BINDING PROTEIN 28-SEP-21 7PU9
TITLE CRYSTAL STRUCTURE OF CAM IN COMPLEX WITH CDZ (FORM 2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CALM1, CALM, CAM, CAM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CALMODULIN, CDZ, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.E.MECHALY,C.LEGER,A.HAOUZ,A.CHENAL
REVDAT 1 17-AUG-22 7PU9 0
JRNL AUTH C.LEGER,I.PITARD,M.SADI,N.CARVALHO,S.BRIER,A.MECHALY,
JRNL AUTH 2 D.RAOUX-BARBOT,M.DAVI,S.HOOS,P.WEBER,P.VACHETTE,D.DURAND,
JRNL AUTH 3 A.HAOUZ,J.I.GUIJARRO,D.LADANT,A.CHENAL
JRNL TITL DYNAMICS AND STRUCTURAL CHANGES OF CALMODULIN UPON
JRNL TITL 2 INTERACTION WITH THE ANTAGONIST CALMIDAZOLIUM.
JRNL REF BMC BIOL. V. 20 176 2022
JRNL REFN ESSN 1741-7007
JRNL PMID 35945584
JRNL DOI 10.1186/S12915-022-01381-5
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 8009
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 406
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.32
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE : 0.2000
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 12
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1134
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 41
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.98220
REMARK 3 B22 (A**2) : -5.98220
REMARK 3 B33 (A**2) : 11.96450
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.390
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.429
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.254
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.344
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.238
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.917
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1234 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 1663 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 447 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 290 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1234 ; 10.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 153 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 1124 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.88
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.59
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.98
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -9.827 16.9688 12.4669
REMARK 3 T TENSOR
REMARK 3 T11: 0.0361 T22: -0.1099
REMARK 3 T33: -0.1031 T12: 0.0088
REMARK 3 T13: -0.0052 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 1.2211 L22: 3.7628
REMARK 3 L33: 0.9953 L12: 1.2961
REMARK 3 L13: -0.1862 L23: -0.9833
REMARK 3 S TENSOR
REMARK 3 S11: 0.0494 S12: -0.0488 S13: -0.0237
REMARK 3 S21: -0.0488 S22: -0.0962 S23: 0.025
REMARK 3 S31: -0.0237 S32: 0.025 S33: 0.0468
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7PU9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1292118364.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8266
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROCESS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROCESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8009
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.279
REMARK 200 RESOLUTION RANGE LOW (A) : 56.153
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 34.80
REMARK 200 R MERGE (I) : 0.15600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 2.11200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
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: 1CTR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CACL2, 0.1 M TRIS PH 8.5 AND 25
REMARK 280 %W/V PEG 4K, VAPOR DIFFUSION, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
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+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 112.30667
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 224.61333
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 168.46000
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 280.76667
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 56.15333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 112.30667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 224.61333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 280.76667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 168.46000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 56.15333
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 TOTAL BURIED SURFACE AREA: 350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
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 ALA A 1
REMARK 465 ASP A 2
REMARK 465 GLN A 3
REMARK 465 LYS A 148
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG A 90 OD1 ASN A 111 8665 1.83
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 THR A 79 36.29 -82.54
REMARK 500 SER A 81 34.70 -77.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 206 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 80.7
REMARK 620 3 ASP A 24 OD1 87.8 79.3
REMARK 620 4 THR A 26 O 81.6 151.1 77.4
REMARK 620 5 GLU A 31 OE1 105.2 136.1 143.1 70.9
REMARK 620 6 GLU A 31 OE2 98.0 82.0 159.3 123.1 54.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 205 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 75.4
REMARK 620 3 ASN A 60 OD1 86.6 83.7
REMARK 620 4 THR A 62 O 87.0 154.8 77.2
REMARK 620 5 GLU A 67 OE1 98.1 124.2 152.1 75.6
REMARK 620 6 GLU A 67 OE2 77.5 70.9 152.6 123.3 53.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 95.8
REMARK 620 3 ASN A 97 OD1 85.8 80.1
REMARK 620 4 TYR A 99 O 78.5 165.4 86.0
REMARK 620 5 GLU A 104 OE1 102.7 120.8 155.8 73.8
REMARK 620 6 GLU A 104 OE2 105.0 68.1 147.1 126.2 52.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 83.9
REMARK 620 3 ASP A 133 OD1 92.6 84.3
REMARK 620 4 GLN A 135 O 81.7 155.2 76.3
REMARK 620 5 GLU A 140 OE1 106.9 125.9 144.9 77.9
REMARK 620 6 GLU A 140 OE2 85.4 80.1 164.4 118.5 49.5
REMARK 620 7 HOH A 312 O 169.1 85.6 83.3 107.0 81.9 95.8
REMARK 620 N 1 2 3 4 5 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7PSZ RELATED DB: PDB
DBREF 7PU9 A 1 148 UNP P0DP23 CALM1_HUMAN 2 149
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 A 148 MET MET THR ALA LYS
HET 85H A 201 40
HET 85H A 202 40
HET CA A 203 1
HET CA A 204 1
HET CA A 205 1
HET CA A 206 1
HETNAM 85H 1-[BIS(4-CHLOROPHENYL)METHYL]-3-[(2~{R})-2-(2,4-
HETNAM 2 85H DICHLOROPHENYL)-2-[(2,4-DICHLOROPHENYL)
HETNAM 3 85H METHOXY]ETHYL]IMIDAZOLE
HETNAM CA CALCIUM ION
FORMUL 2 85H 2(C31 H23 CL6 N2 O 1+)
FORMUL 4 CA 4(CA 2+)
FORMUL 8 HOH *41(H2 O)
HELIX 1 AA1 THR A 5 ASP A 20 1 16
HELIX 2 AA2 THR A 28 LEU A 39 1 12
HELIX 3 AA3 THR A 44 ASP A 56 1 13
HELIX 4 AA4 PHE A 65 ASP A 78 1 14
HELIX 5 AA5 SER A 81 ASP A 93 1 13
HELIX 6 AA6 SER A 101 LEU A 112 1 12
HELIX 7 AA7 THR A 117 ASP A 129 1 13
HELIX 8 AA8 TYR A 138 ALA A 147 1 10
SHEET 1 AA1 2 THR A 26 ILE A 27 0
SHEET 2 AA1 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 AA2 2 TYR A 99 ILE A 100 0
SHEET 2 AA2 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
LINK OD1 ASP A 20 CA CA A 206 1555 1555 2.20
LINK OD1 ASP A 22 CA CA A 206 1555 1555 2.40
LINK OD1 ASP A 24 CA CA A 206 1555 1555 2.40
LINK O THR A 26 CA CA A 206 1555 1555 2.40
LINK OE1 GLU A 31 CA CA A 206 1555 1555 2.50
LINK OE2 GLU A 31 CA CA A 206 1555 1555 2.31
LINK OD1 ASP A 56 CA CA A 205 1555 1555 2.17
LINK OD1 ASP A 58 CA CA A 205 1555 1555 2.41
LINK OD1 ASN A 60 CA CA A 205 1555 1555 2.38
LINK O THR A 62 CA CA A 205 1555 1555 2.44
LINK OE1 GLU A 67 CA CA A 205 1555 1555 2.40
LINK OE2 GLU A 67 CA CA A 205 1555 1555 2.44
LINK OD1 ASP A 93 CA CA A 204 1555 1555 2.19
LINK OD1 ASP A 95 CA CA A 204 1555 1555 2.33
LINK OD1 ASN A 97 CA CA A 204 1555 1555 2.40
LINK O TYR A 99 CA CA A 204 1555 1555 2.20
LINK OE1 GLU A 104 CA CA A 204 1555 1555 2.47
LINK OE2 GLU A 104 CA CA A 204 1555 1555 2.45
LINK OD1 ASP A 129 CA CA A 203 1555 1555 2.49
LINK OD1 ASP A 131 CA CA A 203 1555 1555 2.38
LINK OD1 ASP A 133 CA CA A 203 1555 1555 2.45
LINK O GLN A 135 CA CA A 203 1555 1555 2.43
LINK OE1 GLU A 140 CA CA A 203 1555 1555 2.57
LINK OE2 GLU A 140 CA CA A 203 1555 1555 2.69
LINK CA CA A 203 O HOH A 312 1555 1555 2.43
CRYST1 39.351 39.351 336.920 90.00 90.00 120.00 P 61 2 2 12
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 0.025412 0.014672 0.000000 0.00000
SCALE2 0.000000 0.029344 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002968 0.00000
ATOM 1 N LEU A 4 -3.156 24.408 30.109 1.00 80.96 N
ANISOU 1 N LEU A 4 13074 9842 7844 -2227 -1402 236 N
ATOM 2 CA LEU A 4 -4.379 24.069 29.366 1.00 81.07 C
ANISOU 2 CA LEU A 4 12970 9882 7952 -1984 -1113 106 C
ATOM 3 C LEU A 4 -5.382 25.225 29.436 1.00 79.72 C
ANISOU 3 C LEU A 4 12994 9651 7646 -1951 -837 -121 C
ATOM 4 O LEU A 4 -5.746 25.671 30.534 1.00 79.75 O
ANISOU 4 O LEU A 4 13312 9610 7381 -2133 -774 -205 O
ATOM 5 CB LEU A 4 -5.025 22.783 29.914 1.00 81.91 C
ANISOU 5 CB LEU A 4 13092 10036 7992 -1996 -1089 158 C
ATOM 6 CG LEU A 4 -5.376 21.695 28.883 1.00 84.44 C
ANISOU 6 CG LEU A 4 13109 10407 8568 -1759 -1023 206 C
ATOM 7 CD1 LEU A 4 -6.048 20.503 29.558 1.00 85.30 C
ANISOU 7 CD1 LEU A 4 13270 10555 8586 -1799 -1000 252 C
ATOM 8 CD2 LEU A 4 -6.287 22.222 27.782 1.00 85.15 C
ANISOU 8 CD2 LEU A 4 13087 10484 8781 -1529 -764 45 C
ATOM 9 N THR A 5 -5.822 25.714 28.265 1.00 77.90 N
ANISOU 9 N THR A 5 12588 9407 7605 -1728 -669 -215 N
ATOM 10 CA THR A 5 -6.778 26.817 28.213 1.00 76.58 C
ANISOU 10 CA THR A 5 12557 9166 7374 -1670 -407 -412 C
ATOM 11 C THR A 5 -8.190 26.339 27.846 1.00 74.95 C
ANISOU 11 C THR A 5 12260 8970 7246 -1488 -152 -500 C
ATOM 12 O THR A 5 -8.346 25.261 27.265 1.00 74.53 O
ANISOU 12 O THR A 5 11995 8985 7340 -1368 -187 -414 O
ATOM 13 CB THR A 5 -6.296 27.896 27.220 1.00 77.46 C
ANISOU 13 CB THR A 5 12560 9234 7638 -1573 -412 -449 C
ATOM 14 OG1 THR A 5 -6.371 27.403 25.882 1.00 77.32 O
ANISOU 14 OG1 THR A 5 12241 9261 7877 -1351 -394 -401 O
ATOM 15 CG2 THR A 5 -4.900 28.403 27.536 1.00 78.22 C
ANISOU 15 CG2 THR A 5 12721 9314 7686 -1753 -665 -352 C
ATOM 16 N GLU A 6 -9.211 27.185 28.126 1.00 73.69 N
ANISOU 16 N GLU A 6 12252 8729 7018 -1464 109 -668 N
ATOM 17 CA GLU A 6 -10.604 26.952 27.755 1.00 73.11 C
ANISOU 17 CA GLU A 6 12078 8641 7061 -1291 364 -750 C
ATOM 18 C GLU A 6 -10.705 26.720 26.237 1.00 72.38 C
ANISOU 18 C GLU A 6 11668 8584 7249 -1064 333 -701 C
ATOM 19 O GLU A 6 -11.418 25.817 25.802 1.00 72.64 O
ANISOU 19 O GLU A 6 11542 8660 7398 -946 385 -666 O
ATOM 20 CB GLU A 6 -11.454 28.189 28.076 1.00 75.03 C
ANISOU 20 CB GLU A 6 12489 8758 7260 -1281 639 -928 C
ATOM 21 CG GLU A 6 -11.883 28.360 29.512 1.00 79.42 C
ANISOU 21 CG GLU A 6 13374 9251 7550 -1468 802 -1023 C
ATOM 22 CD GLU A 6 -12.966 29.415 29.618 1.00 86.24 C
ANISOU 22 CD GLU A 6 14332 9975 8461 -1392 1143 -1199 C
ATOM 23 OE1 GLU A 6 -12.849 30.303 30.492 1.00 88.06 O
ANISOU 23 OE1 GLU A 6 14870 10100 8488 -1550 1252 -1312 O
ATOM 24 OE2 GLU A 6 -13.920 29.370 28.807 1.00 88.00 O
ANISOU 24 OE2 GLU A 6 14322 10180 8935 -1179 1297 -1218 O
ATOM 25 N GLU A 7 -9.965 27.527 25.445 1.00 71.18 N
ANISOU 25 N GLU A 7 11445 8408 7192 -1020 241 -694 N
ATOM 26 CA GLU A 7 -9.961 27.497 23.980 1.00 70.30 C
ANISOU 26 CA GLU A 7 11085 8312 7314 -833 214 -656 C
ATOM 27 C GLU A 7 -9.420 26.192 23.408 1.00 68.40 C
ANISOU 27 C GLU A 7 10658 8164 7168 -787 54 -517 C
ATOM 28 O GLU A 7 -10.049 25.652 22.509 1.00 68.37 O
ANISOU 28 O GLU A 7 10491 8179 7310 -639 105 -503 O
ATOM 29 CB GLU A 7 -9.232 28.718 23.406 1.00 74.18 C
ANISOU 29 CB GLU A 7 11584 8749 7854 -830 162 -681 C
ATOM 30 CG GLU A 7 -9.840 30.053 23.828 1.00 82.31 C
ANISOU 30 CG GLU A 7 12785 9662 8825 -851 343 -827 C
ATOM 31 CD GLU A 7 -9.415 30.607 25.181 1.00 91.92 C
ANISOU 31 CD GLU A 7 14293 10832 9801 -1066 338 -885 C
ATOM 32 OE1 GLU A 7 -8.225 30.446 25.544 1.00 94.43 O
ANISOU 32 OE1 GLU A 7 14665 11192 10022 -1213 119 -796 O
ATOM 33 OE2 GLU A 7 -10.272 31.202 25.878 1.00 94.09 O
ANISOU 33 OE2 GLU A 7 14745 11016 9990 -1095 556 -1016 O
ATOM 34 N GLN A 8 -8.316 25.642 23.951 1.00 66.97 N
ANISOU 34 N GLN A 8 10503 8029 6913 -917 -138 -408 N
ATOM 35 CA GLN A 8 -7.807 24.338 23.501 1.00 66.51 C
ANISOU 35 CA GLN A 8 10268 8038 6966 -872 -269 -272 C
ATOM 36 C GLN A 8 -8.855 23.239 23.758 1.00 65.33 C
ANISOU 36 C GLN A 8 10093 7924 6804 -825 -179 -272 C
ATOM 37 O GLN A 8 -9.073 22.396 22.900 1.00 64.97 O
ANISOU 37 O GLN A 8 9880 7906 6901 -702 -178 -226 O
ATOM 38 CB GLN A 8 -6.484 23.983 24.196 1.00 68.93 C
ANISOU 38 CB GLN A 8 10603 8368 7219 -1033 -494 -139 C
ATOM 39 CG GLN A 8 -5.304 24.822 23.723 1.00 74.31 C
ANISOU 39 CG GLN A 8 11236 9019 7980 -1062 -611 -96 C
ATOM 40 CD GLN A 8 -4.138 24.788 24.690 1.00 81.18 C
ANISOU 40 CD GLN A 8 12184 9891 8770 -1268 -838 26 C
ATOM 41 OE1 GLN A 8 -4.289 24.953 25.909 1.00 82.67 O
ANISOU 41 OE1 GLN A 8 12595 10071 8743 -1443 -879 7 O
ATOM 42 NE2 GLN A 8 -2.937 24.596 24.160 1.00 83.02 N
ANISOU 42 NE2 GLN A 8 12241 10123 9179 -1262 -992 161 N
ATOM 43 N ILE A 9 -9.551 23.296 24.913 1.00 64.58 N
ANISOU 43 N ILE A 9 10182 7820 6537 -929 -84 -333 N
ATOM 44 CA ILE A 9 -10.611 22.345 25.275 1.00 63.96 C
ANISOU 44 CA ILE A 9 10096 7768 6439 -902 24 -338 C
ATOM 45 C ILE A 9 -11.751 22.449 24.267 1.00 62.71 C
ANISOU 45 C ILE A 9 9791 7585 6449 -714 189 -406 C
ATOM 46 O ILE A 9 -12.179 21.425 23.724 1.00 62.21 O
ANISOU 46 O ILE A 9 9584 7559 6494 -626 179 -351 O
ATOM 47 CB ILE A 9 -11.114 22.627 26.722 1.00 64.55 C
ANISOU 47 CB ILE A 9 10430 7815 6279 -1065 135 -408 C
ATOM 48 CG1 ILE A 9 -10.034 22.316 27.736 1.00 65.23 C
ANISOU 48 CG1 ILE A 9 10670 7929 6187 -1277 -73 -309 C
ATOM 49 CG2 ILE A 9 -12.405 21.872 27.028 1.00 65.20 C
ANISOU 49 CG2 ILE A 9 10500 7908 6365 -1020 311 -437 C
ATOM 50 CD1 ILE A 9 -10.244 22.976 28.954 1.00 66.73 C
ANISOU 50 CD1 ILE A 9 11157 8069 6128 -1457 14 -393 C
ATOM 51 N ALA A 10 -12.207 23.705 23.988 1.00 61.77 N
ANISOU 51 N ALA A 10 9709 7395 6363 -662 324 -516 N
ATOM 52 CA ALA A 10 -13.264 24.025 23.029 1.00 61.19 C
ANISOU 52 CA ALA A 10 9501 7280 6470 -498 457 -567 C
ATOM 53 C ALA A 10 -12.902 23.561 21.601 1.00 60.32 C
ANISOU 53 C ALA A 10 9196 7200 6523 -378 331 -490 C
ATOM 54 O ALA A 10 -13.790 23.150 20.863 1.00 60.89 O
ANISOU 54 O ALA A 10 9142 7266 6726 -270 378 -480 O
ATOM 55 CB ALA A 10 -13.551 25.516 23.050 1.00 61.27 C
ANISOU 55 CB ALA A 10 9595 7195 6491 -482 589 -679 C
ATOM 56 N GLU A 11 -11.608 23.556 21.240 1.00 58.88 N
ANISOU 56 N GLU A 11 8995 7043 6333 -411 173 -429 N
ATOM 57 CA GLU A 11 -11.152 23.078 19.926 1.00 58.62 C
ANISOU 57 CA GLU A 11 8809 7026 6436 -314 83 -362 C
ATOM 58 C GLU A 11 -11.212 21.551 19.881 1.00 57.97 C
ANISOU 58 C GLU A 11 8646 6996 6383 -301 27 -279 C
ATOM 59 O GLU A 11 -11.595 20.987 18.862 1.00 57.90 O
ANISOU 59 O GLU A 11 8534 6983 6482 -205 29 -257 O
ATOM 60 CB GLU A 11 -9.707 23.507 19.652 1.00 61.08 C
ANISOU 60 CB GLU A 11 9119 7337 6752 -359 -39 -316 C
ATOM 61 CG GLU A 11 -9.522 24.985 19.376 1.00 66.94 C
ANISOU 61 CG GLU A 11 9918 8021 7494 -358 -3 -385 C
ATOM 62 CD GLU A 11 -8.086 25.370 19.077 1.00 75.22 C
ANISOU 62 CD GLU A 11 10947 9068 8566 -407 -123 -327 C
ATOM 63 OE1 GLU A 11 -7.170 24.585 19.416 1.00 77.08 O
ANISOU 63 OE1 GLU A 11 11143 9341 8802 -470 -238 -230 O
ATOM 64 OE2 GLU A 11 -7.874 26.461 18.499 1.00 78.77 O
ANISOU 64 OE2 GLU A 11 11409 9468 9051 -383 -103 -367 O
ATOM 65 N PHE A 12 -10.817 20.880 20.977 1.00 57.29 N
ANISOU 65 N PHE A 12 8623 6949 6195 -409 -33 -227 N
ATOM 66 CA PHE A 12 -10.901 19.427 21.061 1.00 57.57 C
ANISOU 66 CA PHE A 12 8591 7025 6259 -405 -85 -144 C
ATOM 67 C PHE A 12 -12.376 18.983 21.067 1.00 57.57 C
ANISOU 67 C PHE A 12 8570 7025 6279 -350 39 -186 C
ATOM 68 O PHE A 12 -12.699 17.929 20.539 1.00 58.28 O
ANISOU 68 O PHE A 12 8567 7127 6449 -293 18 -137 O
ATOM 69 CB PHE A 12 -10.225 18.915 22.333 1.00 58.27 C
ANISOU 69 CB PHE A 12 8767 7146 6227 -551 -188 -68 C
ATOM 70 CG PHE A 12 -8.724 18.747 22.318 1.00 59.54 C
ANISOU 70 CG PHE A 12 8883 7309 6431 -606 -359 40 C
ATOM 71 CD1 PHE A 12 -8.115 17.893 21.409 1.00 60.33 C
ANISOU 71 CD1 PHE A 12 8826 7401 6696 -522 -418 124 C
ATOM 72 CD2 PHE A 12 -7.938 19.313 23.313 1.00 60.33 C
ANISOU 72 CD2 PHE A 12 9101 7409 6411 -759 -463 73 C
ATOM 73 CE1 PHE A 12 -6.744 17.672 21.452 1.00 60.78 C
ANISOU 73 CE1 PHE A 12 8812 7445 6836 -568 -559 240 C
ATOM 74 CE2 PHE A 12 -6.567 19.089 23.351 1.00 61.00 C
ANISOU 74 CE2 PHE A 12 9116 7489 6572 -819 -642 202 C
ATOM 75 CZ PHE A 12 -5.983 18.256 22.431 1.00 60.59 C
ANISOU 75 CZ PHE A 12 8876 7426 6721 -716 -682 289 C
ATOM 76 N LYS A 13 -13.257 19.780 21.670 1.00 57.11 N
ANISOU 76 N LYS A 13 8596 6941 6163 -369 176 -273 N
ATOM 77 CA LYS A 13 -14.678 19.519 21.764 1.00 56.98 C
ANISOU 77 CA LYS A 13 8544 6909 6197 -322 316 -308 C
ATOM 78 C LYS A 13 -15.310 19.661 20.405 1.00 56.24 C
ANISOU 78 C LYS A 13 8310 6781 6278 -189 326 -313 C
ATOM 79 O LYS A 13 -16.108 18.799 20.023 1.00 56.94 O
ANISOU 79 O LYS A 13 8307 6876 6452 -142 332 -275 O
ATOM 80 CB LYS A 13 -15.330 20.471 22.786 1.00 59.51 C
ANISOU 80 CB LYS A 13 8998 7186 6428 -379 491 -405 C
ATOM 81 CG LYS A 13 -16.791 20.179 23.052 1.00 64.50 C
ANISOU 81 CG LYS A 13 9582 7792 7133 -339 665 -431 C
ATOM 82 CD LYS A 13 -17.364 21.114 24.120 1.00 69.75 C
ANISOU 82 CD LYS A 13 10397 8394 7712 -401 881 -536 C
ATOM 83 CE LYS A 13 -18.732 20.679 24.593 1.00 73.68 C
ANISOU 83 CE LYS A 13 10851 8863 8280 -382 1079 -549 C
ATOM 84 NZ LYS A 13 -18.945 21.062 26.021 1.00 77.65 N
ANISOU 84 NZ LYS A 13 11575 9328 8599 -510 1274 -630 N
ATOM 85 N GLU A 14 -14.917 20.701 19.638 1.00 54.72 N
ANISOU 85 N GLU A 14 8108 6549 6134 -141 307 -348 N
ATOM 86 CA GLU A 14 -15.397 20.944 18.273 1.00 53.60 C
ANISOU 86 CA GLU A 14 7860 6366 6138 -36 287 -341 C
ATOM 87 C GLU A 14 -15.027 19.764 17.373 1.00 52.18 C
ANISOU 87 C GLU A 14 7614 6216 5997 -10 171 -265 C
ATOM 88 O GLU A 14 -15.792 19.414 16.470 1.00 52.84 O
ANISOU 88 O GLU A 14 7625 6274 6179 47 153 -242 O
ATOM 89 CB GLU A 14 -14.736 22.207 17.687 1.00 56.22 C
ANISOU 89 CB GLU A 14 8223 6656 6482 -16 266 -378 C
ATOM 90 CG GLU A 14 -15.413 23.538 17.981 1.00 62.39 C
ANISOU 90 CG GLU A 14 9037 7365 7302 5 389 -455 C
ATOM 91 CD GLU A 14 -14.606 24.741 17.507 1.00 70.28 C
ANISOU 91 CD GLU A 14 10083 8324 8295 8 355 -486 C
ATOM 92 OE1 GLU A 14 -13.779 24.580 16.578 1.00 70.84 O
ANISOU 92 OE1 GLU A 14 10126 8413 8376 22 243 -441 O
ATOM 93 OE2 GLU A 14 -14.796 25.846 18.068 1.00 73.81 O
ANISOU 93 OE2 GLU A 14 10603 8711 8729 -8 455 -559 O
ATOM 94 N ALA A 15 -13.821 19.214 17.559 1.00 50.42 N
ANISOU 94 N ALA A 15 7418 6029 5708 -56 89 -224 N
ATOM 95 CA ALA A 15 -13.334 18.090 16.783 1.00 50.06 C
ANISOU 95 CA ALA A 15 7322 5991 5707 -31 10 -160 C
ATOM 96 C ALA A 15 -14.073 16.831 17.188 1.00 50.37 C
ANISOU 96 C ALA A 15 7331 6053 5753 -43 13 -120 C
ATOM 97 O ALA A 15 -14.418 16.034 16.324 1.00 50.59 O
ANISOU 97 O ALA A 15 7316 6061 5845 -4 -16 -91 O
ATOM 98 CB ALA A 15 -11.844 17.908 16.997 1.00 49.94 C
ANISOU 98 CB ALA A 15 7320 5991 5665 -73 -60 -114 C
ATOM 99 N PHE A 16 -14.328 16.639 18.500 1.00 49.54 N
ANISOU 99 N PHE A 16 7267 5985 5571 -111 50 -117 N
ATOM 100 CA PHE A 16 -15.069 15.475 18.950 1.00 49.53 C
ANISOU 100 CA PHE A 16 7241 6006 5574 -131 62 -75 C
ATOM 101 C PHE A 16 -16.495 15.454 18.315 1.00 49.27 C
ANISOU 101 C PHE A 16 7134 5941 5645 -70 120 -93 C
ATOM 102 O PHE A 16 -16.858 14.463 17.703 1.00 48.05 O
ANISOU 102 O PHE A 16 6928 5777 5552 -49 71 -48 O
ATOM 103 CB PHE A 16 -15.158 15.438 20.478 1.00 48.77 C
ANISOU 103 CB PHE A 16 7229 5945 5356 -230 110 -75 C
ATOM 104 CG PHE A 16 -15.738 14.143 20.987 1.00 49.02 C
ANISOU 104 CG PHE A 16 7242 6002 5383 -265 110 -16 C
ATOM 105 CD1 PHE A 16 -14.930 13.040 21.198 1.00 49.27 C
ANISOU 105 CD1 PHE A 16 7271 6053 5397 -305 -2 72 C
ATOM 106 CD2 PHE A 16 -17.086 14.034 21.277 1.00 49.84 C
ANISOU 106 CD2 PHE A 16 7319 6098 5519 -258 226 -38 C
ATOM 107 CE1 PHE A 16 -15.460 11.862 21.688 1.00 49.84 C
ANISOU 107 CE1 PHE A 16 7332 6141 5464 -342 -6 131 C
ATOM 108 CE2 PHE A 16 -17.618 12.839 21.749 1.00 50.19 C
ANISOU 108 CE2 PHE A 16 7346 6163 5562 -297 228 22 C
ATOM 109 CZ PHE A 16 -16.803 11.762 21.944 1.00 49.76 C
ANISOU 109 CZ PHE A 16 7306 6131 5469 -340 108 103 C
ATOM 110 N SER A 17 -17.239 16.573 18.401 1.00 49.59 N
ANISOU 110 N SER A 17 7168 5951 5722 -45 215 -152 N
ATOM 111 CA SER A 17 -18.597 16.687 17.874 1.00 51.01 C
ANISOU 111 CA SER A 17 7252 6087 6041 8 262 -148 C
ATOM 112 C SER A 17 -18.688 16.485 16.367 1.00 51.62 C
ANISOU 112 C SER A 17 7276 6128 6209 59 146 -111 C
ATOM 113 O SER A 17 -19.730 16.045 15.869 1.00 52.33 O
ANISOU 113 O SER A 17 7286 6189 6409 76 121 -68 O
ATOM 114 CB SER A 17 -19.214 18.018 18.278 1.00 53.92 C
ANISOU 114 CB SER A 17 7618 6409 6459 31 396 -211 C
ATOM 115 OG SER A 17 -19.143 18.134 19.693 1.00 58.53 O
ANISOU 115 OG SER A 17 8296 7016 6927 -39 518 -254 O
ATOM 116 N LEU A 18 -17.599 16.775 15.633 1.00 50.83 N
ANISOU 116 N LEU A 18 7228 6022 6061 70 74 -122 N
ATOM 117 CA LEU A 18 -17.567 16.536 14.205 1.00 51.19 C
ANISOU 117 CA LEU A 18 7271 6026 6152 96 -23 -94 C
ATOM 118 C LEU A 18 -17.633 15.020 13.953 1.00 50.61 C
ANISOU 118 C LEU A 18 7199 5959 6073 72 -80 -44 C
ATOM 119 O LEU A 18 -18.323 14.597 13.026 1.00 51.21 O
ANISOU 119 O LEU A 18 7261 5991 6204 72 -148 -11 O
ATOM 120 CB LEU A 18 -16.298 17.146 13.583 1.00 52.44 C
ANISOU 120 CB LEU A 18 7499 6173 6255 106 -50 -120 C
ATOM 121 CG LEU A 18 -16.022 16.763 12.140 1.00 56.05 C
ANISOU 121 CG LEU A 18 8000 6580 6715 112 -123 -99 C
ATOM 122 CD1 LEU A 18 -17.132 17.252 11.222 1.00 57.87 C
ANISOU 122 CD1 LEU A 18 8213 6756 7019 122 -181 -79 C
ATOM 123 CD2 LEU A 18 -14.683 17.291 11.679 1.00 57.33 C
ANISOU 123 CD2 LEU A 18 8223 6732 6829 118 -113 -122 C
ATOM 124 N PHE A 19 -16.957 14.205 14.784 1.00 49.19 N
ANISOU 124 N PHE A 19 7037 5822 5829 43 -66 -30 N
ATOM 125 CA PHE A 19 -16.996 12.755 14.620 1.00 48.97 C
ANISOU 125 CA PHE A 19 7010 5787 5808 23 -111 19 C
ATOM 126 C PHE A 19 -18.249 12.165 15.278 1.00 49.89 C
ANISOU 126 C PHE A 19 7066 5922 5969 -3 -90 52 C
ATOM 127 O PHE A 19 -18.897 11.310 14.692 1.00 49.90 O
ANISOU 127 O PHE A 19 7049 5891 6020 -14 -144 89 O
ATOM 128 CB PHE A 19 -15.705 12.091 15.120 1.00 48.10 C
ANISOU 128 CB PHE A 19 6929 5696 5648 5 -119 42 C
ATOM 129 CG PHE A 19 -14.457 12.470 14.343 1.00 48.20 C
ANISOU 129 CG PHE A 19 6979 5675 5658 33 -128 26 C
ATOM 130 CD1 PHE A 19 -13.727 13.595 14.676 1.00 48.31 C
ANISOU 130 CD1 PHE A 19 7002 5711 5643 33 -109 -1 C
ATOM 131 CD2 PHE A 19 -14.008 11.691 13.292 1.00 48.83 C
ANISOU 131 CD2 PHE A 19 7095 5690 5768 50 -140 37 C
ATOM 132 CE1 PHE A 19 -12.589 13.950 13.960 1.00 48.95 C
ANISOU 132 CE1 PHE A 19 7103 5757 5739 55 -107 -7 C
ATOM 133 CE2 PHE A 19 -12.847 12.035 12.594 1.00 49.31 C
ANISOU 133 CE2 PHE A 19 7188 5709 5840 75 -113 22 C
ATOM 134 CZ PHE A 19 -12.156 13.172 12.923 1.00 48.79 C
ANISOU 134 CZ PHE A 19 7107 5673 5759 79 -99 6 C
ATOM 135 N ASP A 20 -18.623 12.641 16.468 1.00 50.74 N
ANISOU 135 N ASP A 20 7152 6070 6057 -22 -2 36 N
ATOM 136 CA ASP A 20 -19.822 12.170 17.173 1.00 51.78 C
ANISOU 136 CA ASP A 20 7222 6213 6239 -49 57 65 C
ATOM 137 C ASP A 20 -21.100 12.777 16.539 1.00 53.73 C
ANISOU 137 C ASP A 20 7373 6410 6633 -12 70 72 C
ATOM 138 O ASP A 20 -21.713 13.681 17.103 1.00 53.64 O
ANISOU 138 O ASP A 20 7318 6388 6675 4 184 43 O
ATOM 139 CB ASP A 20 -19.715 12.511 18.658 1.00 52.32 C
ANISOU 139 CB ASP A 20 7335 6327 6218 -95 172 39 C
ATOM 140 CG ASP A 20 -20.862 11.983 19.508 1.00 55.45 C
ANISOU 140 CG ASP A 20 7685 6732 6652 -134 269 68 C
ATOM 141 OD1 ASP A 20 -21.583 11.054 19.043 1.00 55.41 O
ANISOU 141 OD1 ASP A 20 7605 6710 6738 -133 217 126 O
ATOM 142 OD2 ASP A 20 -21.052 12.499 20.628 1.00 56.43 O
ANISOU 142 OD2 ASP A 20 7859 6872 6711 -174 404 31 O
ATOM 143 N LYS A 21 -21.471 12.274 15.348 1.00 55.29 N
ANISOU 143 N LYS A 21 7545 6562 6900 -7 -49 116 N
ATOM 144 CA LYS A 21 -22.582 12.737 14.511 1.00 57.00 C
ANISOU 144 CA LYS A 21 7672 6719 7268 10 -103 155 C
ATOM 145 C LYS A 21 -23.927 12.836 15.219 1.00 58.28 C
ANISOU 145 C LYS A 21 7693 6868 7584 10 -11 195 C
ATOM 146 O LYS A 21 -24.673 13.772 14.946 1.00 59.22 O
ANISOU 146 O LYS A 21 7715 6935 7850 47 9 211 O
ATOM 147 CB LYS A 21 -22.706 11.865 13.251 1.00 58.84 C
ANISOU 147 CB LYS A 21 7944 6905 7508 -26 -267 206 C
ATOM 148 CG LYS A 21 -21.563 12.082 12.254 1.00 63.60 C
ANISOU 148 CG LYS A 21 8681 7485 7998 -19 -332 165 C
ATOM 149 CD LYS A 21 -21.843 13.277 11.332 1.00 68.36 C
ANISOU 149 CD LYS A 21 9279 8036 8658 0 -392 168 C
ATOM 150 CE LYS A 21 -20.636 13.717 10.530 1.00 71.86 C
ANISOU 150 CE LYS A 21 9858 8464 8983 8 -410 117 C
ATOM 151 NZ LYS A 21 -20.149 15.059 10.966 1.00 74.55 N
ANISOU 151 NZ LYS A 21 10179 8827 9321 60 -325 66 N
ATOM 152 N ASP A 22 -24.248 11.882 16.108 1.00 57.94 N
ANISOU 152 N ASP A 22 7629 6861 7525 -30 51 219 N
ATOM 153 CA ASP A 22 -25.526 11.879 16.825 1.00 57.84 C
ANISOU 153 CA ASP A 22 7480 6830 7667 -35 170 261 C
ATOM 154 C ASP A 22 -25.492 12.482 18.237 1.00 58.27 C
ANISOU 154 C ASP A 22 7560 6912 7667 -34 396 195 C
ATOM 155 O ASP A 22 -26.506 12.448 18.936 1.00 58.47 O
ANISOU 155 O ASP A 22 7487 6916 7812 -42 541 220 O
ATOM 156 CB ASP A 22 -26.074 10.456 16.906 1.00 58.50 C
ANISOU 156 CB ASP A 22 7526 6922 7781 -96 110 338 C
ATOM 157 CG ASP A 22 -25.235 9.500 17.732 1.00 60.55 C
ANISOU 157 CG ASP A 22 7904 7247 7856 -143 137 318 C
ATOM 158 OD1 ASP A 22 -24.279 9.962 18.400 1.00 59.15 O
ANISOU 158 OD1 ASP A 22 7831 7113 7532 -138 210 251 O
ATOM 159 OD2 ASP A 22 -25.519 8.291 17.697 1.00 64.05 O
ANISOU 159 OD2 ASP A 22 8336 7690 8309 -192 70 379 O
ATOM 160 N GLY A 23 -24.322 12.934 18.671 1.00 58.19 N
ANISOU 160 N GLY A 23 7693 6945 7473 -38 426 118 N
ATOM 161 CA GLY A 23 -24.129 13.555 19.971 1.00 58.65 C
ANISOU 161 CA GLY A 23 7833 7022 7430 -63 617 47 C
ATOM 162 C GLY A 23 -24.331 12.686 21.191 1.00 59.31 C
ANISOU 162 C GLY A 23 7968 7147 7419 -144 721 63 C
ATOM 163 O GLY A 23 -24.518 13.225 22.287 1.00 60.72 O
ANISOU 163 O GLY A 23 8216 7319 7534 -179 916 8 O
ATOM 164 N ASP A 24 -24.239 11.351 21.055 1.00 58.30 N
ANISOU 164 N ASP A 24 7836 7054 7263 -185 601 135 N
ATOM 165 CA ASP A 24 -24.445 10.469 22.220 1.00 57.80 C
ANISOU 165 CA ASP A 24 7826 7027 7107 -272 688 166 C
ATOM 166 C ASP A 24 -23.235 10.404 23.189 1.00 57.56 C
ANISOU 166 C ASP A 24 7986 7053 6831 -351 681 136 C
ATOM 167 O ASP A 24 -23.344 9.783 24.248 1.00 58.50 O
ANISOU 167 O ASP A 24 8182 7199 6844 -442 751 164 O
ATOM 168 CB ASP A 24 -24.915 9.051 21.808 1.00 58.37 C
ANISOU 168 CB ASP A 24 7818 7102 7257 -295 573 263 C
ATOM 169 CG ASP A 24 -23.885 8.150 21.148 1.00 62.62 C
ANISOU 169 CG ASP A 24 8417 7660 7717 -301 366 296 C
ATOM 170 OD1 ASP A 24 -22.819 8.657 20.751 1.00 63.33 O
ANISOU 170 OD1 ASP A 24 8577 7757 7727 -270 294 253 O
ATOM 171 OD2 ASP A 24 -24.163 6.940 20.996 1.00 65.08 O
ANISOU 171 OD2 ASP A 24 8698 7966 8061 -334 288 367 O
ATOM 172 N GLY A 25 -22.128 11.066 22.859 1.00 56.11 N
ANISOU 172 N GLY A 25 7877 6880 6564 -328 594 92 N
ATOM 173 CA GLY A 25 -20.956 11.071 23.734 1.00 55.54 C
ANISOU 173 CA GLY A 25 7967 6850 6284 -414 554 85 C
ATOM 174 C GLY A 25 -19.875 10.069 23.369 1.00 54.83 C
ANISOU 174 C GLY A 25 7889 6786 6157 -426 352 160 C
ATOM 175 O GLY A 25 -18.826 10.026 24.014 1.00 54.55 O
ANISOU 175 O GLY A 25 7962 6779 5987 -497 281 182 O
ATOM 176 N THR A 26 -20.122 9.234 22.345 1.00 54.15 N
ANISOU 176 N THR A 26 7694 6679 6201 -366 258 207 N
ATOM 177 CA THR A 26 -19.137 8.266 21.847 1.00 53.71 C
ANISOU 177 CA THR A 26 7640 6619 6147 -359 98 270 C
ATOM 178 C THR A 26 -19.048 8.301 20.325 1.00 51.93 C
ANISOU 178 C THR A 26 7346 6346 6039 -266 25 252 C
ATOM 179 O THR A 26 -20.037 8.542 19.642 1.00 52.56 O
ANISOU 179 O THR A 26 7356 6398 6218 -226 53 232 O
ATOM 180 CB THR A 26 -19.440 6.826 22.291 1.00 56.35 C
ANISOU 180 CB THR A 26 7967 6957 6486 -415 60 358 C
ATOM 181 OG1 THR A 26 -20.672 6.385 21.710 1.00 58.66 O
ANISOU 181 OG1 THR A 26 8165 7221 6902 -386 91 367 O
ATOM 182 CG2 THR A 26 -19.458 6.658 23.794 1.00 56.74 C
ANISOU 182 CG2 THR A 26 8114 7049 6395 -530 117 391 C
ATOM 183 N ILE A 27 -17.862 8.044 19.798 1.00 50.06 N
ANISOU 183 N ILE A 27 7132 6090 5797 -242 -69 268 N
ATOM 184 CA ILE A 27 -17.615 7.947 18.374 1.00 48.78 C
ANISOU 184 CA ILE A 27 6946 5871 5715 -173 -125 250 C
ATOM 185 C ILE A 27 -17.562 6.460 18.035 1.00 48.74 C
ANISOU 185 C ILE A 27 6936 5823 5760 -182 -187 311 C
ATOM 186 O ILE A 27 -16.793 5.707 18.630 1.00 48.47 O
ANISOU 186 O ILE A 27 6918 5789 5710 -211 -223 370 O
ATOM 187 CB ILE A 27 -16.310 8.671 17.987 1.00 48.34 C
ANISOU 187 CB ILE A 27 6922 5806 5639 -140 -148 221 C
ATOM 188 CG1 ILE A 27 -16.333 10.141 18.464 1.00 48.90 C
ANISOU 188 CG1 ILE A 27 7014 5914 5650 -144 -89 161 C
ATOM 189 CG2 ILE A 27 -16.031 8.557 16.478 1.00 48.19 C
ANISOU 189 CG2 ILE A 27 6908 5717 5684 -80 -178 197 C
ATOM 190 CD1 ILE A 27 -14.947 10.823 18.387 1.00 49.85 C
ANISOU 190 CD1 ILE A 27 7166 6035 5741 -137 -123 151 C
ATOM 191 N THR A 28 -18.433 6.022 17.138 1.00 48.67 N
ANISOU 191 N THR A 28 6908 5768 5816 -170 -208 308 N
ATOM 192 CA THR A 28 -18.488 4.623 16.717 1.00 48.43 C
ANISOU 192 CA THR A 28 6894 5678 5831 -186 -262 355 C
ATOM 193 C THR A 28 -17.732 4.442 15.390 1.00 48.63 C
ANISOU 193 C THR A 28 6982 5617 5879 -143 -289 321 C
ATOM 194 O THR A 28 -17.396 5.440 14.721 1.00 49.42 O
ANISOU 194 O THR A 28 7104 5711 5961 -107 -274 265 O
ATOM 195 CB THR A 28 -19.966 4.194 16.571 1.00 49.02 C
ANISOU 195 CB THR A 28 6923 5743 5958 -224 -277 379 C
ATOM 196 OG1 THR A 28 -20.542 4.837 15.428 1.00 49.63 O
ANISOU 196 OG1 THR A 28 6999 5782 6076 -203 -311 342 O
ATOM 197 CG2 THR A 28 -20.784 4.488 17.823 1.00 49.00 C
ANISOU 197 CG2 THR A 28 6858 5812 5946 -263 -204 403 C
ATOM 198 N THR A 29 -17.524 3.174 14.961 1.00 47.29 N
ANISOU 198 N THR A 29 6854 5367 5746 -153 -315 349 N
ATOM 199 CA THR A 29 -16.869 2.881 13.695 1.00 46.36 C
ANISOU 199 CA THR A 29 6825 5144 5644 -124 -305 308 C
ATOM 200 C THR A 29 -17.649 3.493 12.525 1.00 45.34 C
ANISOU 200 C THR A 29 6759 4986 5483 -140 -337 255 C
ATOM 201 O THR A 29 -17.038 3.939 11.557 1.00 45.04 O
ANISOU 201 O THR A 29 6803 4893 5417 -117 -309 202 O
ATOM 202 CB THR A 29 -16.730 1.372 13.512 1.00 47.05 C
ANISOU 202 CB THR A 29 6960 5136 5782 -142 -312 344 C
ATOM 203 OG1 THR A 29 -18.036 0.794 13.597 1.00 48.06 O
ANISOU 203 OG1 THR A 29 7082 5270 5910 -206 -374 373 O
ATOM 204 CG2 THR A 29 -15.805 0.742 14.540 1.00 46.96 C
ANISOU 204 CG2 THR A 29 6886 5128 5827 -124 -297 415 C
ATOM 205 N LYS A 30 -18.993 3.507 12.619 1.00 44.52 N
ANISOU 205 N LYS A 30 6612 4911 5393 -188 -399 281 N
ATOM 206 CA LYS A 30 -19.849 4.074 11.590 1.00 44.41 C
ANISOU 206 CA LYS A 30 6634 4865 5375 -220 -469 264 C
ATOM 207 C LYS A 30 -19.650 5.556 11.486 1.00 45.16 C
ANISOU 207 C LYS A 30 6698 5007 5453 -176 -444 226 C
ATOM 208 O LYS A 30 -19.517 6.055 10.385 1.00 45.76 O
ANISOU 208 O LYS A 30 6863 5030 5492 -183 -476 193 O
ATOM 209 CB LYS A 30 -21.314 3.775 11.850 1.00 44.54 C
ANISOU 209 CB LYS A 30 6565 4897 5459 -278 -544 327 C
ATOM 210 CG LYS A 30 -21.667 2.305 11.789 1.00 46.32 C
ANISOU 210 CG LYS A 30 6835 5062 5703 -340 -593 369 C
ATOM 211 CD LYS A 30 -23.177 2.178 11.676 1.00 49.23 C
ANISOU 211 CD LYS A 30 7125 5426 6156 -412 -694 437 C
ATOM 212 CE LYS A 30 -23.877 2.088 12.995 1.00 52.93 C
ANISOU 212 CE LYS A 30 7432 5976 6703 -411 -639 495 C
ATOM 213 NZ LYS A 30 -23.478 0.853 13.731 1.00 57.37 N
ANISOU 213 NZ LYS A 30 8018 6535 7244 -428 -603 521 N
ATOM 214 N GLU A 31 -19.618 6.272 12.609 1.00 45.18 N
ANISOU 214 N GLU A 31 6596 5101 5471 -141 -383 229 N
ATOM 215 CA GLU A 31 -19.416 7.720 12.601 1.00 45.05 C
ANISOU 215 CA GLU A 31 6553 5121 5442 -100 -349 189 C
ATOM 216 C GLU A 31 -18.005 8.029 12.070 1.00 45.85 C
ANISOU 216 C GLU A 31 6740 5195 5484 -63 -313 141 C
ATOM 217 O GLU A 31 -17.860 8.867 11.195 1.00 46.08 O
ANISOU 217 O GLU A 31 6819 5195 5492 -51 -325 107 O
ATOM 218 CB GLU A 31 -19.594 8.281 14.013 1.00 45.28 C
ANISOU 218 CB GLU A 31 6489 5237 5480 -87 -271 193 C
ATOM 219 CG GLU A 31 -21.002 8.109 14.539 1.00 47.99 C
ANISOU 219 CG GLU A 31 6734 5597 5903 -117 -265 238 C
ATOM 220 CD GLU A 31 -21.208 8.592 15.960 1.00 51.39 C
ANISOU 220 CD GLU A 31 7108 6096 6322 -119 -150 232 C
ATOM 221 OE1 GLU A 31 -20.353 8.301 16.828 1.00 53.37 O
ANISOU 221 OE1 GLU A 31 7405 6388 6485 -134 -114 228 O
ATOM 222 OE2 GLU A 31 -22.218 9.284 16.202 1.00 51.65 O
ANISOU 222 OE2 GLU A 31 7055 6130 6440 -111 -94 234 O
ATOM 223 N LEU A 32 -16.975 7.303 12.550 1.00 46.17 N
ANISOU 223 N LEU A 32 6794 5234 5516 -50 -270 151 N
ATOM 224 CA LEU A 32 -15.613 7.506 12.066 1.00 46.95 C
ANISOU 224 CA LEU A 32 6945 5292 5601 -12 -220 122 C
ATOM 225 C LEU A 32 -15.526 7.236 10.546 1.00 47.82 C
ANISOU 225 C LEU A 32 7185 5295 5688 -23 -219 83 C
ATOM 226 O LEU A 32 -14.937 8.015 9.806 1.00 48.25 O
ANISOU 226 O LEU A 32 7298 5322 5712 -5 -184 42 O
ATOM 227 CB LEU A 32 -14.638 6.615 12.839 1.00 46.55 C
ANISOU 227 CB LEU A 32 6859 5236 5593 0 -191 168 C
ATOM 228 CG LEU A 32 -13.174 6.691 12.437 1.00 47.26 C
ANISOU 228 CG LEU A 32 6964 5270 5725 43 -128 161 C
ATOM 229 CD1 LEU A 32 -12.652 8.175 12.433 1.00 48.18 C
ANISOU 229 CD1 LEU A 32 7061 5435 5810 63 -110 126 C
ATOM 230 CD2 LEU A 32 -12.327 5.819 13.368 1.00 46.99 C
ANISOU 230 CD2 LEU A 32 6855 5227 5771 49 -129 240 C
ATOM 231 N GLY A 33 -16.165 6.161 10.105 1.00 47.19 N
ANISOU 231 N GLY A 33 7168 5153 5609 -68 -259 98 N
ATOM 232 CA GLY A 33 -16.207 5.791 8.713 1.00 46.74 C
ANISOU 232 CA GLY A 33 7276 4983 5499 -109 -265 61 C
ATOM 233 C GLY A 33 -16.870 6.842 7.857 1.00 47.26 C
ANISOU 233 C GLY A 33 7399 5048 5508 -145 -340 43 C
ATOM 234 O GLY A 33 -16.337 7.136 6.774 1.00 48.15 O
ANISOU 234 O GLY A 33 7658 5086 5552 -162 -304 -3 O
ATOM 235 N THR A 34 -18.024 7.440 8.316 1.00 46.57 N
ANISOU 235 N THR A 34 7200 5032 5462 -160 -434 86 N
ATOM 236 CA THR A 34 -18.675 8.433 7.461 1.00 47.29 C
ANISOU 236 CA THR A 34 7331 5105 5532 -196 -525 91 C
ATOM 237 C THR A 34 -17.834 9.705 7.390 1.00 47.41 C
ANISOU 237 C THR A 34 7341 5150 5522 -139 -456 48 C
ATOM 238 O THR A 34 -17.826 10.334 6.339 1.00 47.77 O
ANISOU 238 O THR A 34 7496 5143 5511 -173 -499 36 O
ATOM 239 CB THR A 34 -20.191 8.705 7.730 1.00 49.63 C
ANISOU 239 CB THR A 34 7504 5432 5922 -230 -647 163 C
ATOM 240 OG1 THR A 34 -20.389 9.798 8.626 1.00 52.72 O
ANISOU 240 OG1 THR A 34 7737 5905 6389 -165 -599 167 O
ATOM 241 CG2 THR A 34 -20.964 7.502 8.172 1.00 49.01 C
ANISOU 241 CG2 THR A 34 7378 5348 5895 -274 -692 213 C
ATOM 242 N VAL A 35 -17.130 10.086 8.478 1.00 47.00 N
ANISOU 242 N VAL A 35 7178 5175 5505 -69 -363 33 N
ATOM 243 CA VAL A 35 -16.280 11.271 8.444 1.00 47.36 C
ANISOU 243 CA VAL A 35 7220 5244 5531 -24 -304 -3 C
ATOM 244 C VAL A 35 -15.106 11.021 7.520 1.00 49.75 C
ANISOU 244 C VAL A 35 7657 5470 5776 -25 -228 -43 C
ATOM 245 O VAL A 35 -14.846 11.837 6.629 1.00 51.24 O
ANISOU 245 O VAL A 35 7935 5621 5914 -38 -225 -68 O
ATOM 246 CB VAL A 35 -15.839 11.759 9.846 1.00 47.14 C
ANISOU 246 CB VAL A 35 7063 5308 5541 25 -243 -4 C
ATOM 247 CG1 VAL A 35 -14.778 12.856 9.739 1.00 47.46 C
ANISOU 247 CG1 VAL A 35 7116 5356 5559 58 -187 -40 C
ATOM 248 CG2 VAL A 35 -17.038 12.249 10.654 1.00 46.81 C
ANISOU 248 CG2 VAL A 35 6914 5322 5552 24 -274 18 C
ATOM 249 N MET A 36 -14.455 9.865 7.646 1.00 50.27 N
ANISOU 249 N MET A 36 7747 5496 5857 -17 -159 -44 N
ATOM 250 CA MET A 36 -13.334 9.543 6.770 1.00 51.96 C
ANISOU 250 CA MET A 36 8082 5613 6047 -11 -45 -83 C
ATOM 251 C MET A 36 -13.718 9.534 5.285 1.00 53.00 C
ANISOU 251 C MET A 36 8425 5644 6070 -86 -66 -118 C
ATOM 252 O MET A 36 -12.965 10.090 4.497 1.00 53.79 O
ANISOU 252 O MET A 36 8625 5691 6121 -89 18 -156 O
ATOM 253 CB MET A 36 -12.639 8.250 7.195 1.00 53.02 C
ANISOU 253 CB MET A 36 8189 5701 6256 17 39 -68 C
ATOM 254 CG MET A 36 -11.816 8.428 8.459 1.00 54.04 C
ANISOU 254 CG MET A 36 8143 5906 6484 77 66 -24 C
ATOM 255 SD MET A 36 -11.033 6.884 8.911 1.00 57.30 S
ANISOU 255 SD MET A 36 8509 6243 7018 107 139 22 S
ATOM 256 CE MET A 36 -9.767 6.801 7.672 1.00 54.00 C
ANISOU 256 CE MET A 36 8197 5678 6643 138 325 -26 C
ATOM 257 N ARG A 37 -14.906 9.005 4.899 1.00 52.55 N
ANISOU 257 N ARG A 37 8441 5559 5968 -162 -189 -97 N
ATOM 258 CA ARG A 37 -15.324 9.068 3.485 1.00 52.29 C
ANISOU 258 CA ARG A 37 8635 5426 5807 -265 -248 -116 C
ATOM 259 C ARG A 37 -15.573 10.521 3.037 1.00 53.91 C
ANISOU 259 C ARG A 37 8846 5663 5975 -281 -326 -102 C
ATOM 260 O ARG A 37 -15.245 10.860 1.897 1.00 53.78 O
ANISOU 260 O ARG A 37 9027 5565 5843 -344 -304 -132 O
ATOM 261 CB ARG A 37 -16.529 8.184 3.191 1.00 50.65 C
ANISOU 261 CB ARG A 37 8500 5175 5571 -361 -394 -78 C
ATOM 262 CG ARG A 37 -16.188 6.711 3.255 1.00 50.33 C
ANISOU 262 CG ARG A 37 8533 5057 5534 -369 -305 -105 C
ATOM 263 CD ARG A 37 -17.372 5.850 2.901 1.00 50.38 C
ANISOU 263 CD ARG A 37 8630 5011 5503 -481 -460 -67 C
ATOM 264 NE ARG A 37 -18.416 5.914 3.921 1.00 50.48 N
ANISOU 264 NE ARG A 37 8413 5132 5634 -461 -591 14 N
ATOM 265 CZ ARG A 37 -18.465 5.136 5.001 1.00 50.59 C
ANISOU 265 CZ ARG A 37 8280 5195 5747 -408 -553 38 C
ATOM 266 NH1 ARG A 37 -17.520 4.224 5.216 1.00 46.12 N
ANISOU 266 NH1 ARG A 37 7754 4577 5193 -365 -410 -2 N
ATOM 267 NH2 ARG A 37 -19.442 5.282 5.886 1.00 51.30 N
ANISOU 267 NH2 ARG A 37 8178 5379 5937 -399 -648 108 N
ATOM 268 N SER A 38 -16.076 11.396 3.935 1.00 54.89 N
ANISOU 268 N SER A 38 8767 5894 6195 -225 -395 -61 N
ATOM 269 CA SER A 38 -16.253 12.825 3.578 1.00 56.64 C
ANISOU 269 CA SER A 38 8978 6134 6409 -226 -456 -47 C
ATOM 270 C SER A 38 -14.903 13.526 3.336 1.00 57.48 C
ANISOU 270 C SER A 38 9133 6232 6476 -183 -311 -101 C
ATOM 271 O SER A 38 -14.877 14.621 2.792 1.00 58.51 O
ANISOU 271 O SER A 38 9308 6351 6572 -200 -346 -96 O
ATOM 272 CB SER A 38 -17.003 13.593 4.665 1.00 59.41 C
ANISOU 272 CB SER A 38 9105 6580 6888 -166 -515 -4 C
ATOM 273 OG SER A 38 -17.986 12.825 5.347 1.00 64.10 O
ANISOU 273 OG SER A 38 9590 7205 7562 -173 -579 40 O
ATOM 274 N LEU A 39 -13.800 12.936 3.796 1.00 57.04 N
ANISOU 274 N LEU A 39 9045 6179 6450 -126 -157 -138 N
ATOM 275 CA LEU A 39 -12.455 13.438 3.581 1.00 57.34 C
ANISOU 275 CA LEU A 39 9106 6196 6485 -88 -9 -176 C
ATOM 276 C LEU A 39 -11.730 12.568 2.527 1.00 58.17 C
ANISOU 276 C LEU A 39 9412 6172 6517 -129 131 -221 C
ATOM 277 O LEU A 39 -10.525 12.351 2.636 1.00 59.19 O
ANISOU 277 O LEU A 39 9510 6268 6710 -77 300 -244 O
ATOM 278 CB LEU A 39 -11.675 13.424 4.914 1.00 57.24 C
ANISOU 278 CB LEU A 39 8891 6263 6594 1 61 -164 C
ATOM 279 CG LEU A 39 -12.347 14.129 6.109 1.00 58.48 C
ANISOU 279 CG LEU A 39 8878 6534 6808 33 -38 -134 C
ATOM 280 CD1 LEU A 39 -11.446 14.108 7.322 1.00 59.45 C
ANISOU 280 CD1 LEU A 39 8857 6720 7012 86 20 -120 C
ATOM 281 CD2 LEU A 39 -12.698 15.580 5.788 1.00 58.52 C
ANISOU 281 CD2 LEU A 39 8891 6556 6787 25 -97 -137 C
ATOM 282 N GLY A 40 -12.463 12.057 1.544 1.00 57.59 N
ANISOU 282 N GLY A 40 9543 6015 6324 -229 65 -230 N
ATOM 283 CA GLY A 40 -11.906 11.258 0.466 1.00 58.27 C
ANISOU 283 CA GLY A 40 9874 5959 6309 -292 209 -288 C
ATOM 284 C GLY A 40 -11.277 9.926 0.826 1.00 59.15 C
ANISOU 284 C GLY A 40 9962 6008 6504 -243 364 -315 C
ATOM 285 O GLY A 40 -10.515 9.389 0.019 1.00 59.74 O
ANISOU 285 O GLY A 40 10216 5949 6534 -267 555 -374 O
ATOM 286 N GLN A 41 -11.535 9.386 2.037 1.00 58.95 N
ANISOU 286 N GLN A 41 9723 6066 6610 -174 304 -272 N
ATOM 287 CA GLN A 41 -10.943 8.096 2.425 1.00 59.27 C
ANISOU 287 CA GLN A 41 9727 6039 6752 -126 435 -280 C
ATOM 288 C GLN A 41 -11.916 6.941 2.197 1.00 59.28 C
ANISOU 288 C GLN A 41 9850 5982 6693 -201 349 -283 C
ATOM 289 O GLN A 41 -13.109 7.174 2.020 1.00 59.64 O
ANISOU 289 O GLN A 41 9940 6070 6652 -279 157 -256 O
ATOM 290 CB GLN A 41 -10.508 8.111 3.908 1.00 60.97 C
ANISOU 290 CB GLN A 41 9654 6367 7144 -21 420 -219 C
ATOM 291 CG GLN A 41 -9.641 9.290 4.324 1.00 65.60 C
ANISOU 291 CG GLN A 41 10101 7026 7797 39 461 -202 C
ATOM 292 CD GLN A 41 -8.433 9.428 3.442 1.00 70.88 C
ANISOU 292 CD GLN A 41 10863 7581 8488 54 669 -243 C
ATOM 293 OE1 GLN A 41 -7.506 8.617 3.471 1.00 73.65 O
ANISOU 293 OE1 GLN A 41 11180 7838 8967 103 832 -239 O
ATOM 294 NE2 GLN A 41 -8.449 10.438 2.608 1.00 70.67 N
ANISOU 294 NE2 GLN A 41 10958 7546 8347 9 675 -277 N
ATOM 295 N ASN A 42 -11.420 5.700 2.213 1.00 58.84 N
ANISOU 295 N ASN A 42 9835 5819 6702 -180 484 -305 N
ATOM 296 CA ASN A 42 -12.290 4.535 2.094 1.00 59.18 C
ANISOU 296 CA ASN A 42 9985 5800 6701 -251 405 -305 C
ATOM 297 C ASN A 42 -11.824 3.429 3.035 1.00 57.63 C
ANISOU 297 C ASN A 42 9634 5584 6679 -167 482 -272 C
ATOM 298 O ASN A 42 -11.321 2.405 2.584 1.00 57.99 O
ANISOU 298 O ASN A 42 9806 5473 6754 -169 641 -316 O
ATOM 299 CB ASN A 42 -12.398 4.040 0.652 1.00 62.40 C
ANISOU 299 CB ASN A 42 10744 6033 6934 -374 479 -384 C
ATOM 300 CG ASN A 42 -13.585 3.123 0.438 1.00 69.75 C
ANISOU 300 CG ASN A 42 11806 6918 7779 -489 316 -372 C
ATOM 301 OD1 ASN A 42 -14.555 3.096 1.227 1.00 71.65 O
ANISOU 301 OD1 ASN A 42 11875 7276 8074 -492 114 -295 O
ATOM 302 ND2 ASN A 42 -13.537 2.340 -0.632 1.00 72.44 N
ANISOU 302 ND2 ASN A 42 12461 7077 7985 -596 410 -446 N
ATOM 303 N PRO A 43 -11.941 3.631 4.358 1.00 56.10 N
ANISOU 303 N PRO A 43 9175 5534 6604 -97 383 -194 N
ATOM 304 CA PRO A 43 -11.478 2.599 5.289 1.00 55.18 C
ANISOU 304 CA PRO A 43 8915 5399 6652 -29 432 -143 C
ATOM 305 C PRO A 43 -12.430 1.417 5.354 1.00 54.30 C
ANISOU 305 C PRO A 43 8876 5241 6515 -93 345 -130 C
ATOM 306 O PRO A 43 -13.637 1.609 5.305 1.00 54.69 O
ANISOU 306 O PRO A 43 8958 5358 6464 -171 176 -117 O
ATOM 307 CB PRO A 43 -11.441 3.331 6.627 1.00 55.71 C
ANISOU 307 CB PRO A 43 8727 5641 6799 28 326 -64 C
ATOM 308 CG PRO A 43 -12.486 4.369 6.503 1.00 56.26 C
ANISOU 308 CG PRO A 43 8815 5821 6742 -27 180 -74 C
ATOM 309 CD PRO A 43 -12.486 4.801 5.070 1.00 54.98 C
ANISOU 309 CD PRO A 43 8873 5566 6451 -84 230 -148 C
ATOM 310 N THR A 44 -11.893 0.203 5.480 1.00 53.11 N
ANISOU 310 N THR A 44 8734 4968 6477 -60 458 -124 N
ATOM 311 CA THR A 44 -12.725 -0.983 5.625 1.00 52.73 C
ANISOU 311 CA THR A 44 8747 4868 6421 -119 378 -106 C
ATOM 312 C THR A 44 -13.214 -1.073 7.088 1.00 52.49 C
ANISOU 312 C THR A 44 8474 4993 6477 -92 227 1 C
ATOM 313 O THR A 44 -12.627 -0.450 7.985 1.00 52.53 O
ANISOU 313 O THR A 44 8287 5105 6568 -20 223 55 O
ATOM 314 CB THR A 44 -11.914 -2.247 5.312 1.00 53.62 C
ANISOU 314 CB THR A 44 8946 4780 6649 -84 569 -133 C
ATOM 315 OG1 THR A 44 -10.840 -2.334 6.247 1.00 54.58 O
ANISOU 315 OG1 THR A 44 8833 4919 6986 35 647 -57 O
ATOM 316 CG2 THR A 44 -11.431 -2.301 3.899 1.00 53.96 C
ANISOU 316 CG2 THR A 44 9260 4641 6600 -122 762 -248 C
ATOM 317 N GLU A 45 -14.238 -1.921 7.331 1.00 51.50 N
ANISOU 317 N GLU A 45 8375 4865 6329 -161 112 33 N
ATOM 318 CA GLU A 45 -14.797 -2.217 8.626 1.00 51.64 C
ANISOU 318 CA GLU A 45 8209 5000 6413 -156 -8 129 C
ATOM 319 C GLU A 45 -13.685 -2.681 9.592 1.00 52.32 C
ANISOU 319 C GLU A 45 8138 5075 6666 -65 69 199 C
ATOM 320 O GLU A 45 -13.673 -2.255 10.747 1.00 52.36 O
ANISOU 320 O GLU A 45 7970 5218 6705 -43 -6 275 O
ATOM 321 CB GLU A 45 -15.901 -3.275 8.475 1.00 53.36 C
ANISOU 321 CB GLU A 45 8517 5161 6596 -251 -104 144 C
ATOM 322 CG GLU A 45 -15.456 -4.575 7.815 1.00 59.98 C
ANISOU 322 CG GLU A 45 9523 5793 7474 -265 7 104 C
ATOM 323 CD GLU A 45 -15.436 -4.562 6.296 1.00 69.27 C
ANISOU 323 CD GLU A 45 10978 6822 8521 -334 80 -8 C
ATOM 324 OE1 GLU A 45 -15.784 -3.514 5.692 1.00 71.38 O
ANISOU 324 OE1 GLU A 45 11307 7150 8662 -377 23 -44 O
ATOM 325 OE2 GLU A 45 -15.074 -5.606 5.706 1.00 70.86 O
ANISOU 325 OE2 GLU A 45 11350 6834 8742 -352 200 -58 O
ATOM 326 N ALA A 46 -12.705 -3.477 9.073 1.00 52.54 N
ANISOU 326 N ALA A 46 8234 4927 6801 -17 225 175 N
ATOM 327 CA ALA A 46 -11.570 -3.992 9.829 1.00 53.38 C
ANISOU 327 CA ALA A 46 8186 4983 7113 70 298 259 C
ATOM 328 C ALA A 46 -10.607 -2.877 10.199 1.00 54.48 C
ANISOU 328 C ALA A 46 8181 5208 7311 137 326 288 C
ATOM 329 O ALA A 46 -10.156 -2.840 11.336 1.00 55.72 O
ANISOU 329 O ALA A 46 8158 5441 7573 166 253 398 O
ATOM 330 CB ALA A 46 -10.845 -5.071 9.039 1.00 53.48 C
ANISOU 330 CB ALA A 46 8311 4758 7249 108 485 219 C
ATOM 331 N GLU A 47 -10.312 -1.958 9.278 1.00 54.14 N
ANISOU 331 N GLU A 47 8226 5155 7191 147 415 199 N
ATOM 332 CA GLU A 47 -9.422 -0.834 9.583 1.00 54.07 C
ANISOU 332 CA GLU A 47 8085 5225 7233 201 436 225 C
ATOM 333 C GLU A 47 -10.059 0.118 10.590 1.00 54.31 C
ANISOU 333 C GLU A 47 8007 5466 7163 165 256 270 C
ATOM 334 O GLU A 47 -9.360 0.653 11.454 1.00 54.88 O
ANISOU 334 O GLU A 47 7926 5615 7312 194 215 345 O
ATOM 335 CB GLU A 47 -9.052 -0.078 8.315 1.00 55.31 C
ANISOU 335 CB GLU A 47 8382 5318 7314 206 576 117 C
ATOM 336 CG GLU A 47 -8.121 -0.850 7.403 1.00 58.34 C
ANISOU 336 CG GLU A 47 8861 5480 7824 253 813 72 C
ATOM 337 CD GLU A 47 -8.060 -0.343 5.970 1.00 63.61 C
ANISOU 337 CD GLU A 47 9759 6057 8350 218 962 -57 C
ATOM 338 OE1 GLU A 47 -8.668 0.707 5.668 1.00 62.22 O
ANISOU 338 OE1 GLU A 47 9650 5997 7991 162 861 -98 O
ATOM 339 OE2 GLU A 47 -7.405 -1.011 5.142 1.00 68.30 O
ANISOU 339 OE2 GLU A 47 10479 6452 9020 241 1189 -114 O
ATOM 340 N LEU A 48 -11.387 0.325 10.492 1.00 53.47 N
ANISOU 340 N LEU A 48 7981 5441 6895 95 152 230 N
ATOM 341 CA LEU A 48 -12.110 1.198 11.415 1.00 53.14 C
ANISOU 341 CA LEU A 48 7848 5576 6768 63 20 261 C
ATOM 342 C LEU A 48 -12.075 0.608 12.820 1.00 53.65 C
ANISOU 342 C LEU A 48 7782 5701 6901 53 -60 370 C
ATOM 343 O LEU A 48 -11.795 1.333 13.767 1.00 53.45 O
ANISOU 343 O LEU A 48 7658 5785 6867 50 -115 418 O
ATOM 344 CB LEU A 48 -13.558 1.418 10.960 1.00 52.79 C
ANISOU 344 CB LEU A 48 7894 5575 6589 -5 -60 212 C
ATOM 345 CG LEU A 48 -13.705 2.253 9.716 1.00 53.89 C
ANISOU 345 CG LEU A 48 8160 5682 6634 -20 -31 126 C
ATOM 346 CD1 LEU A 48 -15.104 2.207 9.202 1.00 54.34 C
ANISOU 346 CD1 LEU A 48 8303 5746 6598 -100 -136 108 C
ATOM 347 CD2 LEU A 48 -13.278 3.682 9.974 1.00 54.47 C
ANISOU 347 CD2 LEU A 48 8157 5854 6686 15 -28 115 C
ATOM 348 N GLN A 49 -12.303 -0.710 12.952 1.00 53.59 N
ANISOU 348 N GLN A 49 7793 5613 6957 38 -68 413 N
ATOM 349 CA GLN A 49 -12.232 -1.360 14.263 1.00 54.49 C
ANISOU 349 CA GLN A 49 7798 5770 7135 17 -150 531 C
ATOM 350 C GLN A 49 -10.823 -1.320 14.860 1.00 55.52 C
ANISOU 350 C GLN A 49 7808 5875 7413 65 -142 622 C
ATOM 351 O GLN A 49 -10.687 -1.015 16.043 1.00 55.51 O
ANISOU 351 O GLN A 49 7721 5976 7394 27 -243 710 O
ATOM 352 CB GLN A 49 -12.749 -2.790 14.195 1.00 55.68 C
ANISOU 352 CB GLN A 49 7998 5824 7334 -10 -160 561 C
ATOM 353 CG GLN A 49 -14.251 -2.839 14.216 1.00 58.60 C
ANISOU 353 CG GLN A 49 8423 6265 7577 -87 -233 532 C
ATOM 354 CD GLN A 49 -14.729 -4.241 14.020 1.00 60.55 C
ANISOU 354 CD GLN A 49 8733 6402 7872 -122 -243 556 C
ATOM 355 OE1 GLN A 49 -14.300 -4.940 13.107 1.00 59.00 O
ANISOU 355 OE1 GLN A 49 8633 6047 7738 -96 -161 513 O
ATOM 356 NE2 GLN A 49 -15.623 -4.673 14.895 1.00 62.03 N
ANISOU 356 NE2 GLN A 49 8876 6663 8031 -187 -331 624 N
ATOM 357 N ASP A 50 -9.785 -1.583 14.041 1.00 56.22 N
ANISOU 357 N ASP A 50 7896 5820 7646 138 -20 607 N
ATOM 358 CA ASP A 50 -8.390 -1.508 14.480 1.00 57.83 C
ANISOU 358 CA ASP A 50 7955 5978 8038 188 -8 708 C
ATOM 359 C ASP A 50 -7.991 -0.073 14.910 1.00 59.00 C
ANISOU 359 C ASP A 50 8041 6260 8118 174 -66 712 C
ATOM 360 O ASP A 50 -7.285 0.090 15.897 1.00 59.56 O
ANISOU 360 O ASP A 50 7990 6372 8269 154 -166 833 O
ATOM 361 CB ASP A 50 -7.442 -2.025 13.381 1.00 59.62 C
ANISOU 361 CB ASP A 50 8196 6007 8451 275 182 675 C
ATOM 362 CG ASP A 50 -7.582 -3.514 13.086 1.00 65.57 C
ANISOU 362 CG ASP A 50 9001 6595 9317 293 251 688 C
ATOM 363 OD1 ASP A 50 -8.317 -4.208 13.830 1.00 67.24 O
ANISOU 363 OD1 ASP A 50 9212 6851 9486 239 128 748 O
ATOM 364 OD2 ASP A 50 -6.984 -3.979 12.100 1.00 67.95 O
ANISOU 364 OD2 ASP A 50 9359 6716 9744 356 442 632 O
ATOM 365 N MET A 51 -8.445 0.948 14.180 1.00 59.07 N
ANISOU 365 N MET A 51 8139 6325 7978 173 -16 589 N
ATOM 366 CA MET A 51 -8.182 2.361 14.498 1.00 59.93 C
ANISOU 366 CA MET A 51 8211 6551 8008 157 -60 575 C
ATOM 367 C MET A 51 -8.741 2.700 15.888 1.00 60.12 C
ANISOU 367 C MET A 51 8204 6722 7918 76 -212 636 C
ATOM 368 O MET A 51 -8.099 3.409 16.673 1.00 60.07 O
ANISOU 368 O MET A 51 8131 6779 7914 45 -288 698 O
ATOM 369 CB MET A 51 -8.933 3.258 13.499 1.00 60.85 C
ANISOU 369 CB MET A 51 8453 6702 7967 156 -1 435 C
ATOM 370 CG MET A 51 -8.119 3.771 12.387 1.00 63.69 C
ANISOU 370 CG MET A 51 8844 6976 8379 209 130 375 C
ATOM 371 SD MET A 51 -9.236 4.782 11.393 1.00 67.26 S
ANISOU 371 SD MET A 51 9453 7482 8621 178 140 239 S
ATOM 372 CE MET A 51 -9.540 3.688 10.069 1.00 63.58 C
ANISOU 372 CE MET A 51 9154 6856 8149 179 252 170 C
ATOM 373 N ILE A 52 -9.972 2.231 16.152 1.00 59.90 N
ANISOU 373 N ILE A 52 8239 6739 7780 31 -248 613 N
ATOM 374 CA ILE A 52 -10.678 2.471 17.393 1.00 60.49 C
ANISOU 374 CA ILE A 52 8315 6938 7733 -51 -347 653 C
ATOM 375 C ILE A 52 -10.079 1.668 18.529 1.00 61.98 C
ANISOU 375 C ILE A 52 8436 7117 7997 -98 -447 801 C
ATOM 376 O ILE A 52 -9.927 2.210 19.610 1.00 62.22 O
ANISOU 376 O ILE A 52 8460 7234 7945 -173 -536 858 O
ATOM 377 CB ILE A 52 -12.199 2.236 17.204 1.00 59.85 C
ANISOU 377 CB ILE A 52 8304 6892 7542 -80 -331 587 C
ATOM 378 CG1 ILE A 52 -12.794 3.405 16.400 1.00 59.69 C
ANISOU 378 CG1 ILE A 52 8333 6911 7434 -58 -280 469 C
ATOM 379 CG2 ILE A 52 -12.930 1.991 18.546 1.00 59.80 C
ANISOU 379 CG2 ILE A 52 8295 6977 7449 -167 -400 651 C
ATOM 380 CD1 ILE A 52 -14.239 3.478 16.326 1.00 60.42 C
ANISOU 380 CD1 ILE A 52 8460 7048 7449 -92 -282 425 C
ATOM 381 N ASN A 53 -9.710 0.408 18.293 1.00 63.01 N
ANISOU 381 N ASN A 53 8529 7130 8282 -64 -439 869 N
ATOM 382 CA ASN A 53 -9.142 -0.430 19.347 1.00 64.52 C
ANISOU 382 CA ASN A 53 8649 7296 8571 -111 -553 1033 C
ATOM 383 C ASN A 53 -7.835 0.125 19.868 1.00 64.94 C
ANISOU 383 C ASN A 53 8604 7349 8723 -123 -636 1139 C
ATOM 384 O ASN A 53 -7.590 0.031 21.061 1.00 65.15 O
ANISOU 384 O ASN A 53 8610 7423 8721 -218 -784 1267 O
ATOM 385 CB ASN A 53 -8.989 -1.880 18.909 1.00 66.98 C
ANISOU 385 CB ASN A 53 8932 7458 9058 -60 -515 1085 C
ATOM 386 CG ASN A 53 -8.772 -2.812 20.080 1.00 72.43 C
ANISOU 386 CG ASN A 53 9569 8134 9818 -128 -653 1258 C
ATOM 387 OD1 ASN A 53 -7.635 -3.142 20.455 1.00 74.03 O
ANISOU 387 OD1 ASN A 53 9656 8259 10211 -116 -725 1401 O
ATOM 388 ND2 ASN A 53 -9.860 -3.240 20.703 1.00 73.70 N
ANISOU 388 ND2 ASN A 53 9805 8365 9835 -208 -701 1264 N
ATOM 389 N GLU A 54 -7.029 0.769 19.009 1.00 65.19 N
ANISOU 389 N GLU A 54 8586 7329 8856 -45 -550 1090 N
ATOM 390 CA GLU A 54 -5.761 1.357 19.450 1.00 66.18 C
ANISOU 390 CA GLU A 54 8598 7447 9099 -62 -635 1199 C
ATOM 391 C GLU A 54 -5.951 2.429 20.502 1.00 66.50 C
ANISOU 391 C GLU A 54 8697 7635 8934 -180 -765 1210 C
ATOM 392 O GLU A 54 -5.068 2.634 21.335 1.00 67.30 O
ANISOU 392 O GLU A 54 8730 7744 9097 -253 -915 1351 O
ATOM 393 CB GLU A 54 -5.014 1.985 18.275 1.00 69.23 C
ANISOU 393 CB GLU A 54 8938 7762 9605 37 -491 1122 C
ATOM 394 CG GLU A 54 -4.259 0.996 17.410 1.00 77.58 C
ANISOU 394 CG GLU A 54 9905 8633 10937 145 -357 1158 C
ATOM 395 CD GLU A 54 -3.733 1.592 16.116 1.00 88.82 C
ANISOU 395 CD GLU A 54 11332 9981 12433 234 -164 1049 C
ATOM 396 OE1 GLU A 54 -3.445 0.802 15.186 1.00 92.53 O
ANISOU 396 OE1 GLU A 54 11803 10294 13061 320 8 1016 O
ATOM 397 OE2 GLU A 54 -3.611 2.838 16.026 1.00 90.58 O
ANISOU 397 OE2 GLU A 54 11574 10294 12549 212 -175 993 O
ATOM 398 N VAL A 55 -7.068 3.151 20.439 1.00 65.49 N
ANISOU 398 N VAL A 55 8696 7612 8575 -205 -708 1067 N
ATOM 399 CA VAL A 55 -7.321 4.256 21.357 1.00 65.23 C
ANISOU 399 CA VAL A 55 8745 7701 8338 -311 -784 1047 C
ATOM 400 C VAL A 55 -8.413 3.956 22.403 1.00 64.67 C
ANISOU 400 C VAL A 55 8787 7713 8073 -416 -826 1052 C
ATOM 401 O VAL A 55 -8.576 4.717 23.359 1.00 64.82 O
ANISOU 401 O VAL A 55 8897 7815 7916 -528 -884 1051 O
ATOM 402 CB VAL A 55 -7.623 5.560 20.577 1.00 65.79 C
ANISOU 402 CB VAL A 55 8866 7815 8316 -262 -672 888 C
ATOM 403 CG1 VAL A 55 -6.555 5.822 19.525 1.00 66.66 C
ANISOU 403 CG1 VAL A 55 8879 7839 8610 -167 -610 884 C
ATOM 404 CG2 VAL A 55 -8.983 5.490 19.920 1.00 65.67 C
ANISOU 404 CG2 VAL A 55 8926 7821 8204 -215 -551 753 C
ATOM 405 N ASP A 56 -9.135 2.858 22.238 1.00 63.90 N
ANISOU 405 N ASP A 56 8692 7582 8004 -391 -788 1057 N
ATOM 406 CA ASP A 56 -10.201 2.481 23.136 1.00 64.15 C
ANISOU 406 CA ASP A 56 8817 7681 7877 -485 -803 1065 C
ATOM 407 C ASP A 56 -9.634 1.828 24.387 1.00 65.61 C
ANISOU 407 C ASP A 56 9010 7862 8055 -606 -969 1243 C
ATOM 408 O ASP A 56 -9.481 0.614 24.404 1.00 66.11 O
ANISOU 408 O ASP A 56 9017 7853 8250 -593 -1018 1346 O
ATOM 409 CB ASP A 56 -11.153 1.528 22.406 1.00 63.54 C
ANISOU 409 CB ASP A 56 8732 7558 7852 -417 -711 1014 C
ATOM 410 CG ASP A 56 -12.365 1.134 23.191 1.00 63.39 C
ANISOU 410 CG ASP A 56 8790 7601 7694 -503 -698 1015 C
ATOM 411 OD1 ASP A 56 -12.739 1.880 24.118 1.00 62.60 O
ANISOU 411 OD1 ASP A 56 8774 7589 7421 -598 -696 998 O
ATOM 412 OD2 ASP A 56 -12.942 0.077 22.888 1.00 64.93 O
ANISOU 412 OD2 ASP A 56 8970 7748 7954 -482 -678 1032 O
ATOM 413 N ALA A 57 -9.337 2.629 25.433 1.00 66.27 N
ANISOU 413 N ALA A 57 9182 8017 7982 -737 -1063 1283 N
ATOM 414 CA ALA A 57 -8.787 2.167 26.714 1.00 67.14 C
ANISOU 414 CA ALA A 57 9338 8129 8042 -893 -1255 1463 C
ATOM 415 C ALA A 57 -9.628 1.055 27.354 1.00 68.03 C
ANISOU 415 C ALA A 57 9516 8248 8087 -962 -1263 1524 C
ATOM 416 O ALA A 57 -9.066 0.012 27.711 1.00 68.62 O
ANISOU 416 O ALA A 57 9528 8254 8288 -995 -1404 1695 O
ATOM 417 CB ALA A 57 -8.600 3.335 27.671 1.00 67.20 C
ANISOU 417 CB ALA A 57 9493 8215 7826 -1044 -1322 1452 C
ATOM 418 N ASP A 58 -10.957 1.240 27.478 1.00 68.11 N
ANISOU 418 N ASP A 58 9630 8323 7924 -979 -1112 1397 N
ATOM 419 CA ASP A 58 -11.807 0.131 27.944 1.00 69.00 C
ANISOU 419 CA ASP A 58 9784 8434 8001 -1031 -1098 1452 C
ATOM 420 C ASP A 58 -12.124 -0.769 26.703 1.00 69.97 C
ANISOU 420 C ASP A 58 9771 8477 8338 -870 -1018 1413 C
ATOM 421 O ASP A 58 -11.612 -0.496 25.607 1.00 70.65 O
ANISOU 421 O ASP A 58 9758 8512 8574 -738 -977 1351 O
ATOM 422 CB ASP A 58 -13.066 0.637 28.679 1.00 69.84 C
ANISOU 422 CB ASP A 58 10048 8629 7860 -1130 -962 1355 C
ATOM 423 CG ASP A 58 -13.813 1.750 27.985 1.00 71.98 C
ANISOU 423 CG ASP A 58 10316 8941 8091 -1039 -773 1162 C
ATOM 424 OD1 ASP A 58 -13.624 1.922 26.777 1.00 71.33 O
ANISOU 424 OD1 ASP A 58 10114 8822 8167 -891 -736 1092 O
ATOM 425 OD2 ASP A 58 -14.597 2.439 28.655 1.00 74.34 O
ANISOU 425 OD2 ASP A 58 10741 9298 8206 -1120 -654 1084 O
ATOM 426 N GLY A 59 -12.923 -1.820 26.859 1.00 69.73 N
ANISOU 426 N GLY A 59 9752 8428 8316 -890 -994 1448 N
ATOM 427 CA GLY A 59 -13.233 -2.687 25.714 1.00 69.28 C
ANISOU 427 CA GLY A 59 9600 8283 8441 -762 -929 1410 C
ATOM 428 C GLY A 59 -14.579 -2.425 25.082 1.00 68.11 C
ANISOU 428 C GLY A 59 9472 8174 8234 -718 -773 1261 C
ATOM 429 O GLY A 59 -15.083 -3.286 24.361 1.00 69.31 O
ANISOU 429 O GLY A 59 9585 8258 8491 -662 -738 1245 O
ATOM 430 N ASN A 60 -15.171 -1.237 25.317 1.00 65.76 N
ANISOU 430 N ASN A 60 9231 7969 7785 -746 -682 1156 N
ATOM 431 CA ASN A 60 -16.530 -0.964 24.863 1.00 64.10 C
ANISOU 431 CA ASN A 60 9020 7791 7545 -717 -544 1042 C
ATOM 432 C ASN A 60 -16.719 -0.713 23.346 1.00 62.42 C
ANISOU 432 C ASN A 60 8736 7528 7452 -586 -491 935 C
ATOM 433 O ASN A 60 -17.845 -0.492 22.926 1.00 62.91 O
ANISOU 433 O ASN A 60 8784 7607 7513 -570 -408 862 O
ATOM 434 CB ASN A 60 -17.160 0.163 25.666 1.00 64.47 C
ANISOU 434 CB ASN A 60 9145 7930 7419 -790 -443 975 C
ATOM 435 CG ASN A 60 -16.748 1.556 25.285 1.00 65.57 C
ANISOU 435 CG ASN A 60 9290 8097 7526 -736 -401 873 C
ATOM 436 OD1 ASN A 60 -15.837 1.778 24.482 1.00 65.82 O
ANISOU 436 OD1 ASN A 60 9269 8089 7650 -653 -460 859 O
ATOM 437 ND2 ASN A 60 -17.423 2.525 25.876 1.00 65.94 N
ANISOU 437 ND2 ASN A 60 9406 8203 7447 -786 -282 798 N
ATOM 438 N GLY A 61 -15.651 -0.725 22.564 1.00 60.46 N
ANISOU 438 N GLY A 61 8450 7213 7308 -505 -536 932 N
ATOM 439 CA GLY A 61 -15.750 -0.558 21.120 1.00 59.33 C
ANISOU 439 CA GLY A 61 8280 7010 7253 -402 -485 835 C
ATOM 440 C GLY A 61 -16.041 0.828 20.566 1.00 58.03 C
ANISOU 440 C GLY A 61 8121 6895 7033 -360 -416 718 C
ATOM 441 O GLY A 61 -16.188 0.973 19.347 1.00 57.58 O
ANISOU 441 O GLY A 61 8062 6786 7031 -293 -386 645 O
ATOM 442 N THR A 62 -16.142 1.868 21.429 1.00 56.52 N
ANISOU 442 N THR A 62 7956 6794 6726 -408 -389 697 N
ATOM 443 CA THR A 62 -16.374 3.246 20.956 1.00 55.05 C
ANISOU 443 CA THR A 62 7772 6643 6501 -365 -321 590 C
ATOM 444 C THR A 62 -15.365 4.206 21.612 1.00 53.88 C
ANISOU 444 C THR A 62 7658 6537 6276 -393 -344 592 C
ATOM 445 O THR A 62 -14.725 3.842 22.598 1.00 53.74 O
ANISOU 445 O THR A 62 7671 6535 6214 -468 -416 682 O
ATOM 446 CB THR A 62 -17.814 3.704 21.216 1.00 55.91 C
ANISOU 446 CB THR A 62 7877 6798 6567 -392 -230 540 C
ATOM 447 OG1 THR A 62 -18.057 3.643 22.609 1.00 58.21 O
ANISOU 447 OG1 THR A 62 8219 7146 6752 -490 -198 584 O
ATOM 448 CG2 THR A 62 -18.843 2.864 20.495 1.00 55.79 C
ANISOU 448 CG2 THR A 62 7816 6739 6644 -376 -231 548 C
ATOM 449 N ILE A 63 -15.210 5.425 21.065 1.00 52.58 N
ANISOU 449 N ILE A 63 7495 6384 6099 -343 -300 504 N
ATOM 450 CA ILE A 63 -14.296 6.384 21.654 1.00 51.83 C
ANISOU 450 CA ILE A 63 7440 6323 5931 -379 -327 503 C
ATOM 451 C ILE A 63 -15.075 7.451 22.406 1.00 52.54 C
ANISOU 451 C ILE A 63 7600 6472 5892 -433 -235 431 C
ATOM 452 O ILE A 63 -15.948 8.063 21.815 1.00 52.70 O
ANISOU 452 O ILE A 63 7595 6489 5941 -377 -144 348 O
ATOM 453 CB ILE A 63 -13.380 6.997 20.582 1.00 51.07 C
ANISOU 453 CB ILE A 63 7304 6185 5916 -295 -338 464 C
ATOM 454 CG1 ILE A 63 -12.674 5.914 19.766 1.00 51.27 C
ANISOU 454 CG1 ILE A 63 7269 6126 6085 -235 -378 520 C
ATOM 455 CG2 ILE A 63 -12.391 7.993 21.191 1.00 50.63 C
ANISOU 455 CG2 ILE A 63 7280 6158 5798 -343 -382 473 C
ATOM 456 CD1 ILE A 63 -12.088 6.450 18.509 1.00 52.31 C
ANISOU 456 CD1 ILE A 63 7379 6204 6291 -150 -337 459 C
ATOM 457 N ASP A 64 -14.784 7.678 23.690 1.00 53.11 N
ANISOU 457 N ASP A 64 7767 6584 5828 -547 -255 467 N
ATOM 458 CA ASP A 64 -15.421 8.777 24.435 1.00 54.59 C
ANISOU 458 CA ASP A 64 8054 6807 5881 -606 -135 383 C
ATOM 459 C ASP A 64 -14.466 10.001 24.488 1.00 55.42 C
ANISOU 459 C ASP A 64 8216 6915 5928 -622 -170 342 C
ATOM 460 O ASP A 64 -13.343 9.909 23.990 1.00 55.96 O
ANISOU 460 O ASP A 64 8230 6964 6071 -592 -290 393 O
ATOM 461 CB ASP A 64 -15.880 8.339 25.839 1.00 56.33 C
ANISOU 461 CB ASP A 64 8394 7059 5951 -746 -99 428 C
ATOM 462 CG ASP A 64 -14.784 7.759 26.699 1.00 61.89 C
ANISOU 462 CG ASP A 64 9174 7772 6568 -866 -268 552 C
ATOM 463 OD1 ASP A 64 -13.600 8.020 26.408 1.00 62.58 O
ANISOU 463 OD1 ASP A 64 9232 7845 6701 -853 -398 593 O
ATOM 464 OD2 ASP A 64 -15.110 7.033 27.658 1.00 65.36 O
ANISOU 464 OD2 ASP A 64 9697 8228 6908 -977 -276 622 O
ATOM 465 N PHE A 65 -14.899 11.139 25.073 1.00 55.22 N
ANISOU 465 N PHE A 65 8296 6901 5785 -670 -54 250 N
ATOM 466 CA PHE A 65 -14.060 12.334 25.124 1.00 55.55 C
ANISOU 466 CA PHE A 65 8403 6936 5767 -694 -85 205 C
ATOM 467 C PHE A 65 -12.666 12.086 25.769 1.00 55.91 C
ANISOU 467 C PHE A 65 8507 6991 5744 -808 -278 317 C
ATOM 468 O PHE A 65 -11.689 12.446 25.122 1.00 56.25 O
ANISOU 468 O PHE A 65 8479 7017 5876 -761 -371 338 O
ATOM 469 CB PHE A 65 -14.796 13.521 25.764 1.00 55.37 C
ANISOU 469 CB PHE A 65 8510 6905 5623 -741 88 87 C
ATOM 470 CG PHE A 65 -14.203 14.858 25.401 1.00 56.22 C
ANISOU 470 CG PHE A 65 8648 6988 5725 -717 87 14 C
ATOM 471 CD1 PHE A 65 -14.248 15.323 24.105 1.00 56.97 C
ANISOU 471 CD1 PHE A 65 8609 7058 5979 -574 99 -28 C
ATOM 472 CD2 PHE A 65 -13.627 15.663 26.364 1.00 57.31 C
ANISOU 472 CD2 PHE A 65 8966 7121 5686 -853 71 -11 C
ATOM 473 CE1 PHE A 65 -13.692 16.547 23.770 1.00 57.87 C
ANISOU 473 CE1 PHE A 65 8752 7147 6090 -557 96 -89 C
ATOM 474 CE2 PHE A 65 -13.106 16.904 26.032 1.00 58.00 C
ANISOU 474 CE2 PHE A 65 9085 7180 5773 -836 71 -79 C
ATOM 475 CZ PHE A 65 -13.119 17.327 24.733 1.00 57.65 C
ANISOU 475 CZ PHE A 65 8889 7115 5902 -684 83 -114 C
ATOM 476 N PRO A 66 -12.501 11.456 26.967 1.00 55.85 N
ANISOU 476 N PRO A 66 8615 7005 5601 -959 -355 406 N
ATOM 477 CA PRO A 66 -11.131 11.211 27.476 1.00 55.60 C
ANISOU 477 CA PRO A 66 8608 6969 5547 -1068 -579 543 C
ATOM 478 C PRO A 66 -10.259 10.370 26.527 1.00 55.16 C
ANISOU 478 C PRO A 66 8347 6883 5729 -957 -707 650 C
ATOM 479 O PRO A 66 -9.115 10.730 26.301 1.00 56.14 O
ANISOU 479 O PRO A 66 8415 6984 5931 -962 -829 708 O
ATOM 480 CB PRO A 66 -11.355 10.485 28.810 1.00 56.34 C
ANISOU 480 CB PRO A 66 8857 7084 5467 -1243 -633 631 C
ATOM 481 CG PRO A 66 -12.753 10.737 29.163 1.00 56.79 C
ANISOU 481 CG PRO A 66 9015 7155 5407 -1248 -400 507 C
ATOM 482 CD PRO A 66 -13.520 10.953 27.912 1.00 55.41 C
ANISOU 482 CD PRO A 66 8672 6968 5413 -1049 -249 401 C
ATOM 483 N GLU A 67 -10.793 9.294 25.944 1.00 53.67 N
ANISOU 483 N GLU A 67 8048 6679 5665 -859 -664 671 N
ATOM 484 CA GLU A 67 -10.039 8.459 25.002 1.00 52.90 C
ANISOU 484 CA GLU A 67 7777 6528 5793 -750 -741 753 C
ATOM 485 C GLU A 67 -9.601 9.252 23.789 1.00 53.85 C
ANISOU 485 C GLU A 67 7809 6620 6032 -626 -685 673 C
ATOM 486 O GLU A 67 -8.497 9.053 23.295 1.00 54.25 O
ANISOU 486 O GLU A 67 7752 6621 6239 -584 -764 749 O
ATOM 487 CB GLU A 67 -10.871 7.253 24.540 1.00 51.37 C
ANISOU 487 CB GLU A 67 7518 6314 5685 -674 -677 759 C
ATOM 488 CG GLU A 67 -11.001 6.175 25.591 1.00 50.16 C
ANISOU 488 CG GLU A 67 7414 6169 5476 -786 -765 882 C
ATOM 489 CD GLU A 67 -12.021 5.103 25.262 1.00 52.25 C
ANISOU 489 CD GLU A 67 7640 6420 5794 -732 -687 873 C
ATOM 490 OE1 GLU A 67 -12.853 5.322 24.357 1.00 52.93 O
ANISOU 490 OE1 GLU A 67 7687 6502 5922 -630 -557 759 O
ATOM 491 OE2 GLU A 67 -11.984 4.031 25.903 1.00 50.99 O
ANISOU 491 OE2 GLU A 67 7490 6246 5639 -800 -771 992 O
ATOM 492 N PHE A 68 -10.467 10.152 23.315 1.00 53.64 N
ANISOU 492 N PHE A 68 7823 6614 5944 -571 -544 528 N
ATOM 493 CA PHE A 68 -10.193 11.000 22.178 1.00 54.12 C
ANISOU 493 CA PHE A 68 7826 6648 6088 -467 -486 447 C
ATOM 494 C PHE A 68 -9.022 11.927 22.483 1.00 54.54 C
ANISOU 494 C PHE A 68 7897 6699 6124 -527 -575 477 C
ATOM 495 O PHE A 68 -8.152 12.125 21.632 1.00 54.39 O
ANISOU 495 O PHE A 68 7784 6639 6241 -459 -594 495 O
ATOM 496 CB PHE A 68 -11.458 11.797 21.826 1.00 54.03 C
ANISOU 496 CB PHE A 68 7861 6656 6014 -419 -339 309 C
ATOM 497 CG PHE A 68 -11.331 12.764 20.676 1.00 54.67 C
ANISOU 497 CG PHE A 68 7904 6708 6160 -325 -285 226 C
ATOM 498 CD1 PHE A 68 -11.564 12.352 19.376 1.00 55.54 C
ANISOU 498 CD1 PHE A 68 7941 6776 6386 -219 -250 206 C
ATOM 499 CD2 PHE A 68 -11.035 14.100 20.901 1.00 55.28 C
ANISOU 499 CD2 PHE A 68 8042 6792 6168 -356 -269 168 C
ATOM 500 CE1 PHE A 68 -11.467 13.248 18.320 1.00 55.74 C
ANISOU 500 CE1 PHE A 68 7955 6772 6452 -150 -207 138 C
ATOM 501 CE2 PHE A 68 -10.936 14.992 19.847 1.00 55.51 C
ANISOU 501 CE2 PHE A 68 8042 6793 6258 -275 -224 100 C
ATOM 502 CZ PHE A 68 -11.158 14.559 18.566 1.00 55.50 C
ANISOU 502 CZ PHE A 68 7969 6755 6366 -175 -196 89 C
ATOM 503 N LEU A 69 -8.999 12.493 23.693 1.00 55.16 N
ANISOU 503 N LEU A 69 8109 6815 6034 -667 -623 484 N
ATOM 504 CA LEU A 69 -7.938 13.384 24.132 1.00 56.22 C
ANISOU 504 CA LEU A 69 8288 6946 6128 -760 -733 520 C
ATOM 505 C LEU A 69 -6.629 12.610 24.277 1.00 57.15 C
ANISOU 505 C LEU A 69 8293 7030 6389 -799 -919 700 C
ATOM 506 O LEU A 69 -5.584 13.084 23.837 1.00 57.16 O
ANISOU 506 O LEU A 69 8207 6999 6512 -782 -985 744 O
ATOM 507 CB LEU A 69 -8.317 13.995 25.478 1.00 56.67 C
ANISOU 507 CB LEU A 69 8556 7036 5940 -928 -740 488 C
ATOM 508 CG LEU A 69 -9.467 14.967 25.467 1.00 57.69 C
ANISOU 508 CG LEU A 69 8795 7173 5950 -900 -542 316 C
ATOM 509 CD1 LEU A 69 -9.770 15.444 26.886 1.00 57.54 C
ANISOU 509 CD1 LEU A 69 9014 7167 5681 -1083 -524 285 C
ATOM 510 CD2 LEU A 69 -9.151 16.140 24.593 1.00 58.07 C
ANISOU 510 CD2 LEU A 69 8800 7195 6067 -817 -496 231 C
ATOM 511 N THR A 70 -6.681 11.403 24.869 1.00 57.39 N
ANISOU 511 N THR A 70 8310 7060 6435 -848 -1002 814 N
ATOM 512 CA THR A 70 -5.485 10.581 25.021 1.00 58.42 C
ANISOU 512 CA THR A 70 8310 7141 6746 -877 -1182 1005 C
ATOM 513 C THR A 70 -4.927 10.217 23.654 1.00 59.15 C
ANISOU 513 C THR A 70 8203 7164 7107 -702 -1108 1011 C
ATOM 514 O THR A 70 -3.718 10.342 23.448 1.00 59.69 O
ANISOU 514 O THR A 70 8148 7180 7352 -701 -1200 1117 O
ATOM 515 CB THR A 70 -5.783 9.333 25.816 1.00 60.05 C
ANISOU 515 CB THR A 70 8541 7349 6925 -949 -1266 1120 C
ATOM 516 OG1 THR A 70 -6.286 9.690 27.111 1.00 60.84 O
ANISOU 516 OG1 THR A 70 8860 7507 6751 -1131 -1316 1111 O
ATOM 517 CG2 THR A 70 -4.566 8.416 25.927 1.00 60.65 C
ANISOU 517 CG2 THR A 70 8455 7354 7237 -964 -1453 1336 C
ATOM 518 N MET A 71 -5.824 9.914 22.675 1.00 58.47 N
ANISOU 518 N MET A 71 8101 7071 7045 -565 -928 888 N
ATOM 519 CA MET A 71 -5.454 9.625 21.292 1.00 58.22 C
ANISOU 519 CA MET A 71 7939 6965 7217 -411 -821 860 C
ATOM 520 C MET A 71 -4.664 10.798 20.723 1.00 60.08 C
ANISOU 520 C MET A 71 8138 7187 7505 -388 -800 824 C
ATOM 521 O MET A 71 -3.562 10.595 20.225 1.00 61.16 O
ANISOU 521 O MET A 71 8137 7249 7853 -341 -814 910 O
ATOM 522 CB MET A 71 -6.705 9.318 20.450 1.00 57.08 C
ANISOU 522 CB MET A 71 7841 6825 7023 -314 -660 724 C
ATOM 523 CG MET A 71 -6.479 9.313 18.948 1.00 56.17 C
ANISOU 523 CG MET A 71 7663 6636 7042 -182 -531 657 C
ATOM 524 SD MET A 71 -8.050 9.339 18.040 1.00 55.77 S
ANISOU 524 SD MET A 71 7706 6603 6882 -115 -394 499 S
ATOM 525 CE MET A 71 -8.434 11.107 18.097 1.00 54.04 C
ANISOU 525 CE MET A 71 7565 6452 6515 -141 -367 389 C
ATOM 526 N MET A 72 -5.168 12.022 20.897 1.00 60.49 N
ANISOU 526 N MET A 72 8307 7299 7378 -429 -767 711 N
ATOM 527 CA MET A 72 -4.465 13.208 20.430 1.00 61.74 C
ANISOU 527 CA MET A 72 8447 7445 7568 -420 -756 676 C
ATOM 528 C MET A 72 -3.124 13.453 21.131 1.00 63.74 C
ANISOU 528 C MET A 72 8633 7678 7908 -526 -932 826 C
ATOM 529 O MET A 72 -2.176 13.848 20.466 1.00 63.56 O
ANISOU 529 O MET A 72 8499 7605 8047 -483 -921 861 O
ATOM 530 CB MET A 72 -5.363 14.447 20.499 1.00 61.45 C
ANISOU 530 CB MET A 72 8553 7461 7334 -440 -679 524 C
ATOM 531 CG MET A 72 -6.478 14.416 19.473 1.00 62.76 C
ANISOU 531 CG MET A 72 8738 7624 7485 -321 -518 396 C
ATOM 532 SD MET A 72 -5.849 14.368 17.760 1.00 63.23 S
ANISOU 532 SD MET A 72 8692 7604 7729 -186 -419 377 S
ATOM 533 CE MET A 72 -4.902 15.919 17.740 1.00 62.19 C
ANISOU 533 CE MET A 72 8565 7471 7595 -231 -452 366 C
ATOM 534 N ALA A 73 -3.029 13.200 22.448 1.00 65.50 N
ANISOU 534 N ALA A 73 8924 7934 8030 -675 -1099 926 N
ATOM 535 CA ALA A 73 -1.777 13.402 23.190 1.00 67.80 C
ANISOU 535 CA ALA A 73 9160 8202 8401 -806 -1313 1096 C
ATOM 536 C ALA A 73 -0.695 12.408 22.752 1.00 70.64 C
ANISOU 536 C ALA A 73 9281 8471 9088 -737 -1371 1270 C
ATOM 537 O ALA A 73 0.466 12.799 22.654 1.00 71.16 O
ANISOU 537 O ALA A 73 9219 8488 9331 -765 -1464 1381 O
ATOM 538 CB ALA A 73 -2.019 13.297 24.686 1.00 67.81 C
ANISOU 538 CB ALA A 73 9328 8250 8187 -1002 -1484 1165 C
ATOM 539 N ARG A 74 -1.075 11.146 22.449 1.00 72.33 N
ANISOU 539 N ARG A 74 9430 8651 9402 -644 -1300 1293 N
ATOM 540 CA ARG A 74 -0.139 10.128 21.964 1.00 74.84 C
ANISOU 540 CA ARG A 74 9524 8857 10054 -558 -1307 1443 C
ATOM 541 C ARG A 74 0.372 10.532 20.583 1.00 77.18 C
ANISOU 541 C ARG A 74 9705 9085 10533 -412 -1116 1369 C
ATOM 542 O ARG A 74 1.570 10.434 20.315 1.00 77.79 O
ANISOU 542 O ARG A 74 9592 9072 10892 -386 -1144 1503 O
ATOM 543 CB ARG A 74 -0.819 8.746 21.823 1.00 76.63 C
ANISOU 543 CB ARG A 74 9743 9053 10321 -481 -1233 1444 C
ATOM 544 CG ARG A 74 -1.405 8.178 23.084 1.00 80.62 C
ANISOU 544 CG ARG A 74 10363 9616 10653 -614 -1390 1516 C
ATOM 545 CD ARG A 74 -1.705 6.708 22.923 1.00 85.19 C
ANISOU 545 CD ARG A 74 10875 10130 11362 -539 -1349 1574 C
ATOM 546 NE ARG A 74 -2.259 6.131 24.149 1.00 89.80 N
ANISOU 546 NE ARG A 74 11574 10768 11778 -676 -1499 1654 N
ATOM 547 CZ ARG A 74 -3.365 5.390 24.196 1.00 93.21 C
ANISOU 547 CZ ARG A 74 12097 11226 12092 -653 -1414 1583 C
ATOM 548 NH1 ARG A 74 -4.044 5.126 23.084 1.00 93.29 N
ANISOU 548 NH1 ARG A 74 12099 11212 12134 -504 -1201 1434 N
ATOM 549 NH2 ARG A 74 -3.798 4.906 25.352 1.00 93.49 N
ANISOU 549 NH2 ARG A 74 12242 11306 11974 -791 -1547 1667 N
ATOM 550 N LYS A 75 -0.539 10.979 19.705 1.00 78.21 N
ANISOU 550 N LYS A 75 9952 9250 10515 -323 -920 1167 N
ATOM 551 CA LYS A 75 -0.190 11.373 18.345 1.00 79.62 C
ANISOU 551 CA LYS A 75 10072 9365 10815 -201 -726 1081 C
ATOM 552 C LYS A 75 0.651 12.658 18.306 1.00 81.14 C
ANISOU 552 C LYS A 75 10227 9566 11038 -252 -773 1099 C
ATOM 553 O LYS A 75 1.435 12.842 17.376 1.00 81.41 O
ANISOU 553 O LYS A 75 10147 9519 11266 -174 -651 1109 O
ATOM 554 CB LYS A 75 -1.433 11.447 17.451 1.00 81.03 C
ANISOU 554 CB LYS A 75 10397 9573 10819 -117 -546 884 C
ATOM 555 CG LYS A 75 -1.291 10.597 16.195 1.00 85.33 C
ANISOU 555 CG LYS A 75 10887 10004 11529 14 -353 852 C
ATOM 556 CD LYS A 75 -2.103 9.316 16.210 1.00 89.39 C
ANISOU 556 CD LYS A 75 11445 10497 12021 48 -322 839 C
ATOM 557 CE LYS A 75 -2.234 8.729 14.814 1.00 92.71 C
ANISOU 557 CE LYS A 75 11897 10810 12517 158 -108 748 C
ATOM 558 NZ LYS A 75 -2.849 7.365 14.815 1.00 94.41 N
ANISOU 558 NZ LYS A 75 12142 10978 12752 186 -82 755 N
ATOM 559 N MET A 76 0.551 13.509 19.337 1.00 82.07 N
ANISOU 559 N MET A 76 10442 9767 10973 -392 -942 1111 N
ATOM 560 CA MET A 76 1.394 14.704 19.431 1.00 83.66 C
ANISOU 560 CA MET A 76 10615 9970 11203 -465 -1019 1145 C
ATOM 561 C MET A 76 2.843 14.343 19.855 1.00 85.63 C
ANISOU 561 C MET A 76 10649 10143 11746 -525 -1185 1380 C
ATOM 562 O MET A 76 3.787 15.047 19.504 1.00 85.57 O
ANISOU 562 O MET A 76 10530 10091 11891 -534 -1192 1435 O
ATOM 563 CB MET A 76 0.757 15.762 20.349 1.00 83.77 C
ANISOU 563 CB MET A 76 10839 10080 10912 -602 -1124 1061 C
ATOM 564 CG MET A 76 -0.391 16.491 19.677 1.00 85.14 C
ANISOU 564 CG MET A 76 11164 10297 10888 -526 -941 844 C
ATOM 565 SD MET A 76 -1.135 17.833 20.636 1.00 86.60 S
ANISOU 565 SD MET A 76 11588 10560 10757 -662 -1000 726 S
ATOM 566 CE MET A 76 -2.092 16.925 21.806 1.00 82.31 C
ANISOU 566 CE MET A 76 11169 10070 10034 -741 -1059 737 C
ATOM 567 N LYS A 77 3.013 13.217 20.567 1.00 87.30 N
ANISOU 567 N LYS A 77 10785 10327 12059 -562 -1316 1532 N
ATOM 568 CA LYS A 77 4.307 12.695 20.989 1.00 89.24 C
ANISOU 568 CA LYS A 77 10801 10483 12625 -612 -1490 1785 C
ATOM 569 C LYS A 77 4.936 11.847 19.862 1.00 90.91 C
ANISOU 569 C LYS A 77 10782 10558 13200 -431 -1282 1832 C
ATOM 570 O LYS A 77 6.153 11.865 19.693 1.00 91.10 O
ANISOU 570 O LYS A 77 10576 10484 13553 -423 -1318 1995 O
ATOM 571 CB LYS A 77 4.136 11.847 22.266 1.00 91.36 C
ANISOU 571 CB LYS A 77 11109 10774 12831 -740 -1729 1932 C
ATOM 572 CG LYS A 77 5.009 12.299 23.433 1.00 96.15 C
ANISOU 572 CG LYS A 77 11690 11385 13456 -955 -2062 2139 C
ATOM 573 CD LYS A 77 4.711 13.742 23.876 1.00101.20 C
ANISOU 573 CD LYS A 77 12558 12120 13775 -1096 -2128 2016 C
ATOM 574 CE LYS A 77 5.670 14.222 24.946 1.00105.15 C
ANISOU 574 CE LYS A 77 13047 12608 14299 -1327 -2468 2226 C
ATOM 575 NZ LYS A 77 5.388 15.623 25.368 1.00107.54 N
ANISOU 575 NZ LYS A 77 13595 12984 14283 -1470 -2517 2095 N
ATOM 576 N ASP A 78 4.103 11.105 19.098 1.00 91.88 N
ANISOU 576 N ASP A 78 10974 10664 13274 -293 -1058 1690 N
ATOM 577 CA ASP A 78 4.530 10.248 17.982 1.00 93.36 C
ANISOU 577 CA ASP A 78 11010 10710 13753 -126 -817 1694 C
ATOM 578 C ASP A 78 4.369 11.018 16.665 1.00 94.50 C
ANISOU 578 C ASP A 78 11229 10843 13832 -29 -553 1505 C
ATOM 579 O ASP A 78 3.248 11.130 16.163 1.00 95.15 O
ANISOU 579 O ASP A 78 11512 10987 13653 10 -431 1312 O
ATOM 580 CB ASP A 78 3.662 8.969 17.925 1.00 95.53 C
ANISOU 580 CB ASP A 78 11356 10963 13976 -58 -741 1645 C
ATOM 581 CG ASP A 78 3.935 7.925 19.005 1.00100.70 C
ANISOU 581 CG ASP A 78 11905 11584 14771 -123 -956 1853 C
ATOM 582 OD1 ASP A 78 5.016 7.990 19.644 1.00102.01 O
ANISOU 582 OD1 ASP A 78 11886 11702 15172 -199 -1148 2071 O
ATOM 583 OD2 ASP A 78 3.075 7.032 19.201 1.00102.26 O
ANISOU 583 OD2 ASP A 78 12201 11796 14855 -106 -943 1811 O
ATOM 584 N THR A 79 5.470 11.532 16.089 1.00 94.45 N
ANISOU 584 N THR A 79 11062 10753 14071 2 -466 1569 N
ATOM 585 CA THR A 79 5.400 12.328 14.856 1.00 94.91 C
ANISOU 585 CA THR A 79 11204 10796 14061 74 -224 1404 C
ATOM 586 C THR A 79 5.333 11.498 13.546 1.00 94.50 C
ANISOU 586 C THR A 79 11163 10614 14128 223 101 1309 C
ATOM 587 O THR A 79 5.867 11.931 12.522 1.00 94.64 O
ANISOU 587 O THR A 79 11157 10553 14250 281 318 1259 O
ATOM 588 CB THR A 79 6.564 13.341 14.819 1.00 96.65 C
ANISOU 588 CB THR A 79 11271 10988 14463 24 -266 1506 C
ATOM 589 OG1 THR A 79 7.811 12.639 14.817 1.00 97.83 O
ANISOU 589 OG1 THR A 79 11131 10990 15050 66 -242 1712 O
ATOM 590 CG2 THR A 79 6.528 14.308 15.996 1.00 96.95 C
ANISOU 590 CG2 THR A 79 11365 11150 14320 -143 -571 1561 C
ATOM 591 N ASP A 80 4.636 10.349 13.560 1.00 93.65 N
ANISOU 591 N ASP A 80 11124 10481 13978 272 141 1273 N
ATOM 592 CA ASP A 80 4.526 9.475 12.385 1.00 93.00 C
ANISOU 592 CA ASP A 80 11090 10261 13985 393 439 1179 C
ATOM 593 C ASP A 80 3.396 9.843 11.389 1.00 91.28 C
ANISOU 593 C ASP A 80 11153 10092 13436 411 590 946 C
ATOM 594 O ASP A 80 3.547 9.625 10.181 1.00 91.81 O
ANISOU 594 O ASP A 80 11293 10042 13550 482 859 853 O
ATOM 595 CB ASP A 80 4.358 8.008 12.834 1.00 95.13 C
ANISOU 595 CB ASP A 80 11299 10456 14388 430 408 1261 C
ATOM 596 CG ASP A 80 3.019 7.729 13.500 1.00100.61 C
ANISOU 596 CG ASP A 80 12176 11288 14766 370 240 1188 C
ATOM 597 OD1 ASP A 80 2.502 8.633 14.196 1.00101.21 O
ANISOU 597 OD1 ASP A 80 12337 11521 14597 274 50 1161 O
ATOM 598 OD2 ASP A 80 2.479 6.610 13.310 1.00103.22 O
ANISOU 598 OD2 ASP A 80 12566 11555 15096 418 315 1154 O
ATOM 599 N SER A 81 2.282 10.404 11.900 1.00 88.74 N
ANISOU 599 N SER A 81 10993 9933 12793 339 418 861 N
ATOM 600 CA SER A 81 1.049 10.707 11.167 1.00 86.52 C
ANISOU 600 CA SER A 81 10957 9709 12209 341 492 673 C
ATOM 601 C SER A 81 1.060 11.972 10.266 1.00 83.41 C
ANISOU 601 C SER A 81 10670 9334 11688 332 591 566 C
ATOM 602 O SER A 81 0.007 12.610 10.102 1.00 82.90 O
ANISOU 602 O SER A 81 10774 9363 11361 298 538 453 O
ATOM 603 CB SER A 81 -0.113 10.788 12.154 1.00 88.10 C
ANISOU 603 CB SER A 81 11249 10056 12170 272 280 648 C
ATOM 604 OG SER A 81 -1.326 10.271 11.637 1.00 90.39 O
ANISOU 604 OG SER A 81 11711 10356 12279 291 337 527 O
ATOM 605 N GLU A 82 2.213 12.294 9.635 1.00 80.74 N
ANISOU 605 N GLU A 82 10231 8895 11552 364 746 608 N
ATOM 606 CA GLU A 82 2.292 13.434 8.720 1.00 78.57 C
ANISOU 606 CA GLU A 82 10061 8623 11167 351 855 516 C
ATOM 607 C GLU A 82 1.419 13.170 7.492 1.00 74.50 C
ANISOU 607 C GLU A 82 9793 8060 10452 373 1024 359 C
ATOM 608 O GLU A 82 0.673 14.050 7.066 1.00 73.96 O
ANISOU 608 O GLU A 82 9889 8063 10150 333 986 262 O
ATOM 609 CB GLU A 82 3.747 13.694 8.289 1.00 82.82 C
ANISOU 609 CB GLU A 82 10430 9047 11993 380 1014 605 C
ATOM 610 CG GLU A 82 3.928 14.850 7.313 1.00 90.69 C
ANISOU 610 CG GLU A 82 11534 10034 12889 361 1144 521 C
ATOM 611 CD GLU A 82 4.795 14.544 6.102 1.00 99.88 C
ANISOU 611 CD GLU A 82 12695 11023 14231 417 1475 506 C
ATOM 612 OE1 GLU A 82 5.882 15.158 5.977 1.00101.05 O
ANISOU 612 OE1 GLU A 82 12690 11121 14582 415 1552 587 O
ATOM 613 OE2 GLU A 82 4.385 13.696 5.273 1.00103.08 O
ANISOU 613 OE2 GLU A 82 13260 11333 14572 456 1665 412 O
ATOM 614 N GLU A 83 1.483 11.936 6.961 1.00 71.50 N
ANISOU 614 N GLU A 83 9446 7552 10167 427 1194 343 N
ATOM 615 CA GLU A 83 0.725 11.491 5.790 1.00 68.63 C
ANISOU 615 CA GLU A 83 9338 7117 9621 427 1352 205 C
ATOM 616 C GLU A 83 -0.762 11.775 5.868 1.00 64.41 C
ANISOU 616 C GLU A 83 8983 6707 8783 371 1172 118 C
ATOM 617 O GLU A 83 -1.329 12.272 4.892 1.00 64.14 O
ANISOU 617 O GLU A 83 9157 6662 8550 333 1226 18 O
ATOM 618 CB GLU A 83 0.967 10.004 5.509 1.00 71.63 C
ANISOU 618 CB GLU A 83 9716 7341 10158 485 1523 213 C
ATOM 619 CG GLU A 83 2.043 9.754 4.467 1.00 79.08 C
ANISOU 619 CG GLU A 83 10667 8090 11289 532 1857 197 C
ATOM 620 CD GLU A 83 3.376 9.259 4.995 1.00 88.62 C
ANISOU 620 CD GLU A 83 11575 9192 12904 608 1949 348 C
ATOM 621 OE1 GLU A 83 3.375 8.576 6.048 1.00 90.57 O
ANISOU 621 OE1 GLU A 83 11650 9470 13293 630 1780 458 O
ATOM 622 OE2 GLU A 83 4.417 9.539 4.349 1.00 90.62 O
ANISOU 622 OE2 GLU A 83 11762 9323 13348 641 2190 367 O
ATOM 623 N GLU A 84 -1.398 11.465 7.014 1.00 61.07 N
ANISOU 623 N GLU A 84 8480 6391 8331 360 961 166 N
ATOM 624 CA GLU A 84 -2.837 11.684 7.180 1.00 58.63 C
ANISOU 624 CA GLU A 84 8306 6192 7779 313 803 97 C
ATOM 625 C GLU A 84 -3.201 13.141 7.252 1.00 55.69 C
ANISOU 625 C GLU A 84 7968 5925 7266 271 698 65 C
ATOM 626 O GLU A 84 -4.267 13.496 6.788 1.00 55.04 O
ANISOU 626 O GLU A 84 8035 5879 7000 239 646 -9 O
ATOM 627 CB GLU A 84 -3.408 10.912 8.372 1.00 60.29 C
ANISOU 627 CB GLU A 84 8429 6474 8003 308 643 156 C
ATOM 628 CG GLU A 84 -3.344 9.414 8.164 1.00 63.82 C
ANISOU 628 CG GLU A 84 8886 6807 8555 344 739 171 C
ATOM 629 CD GLU A 84 -3.570 8.603 9.422 1.00 69.64 C
ANISOU 629 CD GLU A 84 9501 7597 9362 341 592 262 C
ATOM 630 OE1 GLU A 84 -3.425 9.167 10.530 1.00 70.94 O
ANISOU 630 OE1 GLU A 84 9548 7870 9535 310 435 336 O
ATOM 631 OE2 GLU A 84 -3.885 7.397 9.299 1.00 72.18 O
ANISOU 631 OE2 GLU A 84 9862 7844 9720 358 634 262 O
ATOM 632 N ILE A 85 -2.309 13.986 7.794 1.00 54.44 N
ANISOU 632 N ILE A 85 7672 5804 7208 268 662 127 N
ATOM 633 CA ILE A 85 -2.498 15.433 7.838 1.00 53.76 C
ANISOU 633 CA ILE A 85 7619 5797 7010 229 582 96 C
ATOM 634 C ILE A 85 -2.377 15.974 6.420 1.00 53.37 C
ANISOU 634 C ILE A 85 7716 5671 6890 225 732 25 C
ATOM 635 O ILE A 85 -3.211 16.776 6.009 1.00 52.90 O
ANISOU 635 O ILE A 85 7784 5653 6662 192 671 -37 O
ATOM 636 CB ILE A 85 -1.518 16.133 8.812 1.00 53.55 C
ANISOU 636 CB ILE A 85 7421 5818 7109 208 495 188 C
ATOM 637 CG1 ILE A 85 -1.809 15.711 10.275 1.00 54.02 C
ANISOU 637 CG1 ILE A 85 7389 5962 7174 179 316 255 C
ATOM 638 CG2 ILE A 85 -1.590 17.667 8.654 1.00 53.27 C
ANISOU 638 CG2 ILE A 85 7440 5832 6969 168 450 145 C
ATOM 639 CD1 ILE A 85 -0.791 16.181 11.238 1.00 54.58 C
ANISOU 639 CD1 ILE A 85 7309 6059 7369 134 209 364 C
ATOM 640 N ARG A 86 -1.394 15.471 5.637 1.00 53.50 N
ANISOU 640 N ARG A 86 7727 5561 7038 254 937 37 N
ATOM 641 CA ARG A 86 -1.237 15.845 4.229 1.00 54.24 C
ANISOU 641 CA ARG A 86 7998 5562 7048 235 1113 -34 C
ATOM 642 C ARG A 86 -2.498 15.458 3.449 1.00 53.38 C
ANISOU 642 C ARG A 86 8128 5437 6716 196 1091 -123 C
ATOM 643 O ARG A 86 -2.980 16.251 2.647 1.00 53.68 O
ANISOU 643 O ARG A 86 8332 5475 6588 144 1076 -175 O
ATOM 644 CB ARG A 86 -0.003 15.171 3.600 1.00 56.89 C
ANISOU 644 CB ARG A 86 8290 5745 7582 276 1378 -10 C
ATOM 645 CG ARG A 86 1.314 15.700 4.127 1.00 62.46 C
ANISOU 645 CG ARG A 86 8758 6444 8531 300 1410 93 C
ATOM 646 CD ARG A 86 2.342 15.810 3.021 1.00 68.32 C
ANISOU 646 CD ARG A 86 9535 7039 9385 311 1701 82 C
ATOM 647 NE ARG A 86 3.426 16.757 3.307 1.00 72.17 N
ANISOU 647 NE ARG A 86 9834 7537 10050 307 1707 170 N
ATOM 648 CZ ARG A 86 3.718 17.811 2.545 1.00 74.09 C
ANISOU 648 CZ ARG A 86 10168 7764 10218 264 1796 138 C
ATOM 649 NH1 ARG A 86 2.975 18.100 1.484 1.00 73.61 N
ANISOU 649 NH1 ARG A 86 10392 7683 9895 217 1864 25 N
ATOM 650 NH2 ARG A 86 4.730 18.608 2.865 1.00 73.76 N
ANISOU 650 NH2 ARG A 86 9938 7727 10360 256 1793 229 N
ATOM 651 N GLU A 87 -3.062 14.285 3.734 1.00 52.54 N
ANISOU 651 N GLU A 87 8034 5319 6611 211 1060 -127 N
ATOM 652 CA GLU A 87 -4.285 13.824 3.085 1.00 53.70 C
ANISOU 652 CA GLU A 87 8392 5447 6563 162 1009 -195 C
ATOM 653 C GLU A 87 -5.503 14.662 3.494 1.00 53.35 C
ANISOU 653 C GLU A 87 8359 5531 6380 125 777 -199 C
ATOM 654 O GLU A 87 -6.335 14.970 2.648 1.00 53.87 O
ANISOU 654 O GLU A 87 8607 5579 6284 64 727 -241 O
ATOM 655 CB GLU A 87 -4.501 12.324 3.342 1.00 58.26 C
ANISOU 655 CB GLU A 87 8963 5970 7203 186 1040 -190 C
ATOM 656 CG GLU A 87 -5.850 11.769 2.915 1.00 67.10 C
ANISOU 656 CG GLU A 87 10266 7085 8142 125 938 -239 C
ATOM 657 CD GLU A 87 -6.376 12.060 1.515 1.00 77.78 C
ANISOU 657 CD GLU A 87 11903 8361 9287 34 971 -310 C
ATOM 658 OE1 GLU A 87 -5.676 11.741 0.525 1.00 79.92 O
ANISOU 658 OE1 GLU A 87 12335 8492 9539 13 1188 -359 O
ATOM 659 OE2 GLU A 87 -7.520 12.565 1.412 1.00 80.31 O
ANISOU 659 OE2 GLU A 87 12294 8751 9469 -24 780 -311 O
ATOM 660 N ALA A 88 -5.569 15.106 4.750 1.00 52.61 N
ANISOU 660 N ALA A 88 8080 5553 6357 154 644 -150 N
ATOM 661 CA ALA A 88 -6.654 15.974 5.200 1.00 52.76 C
ANISOU 661 CA ALA A 88 8096 5675 6277 130 467 -157 C
ATOM 662 C ALA A 88 -6.520 17.323 4.460 1.00 52.66 C
ANISOU 662 C ALA A 88 8164 5652 6193 100 474 -180 C
ATOM 663 O ALA A 88 -7.488 17.786 3.858 1.00 53.09 O
ANISOU 663 O ALA A 88 8337 5704 6130 59 391 -203 O
ATOM 664 CB ALA A 88 -6.575 16.185 6.713 1.00 52.62 C
ANISOU 664 CB ALA A 88 7893 5762 6339 155 366 -109 C
ATOM 665 N PHE A 89 -5.287 17.867 4.373 1.00 51.68 N
ANISOU 665 N PHE A 89 7982 5501 6152 114 579 -163 N
ATOM 666 CA PHE A 89 -5.029 19.135 3.686 1.00 51.45 C
ANISOU 666 CA PHE A 89 8026 5456 6067 83 598 -178 C
ATOM 667 C PHE A 89 -5.546 19.111 2.257 1.00 52.78 C
ANISOU 667 C PHE A 89 8431 5540 6083 24 642 -221 C
ATOM 668 O PHE A 89 -6.193 20.055 1.837 1.00 52.42 O
ANISOU 668 O PHE A 89 8471 5507 5938 -16 543 -227 O
ATOM 669 CB PHE A 89 -3.530 19.500 3.715 1.00 50.12 C
ANISOU 669 CB PHE A 89 7757 5252 6035 100 731 -143 C
ATOM 670 CG PHE A 89 -3.229 20.850 3.091 1.00 49.23 C
ANISOU 670 CG PHE A 89 7711 5125 5870 63 748 -152 C
ATOM 671 CD1 PHE A 89 -3.495 22.023 3.777 1.00 48.96 C
ANISOU 671 CD1 PHE A 89 7609 5170 5825 55 607 -141 C
ATOM 672 CD2 PHE A 89 -2.743 20.943 1.790 1.00 48.63 C
ANISOU 672 CD2 PHE A 89 7789 4946 5742 28 913 -176 C
ATOM 673 CE1 PHE A 89 -3.243 23.264 3.195 1.00 49.34 C
ANISOU 673 CE1 PHE A 89 7721 5196 5831 20 616 -146 C
ATOM 674 CE2 PHE A 89 -2.494 22.180 1.213 1.00 48.91 C
ANISOU 674 CE2 PHE A 89 7894 4967 5724 -15 922 -177 C
ATOM 675 CZ PHE A 89 -2.760 23.337 1.911 1.00 48.92 C
ANISOU 675 CZ PHE A 89 7808 5048 5729 -16 764 -158 C
ATOM 676 N ARG A 90 -5.354 17.985 1.559 1.00 54.30 N
ANISOU 676 N ARG A 90 8740 5639 6254 11 774 -247 N
ATOM 677 CA ARG A 90 -5.805 17.812 0.172 1.00 55.84 C
ANISOU 677 CA ARG A 90 9209 5736 6274 -73 820 -290 C
ATOM 678 C ARG A 90 -7.306 17.990 -0.015 1.00 56.36 C
ANISOU 678 C ARG A 90 9372 5838 6204 -131 599 -285 C
ATOM 679 O ARG A 90 -7.733 18.457 -1.065 1.00 56.66 O
ANISOU 679 O ARG A 90 9614 5821 6093 -219 557 -292 O
ATOM 680 CB ARG A 90 -5.403 16.424 -0.351 1.00 57.68 C
ANISOU 680 CB ARG A 90 9552 5852 6513 -78 1005 -328 C
ATOM 681 CG ARG A 90 -3.925 16.313 -0.633 1.00 61.33 C
ANISOU 681 CG ARG A 90 9974 6223 7105 -40 1272 -333 C
ATOM 682 CD ARG A 90 -3.647 15.154 -1.559 1.00 64.96 C
ANISOU 682 CD ARG A 90 10636 6523 7521 -71 1496 -392 C
ATOM 683 NE ARG A 90 -3.914 13.849 -0.947 1.00 67.97 N
ANISOU 683 NE ARG A 90 10941 6894 7992 -23 1482 -389 N
ATOM 684 CZ ARG A 90 -2.980 13.071 -0.400 1.00 69.68 C
ANISOU 684 CZ ARG A 90 10979 7058 8438 66 1637 -359 C
ATOM 685 NH1 ARG A 90 -1.724 13.479 -0.332 1.00 68.08 N
ANISOU 685 NH1 ARG A 90 10631 6817 8420 119 1806 -323 N
ATOM 686 NH2 ARG A 90 -3.299 11.880 0.081 1.00 69.90 N
ANISOU 686 NH2 ARG A 90 10962 7064 8532 99 1614 -354 N
ATOM 687 N VAL A 91 -8.107 17.587 0.981 1.00 56.13 N
ANISOU 687 N VAL A 91 9200 5893 6235 -91 458 -262 N
ATOM 688 CA VAL A 91 -9.558 17.696 0.876 1.00 56.54 C
ANISOU 688 CA VAL A 91 9302 5973 6209 -139 255 -241 C
ATOM 689 C VAL A 91 -10.018 19.115 1.144 1.00 55.47 C
ANISOU 689 C VAL A 91 9087 5898 6092 -131 126 -209 C
ATOM 690 O VAL A 91 -10.911 19.603 0.450 1.00 55.94 O
ANISOU 690 O VAL A 91 9254 5929 6073 -196 -8 -181 O
ATOM 691 CB VAL A 91 -10.264 16.673 1.785 1.00 58.29 C
ANISOU 691 CB VAL A 91 9406 6246 6496 -104 182 -226 C
ATOM 692 CG1 VAL A 91 -11.781 16.796 1.662 1.00 58.89 C
ANISOU 692 CG1 VAL A 91 9507 6340 6528 -155 -22 -189 C
ATOM 693 CG2 VAL A 91 -9.801 15.270 1.416 1.00 59.30 C
ANISOU 693 CG2 VAL A 91 9632 6289 6610 -116 315 -258 C
ATOM 694 N PHE A 92 -9.403 19.783 2.122 1.00 53.62 N
ANISOU 694 N PHE A 92 8674 5735 5965 -60 159 -207 N
ATOM 695 CA PHE A 92 -9.746 21.163 2.419 1.00 53.30 C
ANISOU 695 CA PHE A 92 8567 5735 5950 -49 65 -188 C
ATOM 696 C PHE A 92 -9.292 22.053 1.268 1.00 53.31 C
ANISOU 696 C PHE A 92 8719 5666 5870 -105 98 -186 C
ATOM 697 O PHE A 92 -10.058 22.887 0.836 1.00 53.70 O
ANISOU 697 O PHE A 92 8820 5698 5885 -140 -26 -156 O
ATOM 698 CB PHE A 92 -9.128 21.609 3.745 1.00 53.07 C
ANISOU 698 CB PHE A 92 8350 5785 6031 17 96 -193 C
ATOM 699 CG PHE A 92 -9.804 20.998 4.946 1.00 53.59 C
ANISOU 699 CG PHE A 92 8286 5922 6154 55 37 -187 C
ATOM 700 CD1 PHE A 92 -9.506 19.707 5.346 1.00 54.22 C
ANISOU 700 CD1 PHE A 92 8328 6013 6260 71 89 -185 C
ATOM 701 CD2 PHE A 92 -10.785 21.685 5.630 1.00 54.13 C
ANISOU 701 CD2 PHE A 92 8279 6033 6256 73 -56 -182 C
ATOM 702 CE1 PHE A 92 -10.147 19.133 6.433 1.00 55.01 C
ANISOU 702 CE1 PHE A 92 8325 6176 6400 93 35 -174 C
ATOM 703 CE2 PHE A 92 -11.427 21.107 6.717 1.00 54.90 C
ANISOU 703 CE2 PHE A 92 8275 6188 6397 98 -84 -180 C
ATOM 704 CZ PHE A 92 -11.097 19.839 7.116 1.00 54.89 C
ANISOU 704 CZ PHE A 92 8246 6207 6401 103 -45 -174 C
ATOM 705 N ASP A 93 -8.094 21.820 0.713 1.00 52.76 N
ANISOU 705 N ASP A 93 8725 5544 5777 -119 268 -210 N
ATOM 706 CA ASP A 93 -7.574 22.605 -0.403 1.00 53.19 C
ANISOU 706 CA ASP A 93 8941 5526 5744 -183 332 -209 C
ATOM 707 C ASP A 93 -8.140 22.098 -1.728 1.00 55.21 C
ANISOU 707 C ASP A 93 9463 5687 5827 -289 311 -212 C
ATOM 708 O ASP A 93 -7.431 21.487 -2.521 1.00 55.20 O
ANISOU 708 O ASP A 93 9622 5601 5750 -335 485 -248 O
ATOM 709 CB ASP A 93 -6.039 22.574 -0.411 1.00 52.58 C
ANISOU 709 CB ASP A 93 8819 5420 5738 -157 547 -227 C
ATOM 710 CG ASP A 93 -5.418 23.533 -1.406 1.00 54.19 C
ANISOU 710 CG ASP A 93 9161 5558 5871 -219 630 -222 C
ATOM 711 OD1 ASP A 93 -6.088 24.516 -1.784 1.00 54.75 O
ANISOU 711 OD1 ASP A 93 9307 5628 5867 -265 489 -197 O
ATOM 712 OD2 ASP A 93 -4.269 23.300 -1.812 1.00 54.32 O
ANISOU 712 OD2 ASP A 93 9204 5513 5922 -222 841 -236 O
ATOM 713 N LYS A 94 -9.432 22.345 -1.955 1.00 56.73 N
ANISOU 713 N LYS A 94 9707 5883 5966 -337 100 -170 N
ATOM 714 CA LYS A 94 -10.182 21.885 -3.121 1.00 58.10 C
ANISOU 714 CA LYS A 94 10134 5970 5972 -463 7 -150 C
ATOM 715 C LYS A 94 -9.524 22.165 -4.461 1.00 58.02 C
ANISOU 715 C LYS A 94 10404 5853 5787 -577 117 -164 C
ATOM 716 O LYS A 94 -9.420 21.243 -5.267 1.00 58.61 O
ANISOU 716 O LYS A 94 10708 5840 5719 -664 205 -201 O
ATOM 717 CB LYS A 94 -11.622 22.435 -3.105 1.00 61.73 C
ANISOU 717 CB LYS A 94 10553 6445 6455 -496 -268 -68 C
ATOM 718 CG LYS A 94 -12.600 21.530 -2.330 1.00 69.15 C
ANISOU 718 CG LYS A 94 11354 7436 7484 -455 -374 -53 C
ATOM 719 CD LYS A 94 -12.712 20.122 -2.962 1.00 75.91 C
ANISOU 719 CD LYS A 94 12403 8227 8212 -540 -342 -81 C
ATOM 720 CE LYS A 94 -13.663 19.192 -2.232 1.00 81.09 C
ANISOU 720 CE LYS A 94 12927 8927 8956 -510 -447 -60 C
ATOM 721 NZ LYS A 94 -13.320 19.032 -0.788 1.00 83.73 N
ANISOU 721 NZ LYS A 94 12990 9366 9459 -365 -349 -93 N
ATOM 722 N ASP A 95 -9.075 23.404 -4.709 1.00 57.01 N
ANISOU 722 N ASP A 95 10279 5721 5661 -585 126 -140 N
ATOM 723 CA ASP A 95 -8.449 23.712 -5.991 1.00 56.23 C
ANISOU 723 CA ASP A 95 10462 5518 5385 -705 243 -149 C
ATOM 724 C ASP A 95 -6.945 23.369 -6.051 1.00 55.22 C
ANISOU 724 C ASP A 95 10337 5354 5289 -664 571 -221 C
ATOM 725 O ASP A 95 -6.316 23.616 -7.078 1.00 56.02 O
ANISOU 725 O ASP A 95 10668 5361 5255 -759 720 -237 O
ATOM 726 CB ASP A 95 -8.719 25.163 -6.418 1.00 57.73 C
ANISOU 726 CB ASP A 95 10693 5698 5546 -758 94 -76 C
ATOM 727 CG ASP A 95 -8.162 26.232 -5.506 1.00 62.78 C
ANISOU 727 CG ASP A 95 11074 6412 6366 -641 124 -70 C
ATOM 728 OD1 ASP A 95 -7.583 25.879 -4.463 1.00 64.37 O
ANISOU 728 OD1 ASP A 95 11055 6685 6718 -523 238 -115 O
ATOM 729 OD2 ASP A 95 -8.312 27.427 -5.835 1.00 64.49 O
ANISOU 729 OD2 ASP A 95 11321 6610 6573 -678 20 -14 O
ATOM 730 N GLY A 96 -6.392 22.778 -4.988 1.00 53.17 N
ANISOU 730 N GLY A 96 9833 5157 5213 -534 682 -254 N
ATOM 731 CA GLY A 96 -5.000 22.349 -4.950 1.00 51.82 C
ANISOU 731 CA GLY A 96 9614 4943 5134 -484 979 -299 C
ATOM 732 C GLY A 96 -3.930 23.423 -5.089 1.00 50.72 C
ANISOU 732 C GLY A 96 9420 4793 5059 -476 1108 -282 C
ATOM 733 O GLY A 96 -2.773 23.086 -5.347 1.00 50.64 O
ANISOU 733 O GLY A 96 9410 4713 5116 -461 1378 -309 O
ATOM 734 N ASN A 97 -4.260 24.710 -4.833 1.00 49.16 N
ANISOU 734 N ASN A 97 9145 4657 4876 -477 931 -233 N
ATOM 735 CA ASN A 97 -3.257 25.787 -4.964 1.00 47.97 C
ANISOU 735 CA ASN A 97 8945 4494 4786 -480 1039 -211 C
ATOM 736 C ASN A 97 -2.309 26.002 -3.755 1.00 47.66 C
ANISOU 736 C ASN A 97 8589 4527 4992 -367 1102 -197 C
ATOM 737 O ASN A 97 -1.454 26.881 -3.800 1.00 48.11 O
ANISOU 737 O ASN A 97 8587 4573 5118 -373 1180 -171 O
ATOM 738 CB ASN A 97 -3.917 27.108 -5.333 1.00 47.43 C
ANISOU 738 CB ASN A 97 8961 4434 4627 -543 840 -161 C
ATOM 739 CG ASN A 97 -4.763 27.726 -4.249 1.00 47.72 C
ANISOU 739 CG ASN A 97 8787 4571 4774 -468 595 -130 C
ATOM 740 OD1 ASN A 97 -5.092 27.105 -3.224 1.00 46.72 O
ANISOU 740 OD1 ASN A 97 8481 4518 4754 -382 541 -146 O
ATOM 741 ND2 ASN A 97 -5.139 28.979 -4.471 1.00 47.80 N
ANISOU 741 ND2 ASN A 97 8828 4574 4762 -504 456 -82 N
ATOM 742 N GLY A 98 -2.431 25.189 -2.726 1.00 46.55 N
ANISOU 742 N GLY A 98 8262 4451 4973 -281 1062 -205 N
ATOM 743 CA GLY A 98 -1.578 25.292 -1.550 1.00 46.54 C
ANISOU 743 CA GLY A 98 7981 4514 5190 -198 1086 -176 C
ATOM 744 C GLY A 98 -2.152 26.149 -0.432 1.00 46.58 C
ANISOU 744 C GLY A 98 7832 4626 5243 -163 858 -155 C
ATOM 745 O GLY A 98 -1.496 26.335 0.595 1.00 46.62 O
ANISOU 745 O GLY A 98 7632 4683 5399 -119 844 -127 O
ATOM 746 N TYR A 99 -3.374 26.684 -0.612 1.00 45.48 N
ANISOU 746 N TYR A 99 7792 4506 4984 -189 680 -161 N
ATOM 747 CA TYR A 99 -3.996 27.520 0.392 1.00 45.72 C
ANISOU 747 CA TYR A 99 7695 4612 5064 -154 500 -151 C
ATOM 748 C TYR A 99 -5.450 27.123 0.640 1.00 46.72 C
ANISOU 748 C TYR A 99 7842 4771 5137 -138 343 -160 C
ATOM 749 O TYR A 99 -6.209 26.865 -0.302 1.00 47.68 O
ANISOU 749 O TYR A 99 8128 4843 5145 -188 295 -154 O
ATOM 750 CB TYR A 99 -3.948 28.987 -0.064 1.00 45.64 C
ANISOU 750 CB TYR A 99 7749 4570 5023 -198 451 -130 C
ATOM 751 CG TYR A 99 -2.538 29.509 -0.218 1.00 46.02 C
ANISOU 751 CG TYR A 99 7755 4589 5143 -220 594 -111 C
ATOM 752 CD1 TYR A 99 -1.852 30.039 0.866 1.00 47.06 C
ANISOU 752 CD1 TYR A 99 7702 4768 5409 -191 571 -96 C
ATOM 753 CD2 TYR A 99 -1.880 29.447 -1.443 1.00 46.23 C
ANISOU 753 CD2 TYR A 99 7933 4530 5103 -281 757 -103 C
ATOM 754 CE1 TYR A 99 -0.546 30.495 0.738 1.00 47.70 C
ANISOU 754 CE1 TYR A 99 7722 4819 5584 -219 688 -62 C
ATOM 755 CE2 TYR A 99 -0.562 29.868 -1.573 1.00 47.00 C
ANISOU 755 CE2 TYR A 99 7967 4593 5297 -298 912 -77 C
ATOM 756 CZ TYR A 99 0.097 30.400 -0.478 1.00 48.41 C
ANISOU 756 CZ TYR A 99 7932 4825 5636 -265 866 -50 C
ATOM 757 OH TYR A 99 1.393 30.833 -0.571 1.00 50.95 O
ANISOU 757 OH TYR A 99 8167 5111 6081 -290 996 -7 O
ATOM 758 N ILE A 100 -5.837 27.071 1.894 1.00 46.41 N
ANISOU 758 N ILE A 100 7645 4807 5181 -81 261 -168 N
ATOM 759 CA ILE A 100 -7.220 26.813 2.251 1.00 46.83 C
ANISOU 759 CA ILE A 100 7684 4889 5219 -59 128 -171 C
ATOM 760 C ILE A 100 -7.867 28.169 2.467 1.00 46.60 C
ANISOU 760 C ILE A 100 7634 4853 5220 -54 19 -159 C
ATOM 761 O ILE A 100 -7.493 28.875 3.400 1.00 45.94 O
ANISOU 761 O ILE A 100 7449 4803 5205 -27 23 -176 O
ATOM 762 CB ILE A 100 -7.356 25.930 3.500 1.00 47.01 C
ANISOU 762 CB ILE A 100 7565 4987 5310 -6 123 -187 C
ATOM 763 CG1 ILE A 100 -6.764 24.543 3.252 1.00 47.54 C
ANISOU 763 CG1 ILE A 100 7647 5042 5372 -5 229 -189 C
ATOM 764 CG2 ILE A 100 -8.821 25.829 3.917 1.00 47.46 C
ANISOU 764 CG2 ILE A 100 7592 5069 5373 15 1 -185 C
ATOM 765 CD1 ILE A 100 -6.479 23.873 4.511 1.00 48.27 C
ANISOU 765 CD1 ILE A 100 7588 5201 5549 37 233 -187 C
ATOM 766 N SER A 101 -8.767 28.561 1.559 1.00 46.87 N
ANISOU 766 N SER A 101 7775 4828 5203 -90 -80 -124 N
ATOM 767 CA SER A 101 -9.538 29.802 1.657 1.00 47.32 C
ANISOU 767 CA SER A 101 7805 4853 5321 -79 -191 -97 C
ATOM 768 C SER A 101 -10.721 29.577 2.630 1.00 47.86 C
ANISOU 768 C SER A 101 7742 4955 5486 -17 -264 -102 C
ATOM 769 O SER A 101 -11.003 28.439 3.000 1.00 47.77 O
ANISOU 769 O SER A 101 7692 4990 5466 -1 -251 -116 O
ATOM 770 CB SER A 101 -10.085 30.185 0.283 1.00 48.73 C
ANISOU 770 CB SER A 101 8143 4945 5426 -153 -293 -32 C
ATOM 771 OG SER A 101 -11.138 29.319 -0.110 1.00 51.66 O
ANISOU 771 OG SER A 101 8555 5304 5769 -178 -397 5 O
ATOM 772 N ALA A 102 -11.412 30.651 3.035 1.00 48.47 N
ANISOU 772 N ALA A 102 7753 4999 5667 17 -323 -91 N
ATOM 773 CA ALA A 102 -12.590 30.549 3.893 1.00 49.83 C
ANISOU 773 CA ALA A 102 7800 5179 5954 77 -360 -92 C
ATOM 774 C ALA A 102 -13.729 29.837 3.128 1.00 50.69 C
ANISOU 774 C ALA A 102 7927 5256 6076 52 -484 -17 C
ATOM 775 O ALA A 102 -14.435 29.028 3.709 1.00 51.22 O
ANISOU 775 O ALA A 102 7909 5359 6192 82 -488 -20 O
ATOM 776 CB ALA A 102 -13.037 31.945 4.313 1.00 50.64 C
ANISOU 776 CB ALA A 102 7842 5216 6182 117 -371 -92 C
ATOM 777 N ALA A 103 -13.866 30.093 1.818 1.00 50.89 N
ANISOU 777 N ALA A 103 8079 5211 6045 -19 -591 55 N
ATOM 778 CA ALA A 103 -14.850 29.446 0.955 1.00 51.71 C
ANISOU 778 CA ALA A 103 8240 5272 6136 -78 -743 141 C
ATOM 779 C ALA A 103 -14.617 27.929 0.905 1.00 52.59 C
ANISOU 779 C ALA A 103 8410 5441 6130 -109 -696 105 C
ATOM 780 O ALA A 103 -15.578 27.153 0.939 1.00 53.13 O
ANISOU 780 O ALA A 103 8434 5509 6242 -119 -785 147 O
ATOM 781 CB ALA A 103 -14.758 30.022 -0.446 1.00 51.93 C
ANISOU 781 CB ALA A 103 8447 5214 6071 -179 -857 220 C
ATOM 782 N GLU A 104 -13.340 27.504 0.834 1.00 52.08 N
ANISOU 782 N GLU A 104 8432 5414 5941 -123 -552 35 N
ATOM 783 CA GLU A 104 -13.007 26.087 0.812 1.00 51.49 C
ANISOU 783 CA GLU A 104 8409 5376 5779 -142 -481 -2 C
ATOM 784 C GLU A 104 -13.341 25.467 2.158 1.00 51.33 C
ANISOU 784 C GLU A 104 8208 5434 5860 -61 -440 -38 C
ATOM 785 O GLU A 104 -13.958 24.387 2.208 1.00 50.46 O
ANISOU 785 O GLU A 104 8091 5337 5744 -73 -479 -25 O
ATOM 786 CB GLU A 104 -11.531 25.867 0.459 1.00 52.76 C
ANISOU 786 CB GLU A 104 8673 5538 5836 -163 -315 -57 C
ATOM 787 CG GLU A 104 -11.269 26.006 -1.039 1.00 55.36 C
ANISOU 787 CG GLU A 104 9241 5779 6015 -272 -327 -29 C
ATOM 788 CD GLU A 104 -9.802 26.046 -1.421 1.00 57.98 C
ANISOU 788 CD GLU A 104 9660 6093 6278 -288 -133 -76 C
ATOM 789 OE1 GLU A 104 -8.967 26.387 -0.559 1.00 59.48 O
ANISOU 789 OE1 GLU A 104 9703 6336 6563 -217 -30 -110 O
ATOM 790 OE2 GLU A 104 -9.482 25.718 -2.581 1.00 60.30 O
ANISOU 790 OE2 GLU A 104 10174 6312 6427 -382 -78 -76 O
ATOM 791 N LEU A 105 -12.998 26.175 3.269 1.00 50.61 N
ANISOU 791 N LEU A 105 7985 5389 5854 10 -368 -79 N
ATOM 792 CA LEU A 105 -13.316 25.630 4.585 1.00 50.48 C
ANISOU 792 CA LEU A 105 7829 5443 5909 68 -324 -111 C
ATOM 793 C LEU A 105 -14.840 25.529 4.767 1.00 51.39 C
ANISOU 793 C LEU A 105 7857 5537 6131 85 -423 -62 C
ATOM 794 O LEU A 105 -15.338 24.491 5.195 1.00 50.91 O
ANISOU 794 O LEU A 105 7746 5514 6085 91 -425 -59 O
ATOM 795 CB LEU A 105 -12.649 26.431 5.709 1.00 49.91 C
ANISOU 795 CB LEU A 105 7677 5410 5877 110 -236 -164 C
ATOM 796 CG LEU A 105 -12.892 25.943 7.145 1.00 50.71 C
ANISOU 796 CG LEU A 105 7669 5578 6019 146 -183 -201 C
ATOM 797 CD1 LEU A 105 -12.550 24.473 7.310 1.00 50.93 C
ANISOU 797 CD1 LEU A 105 7698 5658 5995 134 -158 -199 C
ATOM 798 CD2 LEU A 105 -12.035 26.725 8.112 1.00 51.41 C
ANISOU 798 CD2 LEU A 105 7736 5695 6103 151 -112 -250 C
ATOM 799 N ARG A 106 -15.572 26.568 4.342 1.00 52.23 N
ANISOU 799 N ARG A 106 7944 5574 6327 87 -510 -10 N
ATOM 800 CA ARG A 106 -17.024 26.613 4.424 1.00 54.61 C
ANISOU 800 CA ARG A 106 8135 5833 6783 106 -608 61 C
ATOM 801 C ARG A 106 -17.650 25.445 3.662 1.00 55.77 C
ANISOU 801 C ARG A 106 8335 5968 6887 38 -730 126 C
ATOM 802 O ARG A 106 -18.505 24.751 4.199 1.00 56.32 O
ANISOU 802 O ARG A 106 8296 6057 7046 56 -746 149 O
ATOM 803 CB ARG A 106 -17.537 27.945 3.865 1.00 57.34 C
ANISOU 803 CB ARG A 106 8462 6081 7243 110 -699 128 C
ATOM 804 CG ARG A 106 -18.939 28.307 4.312 1.00 63.28 C
ANISOU 804 CG ARG A 106 9036 6775 8234 164 -746 195 C
ATOM 805 CD ARG A 106 -19.325 29.697 3.794 1.00 68.95 C
ANISOU 805 CD ARG A 106 9725 7381 9093 177 -827 267 C
ATOM 806 NE ARG A 106 -18.494 30.759 4.378 1.00 73.82 N
ANISOU 806 NE ARG A 106 10360 7996 9694 226 -687 176 N
ATOM 807 CZ ARG A 106 -17.677 31.547 3.682 1.00 77.46 C
ANISOU 807 CZ ARG A 106 10944 8425 10063 188 -716 176 C
ATOM 808 NH1 ARG A 106 -17.580 31.418 2.361 1.00 77.95 N
ANISOU 808 NH1 ARG A 106 11138 8454 10027 98 -868 260 N
ATOM 809 NH2 ARG A 106 -16.952 32.471 4.300 1.00 77.56 N
ANISOU 809 NH2 ARG A 106 10964 8434 10070 226 -592 94 N
ATOM 810 N HIS A 107 -17.176 25.187 2.443 1.00 55.87 N
ANISOU 810 N HIS A 107 8533 5946 6750 -50 -800 150 N
ATOM 811 CA HIS A 107 -17.698 24.097 1.615 1.00 56.22 C
ANISOU 811 CA HIS A 107 8681 5961 6717 -142 -920 205 C
ATOM 812 C HIS A 107 -17.453 22.733 2.279 1.00 55.56 C
ANISOU 812 C HIS A 107 8575 5948 6586 -123 -820 143 C
ATOM 813 O HIS A 107 -18.387 21.945 2.427 1.00 55.03 O
ANISOU 813 O HIS A 107 8447 5881 6580 -141 -901 189 O
ATOM 814 CB HIS A 107 -17.083 24.181 0.199 1.00 57.78 C
ANISOU 814 CB HIS A 107 9132 6095 6728 -254 -974 221 C
ATOM 815 CG HIS A 107 -17.678 23.228 -0.788 1.00 61.78 C
ANISOU 815 CG HIS A 107 9798 6545 7131 -379 -1121 283 C
ATOM 816 ND1 HIS A 107 -18.951 23.421 -1.306 1.00 63.79 N
ANISOU 816 ND1 HIS A 107 10027 6732 7478 -449 -1358 415 N
ATOM 817 CD2 HIS A 107 -17.141 22.116 -1.343 1.00 63.08 C
ANISOU 817 CD2 HIS A 107 10156 6697 7114 -454 -1062 233 C
ATOM 818 CE1 HIS A 107 -19.146 22.416 -2.138 1.00 64.62 C
ANISOU 818 CE1 HIS A 107 10325 6794 7433 -577 -1453 440 C
ATOM 819 NE2 HIS A 107 -18.084 21.605 -2.187 1.00 64.58 N
ANISOU 819 NE2 HIS A 107 10465 6816 7255 -581 -1266 323 N
ATOM 820 N VAL A 108 -16.224 22.506 2.781 1.00 55.28 N
ANISOU 820 N VAL A 108 8563 5970 6471 -82 -650 50 N
ATOM 821 CA VAL A 108 -15.847 21.262 3.459 1.00 55.19 C
ANISOU 821 CA VAL A 108 8523 6018 6430 -59 -553 0 C
ATOM 822 C VAL A 108 -16.618 21.050 4.775 1.00 55.21 C
ANISOU 822 C VAL A 108 8333 6081 6565 5 -538 3 C
ATOM 823 O VAL A 108 -17.113 19.950 5.010 1.00 55.57 O
ANISOU 823 O VAL A 108 8353 6143 6619 -9 -559 18 O
ATOM 824 CB VAL A 108 -14.315 21.152 3.654 1.00 55.81 C
ANISOU 824 CB VAL A 108 8649 6126 6431 -35 -391 -72 C
ATOM 825 CG1 VAL A 108 -13.959 19.926 4.479 1.00 57.39 C
ANISOU 825 CG1 VAL A 108 8788 6378 6638 -5 -307 -103 C
ATOM 826 CG2 VAL A 108 -13.603 21.098 2.315 1.00 55.82 C
ANISOU 826 CG2 VAL A 108 8855 6054 6300 -107 -366 -79 C
ATOM 827 N MET A 109 -16.777 22.097 5.601 1.00 54.51 N
ANISOU 827 N MET A 109 8124 6012 6576 68 -494 -11 N
ATOM 828 CA MET A 109 -17.542 21.982 6.843 1.00 54.56 C
ANISOU 828 CA MET A 109 7974 6060 6699 119 -447 -16 C
ATOM 829 C MET A 109 -19.002 21.714 6.528 1.00 55.39 C
ANISOU 829 C MET A 109 7998 6117 6929 102 -566 71 C
ATOM 830 O MET A 109 -19.611 20.901 7.212 1.00 55.84 O
ANISOU 830 O MET A 109 7968 6207 7041 110 -543 82 O
ATOM 831 CB MET A 109 -17.384 23.233 7.734 1.00 55.49 C
ANISOU 831 CB MET A 109 8018 6184 6883 177 -353 -61 C
ATOM 832 CG MET A 109 -15.971 23.467 8.218 1.00 58.23 C
ANISOU 832 CG MET A 109 8424 6579 7121 180 -255 -133 C
ATOM 833 SD MET A 109 -15.270 22.094 9.182 1.00 67.69 S
ANISOU 833 SD MET A 109 9615 7866 8238 169 -184 -165 S
ATOM 834 CE MET A 109 -16.351 22.110 10.580 1.00 64.18 C
ANISOU 834 CE MET A 109 9056 7449 7879 197 -120 -177 C
ATOM 835 N THR A 110 -19.554 22.310 5.449 1.00 55.94 N
ANISOU 835 N THR A 110 8101 6106 7048 63 -708 149 N
ATOM 836 CA THR A 110 -20.938 22.032 5.061 1.00 57.63 C
ANISOU 836 CA THR A 110 8228 6263 7405 29 -859 260 C
ATOM 837 C THR A 110 -21.088 20.580 4.598 1.00 60.14 C
ANISOU 837 C THR A 110 8634 6592 7623 -52 -940 284 C
ATOM 838 O THR A 110 -22.081 19.939 4.929 1.00 60.52 O
ANISOU 838 O THR A 110 8568 6638 7789 -61 -991 343 O
ATOM 839 CB THR A 110 -21.451 23.028 4.010 1.00 57.83 C
ANISOU 839 CB THR A 110 8272 6189 7510 -10 -1025 360 C
ATOM 840 OG1 THR A 110 -21.398 24.344 4.560 1.00 58.11 O
ANISOU 840 OG1 THR A 110 8208 6202 7668 75 -933 336 O
ATOM 841 CG2 THR A 110 -22.884 22.720 3.582 1.00 57.64 C
ANISOU 841 CG2 THR A 110 8142 6096 7663 -60 -1217 504 C
ATOM 842 N ASN A 111 -20.078 20.047 3.884 1.00 61.94 N
ANISOU 842 N ASN A 111 9065 6823 7645 -109 -927 234 N
ATOM 843 CA ASN A 111 -20.056 18.644 3.441 1.00 63.85 C
ANISOU 843 CA ASN A 111 9427 7059 7775 -185 -968 234 C
ATOM 844 C ASN A 111 -20.051 17.724 4.651 1.00 65.49 C
ANISOU 844 C ASN A 111 9517 7343 8023 -128 -851 190 C
ATOM 845 O ASN A 111 -20.764 16.725 4.666 1.00 65.92 O
ANISOU 845 O ASN A 111 9552 7389 8106 -173 -920 234 O
ATOM 846 CB ASN A 111 -18.851 18.350 2.512 1.00 65.12 C
ANISOU 846 CB ASN A 111 9830 7190 7723 -243 -914 171 C
ATOM 847 CG ASN A 111 -18.967 19.064 1.181 1.00 69.32 C
ANISOU 847 CG ASN A 111 10527 7634 8177 -337 -1050 227 C
ATOM 848 OD1 ASN A 111 -20.066 19.419 0.752 1.00 69.26 O
ANISOU 848 OD1 ASN A 111 10479 7575 8260 -392 -1242 335 O
ATOM 849 ND2 ASN A 111 -17.853 19.348 0.501 1.00 70.87 N
ANISOU 849 ND2 ASN A 111 10904 7804 8218 -364 -960 168 N
ATOM 850 N LEU A 112 -19.286 18.081 5.687 1.00 66.53 N
ANISOU 850 N LEU A 112 9576 7544 8158 -43 -688 115 N
ATOM 851 CA LEU A 112 -19.228 17.322 6.932 1.00 68.11 C
ANISOU 851 CA LEU A 112 9676 7817 8385 0 -582 82 C
ATOM 852 C LEU A 112 -20.501 17.481 7.797 1.00 69.37 C
ANISOU 852 C LEU A 112 9651 7990 8716 31 -585 130 C
ATOM 853 O LEU A 112 -20.447 17.212 8.984 1.00 69.69 O
ANISOU 853 O LEU A 112 9612 8091 8775 69 -471 96 O
ATOM 854 CB LEU A 112 -18.031 17.803 7.749 1.00 68.62 C
ANISOU 854 CB LEU A 112 9736 7940 8397 57 -437 4 C
ATOM 855 CG LEU A 112 -16.666 17.455 7.211 1.00 70.62 C
ANISOU 855 CG LEU A 112 10121 8186 8524 42 -385 -39 C
ATOM 856 CD1 LEU A 112 -15.588 18.189 7.975 1.00 71.13 C
ANISOU 856 CD1 LEU A 112 10153 8298 8575 88 -280 -90 C
ATOM 857 CD2 LEU A 112 -16.418 15.983 7.320 1.00 71.81 C
ANISOU 857 CD2 LEU A 112 10307 8343 8634 21 -362 -41 C
ATOM 858 N GLY A 113 -21.596 17.970 7.224 1.00 69.93 N
ANISOU 858 N GLY A 113 9655 7996 8917 11 -707 214 N
ATOM 859 CA GLY A 113 -22.850 18.183 7.935 1.00 70.54 C
ANISOU 859 CA GLY A 113 9535 8061 9205 45 -694 273 C
ATOM 860 C GLY A 113 -22.792 19.211 9.049 1.00 70.76 C
ANISOU 860 C GLY A 113 9459 8111 9316 132 -521 215 C
ATOM 861 O GLY A 113 -23.592 19.139 9.985 1.00 71.17 O
ANISOU 861 O GLY A 113 9369 8168 9503 165 -424 227 O
ATOM 862 N GLU A 114 -21.872 20.190 8.957 1.00 70.37 N
ANISOU 862 N GLU A 114 9489 8062 9185 162 -469 150 N
ATOM 863 CA GLU A 114 -21.739 21.202 10.005 1.00 70.67 C
ANISOU 863 CA GLU A 114 9467 8108 9276 228 -304 83 C
ATOM 864 C GLU A 114 -22.404 22.530 9.684 1.00 71.95 C
ANISOU 864 C GLU A 114 9542 8176 9619 272 -319 124 C
ATOM 865 O GLU A 114 -22.028 23.200 8.720 1.00 72.07 O
ANISOU 865 O GLU A 114 9629 8147 9605 258 -422 146 O
ATOM 866 CB GLU A 114 -20.269 21.430 10.383 1.00 71.79 C
ANISOU 866 CB GLU A 114 9739 8311 9229 229 -220 -16 C
ATOM 867 CG GLU A 114 -19.521 20.164 10.752 1.00 75.79 C
ANISOU 867 CG GLU A 114 10312 8895 9588 193 -202 -43 C
ATOM 868 CD GLU A 114 -19.896 19.552 12.087 1.00 80.72 C
ANISOU 868 CD GLU A 114 10874 9573 10225 195 -93 -62 C
ATOM 869 OE1 GLU A 114 -19.643 20.202 13.127 1.00 81.46 O
ANISOU 869 OE1 GLU A 114 10971 9686 10296 210 32 -123 O
ATOM 870 OE2 GLU A 114 -20.428 18.417 12.097 1.00 82.39 O
ANISOU 870 OE2 GLU A 114 11050 9799 10454 169 -132 -17 O
ATOM 871 N LYS A 115 -23.339 22.949 10.549 1.00 72.87 N
ANISOU 871 N LYS A 115 9509 8252 9927 326 -195 130 N
ATOM 872 CA LYS A 115 -24.046 24.224 10.416 1.00 74.08 C
ANISOU 872 CA LYS A 115 9549 8294 10305 384 -171 170 C
ATOM 873 C LYS A 115 -23.260 25.328 11.122 1.00 74.59 C
ANISOU 873 C LYS A 115 9690 8352 10297 427 -3 51 C
ATOM 874 O LYS A 115 -23.561 25.670 12.265 1.00 75.34 O
ANISOU 874 O LYS A 115 9740 8430 10456 467 202 -16 O
ATOM 875 CB LYS A 115 -25.463 24.127 11.008 1.00 76.51 C
ANISOU 875 CB LYS A 115 9644 8537 10890 427 -83 237 C
ATOM 876 CG LYS A 115 -26.569 23.990 9.964 1.00 81.87 C
ANISOU 876 CG LYS A 115 10176 9129 11801 406 -296 409 C
ATOM 877 CD LYS A 115 -26.559 22.634 9.259 1.00 87.59 C
ANISOU 877 CD LYS A 115 10968 9916 12396 310 -493 473 C
ATOM 878 CE LYS A 115 -26.855 21.501 10.210 1.00 92.17 C
ANISOU 878 CE LYS A 115 11501 10568 12953 300 -374 443 C
ATOM 879 NZ LYS A 115 -26.890 20.189 9.512 1.00 95.33 N
ANISOU 879 NZ LYS A 115 11968 11008 13243 206 -564 505 N
ATOM 880 N LEU A 116 -22.239 25.865 10.453 1.00 74.00 N
ANISOU 880 N LEU A 116 9749 8288 10080 406 -83 23 N
ATOM 881 CA LEU A 116 -21.414 26.933 11.013 1.00 73.66 C
ANISOU 881 CA LEU A 116 9791 8234 9962 429 43 -81 C
ATOM 882 C LEU A 116 -21.799 28.250 10.397 1.00 73.23 C
ANISOU 882 C LEU A 116 9687 8057 10082 472 5 -35 C
ATOM 883 O LEU A 116 -22.019 28.308 9.178 1.00 73.71 O
ANISOU 883 O LEU A 116 9737 8076 10193 450 -185 69 O
ATOM 884 CB LEU A 116 -19.936 26.709 10.672 1.00 73.71 C
ANISOU 884 CB LEU A 116 9965 8325 9717 374 -15 -132 C
ATOM 885 CG LEU A 116 -19.228 25.536 11.305 1.00 75.27 C
ANISOU 885 CG LEU A 116 10229 8636 9736 331 20 -178 C
ATOM 886 CD1 LEU A 116 -17.792 25.483 10.830 1.00 75.98 C
ANISOU 886 CD1 LEU A 116 10448 8776 9645 289 -34 -207 C
ATOM 887 CD2 LEU A 116 -19.264 25.622 12.812 1.00 75.80 C
ANISOU 887 CD2 LEU A 116 10295 8728 9777 336 198 -260 C
ATOM 888 N THR A 117 -21.776 29.330 11.195 1.00 71.95 N
ANISOU 888 N THR A 117 9523 7830 9986 520 177 -115 N
ATOM 889 CA THR A 117 -22.023 30.660 10.641 1.00 71.44 C
ANISOU 889 CA THR A 117 9419 7635 10089 566 150 -77 C
ATOM 890 C THR A 117 -20.802 31.081 9.789 1.00 70.17 C
ANISOU 890 C THR A 117 9416 7508 9739 514 21 -87 C
ATOM 891 O THR A 117 -19.740 30.455 9.879 1.00 69.49 O
ANISOU 891 O THR A 117 9455 7535 9414 458 9 -145 O
ATOM 892 CB THR A 117 -22.319 31.678 11.762 1.00 72.92 C
ANISOU 892 CB THR A 117 9584 7726 10398 628 397 -173 C
ATOM 893 OG1 THR A 117 -21.129 31.912 12.515 1.00 74.28 O
ANISOU 893 OG1 THR A 117 9937 7965 10320 581 498 -310 O
ATOM 894 CG2 THR A 117 -23.439 31.230 12.690 1.00 73.02 C
ANISOU 894 CG2 THR A 117 9460 7703 10581 672 576 -177 C
ATOM 895 N ASP A 118 -20.948 32.131 8.967 1.00 69.73 N
ANISOU 895 N ASP A 118 9344 7344 9805 533 -69 -22 N
ATOM 896 CA ASP A 118 -19.829 32.601 8.153 1.00 69.71 C
ANISOU 896 CA ASP A 118 9491 7362 9634 480 -172 -28 C
ATOM 897 C ASP A 118 -18.721 33.194 9.025 1.00 69.01 C
ANISOU 897 C ASP A 118 9518 7308 9397 472 -21 -167 C
ATOM 898 O ASP A 118 -17.553 32.957 8.741 1.00 69.42 O
ANISOU 898 O ASP A 118 9693 7442 9244 412 -64 -198 O
ATOM 899 CB ASP A 118 -20.286 33.538 7.032 1.00 71.94 C
ANISOU 899 CB ASP A 118 9741 7519 10076 487 -324 92 C
ATOM 900 CG ASP A 118 -20.889 32.799 5.839 1.00 78.19 C
ANISOU 900 CG ASP A 118 10509 8307 10892 430 -554 240 C
ATOM 901 OD1 ASP A 118 -21.285 31.615 6.002 1.00 78.15 O
ANISOU 901 OD1 ASP A 118 10464 8373 10858 411 -573 255 O
ATOM 902 OD2 ASP A 118 -20.974 33.406 4.743 1.00 81.82 O
ANISOU 902 OD2 ASP A 118 11006 8687 11393 393 -724 346 O
ATOM 903 N GLU A 119 -19.092 33.861 10.144 1.00 67.69 N
ANISOU 903 N GLU A 119 9316 7074 9331 522 166 -249 N
ATOM 904 CA GLU A 119 -18.180 34.426 11.150 1.00 66.68 C
ANISOU 904 CA GLU A 119 9313 6961 9060 495 311 -383 C
ATOM 905 C GLU A 119 -17.395 33.286 11.850 1.00 64.09 C
ANISOU 905 C GLU A 119 9065 6787 8501 428 334 -443 C
ATOM 906 O GLU A 119 -16.206 33.434 12.109 1.00 64.00 O
ANISOU 906 O GLU A 119 9171 6831 8314 366 329 -498 O
ATOM 907 CB GLU A 119 -18.951 35.236 12.214 1.00 70.71 C
ANISOU 907 CB GLU A 119 9788 7349 9730 553 528 -460 C
ATOM 908 CG GLU A 119 -20.118 36.060 11.679 1.00 79.91 C
ANISOU 908 CG GLU A 119 10802 8346 11214 645 532 -375 C
ATOM 909 CD GLU A 119 -21.404 35.288 11.417 1.00 89.65 C
ANISOU 909 CD GLU A 119 11843 9561 12658 696 495 -264 C
ATOM 910 OE1 GLU A 119 -21.665 34.953 10.237 1.00 90.74 O
ANISOU 910 OE1 GLU A 119 11912 9709 12856 685 273 -126 O
ATOM 911 OE2 GLU A 119 -22.144 35.011 12.390 1.00 93.29 O
ANISOU 911 OE2 GLU A 119 12234 9994 13219 734 687 -311 O
ATOM 912 N GLU A 120 -18.050 32.153 12.133 1.00 61.97 N
ANISOU 912 N GLU A 120 8720 6577 8250 437 346 -416 N
ATOM 913 CA GLU A 120 -17.379 31.000 12.736 1.00 60.74 C
ANISOU 913 CA GLU A 120 8625 6554 7898 376 350 -451 C
ATOM 914 C GLU A 120 -16.291 30.466 11.801 1.00 59.66 C
ANISOU 914 C GLU A 120 8548 6500 7622 328 196 -406 C
ATOM 915 O GLU A 120 -15.199 30.151 12.251 1.00 59.59 O
ANISOU 915 O GLU A 120 8619 6566 7455 271 200 -446 O
ATOM 916 CB GLU A 120 -18.386 29.906 13.117 1.00 61.90 C
ANISOU 916 CB GLU A 120 8672 6734 8113 396 387 -418 C
ATOM 917 CG GLU A 120 -18.997 30.144 14.483 1.00 67.33 C
ANISOU 917 CG GLU A 120 9360 7380 8841 408 600 -500 C
ATOM 918 CD GLU A 120 -20.307 29.445 14.805 1.00 74.74 C
ANISOU 918 CD GLU A 120 10162 8300 9937 449 679 -458 C
ATOM 919 OE1 GLU A 120 -20.603 28.395 14.190 1.00 74.92 O
ANISOU 919 OE1 GLU A 120 10107 8382 9977 445 549 -371 O
ATOM 920 OE2 GLU A 120 -21.035 29.949 15.693 1.00 77.81 O
ANISOU 920 OE2 GLU A 120 10527 8603 10433 480 885 -515 O
ATOM 921 N VAL A 121 -16.573 30.432 10.496 1.00 59.26 N
ANISOU 921 N VAL A 121 8462 6416 7637 342 65 -318 N
ATOM 922 CA VAL A 121 -15.633 29.991 9.464 1.00 59.11 C
ANISOU 922 CA VAL A 121 8518 6447 7495 295 -49 -279 C
ATOM 923 C VAL A 121 -14.442 30.935 9.436 1.00 58.78 C
ANISOU 923 C VAL A 121 8566 6395 7373 264 -30 -322 C
ATOM 924 O VAL A 121 -13.298 30.487 9.465 1.00 59.22 O
ANISOU 924 O VAL A 121 8679 6519 7302 218 -33 -338 O
ATOM 925 CB VAL A 121 -16.328 29.879 8.071 1.00 59.60 C
ANISOU 925 CB VAL A 121 8561 6453 7631 295 -193 -174 C
ATOM 926 CG1 VAL A 121 -15.303 29.686 6.959 1.00 60.16 C
ANISOU 926 CG1 VAL A 121 8751 6544 7561 236 -271 -149 C
ATOM 927 CG2 VAL A 121 -17.341 28.736 8.059 1.00 59.82 C
ANISOU 927 CG2 VAL A 121 8507 6503 7717 301 -237 -122 C
ATOM 928 N ASP A 122 -14.709 32.237 9.441 1.00 58.17 N
ANISOU 928 N ASP A 122 8490 6223 7391 290 -4 -336 N
ATOM 929 CA ASP A 122 -13.675 33.261 9.444 1.00 58.30 C
ANISOU 929 CA ASP A 122 8590 6212 7348 257 12 -374 C
ATOM 930 C ASP A 122 -12.776 33.134 10.670 1.00 57.02 C
ANISOU 930 C ASP A 122 8481 6116 7067 208 92 -456 C
ATOM 931 O ASP A 122 -11.563 33.213 10.535 1.00 56.74 O
ANISOU 931 O ASP A 122 8502 6120 6938 152 62 -458 O
ATOM 932 CB ASP A 122 -14.314 34.653 9.411 1.00 61.58 C
ANISOU 932 CB ASP A 122 8990 6496 7912 300 42 -380 C
ATOM 933 CG ASP A 122 -14.999 34.981 8.106 1.00 68.52 C
ANISOU 933 CG ASP A 122 9830 7295 8910 326 -80 -273 C
ATOM 934 OD1 ASP A 122 -14.624 34.376 7.065 1.00 69.48 O
ANISOU 934 OD1 ASP A 122 9995 7461 8942 283 -191 -208 O
ATOM 935 OD2 ASP A 122 -15.911 35.839 8.117 1.00 71.43 O
ANISOU 935 OD2 ASP A 122 10132 7544 9463 382 -64 -249 O
ATOM 936 N GLU A 123 -13.377 32.915 11.853 1.00 56.18 N
ANISOU 936 N GLU A 123 8359 6016 6970 218 191 -514 N
ATOM 937 CA GLU A 123 -12.703 32.727 13.141 1.00 56.01 C
ANISOU 937 CA GLU A 123 8410 6049 6820 149 253 -584 C
ATOM 938 C GLU A 123 -11.704 31.569 13.029 1.00 54.44 C
ANISOU 938 C GLU A 123 8209 5966 6510 98 171 -539 C
ATOM 939 O GLU A 123 -10.553 31.714 13.412 1.00 54.50 O
ANISOU 939 O GLU A 123 8272 6006 6430 26 142 -546 O
ATOM 940 CB GLU A 123 -13.764 32.453 14.233 1.00 59.95 C
ANISOU 940 CB GLU A 123 8896 6531 7349 170 381 -637 C
ATOM 941 CG GLU A 123 -13.256 31.915 15.563 1.00 68.52 C
ANISOU 941 CG GLU A 123 10072 7687 8277 81 429 -690 C
ATOM 942 CD GLU A 123 -14.131 30.839 16.201 1.00 78.70 C
ANISOU 942 CD GLU A 123 11315 9020 9567 95 496 -687 C
ATOM 943 OE1 GLU A 123 -14.263 30.855 17.450 1.00 80.68 O
ANISOU 943 OE1 GLU A 123 11661 9266 9726 35 606 -756 O
ATOM 944 OE2 GLU A 123 -14.671 29.977 15.460 1.00 79.35 O
ANISOU 944 OE2 GLU A 123 11283 9137 9728 152 439 -616 O
ATOM 945 N MET A 124 -12.139 30.448 12.441 1.00 52.93 N
ANISOU 945 N MET A 124 7946 5821 6342 134 129 -482 N
ATOM 946 CA MET A 124 -11.316 29.276 12.214 1.00 52.21 C
ANISOU 946 CA MET A 124 7842 5815 6180 103 71 -436 C
ATOM 947 C MET A 124 -10.102 29.576 11.321 1.00 51.09 C
ANISOU 947 C MET A 124 7726 5669 6018 76 21 -401 C
ATOM 948 O MET A 124 -9.015 29.076 11.600 1.00 51.31 O
ANISOU 948 O MET A 124 7750 5746 5999 29 3 -380 O
ATOM 949 CB MET A 124 -12.156 28.159 11.590 1.00 52.72 C
ANISOU 949 CB MET A 124 7846 5900 6285 146 43 -389 C
ATOM 950 CG MET A 124 -13.039 27.453 12.574 1.00 55.04 C
ANISOU 950 CG MET A 124 8100 6225 6587 155 94 -406 C
ATOM 951 SD MET A 124 -14.193 26.226 11.857 1.00 60.84 S
ANISOU 951 SD MET A 124 8756 6968 7391 197 47 -343 S
ATOM 952 CE MET A 124 -13.244 25.400 10.851 1.00 59.31 C
ANISOU 952 CE MET A 124 8598 6805 7133 175 -26 -299 C
ATOM 953 N ILE A 125 -10.298 30.339 10.241 1.00 49.94 N
ANISOU 953 N ILE A 125 7598 5457 5919 101 -2 -383 N
ATOM 954 CA ILE A 125 -9.234 30.699 9.314 1.00 50.21 C
ANISOU 954 CA ILE A 125 7669 5474 5934 72 -26 -350 C
ATOM 955 C ILE A 125 -8.236 31.606 10.045 1.00 51.21 C
ANISOU 955 C ILE A 125 7823 5595 6040 17 -13 -379 C
ATOM 956 O ILE A 125 -7.039 31.366 10.027 1.00 51.30 O
ANISOU 956 O ILE A 125 7824 5638 6032 -29 -22 -349 O
ATOM 957 CB ILE A 125 -9.826 31.409 8.029 1.00 50.36 C
ANISOU 957 CB ILE A 125 7726 5413 5997 96 -65 -317 C
ATOM 958 CG1 ILE A 125 -10.652 30.449 7.151 1.00 50.71 C
ANISOU 958 CG1 ILE A 125 7767 5456 6042 117 -111 -269 C
ATOM 959 CG2 ILE A 125 -8.725 32.073 7.200 1.00 50.17 C
ANISOU 959 CG2 ILE A 125 7760 5357 5945 54 -67 -293 C
ATOM 960 CD1 ILE A 125 -9.801 29.239 6.578 1.00 51.92 C
ANISOU 960 CD1 ILE A 125 7952 5656 6119 87 -92 -246 C
ATOM 961 N ARG A 126 -8.745 32.613 10.726 1.00 51.87 N
ANISOU 961 N ARG A 126 7939 5628 6141 17 11 -434 N
ATOM 962 CA ARG A 126 -7.950 33.589 11.442 1.00 53.66 C
ANISOU 962 CA ARG A 126 8222 5830 6337 -50 16 -471 C
ATOM 963 C ARG A 126 -7.121 32.967 12.570 1.00 53.81 C
ANISOU 963 C ARG A 126 8245 5921 6281 -129 -6 -471 C
ATOM 964 O ARG A 126 -5.943 33.297 12.709 1.00 53.44 O
ANISOU 964 O ARG A 126 8207 5879 6217 -203 -52 -443 O
ATOM 965 CB ARG A 126 -8.885 34.699 11.915 1.00 57.01 C
ANISOU 965 CB ARG A 126 8696 6162 6802 -24 74 -540 C
ATOM 966 CG ARG A 126 -8.314 35.708 12.888 1.00 64.54 C
ANISOU 966 CG ARG A 126 9746 7071 7705 -104 96 -604 C
ATOM 967 CD ARG A 126 -9.063 37.057 12.835 1.00 70.65 C
ANISOU 967 CD ARG A 126 10571 7713 8559 -64 162 -660 C
ATOM 968 NE ARG A 126 -10.524 36.917 12.756 1.00 75.93 N
ANISOU 968 NE ARG A 126 11183 8334 9335 35 235 -673 N
ATOM 969 CZ ARG A 126 -11.256 37.272 11.701 1.00 80.09 C
ANISOU 969 CZ ARG A 126 11643 8792 9995 116 211 -620 C
ATOM 970 NH1 ARG A 126 -10.675 37.793 10.624 1.00 80.03 N
ANISOU 970 NH1 ARG A 126 11645 8761 10003 105 127 -561 N
ATOM 971 NH2 ARG A 126 -12.572 37.093 11.708 1.00 80.45 N
ANISOU 971 NH2 ARG A 126 11612 8790 10166 198 264 -614 N
ATOM 972 N GLU A 127 -7.701 31.996 13.308 1.00 53.92 N
ANISOU 972 N GLU A 127 8241 5989 6260 -120 12 -483 N
ATOM 973 CA GLU A 127 -7.004 31.307 14.389 1.00 54.29 C
ANISOU 973 CA GLU A 127 8295 6100 6231 -204 -30 -464 C
ATOM 974 C GLU A 127 -5.893 30.393 13.864 1.00 53.04 C
ANISOU 974 C GLU A 127 8046 5995 6110 -217 -94 -369 C
ATOM 975 O GLU A 127 -4.901 30.202 14.553 1.00 53.49 O
ANISOU 975 O GLU A 127 8094 6081 6148 -304 -164 -323 O
ATOM 976 CB GLU A 127 -7.976 30.518 15.281 1.00 59.06 C
ANISOU 976 CB GLU A 127 8914 6740 6787 -195 16 -497 C
ATOM 977 CG GLU A 127 -8.741 31.350 16.301 1.00 69.27 C
ANISOU 977 CG GLU A 127 10319 7976 8023 -226 104 -593 C
ATOM 978 CD GLU A 127 -7.950 31.823 17.512 1.00 82.94 C
ANISOU 978 CD GLU A 127 12183 9703 9627 -369 67 -621 C
ATOM 979 OE1 GLU A 127 -8.267 31.370 18.638 1.00 87.17 O
ANISOU 979 OE1 GLU A 127 12801 10262 10059 -436 97 -650 O
ATOM 980 OE2 GLU A 127 -7.028 32.657 17.344 1.00 86.44 O
ANISOU 980 OE2 GLU A 127 12661 10113 10068 -427 5 -611 O
ATOM 981 N ALA A 128 -6.053 29.828 12.661 1.00 51.46 N
ANISOU 981 N ALA A 128 7786 5795 5972 -140 -70 -335 N
ATOM 982 CA ALA A 128 -5.018 28.961 12.090 1.00 50.74 C
ANISOU 982 CA ALA A 128 7616 5729 5936 -142 -85 -255 C
ATOM 983 C ALA A 128 -3.955 29.734 11.274 1.00 49.29 C
ANISOU 983 C ALA A 128 7420 5500 5808 -165 -77 -220 C
ATOM 984 O ALA A 128 -2.825 29.250 11.110 1.00 49.44 O
ANISOU 984 O ALA A 128 7360 5525 5898 -190 -81 -148 O
ATOM 985 CB ALA A 128 -5.650 27.867 11.237 1.00 50.69 C
ANISOU 985 CB ALA A 128 7582 5732 5948 -67 -43 -243 C
ATOM 986 N ASP A 129 -4.322 30.928 10.787 1.00 47.37 N
ANISOU 986 N ASP A 129 7245 5201 5551 -156 -62 -264 N
ATOM 987 CA ASP A 129 -3.501 31.811 9.968 1.00 46.43 C
ANISOU 987 CA ASP A 129 7137 5031 5474 -180 -48 -237 C
ATOM 988 C ASP A 129 -2.342 32.385 10.793 1.00 46.26 C
ANISOU 988 C ASP A 129 7089 5010 5476 -277 -107 -205 C
ATOM 989 O ASP A 129 -2.558 33.032 11.811 1.00 46.42 O
ANISOU 989 O ASP A 129 7171 5025 5441 -331 -157 -250 O
ATOM 990 CB ASP A 129 -4.401 32.917 9.389 1.00 47.44 C
ANISOU 990 CB ASP A 129 7349 5094 5582 -148 -36 -287 C
ATOM 991 CG ASP A 129 -3.781 33.848 8.360 1.00 51.24 C
ANISOU 991 CG ASP A 129 7865 5513 6092 -169 -19 -259 C
ATOM 992 OD1 ASP A 129 -2.727 33.496 7.797 1.00 51.75 O
ANISOU 992 OD1 ASP A 129 7886 5582 6193 -194 16 -202 O
ATOM 993 OD2 ASP A 129 -4.355 34.934 8.119 1.00 52.31 O
ANISOU 993 OD2 ASP A 129 8066 5585 6226 -160 -31 -289 O
ATOM 994 N ILE A 130 -1.112 32.146 10.358 1.00 46.20 N
ANISOU 994 N ILE A 130 6997 4998 5558 -306 -98 -124 N
ATOM 995 CA ILE A 130 0.079 32.644 11.047 1.00 46.72 C
ANISOU 995 CA ILE A 130 7013 5058 5682 -409 -176 -64 C
ATOM 996 C ILE A 130 0.688 33.849 10.310 1.00 46.66 C
ANISOU 996 C ILE A 130 7026 4985 5716 -442 -153 -52 C
ATOM 997 O ILE A 130 1.046 34.842 10.954 1.00 46.67 O
ANISOU 997 O ILE A 130 7071 4961 5701 -530 -231 -59 O
ATOM 998 CB ILE A 130 1.126 31.515 11.180 1.00 47.37 C
ANISOU 998 CB ILE A 130 6942 5166 5889 -425 -189 47 C
ATOM 999 CG1 ILE A 130 0.573 30.337 12.010 1.00 47.79 C
ANISOU 999 CG1 ILE A 130 6978 5280 5900 -406 -231 46 C
ATOM 1000 CG2 ILE A 130 2.454 32.064 11.743 1.00 47.79 C
ANISOU 1000 CG2 ILE A 130 6913 5200 6044 -542 -289 142 C
ATOM 1001 CD1 ILE A 130 1.436 29.148 12.014 1.00 48.74 C
ANISOU 1001 CD1 ILE A 130 6945 5410 6163 -399 -229 156 C
ATOM 1002 N ASP A 131 0.844 33.750 8.980 1.00 45.59 N
ANISOU 1002 N ASP A 131 6879 4817 5627 -387 -44 -32 N
ATOM 1003 CA ASP A 131 1.462 34.834 8.224 1.00 45.12 C
ANISOU 1003 CA ASP A 131 6842 4694 5607 -425 -11 -10 C
ATOM 1004 C ASP A 131 0.529 36.025 7.972 1.00 45.37 C
ANISOU 1004 C ASP A 131 7014 4678 5547 -414 -28 -88 C
ATOM 1005 O ASP A 131 1.005 37.094 7.642 1.00 46.29 O
ANISOU 1005 O ASP A 131 7163 4739 5688 -463 -33 -73 O
ATOM 1006 CB ASP A 131 2.114 34.340 6.931 1.00 46.49 C
ANISOU 1006 CB ASP A 131 6969 4835 5859 -394 130 47 C
ATOM 1007 CG ASP A 131 1.195 33.597 5.987 1.00 52.26 C
ANISOU 1007 CG ASP A 131 7783 5565 6509 -312 219 4 C
ATOM 1008 OD1 ASP A 131 -0.027 33.866 6.008 1.00 52.95 O
ANISOU 1008 OD1 ASP A 131 7972 5657 6489 -277 168 -63 O
ATOM 1009 OD2 ASP A 131 1.699 32.761 5.210 1.00 55.22 O
ANISOU 1009 OD2 ASP A 131 8124 5920 6936 -288 345 41 O
ATOM 1010 N GLY A 132 -0.766 35.855 8.157 1.00 45.15 N
ANISOU 1010 N GLY A 132 7055 4662 5437 -351 -38 -159 N
ATOM 1011 CA GLY A 132 -1.726 36.933 8.000 1.00 45.20 C
ANISOU 1011 CA GLY A 132 7168 4607 5400 -329 -53 -220 C
ATOM 1012 C GLY A 132 -2.307 37.117 6.616 1.00 46.03 C
ANISOU 1012 C GLY A 132 7332 4664 5494 -278 -11 -207 C
ATOM 1013 O GLY A 132 -3.041 38.081 6.400 1.00 47.15 O
ANISOU 1013 O GLY A 132 7545 4738 5630 -262 -37 -234 O
ATOM 1014 N ASP A 133 -2.041 36.196 5.681 1.00 45.56 N
ANISOU 1014 N ASP A 133 7258 4625 5429 -259 52 -163 N
ATOM 1015 CA ASP A 133 -2.584 36.352 4.326 1.00 45.66 C
ANISOU 1015 CA ASP A 133 7368 4585 5397 -241 76 -143 C
ATOM 1016 C ASP A 133 -4.082 36.018 4.218 1.00 46.31 C
ANISOU 1016 C ASP A 133 7490 4664 5441 -179 21 -170 C
ATOM 1017 O ASP A 133 -4.609 36.060 3.134 1.00 46.79 O
ANISOU 1017 O ASP A 133 7637 4679 5460 -179 8 -140 O
ATOM 1018 CB ASP A 133 -1.766 35.551 3.295 1.00 46.06 C
ANISOU 1018 CB ASP A 133 7431 4635 5436 -262 186 -95 C
ATOM 1019 CG ASP A 133 -1.944 34.048 3.363 1.00 48.82 C
ANISOU 1019 CG ASP A 133 7741 5038 5772 -220 231 -102 C
ATOM 1020 OD1 ASP A 133 -2.721 33.574 4.223 1.00 48.03 O
ANISOU 1020 OD1 ASP A 133 7596 4986 5666 -177 165 -137 O
ATOM 1021 OD2 ASP A 133 -1.272 33.340 2.591 1.00 51.69 O
ANISOU 1021 OD2 ASP A 133 8119 5384 6136 -233 348 -74 O
ATOM 1022 N GLY A 134 -4.739 35.653 5.309 1.00 46.26 N
ANISOU 1022 N GLY A 134 7426 4702 5450 -138 -11 -216 N
ATOM 1023 CA GLY A 134 -6.163 35.330 5.298 1.00 46.32 C
ANISOU 1023 CA GLY A 134 7441 4702 5457 -79 -55 -232 C
ATOM 1024 C GLY A 134 -6.504 33.952 4.784 1.00 46.32 C
ANISOU 1024 C GLY A 134 7439 4746 5413 -58 -44 -210 C
ATOM 1025 O GLY A 134 -7.670 33.642 4.545 1.00 47.18 O
ANISOU 1025 O GLY A 134 7558 4841 5526 -23 -95 -202 O
ATOM 1026 N GLN A 135 -5.497 33.112 4.600 1.00 45.20 N
ANISOU 1026 N GLN A 135 7281 4645 5246 -83 25 -195 N
ATOM 1027 CA GLN A 135 -5.667 31.747 4.140 1.00 44.31 C
ANISOU 1027 CA GLN A 135 7181 4561 5094 -69 58 -183 C
ATOM 1028 C GLN A 135 -4.809 30.831 5.011 1.00 44.62 C
ANISOU 1028 C GLN A 135 7116 4665 5172 -64 113 -187 C
ATOM 1029 O GLN A 135 -3.971 31.310 5.781 1.00 45.05 O
ANISOU 1029 O GLN A 135 7103 4737 5277 -88 114 -183 O
ATOM 1030 CB GLN A 135 -5.243 31.631 2.664 1.00 45.14 C
ANISOU 1030 CB GLN A 135 7408 4609 5135 -113 118 -148 C
ATOM 1031 CG GLN A 135 -5.955 32.605 1.744 1.00 46.52 C
ANISOU 1031 CG GLN A 135 7700 4710 5267 -142 39 -120 C
ATOM 1032 CD GLN A 135 -6.099 32.033 0.369 1.00 48.60 C
ANISOU 1032 CD GLN A 135 8123 4923 5419 -195 60 -88 C
ATOM 1033 OE1 GLN A 135 -7.056 31.323 0.069 1.00 52.58 O
ANISOU 1033 OE1 GLN A 135 8676 5425 5878 -195 -9 -79 O
ATOM 1034 NE2 GLN A 135 -5.151 32.313 -0.482 1.00 44.12 N
ANISOU 1034 NE2 GLN A 135 7653 4310 4802 -255 161 -71 N
ATOM 1035 N VAL A 136 -5.013 29.505 4.903 1.00 43.94 N
ANISOU 1035 N VAL A 136 7019 4607 5071 -40 143 -184 N
ATOM 1036 CA VAL A 136 -4.262 28.555 5.704 1.00 43.25 C
ANISOU 1036 CA VAL A 136 6824 4569 5040 -33 182 -170 C
ATOM 1037 C VAL A 136 -3.416 27.686 4.773 1.00 43.57 C
ANISOU 1037 C VAL A 136 6884 4569 5101 -37 307 -141 C
ATOM 1038 O VAL A 136 -3.977 26.865 4.053 1.00 43.61 O
ANISOU 1038 O VAL A 136 6972 4551 5047 -26 339 -153 O
ATOM 1039 CB VAL A 136 -5.223 27.725 6.594 1.00 43.12 C
ANISOU 1039 CB VAL A 136 6765 4610 5009 2 123 -192 C
ATOM 1040 CG1 VAL A 136 -4.490 26.615 7.343 1.00 43.45 C
ANISOU 1040 CG1 VAL A 136 6706 4695 5109 4 148 -161 C
ATOM 1041 CG2 VAL A 136 -5.979 28.622 7.567 1.00 42.73 C
ANISOU 1041 CG2 VAL A 136 6704 4581 4951 4 47 -228 C
ATOM 1042 N ASN A 137 -2.081 27.903 4.723 1.00 43.84 N
ANISOU 1042 N ASN A 137 6850 4580 5227 -61 388 -101 N
ATOM 1043 CA ASN A 137 -1.250 27.057 3.852 1.00 45.12 C
ANISOU 1043 CA ASN A 137 7021 4683 5438 -57 553 -76 C
ATOM 1044 C ASN A 137 -0.970 25.701 4.541 1.00 46.90 C
ANISOU 1044 C ASN A 137 7127 4932 5759 -18 577 -50 C
ATOM 1045 O ASN A 137 -1.471 25.459 5.654 1.00 47.49 O
ANISOU 1045 O ASN A 137 7131 5078 5834 -6 453 -51 O
ATOM 1046 CB ASN A 137 0.020 27.782 3.383 1.00 44.75 C
ANISOU 1046 CB ASN A 137 6941 4582 5481 -94 659 -33 C
ATOM 1047 CG ASN A 137 0.944 28.139 4.509 1.00 45.95 C
ANISOU 1047 CG ASN A 137 6908 4771 5781 -111 594 26 C
ATOM 1048 OD1 ASN A 137 0.884 27.572 5.595 1.00 46.88 O
ANISOU 1048 OD1 ASN A 137 6920 4944 5949 -97 503 46 O
ATOM 1049 ND2 ASN A 137 1.824 29.089 4.275 1.00 45.26 N
ANISOU 1049 ND2 ASN A 137 6788 4647 5761 -156 629 65 N
ATOM 1050 N TYR A 138 -0.168 24.831 3.908 1.00 47.22 N
ANISOU 1050 N TYR A 138 7151 4905 5887 -2 747 -26 N
ATOM 1051 CA TYR A 138 0.132 23.535 4.482 1.00 48.43 C
ANISOU 1051 CA TYR A 138 7185 5059 6156 39 777 9 C
ATOM 1052 C TYR A 138 0.785 23.625 5.864 1.00 48.86 C
ANISOU 1052 C TYR A 138 7037 5172 6355 31 657 87 C
ATOM 1053 O TYR A 138 0.301 22.988 6.804 1.00 49.16 O
ANISOU 1053 O TYR A 138 7024 5269 6386 43 545 97 O
ATOM 1054 CB TYR A 138 0.969 22.676 3.534 1.00 48.99 C
ANISOU 1054 CB TYR A 138 7268 5017 6329 61 1014 22 C
ATOM 1055 CG TYR A 138 1.241 21.337 4.162 1.00 50.22 C
ANISOU 1055 CG TYR A 138 7291 5160 6628 111 1037 66 C
ATOM 1056 CD1 TYR A 138 0.197 20.485 4.497 1.00 51.13 C
ANISOU 1056 CD1 TYR A 138 7465 5317 6646 131 949 28 C
ATOM 1057 CD2 TYR A 138 2.521 20.988 4.567 1.00 51.94 C
ANISOU 1057 CD2 TYR A 138 7300 5330 7104 133 1114 164 C
ATOM 1058 CE1 TYR A 138 0.427 19.295 5.169 1.00 52.73 C
ANISOU 1058 CE1 TYR A 138 7541 5510 6982 172 949 78 C
ATOM 1059 CE2 TYR A 138 2.765 19.791 5.231 1.00 53.28 C
ANISOU 1059 CE2 TYR A 138 7330 5484 7428 178 1107 225 C
ATOM 1060 CZ TYR A 138 1.716 18.937 5.510 1.00 54.24 C
ANISOU 1060 CZ TYR A 138 7535 5646 7430 197 1029 177 C
ATOM 1061 OH TYR A 138 1.936 17.770 6.195 1.00 56.76 O
ANISOU 1061 OH TYR A 138 7722 5946 7898 235 1010 243 O
ATOM 1062 N GLU A 139 1.866 24.400 5.993 1.00 48.50 N
ANISOU 1062 N GLU A 139 6887 5107 6434 -3 668 150 N
ATOM 1063 CA GLU A 139 2.577 24.563 7.257 1.00 48.91 C
ANISOU 1063 CA GLU A 139 6763 5202 6620 -41 528 241 C
ATOM 1064 C GLU A 139 1.642 25.012 8.403 1.00 48.14 C
ANISOU 1064 C GLU A 139 6717 5203 6372 -78 321 202 C
ATOM 1065 O GLU A 139 1.689 24.462 9.511 1.00 48.29 O
ANISOU 1065 O GLU A 139 6651 5266 6429 -99 202 253 O
ATOM 1066 CB GLU A 139 3.719 25.566 7.071 1.00 52.91 C
ANISOU 1066 CB GLU A 139 7183 5667 7251 -91 556 306 C
ATOM 1067 CG GLU A 139 4.628 25.663 8.285 1.00 64.50 C
ANISOU 1067 CG GLU A 139 8461 7160 8887 -152 400 428 C
ATOM 1068 CD GLU A 139 5.237 24.352 8.762 1.00 75.82 C
ANISOU 1068 CD GLU A 139 9716 8565 10527 -121 405 535 C
ATOM 1069 OE1 GLU A 139 5.671 23.545 7.902 1.00 78.93 O
ANISOU 1069 OE1 GLU A 139 10058 8871 11061 -51 613 552 O
ATOM 1070 OE2 GLU A 139 5.277 24.135 9.997 1.00 77.43 O
ANISOU 1070 OE2 GLU A 139 9844 8824 10752 -173 207 604 O
ATOM 1071 N GLU A 140 0.738 25.957 8.100 1.00 46.25 N
ANISOU 1071 N GLU A 140 6625 4984 5963 -87 291 113 N
ATOM 1072 CA GLU A 140 -0.201 26.440 9.094 1.00 44.56 C
ANISOU 1072 CA GLU A 140 6471 4840 5621 -113 146 62 C
ATOM 1073 C GLU A 140 -1.239 25.376 9.430 1.00 44.24 C
ANISOU 1073 C GLU A 140 6460 4839 5509 -70 126 28 C
ATOM 1074 O GLU A 140 -1.694 25.296 10.569 1.00 43.48 O
ANISOU 1074 O GLU A 140 6360 4799 5361 -98 21 22 O
ATOM 1075 CB GLU A 140 -0.864 27.725 8.624 1.00 43.51 C
ANISOU 1075 CB GLU A 140 6465 4693 5375 -122 138 -11 C
ATOM 1076 CG GLU A 140 0.129 28.832 8.335 1.00 44.01 C
ANISOU 1076 CG GLU A 140 6507 4714 5501 -174 150 23 C
ATOM 1077 CD GLU A 140 -0.504 30.008 7.620 1.00 44.95 C
ANISOU 1077 CD GLU A 140 6756 4800 5524 -174 160 -40 C
ATOM 1078 OE1 GLU A 140 -1.437 29.764 6.824 1.00 45.27 O
ANISOU 1078 OE1 GLU A 140 6892 4825 5484 -128 201 -85 O
ATOM 1079 OE2 GLU A 140 -0.092 31.168 7.862 1.00 44.72 O
ANISOU 1079 OE2 GLU A 140 6737 4751 5504 -229 113 -36 O
ATOM 1080 N PHE A 141 -1.630 24.568 8.443 1.00 44.88 N
ANISOU 1080 N PHE A 141 6589 4885 5577 -13 229 4 N
ATOM 1081 CA PHE A 141 -2.580 23.493 8.663 1.00 45.80 C
ANISOU 1081 CA PHE A 141 6731 5031 5640 22 212 -20 C
ATOM 1082 C PHE A 141 -1.947 22.451 9.595 1.00 47.21 C
ANISOU 1082 C PHE A 141 6780 5230 5928 18 177 57 C
ATOM 1083 O PHE A 141 -2.625 21.990 10.510 1.00 47.36 O
ANISOU 1083 O PHE A 141 6796 5305 5893 9 91 52 O
ATOM 1084 CB PHE A 141 -2.959 22.863 7.337 1.00 45.46 C
ANISOU 1084 CB PHE A 141 6785 4926 5560 60 326 -54 C
ATOM 1085 CG PHE A 141 -4.055 21.840 7.441 1.00 46.09 C
ANISOU 1085 CG PHE A 141 6908 5029 5576 86 295 -82 C
ATOM 1086 CD1 PHE A 141 -5.382 22.231 7.552 1.00 46.48 C
ANISOU 1086 CD1 PHE A 141 7028 5114 5519 85 210 -129 C
ATOM 1087 CD2 PHE A 141 -3.767 20.483 7.384 1.00 46.19 C
ANISOU 1087 CD2 PHE A 141 6883 5011 5657 113 359 -53 C
ATOM 1088 CE1 PHE A 141 -6.397 21.283 7.595 1.00 46.79 C
ANISOU 1088 CE1 PHE A 141 7096 5167 5517 102 181 -143 C
ATOM 1089 CE2 PHE A 141 -4.785 19.538 7.430 1.00 46.41 C
ANISOU 1089 CE2 PHE A 141 6958 5052 5624 128 328 -77 C
ATOM 1090 CZ PHE A 141 -6.093 19.944 7.523 1.00 46.25 C
ANISOU 1090 CZ PHE A 141 7004 5074 5493 119 235 -119 C
ATOM 1091 N VAL A 142 -0.624 22.161 9.436 1.00 47.74 N
ANISOU 1091 N VAL A 142 6729 5245 6165 16 237 140 N
ATOM 1092 CA VAL A 142 0.084 21.223 10.324 1.00 48.81 C
ANISOU 1092 CA VAL A 142 6715 5383 6446 6 181 244 C
ATOM 1093 C VAL A 142 0.022 21.741 11.768 1.00 50.06 C
ANISOU 1093 C VAL A 142 6853 5621 6549 -78 -10 278 C
ATOM 1094 O VAL A 142 -0.438 21.018 12.654 1.00 50.79 O
ANISOU 1094 O VAL A 142 6939 5757 6600 -94 -97 299 O
ATOM 1095 CB VAL A 142 1.565 20.981 9.905 1.00 49.22 C
ANISOU 1095 CB VAL A 142 6612 5348 6740 17 279 347 C
ATOM 1096 CG1 VAL A 142 2.291 20.115 10.937 1.00 49.60 C
ANISOU 1096 CG1 VAL A 142 6483 5394 6967 -4 177 483 C
ATOM 1097 CG2 VAL A 142 1.653 20.351 8.540 1.00 49.55 C
ANISOU 1097 CG2 VAL A 142 6704 5295 6828 89 504 305 C
ATOM 1098 N GLN A 143 0.436 23.003 11.995 1.00 49.85 N
ANISOU 1098 N GLN A 143 6839 5603 6498 -141 -71 278 N
ATOM 1099 CA GLN A 143 0.418 23.610 13.320 1.00 50.82 C
ANISOU 1099 CA GLN A 143 6988 5782 6541 -244 -241 298 C
ATOM 1100 C GLN A 143 -0.976 23.624 13.918 1.00 51.29 C
ANISOU 1100 C GLN A 143 7184 5900 6402 -245 -272 199 C
ATOM 1101 O GLN A 143 -1.094 23.370 15.099 1.00 51.99 O
ANISOU 1101 O GLN A 143 7291 6032 6432 -318 -385 230 O
ATOM 1102 CB GLN A 143 1.037 25.021 13.305 1.00 52.54 C
ANISOU 1102 CB GLN A 143 7223 5981 6758 -313 -281 298 C
ATOM 1103 CG GLN A 143 2.483 24.983 12.877 1.00 57.60 C
ANISOU 1103 CG GLN A 143 7699 6561 7625 -325 -259 419 C
ATOM 1104 CD GLN A 143 3.242 26.219 13.285 1.00 63.57 C
ANISOU 1104 CD GLN A 143 8447 7307 8401 -433 -365 460 C
ATOM 1105 OE1 GLN A 143 2.997 26.818 14.351 1.00 65.25 O
ANISOU 1105 OE1 GLN A 143 8752 7558 8481 -536 -515 443 O
ATOM 1106 NE2 GLN A 143 4.190 26.610 12.447 1.00 63.60 N
ANISOU 1106 NE2 GLN A 143 8351 7247 8566 -420 -278 514 N
ATOM 1107 N MET A 144 -2.031 23.882 13.122 1.00 50.94 N
ANISOU 1107 N MET A 144 7237 5852 6266 -174 -175 91 N
ATOM 1108 CA MET A 144 -3.396 23.811 13.640 1.00 51.52 C
ANISOU 1108 CA MET A 144 7407 5968 6199 -164 -185 11 C
ATOM 1109 C MET A 144 -3.719 22.367 14.098 1.00 52.83 C
ANISOU 1109 C MET A 144 7530 6164 6379 -148 -202 53 C
ATOM 1110 O MET A 144 -4.337 22.171 15.137 1.00 53.57 O
ANISOU 1110 O MET A 144 7670 6303 6381 -192 -257 40 O
ATOM 1111 CB MET A 144 -4.410 24.315 12.597 1.00 50.99 C
ANISOU 1111 CB MET A 144 7419 5876 6080 -93 -99 -79 C
ATOM 1112 CG MET A 144 -5.848 24.192 13.039 1.00 51.36 C
ANISOU 1112 CG MET A 144 7528 5952 6035 -72 -97 -144 C
ATOM 1113 SD MET A 144 -6.576 22.544 12.772 1.00 52.60 S
ANISOU 1113 SD MET A 144 7653 6127 6207 -17 -72 -124 S
ATOM 1114 CE MET A 144 -6.487 22.449 11.014 1.00 46.42 C
ANISOU 1114 CE MET A 144 6894 5278 5466 42 3 -132 C
ATOM 1115 N MET A 145 -3.295 21.366 13.335 1.00 53.15 N
ANISOU 1115 N MET A 145 7495 6170 6532 -90 -143 101 N
ATOM 1116 CA MET A 145 -3.582 19.961 13.657 1.00 53.89 C
ANISOU 1116 CA MET A 145 7547 6274 6654 -68 -151 142 C
ATOM 1117 C MET A 145 -2.772 19.420 14.833 1.00 55.99 C
ANISOU 1117 C MET A 145 7727 6560 6988 -140 -270 258 C
ATOM 1118 O MET A 145 -3.270 18.556 15.540 1.00 56.61 O
ANISOU 1118 O MET A 145 7811 6670 7028 -156 -318 282 O
ATOM 1119 CB MET A 145 -3.380 19.042 12.421 1.00 52.33 C
ANISOU 1119 CB MET A 145 7318 6008 6556 14 -30 149 C
ATOM 1120 CG MET A 145 -4.326 19.344 11.290 1.00 52.74 C
ANISOU 1120 CG MET A 145 7484 6038 6516 61 53 51 C
ATOM 1121 SD MET A 145 -6.027 18.817 11.631 1.00 57.01 S
ANISOU 1121 SD MET A 145 8099 6629 6934 72 14 -6 S
ATOM 1122 CE MET A 145 -5.902 17.130 11.274 1.00 51.70 C
ANISOU 1122 CE MET A 145 7395 5910 6338 108 63 36 C
ATOM 1123 N THR A 146 -1.534 19.888 15.027 1.00 56.78 N
ANISOU 1123 N THR A 146 7743 6635 7198 -191 -329 343 N
ATOM 1124 CA THR A 146 -0.635 19.327 16.031 1.00 58.65 C
ANISOU 1124 CA THR A 146 7875 6872 7538 -270 -470 487 C
ATOM 1125 C THR A 146 -0.336 20.202 17.279 1.00 61.10 C
ANISOU 1125 C THR A 146 8245 7224 7744 -418 -644 525 C
ATOM 1126 O THR A 146 0.124 19.660 18.289 1.00 61.44 O
ANISOU 1126 O THR A 146 8249 7279 7818 -510 -797 644 O
ATOM 1127 CB THR A 146 0.679 18.935 15.338 1.00 59.60 C
ANISOU 1127 CB THR A 146 7816 6908 7922 -226 -420 599 C
ATOM 1128 OG1 THR A 146 1.303 20.118 14.856 1.00 60.12 O
ANISOU 1128 OG1 THR A 146 7873 6951 8021 -245 -393 584 O
ATOM 1129 CG2 THR A 146 0.456 17.981 14.159 1.00 59.50 C
ANISOU 1129 CG2 THR A 146 7777 6831 8000 -98 -232 559 C
ATOM 1130 N ALA A 147 -0.577 21.523 17.215 1.00 62.39 N
ANISOU 1130 N ALA A 147 8518 7400 7787 -451 -628 430 N
ATOM 1131 CA ALA A 147 -0.356 22.476 18.311 1.00 64.26 C
ANISOU 1131 CA ALA A 147 8857 7660 7898 -601 -768 437 C
ATOM 1132 C ALA A 147 1.034 22.384 18.975 1.00 65.93 C
ANISOU 1132 C ALA A 147 8958 7848 8245 -723 -958 614 C
ATOM 1133 O ALA A 147 2.047 22.687 18.336 1.00 67.03 O
ANISOU 1133 O ALA A 147 8960 7937 8572 -705 -953 687 O
ATOM 1134 CB ALA A 147 -1.451 22.350 19.359 1.00 64.50 C
ANISOU 1134 CB ALA A 147 9055 7743 7711 -664 -793 366 C
TER 1135 ALA A 147
HETATM 1136 N1 85H A 201 -5.712 9.445 13.885 1.00 54.24 N
ANISOU 1136 N1 85H A 201 7424 6103 7083 142 -42 407 N
HETATM 1137 C7 85H A 201 -3.452 13.444 13.358 1.00 56.08 C
ANISOU 1137 C7 85H A 201 7584 6381 7340 104 -26 377 C
HETATM 1138 C8 85H A 201 -3.956 14.639 13.850 1.00 56.45 C
ANISOU 1138 C8 85H A 201 7699 6516 7233 50 -101 323 C
HETATM 1139 C9 85H A 201 -3.238 15.394 14.760 1.00 57.13 C
ANISOU 1139 C9 85H A 201 7735 6641 7331 -23 -212 387 C
HETATM 1140 C1 85H A 201 -6.419 14.039 9.796 1.00 54.85 C
ANISOU 1140 C1 85H A 201 7869 6159 6813 179 215 37 C
HETATM 1141 C5 85H A 201 -7.817 13.728 11.716 1.00 55.26 C
ANISOU 1141 C5 85H A 201 7866 6354 6777 134 35 66 C
HETATM 1142 C6 85H A 201 -4.323 12.480 12.566 1.00 55.39 C
ANISOU 1142 C6 85H A 201 7583 6250 7214 156 67 311 C
HETATM 1143 C4 85H A 201 -6.734 13.226 12.413 1.00 55.31 C
ANISOU 1143 C4 85H A 201 7771 6350 6895 128 19 152 C
HETATM 1144 C3 85H A 201 -5.483 13.128 11.823 1.00 55.26 C
ANISOU 1144 C3 85H A 201 7710 6264 7023 159 100 189 C
HETATM 1145 C2 85H A 201 -5.340 13.547 10.508 1.00 55.01 C
ANISOU 1145 C2 85H A 201 7759 6165 6978 188 215 124 C
HETATM 1146 CL1 85H A 201 -1.234 15.695 16.549 1.00 58.53 CL
ANISOU 1146 CL1 85H A 201 7731 6825 7682 -181 -475 632 CL
HETATM 1147 C10 85H A 201 -2.004 14.939 15.179 1.00 57.67 C
ANISOU 1147 C10 85H A 201 7663 6666 7584 -46 -273 525 C
HETATM 1148 C11 85H A 201 -1.444 13.806 14.641 1.00 57.04 C
ANISOU 1148 C11 85H A 201 7482 6493 7698 23 -190 591 C
HETATM 1149 C12 85H A 201 -2.175 13.062 13.735 1.00 56.49 C
ANISOU 1149 C12 85H A 201 7486 6380 7597 99 -55 506 C
HETATM 1150 C 85H A 201 -7.643 14.139 10.418 1.00 54.78 C
ANISOU 1150 C 85H A 201 7881 6228 6705 156 116 17 C
HETATM 1151 CL 85H A 201 -8.966 14.897 9.584 1.00 54.45 CL
ANISOU 1151 CL 85H A 201 7958 6193 6538 143 89 -59 CL
HETATM 1152 N 85H A 201 -4.846 11.368 13.437 1.00 54.63 N
ANISOU 1152 N 85H A 201 7464 6178 7115 137 -13 364 N
HETATM 1153 C13 85H A 201 -5.235 11.397 14.759 1.00 54.30 C
ANISOU 1153 C13 85H A 201 7410 6227 6996 68 -152 411 C
HETATM 1154 C14 85H A 201 -5.786 10.200 15.035 1.00 53.74 C
ANISOU 1154 C14 85H A 201 7342 6143 6933 71 -168 440 C
HETATM 1155 C30 85H A 201 -5.124 10.165 12.943 1.00 54.41 C
ANISOU 1155 C30 85H A 201 7457 6078 7140 177 56 361 C
HETATM 1156 C15 85H A 201 -6.197 8.072 13.724 1.00 54.31 C
ANISOU 1156 C15 85H A 201 7453 6053 7129 164 -13 419 C
HETATM 1157 C16 85H A 201 -7.559 8.062 13.047 1.00 54.32 C
ANISOU 1157 C16 85H A 201 7591 6074 6975 162 18 309 C
HETATM 1158 C24 85H A 201 -8.630 8.619 13.956 1.00 54.55 C
ANISOU 1158 C24 85H A 201 7643 6227 6857 105 -85 292 C
HETATM 1159 C25 85H A 201 -9.089 9.925 13.793 1.00 54.49 C
ANISOU 1159 C25 85H A 201 7681 6280 6742 93 -88 220 C
HETATM 1160 C26 85H A 201 -10.126 10.433 14.549 1.00 54.53 C
ANISOU 1160 C26 85H A 201 7707 6374 6637 51 -141 195 C
HETATM 1161 C27 85H A 201 -10.719 9.629 15.486 1.00 55.04 C
ANISOU 1161 C27 85H A 201 7758 6476 6680 12 -188 241 C
HETATM 1162 CL4 85H A 201 -12.097 10.222 16.368 1.00 55.70 CL
ANISOU 1162 CL4 85H A 201 7871 6649 6643 -37 -199 202 CL
HETATM 1163 C28 85H A 201 -10.287 8.338 15.708 1.00 54.97 C
ANISOU 1163 C28 85H A 201 7709 6420 6755 12 -208 319 C
HETATM 1164 C29 85H A 201 -9.249 7.850 14.938 1.00 55.28 C
ANISOU 1164 C29 85H A 201 7719 6364 6922 63 -159 344 C
HETATM 1165 CL5 85H A 201 -8.736 6.213 15.218 1.00 56.47 CL
ANISOU 1165 CL5 85H A 201 7810 6430 7218 74 -170 447 CL
HETATM 1166 O 85H A 201 -7.412 8.848 11.858 1.00 54.26 O
ANISOU 1166 O 85H A 201 7658 6025 6932 188 113 224 O
HETATM 1167 C17 85H A 201 -8.300 8.464 10.810 1.00 53.92 C
ANISOU 1167 C17 85H A 201 7751 5930 6806 189 165 145 C
HETATM 1168 C18 85H A 201 -8.135 9.413 9.652 1.00 53.48 C
ANISOU 1168 C18 85H A 201 7791 5839 6689 195 241 69 C
HETATM 1169 C19 85H A 201 -7.140 9.201 8.698 1.00 53.66 C
ANISOU 1169 C19 85H A 201 7854 5741 6792 227 394 52 C
HETATM 1170 C20 85H A 201 -6.956 10.070 7.636 1.00 53.46 C
ANISOU 1170 C20 85H A 201 7936 5680 6697 220 472 -12 C
HETATM 1171 C21 85H A 201 -7.789 11.154 7.511 1.00 53.41 C
ANISOU 1171 C21 85H A 201 7986 5756 6553 184 376 -51 C
HETATM 1172 CL2 85H A 201 -7.658 12.176 6.109 1.00 53.99 CL
ANISOU 1172 CL2 85H A 201 8218 5773 6524 157 453 -119 CL
HETATM 1173 C22 85H A 201 -8.787 11.404 8.426 1.00 52.93 C
ANISOU 1173 C22 85H A 201 7870 5805 6438 164 231 -35 C
HETATM 1174 C23 85H A 201 -8.945 10.532 9.483 1.00 52.94 C
ANISOU 1174 C23 85H A 201 7776 5843 6496 167 177 20 C
HETATM 1175 CL3 85H A 201 -10.201 10.876 10.634 1.00 52.84 CL
ANISOU 1175 CL3 85H A 201 7711 5956 6409 134 40 33 CL
HETATM 1176 N1 85H A 202 -9.575 22.291 16.036 1.00 65.57 N
ANISOU 1176 N1 85H A 202 9406 7876 7631 -95 -65 -228 N
HETATM 1177 C7 85H A 202 -7.252 18.803 16.474 1.00 64.20 C
ANISOU 1177 C7 85H A 202 9046 7748 7598 -145 -236 36 C
HETATM 1178 C8 85H A 202 -7.849 18.039 17.469 1.00 63.80 C
ANISOU 1178 C8 85H A 202 9019 7737 7484 -190 -264 58 C
HETATM 1179 C9 85H A 202 -8.400 16.801 17.187 1.00 63.20 C
ANISOU 1179 C9 85H A 202 8905 7660 7449 -144 -243 82 C
HETATM 1180 C1 85H A 202 -4.148 20.087 19.578 1.00 67.53 C
ANISOU 1180 C1 85H A 202 9513 8202 7942 -517 -611 257 C
HETATM 1181 C5 85H A 202 -6.056 21.328 20.347 1.00 67.40 C
ANISOU 1181 C5 85H A 202 9749 8212 7648 -550 -468 44 C
HETATM 1182 C6 85H A 202 -6.709 20.197 16.763 1.00 65.43 C
ANISOU 1182 C6 85H A 202 9249 7900 7712 -200 -260 7 C
HETATM 1183 C4 85H A 202 -6.685 21.092 19.137 1.00 66.97 C
ANISOU 1183 C4 85H A 202 9614 8143 7688 -406 -359 -4 C
HETATM 1184 C3 85H A 202 -6.057 20.367 18.130 1.00 66.46 C
ANISOU 1184 C3 85H A 202 9418 8058 7774 -327 -367 63 C
HETATM 1185 C2 85H A 202 -4.787 19.864 18.372 1.00 66.86 C
ANISOU 1185 C2 85H A 202 9382 8100 7921 -376 -475 187 C
HETATM 1186 CL1 85H A 202 -9.079 14.788 15.518 1.00 62.69 CL
ANISOU 1186 CL1 85H A 202 8776 7528 7516 -18 -172 98 CL
HETATM 1187 C10 85H A 202 -8.346 16.324 15.896 1.00 62.79 C
ANISOU 1187 C10 85H A 202 8809 7559 7490 -60 -194 77 C
HETATM 1188 C11 85H A 202 -7.738 17.044 14.895 1.00 62.87 C
ANISOU 1188 C11 85H A 202 8813 7526 7549 -22 -156 52 C
HETATM 1189 C12 85H A 202 -7.197 18.282 15.190 1.00 63.41 C
ANISOU 1189 C12 85H A 202 8900 7603 7588 -61 -178 36 C
HETATM 1190 C 85H A 202 -4.791 20.822 20.553 1.00 67.86 C
ANISOU 1190 C 85H A 202 9723 8269 7793 -612 -613 181 C
HETATM 1191 CL 85H A 202 -4.001 21.089 22.087 1.00 68.53 CL
ANISOU 1191 CL 85H A 202 9922 8364 7751 -827 -801 268 CL
HETATM 1192 N 85H A 202 -7.720 21.287 16.490 1.00 65.38 N
ANISOU 1192 N 85H A 202 9319 7882 7640 -169 -183 -101 N
HETATM 1193 C13 85H A 202 -7.407 22.590 16.171 1.00 65.27 C
ANISOU 1193 C13 85H A 202 9343 7837 7621 -175 -169 -146 C
HETATM 1194 C14 85H A 202 -8.566 23.217 15.893 1.00 65.47 C
ANISOU 1194 C14 85H A 202 9412 7842 7621 -127 -95 -227 C
HETATM 1195 C30 85H A 202 -9.043 21.144 16.430 1.00 65.51 C
ANISOU 1195 C30 85H A 202 9360 7903 7628 -125 -118 -157 C
HETATM 1196 C15 85H A 202 -10.958 22.478 15.572 1.00 65.03 C
ANISOU 1196 C15 85H A 202 9333 7782 7592 -29 3 -278 C
HETATM 1197 C16 85H A 202 -10.748 22.252 14.081 1.00 64.87 C
ANISOU 1197 C16 85H A 202 9275 7730 7643 32 -19 -251 C
HETATM 1198 C24 85H A 202 -10.778 20.821 13.613 1.00 64.65 C
ANISOU 1198 C24 85H A 202 9207 7714 7643 53 -39 -201 C
HETATM 1199 C25 85H A 202 -9.612 20.281 13.080 1.00 64.91 C
ANISOU 1199 C25 85H A 202 9220 7734 7707 52 -55 -156 C
HETATM 1200 C26 85H A 202 -9.558 18.985 12.611 1.00 65.37 C
ANISOU 1200 C26 85H A 202 9257 7780 7801 72 -52 -118 C
HETATM 1201 C27 85H A 202 -10.677 18.201 12.697 1.00 65.63 C
ANISOU 1201 C27 85H A 202 9288 7824 7823 84 -58 -120 C
HETATM 1202 CL4 85H A 202 -10.627 16.586 12.068 1.00 66.64 CL
ANISOU 1202 CL4 85H A 202 9413 7919 7990 100 -53 -80 CL
HETATM 1203 C28 85H A 202 -11.854 18.678 13.228 1.00 64.99 C
ANISOU 1203 C28 85H A 202 9209 7764 7719 82 -54 -153 C
HETATM 1204 C29 85H A 202 -11.900 19.991 13.654 1.00 64.30 C
ANISOU 1204 C29 85H A 202 9141 7678 7611 72 -33 -195 C
HETATM 1205 CL5 85H A 202 -13.451 20.614 14.150 1.00 62.82 CL
ANISOU 1205 CL5 85H A 202 8943 7482 7443 88 16 -238 CL
HETATM 1206 O 85H A 202 -11.512 23.204 13.348 1.00 64.88 O
ANISOU 1206 O 85H A 202 9289 7680 7682 75 5 -289 O
HETATM 1207 C17 85H A 202 -10.769 24.366 13.028 1.00 63.91 C
ANISOU 1207 C17 85H A 202 9202 7524 7556 64 3 -308 C
HETATM 1208 C18 85H A 202 -10.039 24.414 11.710 1.00 63.03 C
ANISOU 1208 C18 85H A 202 9098 7380 7470 81 -19 -278 C
HETATM 1209 C19 85H A 202 -9.208 25.510 11.508 1.00 62.03 C
ANISOU 1209 C19 85H A 202 9000 7225 7343 59 -18 -289 C
HETATM 1210 C20 85H A 202 -8.600 25.755 10.294 1.00 61.24 C
ANISOU 1210 C20 85H A 202 8923 7083 7261 67 -15 -267 C
HETATM 1211 C21 85H A 202 -8.810 24.887 9.258 1.00 61.23 C
ANISOU 1211 C21 85H A 202 8939 7063 7262 90 -8 -241 C
HETATM 1212 CL2 85H A 202 -8.119 25.246 7.704 1.00 60.28 CL
ANISOU 1212 CL2 85H A 202 8895 6876 7134 80 24 -223 CL
HETATM 1213 C22 85H A 202 -9.593 23.760 9.408 1.00 62.24 C
ANISOU 1213 C22 85H A 202 9047 7215 7388 107 -20 -232 C
HETATM 1214 C23 85H A 202 -10.201 23.544 10.633 1.00 63.43 C
ANISOU 1214 C23 85H A 202 9151 7413 7537 106 -28 -247 C
HETATM 1215 CL3 85H A 202 -11.235 22.151 10.783 1.00 64.54 CL
ANISOU 1215 CL3 85H A 202 9261 7577 7683 123 -43 -227 CL
HETATM 1216 CA CA A 203 -1.701 32.169 5.954 1.00 46.06 CA2+
HETATM 1217 CA CA A 204 -7.148 26.383 -2.231 1.00 53.59 CA2+
HETATM 1218 CA CA A 205 -14.113 3.358 24.911 1.00 55.03 CA2+
HETATM 1219 CA CA A 206 -22.093 8.985 18.490 1.00 52.54 CA2+
HETATM 1220 O HOH A 301 -5.833 27.771 31.845 1.00 75.08 O
HETATM 1221 O HOH A 302 -1.892 27.274 12.368 1.00 42.70 O
HETATM 1222 O HOH A 303 -6.836 6.451 24.082 1.00 62.59 O
HETATM 1223 O HOH A 304 -17.487 22.451 27.627 1.00 76.49 O
HETATM 1224 O HOH A 305 -15.237 3.332 3.747 1.00 57.57 O
HETATM 1225 O HOH A 306 -23.120 5.381 15.348 1.00 50.88 O
HETATM 1226 O HOH A 307 -12.176 -1.927 21.345 1.00 79.71 O
HETATM 1227 O HOH A 308 -15.577 18.007 0.793 1.00 56.92 O
HETATM 1228 O HOH A 309 1.007 33.754 1.271 1.00 50.24 O
HETATM 1229 O HOH A 310 -4.473 32.061 16.869 1.00 73.20 O
HETATM 1230 O HOH A 311 -19.597 10.312 4.328 1.00 53.67 O
HETATM 1231 O HOH A 312 -0.455 31.260 4.078 1.00 40.69 O
HETATM 1232 O HOH A 313 -21.149 16.300 13.598 1.00 72.47 O
HETATM 1233 O HOH A 314 -4.530 6.895 16.867 1.00 58.89 O
HETATM 1234 O HOH A 315 0.939 25.259 1.046 1.00 42.57 O
HETATM 1235 O HOH A 316 -13.938 25.602 26.865 1.00 62.88 O
HETATM 1236 O HOH A 317 -12.138 35.893 14.738 1.00 59.32 O
HETATM 1237 O HOH A 318 -9.675 33.199 2.672 1.00 51.08 O
HETATM 1238 O HOH A 319 1.769 32.318 -2.912 1.00 59.94 O
HETATM 1239 O HOH A 320 -5.750 4.701 15.847 1.00 61.12 O
HETATM 1240 O HOH A 321 -24.206 16.183 13.573 1.00 70.43 O
HETATM 1241 O HOH A 322 -15.122 -0.754 17.361 1.00 60.55 O
HETATM 1242 O HOH A 323 -20.931 19.088 15.405 1.00 55.20 O
HETATM 1243 O HOH A 324 -8.655 1.281 2.880 1.00 72.40 O
HETATM 1244 O HOH A 325 0.113 17.982 1.270 1.00 63.10 O
HETATM 1245 O HOH A 326 3.042 25.606 3.613 1.00 56.25 O
HETATM 1246 O HOH A 327 -17.762 11.774 26.123 1.00 60.47 O
HETATM 1247 O HOH A 328 -8.634 4.777 2.447 1.00 69.62 O
HETATM 1248 O HOH A 329 -24.707 19.133 12.731 1.00 62.02 O
HETATM 1249 O HOH A 330 3.600 21.641 16.014 1.00 69.21 O
HETATM 1250 O HOH A 331 -8.002 27.310 13.819 1.00 61.71 O
HETATM 1251 O HOH A 332 -3.980 24.342 17.221 1.00 51.69 O
HETATM 1252 O HOH A 333 -8.330 29.700 29.639 1.00 92.02 O
HETATM 1253 O HOH A 334 -17.113 -2.508 16.587 1.00 65.45 O
HETATM 1254 O HOH A 335 -5.739 27.085 15.083 1.00 53.57 O
HETATM 1255 O HOH A 336 -7.291 6.480 26.845 1.00 63.61 O
HETATM 1256 O HOH A 337 -17.908 11.276 -0.173 1.00 55.45 O
HETATM 1257 O HOH A 338 -8.172 29.466 -2.974 1.00 63.99 O
HETATM 1258 O HOH A 339 -3.342 7.185 19.463 1.00 63.75 O
HETATM 1259 O HOH A 340 -2.553 26.878 14.943 1.00 63.00 O
HETATM 1260 O HOH A 341 -4.139 9.366 4.650 1.00 65.58 O
CONECT 141 1219
CONECT 158 1219
CONECT 170 1219
CONECT 179 1219
CONECT 221 1219
CONECT 222 1219
CONECT 411 1218
CONECT 424 1218
CONECT 436 1218
CONECT 445 1218
CONECT 490 1218
CONECT 491 1218
CONECT 711 1217
CONECT 728 1217
CONECT 740 1217
CONECT 749 1217
CONECT 789 1217
CONECT 790 1217
CONECT 992 1216
CONECT 1008 1216
CONECT 1020 1216
CONECT 1029 1216
CONECT 1078 1216
CONECT 1079 1216
CONECT 1136 1154 1155 1156
CONECT 1137 1138 1142 1149
CONECT 1138 1137 1139
CONECT 1139 1138 1147
CONECT 1140 1145 1150
CONECT 1141 1143 1150
CONECT 1142 1137 1144 1152
CONECT 1143 1141 1144
CONECT 1144 1142 1143 1145
CONECT 1145 1140 1144
CONECT 1146 1147
CONECT 1147 1139 1146 1148
CONECT 1148 1147 1149
CONECT 1149 1137 1148
CONECT 1150 1140 1141 1151
CONECT 1151 1150
CONECT 1152 1142 1153 1155
CONECT 1153 1152 1154
CONECT 1154 1136 1153
CONECT 1155 1136 1152
CONECT 1156 1136 1157
CONECT 1157 1156 1158 1166
CONECT 1158 1157 1159 1164
CONECT 1159 1158 1160
CONECT 1160 1159 1161
CONECT 1161 1160 1162 1163
CONECT 1162 1161
CONECT 1163 1161 1164
CONECT 1164 1158 1163 1165
CONECT 1165 1164
CONECT 1166 1157 1167
CONECT 1167 1166 1168
CONECT 1168 1167 1169 1174
CONECT 1169 1168 1170
CONECT 1170 1169 1171
CONECT 1171 1170 1172 1173
CONECT 1172 1171
CONECT 1173 1171 1174
CONECT 1174 1168 1173 1175
CONECT 1175 1174
CONECT 1176 1194 1195 1196
CONECT 1177 1178 1182 1189
CONECT 1178 1177 1179
CONECT 1179 1178 1187
CONECT 1180 1185 1190
CONECT 1181 1183 1190
CONECT 1182 1177 1184 1192
CONECT 1183 1181 1184
CONECT 1184 1182 1183 1185
CONECT 1185 1180 1184
CONECT 1186 1187
CONECT 1187 1179 1186 1188
CONECT 1188 1187 1189
CONECT 1189 1177 1188
CONECT 1190 1180 1181 1191
CONECT 1191 1190
CONECT 1192 1182 1193 1195
CONECT 1193 1192 1194
CONECT 1194 1176 1193
CONECT 1195 1176 1192
CONECT 1196 1176 1197
CONECT 1197 1196 1198 1206
CONECT 1198 1197 1199 1204
CONECT 1199 1198 1200
CONECT 1200 1199 1201
CONECT 1201 1200 1202 1203
CONECT 1202 1201
CONECT 1203 1201 1204
CONECT 1204 1198 1203 1205
CONECT 1205 1204
CONECT 1206 1197 1207
CONECT 1207 1206 1208
CONECT 1208 1207 1209 1214
CONECT 1209 1208 1210
CONECT 1210 1209 1211
CONECT 1211 1210 1212 1213
CONECT 1212 1211
CONECT 1213 1211 1214
CONECT 1214 1208 1213 1215
CONECT 1215 1214
CONECT 1216 992 1008 1020 1029
CONECT 1216 1078 1079 1231
CONECT 1217 711 728 740 749
CONECT 1217 789 790
CONECT 1218 411 424 436 445
CONECT 1218 490 491
CONECT 1219 141 158 170 179
CONECT 1219 221 222
CONECT 1231 1216
MASTER 365 0 6 8 4 0 0 6 1259 1 113 12
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