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7NT4.pdb
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HEADER HYDROLASE 09-MAR-21 7NT4
TITLE X-RAY STRUCTURE OF SCOV2-PLPRO IN COMPLEX WITH SMALL MOLECULE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-STRUCTURAL PROTEIN 3;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NSP3,PL2-PRO,PAPAIN-LIKE PROTEASE,PAPAIN-LIKE PROTEINASE,PL-
COMPND 5 PRO;
COMPND 6 EC: 3.4.19.12,3.4.22.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS
SOURCE 3 2;
SOURCE 4 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2;
SOURCE 5 ORGANISM_TAXID: 2697049;
SOURCE 6 GENE: REP, 1A-1B;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DRUG REPURPOSING, SCOV2-PLPRO INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.NAPOLITANO,A.MOURAO,M.BOSTOCK,A.MATSUDA,A.CZARNA,G.M.POPOWICZ
REVDAT 2 01-JUN-22 7NT4 1 JRNL
REVDAT 1 02-FEB-22 7NT4 0
JRNL AUTH V.NAPOLITANO,A.DABROWSKA,K.SCHORPP,A.MOURAO,E.BARRETO-DURAN,
JRNL AUTH 2 M.BENEDYK,P.BOTWINA,S.BRANDNER,M.BOSTOCK,Y.CHYKUNOVA,
JRNL AUTH 3 A.CZARNA,G.DUBIN,T.FROHLICH,M.HOLSCHER,M.JEDRYSIK,A.MATSUDA,
JRNL AUTH 4 K.OWCZAREK,M.PACHOTA,O.PLETTENBURG,J.POTEMPA,I.ROTHENAIGNER,
JRNL AUTH 5 F.SCHLAUDERER,K.SLYSZ,A.SZCZEPANSKI,K.GREVE-ISDAHL MOHN,
JRNL AUTH 6 B.BLOMBERG,M.SATTLER,K.HADIAN,G.M.POPOWICZ,K.PYRC
JRNL TITL ACRIFLAVINE, A CLINICALLY APPROVED DRUG, INHIBITS SARS-COV-2
JRNL TITL 2 AND OTHER BETACORONAVIRUSES.
JRNL REF CELL CHEM BIOL V. 29 774 2022
JRNL REFN ESSN 2451-9456
JRNL PMID 35021060
JRNL DOI 10.1016/J.CHEMBIOL.2021.11.006
REMARK 2
REMARK 2 RESOLUTION. 2.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 72.6
REMARK 3 NUMBER OF REFLECTIONS : 20369
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1001
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.68
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 88
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 4.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.3500
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4805
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 151
REMARK 3 SOLVENT ATOMS : 193
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.76000
REMARK 3 B22 (A**2) : -0.76000
REMARK 3 B33 (A**2) : 2.48000
REMARK 3 B12 (A**2) : -0.38000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.403
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.278
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.963
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.868
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5116 ; 0.013 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6971 ; 2.011 ; 1.651
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 629 ; 8.171 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 233 ;44.760 ;23.820
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 779 ;21.707 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;18.846 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 674 ; 0.148 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3955 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 9 315 B 9 315 9139 0.130 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 9 A 701
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1267 35.5942 3.7269
REMARK 3 T TENSOR
REMARK 3 T11: 0.1576 T22: 0.3288
REMARK 3 T33: 0.1114 T12: 0.1240
REMARK 3 T13: 0.0024 T23: -0.0491
REMARK 3 L TENSOR
REMARK 3 L11: 2.4030 L22: 2.4526
REMARK 3 L33: 2.2328 L12: 0.5514
REMARK 3 L13: -0.2395 L23: -0.9201
REMARK 3 S TENSOR
REMARK 3 S11: -0.0873 S12: 0.0506 S13: -0.5019
REMARK 3 S21: -0.1726 S22: 0.0563 S23: -0.1826
REMARK 3 S31: 0.5434 S32: 0.1497 S33: 0.0310
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): 63.1580 37.8824 0.9805
REMARK 3 T TENSOR
REMARK 3 T11: 0.0325 T22: 0.2946
REMARK 3 T33: 0.0365 T12: -0.0142
REMARK 3 T13: 0.0131 T23: 0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.3586 L22: 3.4214
REMARK 3 L33: 1.4156 L12: 0.2380
REMARK 3 L13: -0.3978 L23: -0.5165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0294 S12: 0.0450 S13: 0.0872
REMARK 3 S21: -0.0150 S22: -0.0930 S23: 0.2556
REMARK 3 S31: 0.1321 S32: -0.1826 S33: 0.0636
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 7NT4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAR-21.
REMARK 100 THE DEPOSITION ID IS D_1292114584.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-20
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 : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21442
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.678
REMARK 200 RESOLUTION RANGE LOW (A) : 49.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 38.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6W9C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M SODIUM CACODYLATE PH 6.5 0.2 M
REMARK 280 POTASSIUM CHLORIDE, 0.1 M MAGNESIUM ACETATE 10 %(W/V) PEG 8000,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 169.04400
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 84.52200
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 126.78300
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 42.26100
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 211.30500
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 169.04400
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 84.52200
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 42.26100
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 126.78300
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 211.30500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 N10 PRL A 403 LIES ON A SPECIAL POSITION.
REMARK 375 N10 PRL B 401 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 525 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 583 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 VAL A 3
REMARK 465 ARG A 4
REMARK 465 THR A 5
REMARK 465 ILE A 6
REMARK 465 LYS A 7
REMARK 465 VAL A 8
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 VAL B 3
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE A 9 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 20 CG CD OE1 NE2
REMARK 470 MET A 24 CG SD CE
REMARK 470 MET A 26 CG SD CE
REMARK 470 TYR A 28 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE A 32 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 37 CG CD1 CD2
REMARK 470 LYS A 44 CG CD CE NZ
REMARK 470 LYS A 46 CG CD CE NZ
REMARK 470 ASN A 49 CG OD1 ND2
REMARK 470 GLU A 52 CG CD OE1 OE2
REMARK 470 LYS A 54 CG CD CE NZ
REMARK 470 PHE A 56 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 59 CG CD1 CD2
REMARK 470 ASP A 63 CG OD1 OD2
REMARK 470 LYS A 92 CG CD CE NZ
REMARK 470 LYS A 95 CG CD CE NZ
REMARK 470 LYS A 127 CG CD CE NZ
REMARK 470 GLU A 144 CG CD OE1 OE2
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 LYS A 201 CG CD CE NZ
REMARK 470 LYS A 298 CG CD CE NZ
REMARK 470 LYS A 316 CG CD CE NZ
REMARK 470 ARG B 4 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 30 CG CD OE1 NE2
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 LYS B 46 CG CD CE NZ
REMARK 470 LYS B 229 CG CD CE NZ
REMARK 470 GLN B 230 CG CD OE1 NE2
REMARK 470 LYS B 316 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HIS A 48 N SER A 50 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 139 CG ARG A 139 CD 0.639
REMARK 500 ARG A 139 NE ARG A 139 CZ -0.123
REMARK 500 GLU A 168 CD GLU A 168 OE1 0.079
REMARK 500 GLU B 125 CD GLU B 125 OE1 0.077
REMARK 500 GLU B 125 CD GLU B 125 OE2 0.069
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 139 CG - CD - NE ANGL. DEV. = -15.2 DEGREES
REMARK 500 ARG A 139 NE - CZ - NH1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG A 139 NE - CZ - NH2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 GLU A 162 CB - CA - C ANGL. DEV. = 12.2 DEGREES
REMARK 500 CYS A 193 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 ARG B 141 CB - CG - CD ANGL. DEV. = 17.0 DEGREES
REMARK 500 ARG B 141 CG - CD - NE ANGL. DEV. = 13.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 22 75.60 -117.25
REMARK 500 SER A 25 89.55 175.03
REMARK 500 MET A 26 -101.95 -104.30
REMARK 500 THR A 27 36.62 73.40
REMARK 500 GLN A 30 58.67 33.12
REMARK 500 GLN A 31 43.73 -68.09
REMARK 500 LYS A 44 34.49 -97.76
REMARK 500 ASN A 49 -64.22 26.52
REMARK 500 SER A 50 30.91 -76.88
REMARK 500 SER A 104 -166.90 -115.48
REMARK 500 SER A 181 34.09 -77.22
REMARK 500 GLN A 196 108.38 -161.44
REMARK 500 LYS A 280 -128.33 -125.16
REMARK 500 ASN A 309 -80.87 -127.29
REMARK 500 LYS B 44 35.42 -97.74
REMARK 500 SER B 50 37.04 -80.73
REMARK 500 GLU B 52 110.85 -37.18
REMARK 500 SER B 104 -169.90 -113.34
REMARK 500 LEU B 126 133.77 -170.86
REMARK 500 SER B 181 32.47 -68.91
REMARK 500 LYS B 191 -69.04 66.25
REMARK 500 GLN B 196 104.94 -163.53
REMARK 500 LYS B 280 -130.27 -91.54
REMARK 500 LYS B 280 -130.27 -127.39
REMARK 500 ASN B 309 -81.30 -127.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 27 TYR A 28 135.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 606 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B 607 DISTANCE = 6.38 ANGSTROMS
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 ZN A 408 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 190 SG
REMARK 620 2 CYS A 193 SG 104.4
REMARK 620 3 CYS A 225 SG 98.9 107.2
REMARK 620 4 CYS A 227 SG 132.5 108.2 103.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 407 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 190 SG
REMARK 620 2 CYS B 193 SG 104.8
REMARK 620 3 CYS B 225 SG 63.0 117.8
REMARK 620 4 CYS B 227 SG 162.1 92.6 112.5
REMARK 620 N 1 2 3
DBREF 7NT4 A 2 316 UNP P0DTD1 R1AB_SARS2 1564 1878
DBREF 7NT4 B 2 316 UNP P0DTD1 R1AB_SARS2 1564 1878
SEQADV 7NT4 GLY A -1 UNP P0DTD1 EXPRESSION TAG
SEQADV 7NT4 ALA A 0 UNP P0DTD1 EXPRESSION TAG
SEQADV 7NT4 MET A 1 UNP P0DTD1 EXPRESSION TAG
SEQADV 7NT4 GLY B -1 UNP P0DTD1 EXPRESSION TAG
SEQADV 7NT4 ALA B 0 UNP P0DTD1 EXPRESSION TAG
SEQADV 7NT4 MET B 1 UNP P0DTD1 EXPRESSION TAG
SEQRES 1 A 318 GLY ALA MET GLU VAL ARG THR ILE LYS VAL PHE THR THR
SEQRES 2 A 318 VAL ASP ASN ILE ASN LEU HIS THR GLN VAL VAL ASP MET
SEQRES 3 A 318 SER MET THR TYR GLY GLN GLN PHE GLY PRO THR TYR LEU
SEQRES 4 A 318 ASP GLY ALA ASP VAL THR LYS ILE LYS PRO HIS ASN SER
SEQRES 5 A 318 HIS GLU GLY LYS THR PHE TYR VAL LEU PRO ASN ASP ASP
SEQRES 6 A 318 THR LEU ARG VAL GLU ALA PHE GLU TYR TYR HIS THR THR
SEQRES 7 A 318 ASP PRO SER PHE LEU GLY ARG TYR MET SER ALA LEU ASN
SEQRES 8 A 318 HIS THR LYS LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU
SEQRES 9 A 318 THR SER ILE LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA
SEQRES 10 A 318 THR ALA LEU LEU THR LEU GLN GLN ILE GLU LEU LYS PHE
SEQRES 11 A 318 ASN PRO PRO ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG
SEQRES 12 A 318 ALA GLY GLU ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA
SEQRES 13 A 318 TYR CYS ASN LYS THR VAL GLY GLU LEU GLY ASP VAL ARG
SEQRES 14 A 318 GLU THR MET SER TYR LEU PHE GLN HIS ALA ASN LEU ASP
SEQRES 15 A 318 SER CYS LYS ARG VAL LEU ASN VAL VAL CYS LYS THR CYS
SEQRES 16 A 318 GLY GLN GLN GLN THR THR LEU LYS GLY VAL GLU ALA VAL
SEQRES 17 A 318 MET TYR MET GLY THR LEU SER TYR GLU GLN PHE LYS LYS
SEQRES 18 A 318 GLY VAL GLN ILE PRO CYS THR CYS GLY LYS GLN ALA THR
SEQRES 19 A 318 LYS TYR LEU VAL GLN GLN GLU SER PRO PHE VAL MET MET
SEQRES 20 A 318 SER ALA PRO PRO ALA GLN TYR GLU LEU LYS HIS GLY THR
SEQRES 21 A 318 PHE THR CYS ALA SER GLU TYR THR GLY ASN TYR GLN CYS
SEQRES 22 A 318 GLY HIS TYR LYS HIS ILE THR SER LYS GLU THR LEU TYR
SEQRES 23 A 318 CYS ILE ASP GLY ALA LEU LEU THR LYS SER SER GLU TYR
SEQRES 24 A 318 LYS GLY PRO ILE THR ASP VAL PHE TYR LYS GLU ASN SER
SEQRES 25 A 318 TYR THR THR THR ILE LYS
SEQRES 1 B 318 GLY ALA MET GLU VAL ARG THR ILE LYS VAL PHE THR THR
SEQRES 2 B 318 VAL ASP ASN ILE ASN LEU HIS THR GLN VAL VAL ASP MET
SEQRES 3 B 318 SER MET THR TYR GLY GLN GLN PHE GLY PRO THR TYR LEU
SEQRES 4 B 318 ASP GLY ALA ASP VAL THR LYS ILE LYS PRO HIS ASN SER
SEQRES 5 B 318 HIS GLU GLY LYS THR PHE TYR VAL LEU PRO ASN ASP ASP
SEQRES 6 B 318 THR LEU ARG VAL GLU ALA PHE GLU TYR TYR HIS THR THR
SEQRES 7 B 318 ASP PRO SER PHE LEU GLY ARG TYR MET SER ALA LEU ASN
SEQRES 8 B 318 HIS THR LYS LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU
SEQRES 9 B 318 THR SER ILE LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA
SEQRES 10 B 318 THR ALA LEU LEU THR LEU GLN GLN ILE GLU LEU LYS PHE
SEQRES 11 B 318 ASN PRO PRO ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG
SEQRES 12 B 318 ALA GLY GLU ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA
SEQRES 13 B 318 TYR CYS ASN LYS THR VAL GLY GLU LEU GLY ASP VAL ARG
SEQRES 14 B 318 GLU THR MET SER TYR LEU PHE GLN HIS ALA ASN LEU ASP
SEQRES 15 B 318 SER CYS LYS ARG VAL LEU ASN VAL VAL CYS LYS THR CYS
SEQRES 16 B 318 GLY GLN GLN GLN THR THR LEU LYS GLY VAL GLU ALA VAL
SEQRES 17 B 318 MET TYR MET GLY THR LEU SER TYR GLU GLN PHE LYS LYS
SEQRES 18 B 318 GLY VAL GLN ILE PRO CYS THR CYS GLY LYS GLN ALA THR
SEQRES 19 B 318 LYS TYR LEU VAL GLN GLN GLU SER PRO PHE VAL MET MET
SEQRES 20 B 318 SER ALA PRO PRO ALA GLN TYR GLU LEU LYS HIS GLY THR
SEQRES 21 B 318 PHE THR CYS ALA SER GLU TYR THR GLY ASN TYR GLN CYS
SEQRES 22 B 318 GLY HIS TYR LYS HIS ILE THR SER LYS GLU THR LEU TYR
SEQRES 23 B 318 CYS ILE ASP GLY ALA LEU LEU THR LYS SER SER GLU TYR
SEQRES 24 B 318 LYS GLY PRO ILE THR ASP VAL PHE TYR LYS GLU ASN SER
SEQRES 25 B 318 TYR THR THR THR ILE LYS
HET PRL A 401 16
HET PRL A 402 16
HET PRL A 403 16
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET ZN A 408 1
HET SO4 A 409 5
HET SO4 A 410 5
HET PRL B 401 16
HET PRL B 402 16
HET PRL B 403 16
HET EDO B 404 4
HET EDO B 405 4
HET EDO B 406 4
HET ZN B 407 1
HET SO4 B 408 5
HET SO4 B 409 5
HET SO4 B 410 5
HETNAM PRL PROFLAVIN
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 PRL 6(C13 H11 N3)
FORMUL 6 EDO 7(C2 H6 O2)
FORMUL 10 ZN 2(ZN 2+)
FORMUL 11 SO4 5(O4 S 2-)
FORMUL 23 HOH *193(H2 O)
HELIX 1 AA1 ASP A 62 HIS A 74 1 13
HELIX 2 AA2 PRO A 78 LYS A 92 1 15
HELIX 3 AA3 ASN A 111 GLN A 122 1 12
HELIX 4 AA4 PRO A 130 GLY A 143 1 14
HELIX 5 AA5 ALA A 145 ASN A 157 1 13
HELIX 6 AA6 ASP A 165 GLN A 175 1 11
HELIX 7 AA7 VAL A 203 ALA A 205 5 3
HELIX 8 AA8 SER A 213 GLY A 220 1 8
HELIX 9 AA9 THR B 27 GLY B 33 1 7
HELIX 10 AB1 HIS B 48 GLU B 52 5 5
HELIX 11 AB2 ASP B 62 HIS B 74 1 13
HELIX 12 AB3 SER B 79 LYS B 92 1 14
HELIX 13 AB4 ASN B 111 GLN B 122 1 12
HELIX 14 AB5 PRO B 130 ALA B 142 1 13
HELIX 15 AB6 ALA B 145 ASN B 157 1 13
HELIX 16 AB7 ASP B 165 GLN B 175 1 11
HELIX 17 AB8 VAL B 203 ALA B 205 5 3
HELIX 18 AB9 SER B 213 GLY B 220 1 8
SHEET 1 AA1 4 THR A 10 THR A 11 0
SHEET 2 AA1 4 PHE A 56 VAL A 58 1 O PHE A 56 N THR A 11
SHEET 3 AA1 4 THR A 35 LEU A 37 -1 N TYR A 36 O TYR A 57
SHEET 4 AA1 4 ALA A 40 ASP A 41 -1 O ALA A 40 N LEU A 37
SHEET 1 AA2 2 GLN A 98 VAL A 99 0
SHEET 2 AA2 2 LEU A 102 THR A 103 -1 O LEU A 102 N VAL A 99
SHEET 1 AA3 4 GLY A 194 LYS A 201 0
SHEET 2 AA3 4 LYS A 183 CYS A 190 -1 N ARG A 184 O LEU A 200
SHEET 3 AA3 4 GLN A 230 GLU A 239 -1 O GLU A 239 N LYS A 183
SHEET 4 AA3 4 VAL A 221 PRO A 224 -1 N VAL A 221 O LYS A 233
SHEET 1 AA4 4 GLY A 194 LYS A 201 0
SHEET 2 AA4 4 LYS A 183 CYS A 190 -1 N ARG A 184 O LEU A 200
SHEET 3 AA4 4 GLN A 230 GLU A 239 -1 O GLU A 239 N LYS A 183
SHEET 4 AA4 4 SER A 310 THR A 312 -1 O TYR A 311 N GLN A 238
SHEET 1 AA5 7 MET A 207 MET A 209 0
SHEET 2 AA5 7 PHE A 242 GLU A 253 1 O MET A 244 N TYR A 208
SHEET 3 AA5 7 LYS A 298 LYS A 307 -1 O VAL A 304 N MET A 245
SHEET 4 AA5 7 CYS A 261 GLY A 267 -1 N CYS A 261 O PHE A 305
SHEET 5 AA5 7 GLY A 272 SER A 279 -1 O ILE A 277 N ALA A 262
SHEET 6 AA5 7 LEU A 283 ASP A 287 -1 O ILE A 286 N HIS A 276
SHEET 7 AA5 7 LEU A 290 SER A 294 -1 O THR A 292 N CYS A 285
SHEET 1 AA6 5 HIS B 18 ASP B 23 0
SHEET 2 AA6 5 THR B 5 THR B 11 -1 N THR B 10 O HIS B 18
SHEET 3 AA6 5 THR B 55 VAL B 58 1 O PHE B 56 N PHE B 9
SHEET 4 AA6 5 THR B 35 LEU B 37 -1 N TYR B 36 O TYR B 57
SHEET 5 AA6 5 ALA B 40 ASP B 41 -1 O ALA B 40 N LEU B 37
SHEET 1 AA7 2 GLN B 98 VAL B 99 0
SHEET 2 AA7 2 LEU B 102 THR B 103 -1 O LEU B 102 N VAL B 99
SHEET 1 AA8 4 GLN B 195 LYS B 201 0
SHEET 2 AA8 4 LYS B 183 VAL B 189 -1 N ARG B 184 O LEU B 200
SHEET 3 AA8 4 GLN B 230 GLU B 239 -1 O GLN B 237 N VAL B 185
SHEET 4 AA8 4 VAL B 221 PRO B 224 -1 N VAL B 221 O LYS B 233
SHEET 1 AA9 4 GLN B 195 LYS B 201 0
SHEET 2 AA9 4 LYS B 183 VAL B 189 -1 N ARG B 184 O LEU B 200
SHEET 3 AA9 4 GLN B 230 GLU B 239 -1 O GLN B 237 N VAL B 185
SHEET 4 AA9 4 SER B 310 THR B 312 -1 O TYR B 311 N GLN B 238
SHEET 1 AB1 7 MET B 207 MET B 209 0
SHEET 2 AB1 7 PHE B 242 GLU B 253 1 O MET B 244 N TYR B 208
SHEET 3 AB1 7 LYS B 298 LYS B 307 -1 O VAL B 304 N MET B 245
SHEET 4 AB1 7 CYS B 261 GLY B 267 -1 N SER B 263 O ASP B 303
SHEET 5 AB1 7 GLY B 272 SER B 279 -1 O HIS B 273 N THR B 266
SHEET 6 AB1 7 LEU B 283 ASP B 287 -1 O ILE B 286 N HIS B 276
SHEET 7 AB1 7 LEU B 290 SER B 294 -1 O THR B 292 N CYS B 285
SSBOND 1 CYS A 271 CYS A 271 1555 10665 2.01
SSBOND 2 CYS B 271 CYS B 271 1555 10665 2.11
LINK SG CYS A 190 ZN ZN A 408 1555 1555 2.43
LINK SG CYS A 193 ZN ZN A 408 1555 1555 2.42
LINK SG CYS A 225 ZN ZN A 408 1555 1555 2.38
LINK SG CYS A 227 ZN ZN A 408 1555 1555 2.41
LINK SG CYS B 190 ZN ZN B 407 1555 1555 2.36
LINK SG CYS B 193 ZN ZN B 407 1555 1555 2.39
LINK SG CYS B 225 ZN ZN B 407 1555 1555 2.39
LINK SG CYS B 227 ZN ZN B 407 1555 1555 2.38
CRYST1 116.370 116.370 253.566 90.00 90.00 120.00 P 65 2 2 24
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 0.008593 0.004961 0.000000 0.00000
SCALE2 0.000000 0.009923 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003944 0.00000
ATOM 1 N PHE A 9 22.902 5.300 10.921 1.00 97.23 N
ANISOU 1 N PHE A 9 15248 6492 15200 -305 158 1431 N
ATOM 2 CA PHE A 9 23.620 5.315 9.615 1.00 97.58 C
ANISOU 2 CA PHE A 9 15440 6393 15243 -167 227 1031 C
ATOM 3 C PHE A 9 24.885 6.184 9.700 1.00 95.29 C
ANISOU 3 C PHE A 9 14984 6383 14837 212 285 1009 C
ATOM 4 O PHE A 9 25.077 6.959 10.641 1.00 92.82 O
ANISOU 4 O PHE A 9 14436 6435 14397 321 246 1252 O
ATOM 5 CB PHE A 9 22.638 5.642 8.483 1.00 96.07 C
ANISOU 5 CB PHE A 9 15308 6285 14906 -498 161 715 C
ATOM 6 N THR A 10 25.778 5.990 8.716 1.00 96.45 N
ANISOU 6 N THR A 10 15268 6337 15039 413 386 716 N
ATOM 7 CA THR A 10 27.016 6.742 8.495 1.00 94.41 C
ANISOU 7 CA THR A 10 14877 6301 14691 756 458 626 C
ATOM 8 C THR A 10 26.831 7.746 7.335 1.00 91.91 C
ANISOU 8 C THR A 10 14523 6279 14119 658 451 277 C
ATOM 9 O THR A 10 26.211 7.391 6.322 1.00 94.22 O
ANISOU 9 O THR A 10 15012 6391 14394 431 450 0 O
ATOM 10 CB THR A 10 28.187 5.745 8.332 1.00 97.17 C
ANISOU 10 CB THR A 10 15389 6216 15315 1077 600 600 C
ATOM 11 OG1 THR A 10 29.451 6.392 8.460 1.00 95.52 O
ANISOU 11 OG1 THR A 10 14996 6232 15066 1435 661 631 O
ATOM 12 CG2 THR A 10 28.210 4.964 7.034 1.00 99.56 C
ANISOU 12 CG2 THR A 10 15996 6105 15724 1028 708 220 C
ATOM 13 N THR A 11 27.359 8.987 7.454 1.00 86.88 N
ANISOU 13 N THR A 11 13643 6085 13279 812 438 289 N
ATOM 14 CA THR A 11 27.153 9.985 6.410 1.00 83.32 C
ANISOU 14 CA THR A 11 13146 5927 12585 714 423 -2 C
ATOM 15 C THR A 11 28.359 10.917 6.261 1.00 80.97 C
ANISOU 15 C THR A 11 12675 5907 12179 1020 489 -56 C
ATOM 16 O THR A 11 29.190 10.970 7.163 1.00 80.63 O
ANISOU 16 O THR A 11 12494 5921 12217 1269 507 179 O
ATOM 17 CB THR A 11 25.878 10.787 6.676 1.00 80.54 C
ANISOU 17 CB THR A 11 12647 5915 12040 405 283 76 C
ATOM 18 OG1 THR A 11 25.642 11.540 5.486 1.00 78.57 O
ANISOU 18 OG1 THR A 11 12404 5860 11590 294 268 -225 O
ATOM 19 CG2 THR A 11 26.006 11.708 7.869 1.00 77.99 C
ANISOU 19 CG2 THR A 11 12048 5975 11610 507 230 368 C
ATOM 20 N VAL A 12 28.447 11.633 5.120 1.00 79.20 N
ANISOU 20 N VAL A 12 12458 5859 11773 988 517 -354 N
ATOM 21 CA VAL A 12 29.400 12.726 4.945 1.00 76.40 C
ANISOU 21 CA VAL A 12 11909 5838 11278 1212 560 -400 C
ATOM 22 C VAL A 12 28.690 14.057 4.675 1.00 72.74 C
ANISOU 22 C VAL A 12 11287 5810 10539 1020 456 -459 C
ATOM 23 O VAL A 12 29.312 15.110 4.767 1.00 69.66 O
ANISOU 23 O VAL A 12 10703 5742 10021 1164 459 -436 O
ATOM 24 CB VAL A 12 30.485 12.449 3.882 1.00 77.87 C
ANISOU 24 CB VAL A 12 12216 5854 11514 1438 727 -668 C
ATOM 25 CG1 VAL A 12 31.553 11.492 4.382 1.00 80.97 C
ANISOU 25 CG1 VAL A 12 12650 5927 12184 1749 844 -537 C
ATOM 26 CG2 VAL A 12 29.954 12.061 2.504 1.00 79.42 C
ANISOU 26 CG2 VAL A 12 12674 5865 11637 1239 772 -1026 C
ATOM 27 N ASP A 13 27.394 14.007 4.349 1.00 73.31 N
ANISOU 27 N ASP A 13 11434 5885 10533 693 360 -524 N
ATOM 28 CA ASP A 13 26.654 15.197 3.948 1.00 70.69 C
ANISOU 28 CA ASP A 13 10965 5929 9961 507 265 -593 C
ATOM 29 C ASP A 13 25.329 15.290 4.707 1.00 70.18 C
ANISOU 29 C ASP A 13 10811 5971 9880 243 137 -390 C
ATOM 30 O ASP A 13 24.685 16.337 4.722 1.00 68.45 O
ANISOU 30 O ASP A 13 10425 6089 9494 121 57 -362 O
ATOM 31 CB ASP A 13 26.402 15.230 2.436 1.00 71.43 C
ANISOU 31 CB ASP A 13 11222 5983 9931 361 278 -931 C
ATOM 32 CG ASP A 13 25.821 13.946 1.861 1.00 75.41 C
ANISOU 32 CG ASP A 13 12014 6084 10553 164 279 -1081 C
ATOM 33 OD1 ASP A 13 25.261 13.138 2.651 1.00 76.97 O
ANISOU 33 OD1 ASP A 13 12256 6070 10917 60 236 -897 O
ATOM 34 OD2 ASP A 13 25.986 13.722 0.627 1.00 77.24 O
ANISOU 34 OD2 ASP A 13 12439 6199 10709 119 333 -1385 O
ATOM 35 N ASN A 14 24.914 14.174 5.313 1.00 71.95 N
ANISOU 35 N ASN A 14 11149 5896 10292 157 128 -246 N
ATOM 36 CA ASN A 14 23.679 14.121 6.072 1.00 71.11 C
ANISOU 36 CA ASN A 14 10962 5861 10195 -91 29 -34 C
ATOM 37 C ASN A 14 22.457 14.165 5.154 1.00 71.76 C
ANISOU 37 C ASN A 14 11101 5967 10194 -432 -64 -200 C
ATOM 38 O ASN A 14 21.339 14.350 5.628 1.00 71.41 O
ANISOU 38 O ASN A 14 10941 6059 10131 -657 -150 -44 O
ATOM 39 CB ASN A 14 23.657 15.151 7.198 1.00 67.24 C
ANISOU 39 CB ASN A 14 10206 5745 9596 -5 0 214 C
ATOM 40 CG ASN A 14 22.663 14.793 8.275 1.00 67.54 C
ANISOU 40 CG ASN A 14 10183 5779 9698 -183 -49 493 C
ATOM 41 OD1 ASN A 14 22.610 13.662 8.738 1.00 69.59 O
ANISOU 41 OD1 ASN A 14 10572 5727 10141 -211 -31 622 O
ATOM 42 ND2 ASN A 14 21.862 15.759 8.674 1.00 65.62 N
ANISOU 42 ND2 ASN A 14 9742 5879 9310 -303 -102 592 N
ATOM 43 N ILE A 15 22.660 13.999 3.840 1.00 73.07 N
ANISOU 43 N ILE A 15 11439 6015 10306 -475 -47 -511 N
ATOM 44 CA ILE A 15 21.514 13.734 2.980 1.00 75.42 C
ANISOU 44 CA ILE A 15 11842 6257 10555 -826 -153 -662 C
ATOM 45 C ILE A 15 21.512 12.246 2.647 1.00 79.76 C
ANISOU 45 C ILE A 15 12696 6312 11295 -921 -119 -775 C
ATOM 46 O ILE A 15 20.467 11.600 2.642 1.00 81.42 O
ANISOU 46 O ILE A 15 12982 6369 11583 -1224 -211 -738 O
ATOM 47 CB ILE A 15 21.463 14.636 1.722 1.00 74.50 C
ANISOU 47 CB ILE A 15 11711 6387 10206 -891 -195 -920 C
ATOM 48 CG1 ILE A 15 21.615 16.127 2.053 1.00 71.03 C
ANISOU 48 CG1 ILE A 15 10984 6400 9600 -759 -211 -811 C
ATOM 49 CG2 ILE A 15 20.204 14.375 0.900 1.00 75.70 C
ANISOU 49 CG2 ILE A 15 11950 6510 10300 -1279 -338 -1041 C
ATOM 50 CD1 ILE A 15 20.469 16.721 2.868 1.00 70.12 C
ANISOU 50 CD1 ILE A 15 10631 6543 9465 -931 -314 -562 C
ATOM 51 N ASN A 16 22.715 11.709 2.416 1.00 81.63 N
ANISOU 51 N ASN A 16 13096 6295 11623 -650 22 -899 N
ATOM 52 CA ASN A 16 22.944 10.333 2.006 1.00 86.12 C
ANISOU 52 CA ASN A 16 13980 6360 12379 -672 94 -1048 C
ATOM 53 C ASN A 16 23.388 9.506 3.200 1.00 88.07 C
ANISOU 53 C ASN A 16 14236 6340 12885 -493 162 -773 C
ATOM 54 O ASN A 16 24.512 9.702 3.662 1.00 87.91 O
ANISOU 54 O ASN A 16 14131 6357 12913 -150 267 -684 O
ATOM 55 CB ASN A 16 24.221 10.239 1.177 1.00 86.60 C
ANISOU 55 CB ASN A 16 14192 6292 12421 -388 255 -1313 C
ATOM 56 CG ASN A 16 23.995 10.461 -0.292 1.00 87.05 C
ANISOU 56 CG ASN A 16 14410 6392 12272 -557 239 -1677 C
ATOM 57 OD1 ASN A 16 23.654 9.519 -0.997 1.00 90.29 O
ANISOU 57 OD1 ASN A 16 15110 6460 12735 -742 242 -1891 O
ATOM 58 ND2 ASN A 16 24.216 11.681 -0.744 1.00 83.78 N
ANISOU 58 ND2 ASN A 16 13824 6383 11622 -494 224 -1744 N
ATOM 59 N LEU A 17 22.560 8.547 3.626 1.00 90.62 N
ANISOU 59 N LEU A 17 14670 6381 13378 -727 103 -646 N
ATOM 60 CA LEU A 17 22.902 7.767 4.805 1.00 92.39 C
ANISOU 60 CA LEU A 17 14897 6361 13843 -578 155 -347 C
ATOM 61 C LEU A 17 23.248 6.339 4.386 1.00 97.55 C
ANISOU 61 C LEU A 17 15890 6432 14743 -557 247 -489 C
ATOM 62 O LEU A 17 22.521 5.739 3.604 1.00100.04 O
ANISOU 62 O LEU A 17 16423 6511 15076 -850 199 -698 O
ATOM 63 CB LEU A 17 21.736 7.780 5.801 1.00 91.33 C
ANISOU 63 CB LEU A 17 14610 6355 13735 -836 37 -30 C
ATOM 64 CG LEU A 17 21.006 9.102 6.053 1.00 87.05 C
ANISOU 64 CG LEU A 17 13769 6349 12958 -959 -61 67 C
ATOM 65 CD1 LEU A 17 21.953 10.294 6.195 1.00 83.08 C
ANISOU 65 CD1 LEU A 17 13066 6216 12282 -646 -10 64 C
ATOM 66 CD2 LEU A 17 19.928 9.347 5.003 1.00 87.06 C
ANISOU 66 CD2 LEU A 17 13803 6445 12829 -1311 -176 -154 C
ATOM 67 N HIS A 18 24.364 5.813 4.904 1.00 99.59 N
ANISOU 67 N HIS A 18 16190 6458 15192 -211 376 -374 N
ATOM 68 CA HIS A 18 24.803 4.451 4.652 1.00104.70 C
ANISOU 68 CA HIS A 18 17143 6524 16111 -130 487 -469 C
ATOM 69 C HIS A 18 24.780 3.681 5.975 1.00107.26 C
ANISOU 69 C HIS A 18 17438 6626 16689 -70 478 -65 C
ATOM 70 O HIS A 18 25.679 3.862 6.796 1.00107.41 O
ANISOU 70 O HIS A 18 17300 6737 16773 253 532 173 O
ATOM 71 CB HIS A 18 26.227 4.452 4.062 1.00104.82 C
ANISOU 71 CB HIS A 18 17228 6435 16162 266 668 -673 C
ATOM 72 CG HIS A 18 26.508 5.439 2.974 1.00102.51 C
ANISOU 72 CG HIS A 18 16889 6465 15594 294 696 -992 C
ATOM 73 ND1 HIS A 18 26.980 5.033 1.735 1.00105.01 N
ANISOU 73 ND1 HIS A 18 17469 6531 15898 351 829 -1381 N
ATOM 74 CD2 HIS A 18 26.509 6.794 2.937 1.00 98.21 C
ANISOU 74 CD2 HIS A 18 16078 6452 14783 309 631 -978 C
ATOM 75 CE1 HIS A 18 27.198 6.089 0.971 1.00101.88 C
ANISOU 75 CE1 HIS A 18 16966 6514 15228 375 835 -1581 C
ATOM 76 NE2 HIS A 18 26.908 7.184 1.684 1.00 97.74 N
ANISOU 76 NE2 HIS A 18 16116 6465 14554 348 709 -1336 N
ATOM 77 N THR A 19 23.759 2.844 6.219 1.00109.61 N
ANISOU 77 N THR A 19 17873 6649 17123 -391 402 33 N
ATOM 78 CA THR A 19 23.766 2.075 7.458 1.00110.40 C
ANISOU 78 CA THR A 19 17960 6523 17464 -334 402 431 C
ATOM 79 C THR A 19 24.736 0.900 7.326 1.00113.79 C
ANISOU 79 C THR A 19 18645 6388 18200 -64 551 386 C
ATOM 80 O THR A 19 24.361 -0.252 7.525 1.00117.19 O
ANISOU 80 O THR A 19 19293 6350 18882 -199 558 472 O
ATOM 81 CB THR A 19 22.360 1.821 8.027 1.00111.15 C
ANISOU 81 CB THR A 19 18018 6638 17575 -746 267 649 C
ATOM 82 OG1 THR A 19 21.578 1.236 6.986 1.00113.79 O
ANISOU 82 OG1 THR A 19 18603 6690 17942 -1085 226 347 O
ATOM 83 CG2 THR A 19 21.697 3.066 8.574 1.00106.38 C
ANISOU 83 CG2 THR A 19 17080 6633 16704 -867 161 819 C
ATOM 84 N GLN A 20 25.986 1.224 6.955 1.00112.64 N
ANISOU 84 N GLN A 20 18468 6290 18040 320 678 246 N
ATOM 85 CA GLN A 20 27.156 0.402 7.236 1.00114.99 C
ANISOU 85 CA GLN A 20 18863 6200 18625 705 825 344 C
ATOM 86 C GLN A 20 27.658 0.784 8.632 1.00112.93 C
ANISOU 86 C GLN A 20 18309 6210 18386 936 776 806 C
ATOM 87 O GLN A 20 28.774 1.280 8.790 1.00111.29 O
ANISOU 87 O GLN A 20 17935 6192 18157 1294 841 855 O
ATOM 88 CB GLN A 20 28.199 0.552 6.123 1.00114.82 C
ANISOU 88 CB GLN A 20 18937 6108 18578 985 992 -31 C
ATOM 89 N VAL A 21 26.757 0.596 9.622 1.00112.48 N
ANISOU 89 N VAL A 21 18187 6201 18347 696 654 1141 N
ATOM 90 CA VAL A 21 26.945 0.769 11.066 1.00110.20 C
ANISOU 90 CA VAL A 21 17673 6124 18072 818 587 1618 C
ATOM 91 C VAL A 21 27.129 -0.630 11.712 1.00114.18 C
ANISOU 91 C VAL A 21 18361 6080 18940 897 629 1899 C
ATOM 92 O VAL A 21 26.992 -1.658 11.044 1.00117.74 O
ANISOU 92 O VAL A 21 19109 6004 19622 823 704 1710 O
ATOM 93 CB VAL A 21 25.854 1.691 11.715 1.00106.29 C
ANISOU 93 CB VAL A 21 16954 6132 17299 515 442 1790 C
ATOM 94 CG1 VAL A 21 26.411 2.868 12.513 1.00101.63 C
ANISOU 94 CG1 VAL A 21 16044 6089 16479 722 397 1990 C
ATOM 95 CG2 VAL A 21 24.783 2.209 10.752 1.00104.17 C
ANISOU 95 CG2 VAL A 21 16718 6031 16831 157 385 1464 C
ATOM 96 N VAL A 22 27.542 -0.698 12.994 1.00113.28 N
ANISOU 96 N VAL A 22 18086 6065 18889 1074 587 2348 N
ATOM 97 CA VAL A 22 27.501 -1.926 13.780 1.00116.63 C
ANISOU 97 CA VAL A 22 18652 6036 19623 1089 593 2695 C
ATOM 98 C VAL A 22 26.542 -1.695 14.963 1.00115.45 C
ANISOU 98 C VAL A 22 18356 6175 19334 819 463 3085 C
ATOM 99 O VAL A 22 26.992 -1.546 16.099 1.00115.44 O
ANISOU 99 O VAL A 22 18185 6368 19307 993 416 3479 O
ATOM 100 CB VAL A 22 28.907 -2.384 14.239 1.00118.28 C
ANISOU 100 CB VAL A 22 18826 6046 20069 1559 668 2914 C
ATOM 101 CG1 VAL A 22 28.831 -3.645 15.073 1.00122.43 C
ANISOU 101 CG1 VAL A 22 19496 6100 20918 1571 665 3303 C
ATOM 102 CG2 VAL A 22 29.918 -2.578 13.116 1.00119.01 C
ANISOU 102 CG2 VAL A 22 19035 5880 20304 1861 826 2545 C
ATOM 103 N ASP A 23 25.222 -1.712 14.671 1.00114.77 N
ANISOU 103 N ASP A 23 18341 6100 19164 391 409 2976 N
ATOM 104 CA ASP A 23 24.126 -1.030 15.363 1.00111.83 C
ANISOU 104 CA ASP A 23 17779 6166 18543 81 305 3169 C
ATOM 105 C ASP A 23 23.674 -1.703 16.662 1.00114.14 C
ANISOU 105 C ASP A 23 18063 6353 18951 -29 265 3668 C
ATOM 106 O ASP A 23 22.953 -1.070 17.432 1.00111.84 O
ANISOU 106 O ASP A 23 17580 6476 18436 -212 201 3884 O
ATOM 107 CB ASP A 23 22.867 -0.961 14.476 1.00111.53 C
ANISOU 107 CB ASP A 23 17828 6115 18430 -344 267 2871 C
ATOM 108 CG ASP A 23 22.591 0.332 13.703 1.00107.42 C
ANISOU 108 CG ASP A 23 17147 6076 17590 -423 231 2538 C
ATOM 109 OD1 ASP A 23 22.116 1.327 14.319 1.00104.27 O
ANISOU 109 OD1 ASP A 23 16491 6189 16934 -507 170 2688 O
ATOM 110 OD2 ASP A 23 22.793 0.329 12.469 1.00107.47 O
ANISOU 110 OD2 ASP A 23 17295 5934 17601 -417 269 2128 O
ATOM 111 N MET A 24 24.044 -2.980 16.877 1.00118.70 N
ANISOU 111 N MET A 24 18854 6373 19873 68 311 3846 N
ATOM 112 CA MET A 24 23.463 -3.822 17.915 1.00121.82 C
ANISOU 112 CA MET A 24 19303 6558 20422 -104 280 4290 C
ATOM 113 C MET A 24 24.541 -4.466 18.794 1.00124.78 C
ANISOU 113 C MET A 24 19694 6712 21004 257 301 4674 C
ATOM 114 O MET A 24 24.217 -5.076 19.812 1.00127.39 O
ANISOU 114 O MET A 24 20041 6927 21433 167 269 5109 O
ATOM 115 CB MET A 24 22.562 -4.903 17.302 1.00125.03 C
ANISOU 115 CB MET A 24 19989 6429 21086 -447 297 4162 C
ATOM 116 N SER A 25 25.823 -4.317 18.416 1.00124.67 N
ANISOU 116 N SER A 25 19661 6653 21055 667 354 4535 N
ATOM 117 CA SER A 25 26.953 -4.943 19.102 1.00127.63 C
ANISOU 117 CA SER A 25 20039 6793 21661 1048 373 4871 C
ATOM 118 C SER A 25 28.249 -4.658 18.328 1.00126.95 C
ANISOU 118 C SER A 25 19919 6677 21637 1458 453 4585 C
ATOM 119 O SER A 25 28.623 -5.443 17.456 1.00130.02 O
ANISOU 119 O SER A 25 20535 6554 22314 1575 567 4337 O
ATOM 120 CB SER A 25 26.723 -6.459 19.255 1.00133.21 C
ANISOU 120 CB SER A 25 21025 6811 22775 976 418 5077 C
ATOM 121 OG SER A 25 27.161 -6.990 20.509 1.00135.84 O
ANISOU 121 OG SER A 25 21305 7070 23236 1146 371 5631 O
ATOM 122 N MET A 26 28.944 -3.546 18.636 1.00123.26 N
ANISOU 122 N MET A 26 19177 6751 20905 1672 404 4613 N
ATOM 123 CA MET A 26 30.243 -3.248 18.033 1.00122.72 C
ANISOU 123 CA MET A 26 19032 6695 20898 2074 477 4406 C
ATOM 124 C MET A 26 31.353 -3.527 19.043 1.00124.97 C
ANISOU 124 C MET A 26 19177 6981 21324 2443 434 4854 C
ATOM 125 O MET A 26 31.738 -4.678 19.266 1.00129.65 O
ANISOU 125 O MET A 26 19918 7065 22277 2606 482 5076 O
ATOM 126 CB MET A 26 30.353 -1.796 17.549 1.00117.49 C
ANISOU 126 CB MET A 26 18156 6616 19867 2069 451 4100 C
ATOM 127 N THR A 27 31.867 -2.448 19.644 1.00121.68 N
ANISOU 127 N THR A 27 18472 7139 20620 2569 336 4987 N
ATOM 128 CA THR A 27 32.756 -2.546 20.793 1.00123.17 C
ANISOU 128 CA THR A 27 18490 7456 20854 2843 241 5466 C
ATOM 129 C THR A 27 34.150 -3.038 20.378 1.00125.58 C
ANISOU 129 C THR A 27 18771 7460 21482 3299 327 5451 C
ATOM 130 O THR A 27 34.784 -3.825 21.073 1.00129.23 O
ANISOU 130 O THR A 27 19226 7672 22202 3533 299 5847 O
ATOM 131 CB THR A 27 31.999 -3.055 22.034 1.00125.16 C
ANISOU 131 CB THR A 27 18785 7692 21078 2623 139 5944 C
ATOM 132 OG1 THR A 27 31.332 -1.900 22.550 1.00120.97 O
ANISOU 132 OG1 THR A 27 18085 7769 20106 2375 42 5951 O
ATOM 133 CG2 THR A 27 32.862 -3.720 23.088 1.00128.63 C
ANISOU 133 CG2 THR A 27 19161 8001 21711 2904 64 6473 C
ATOM 134 N TYR A 28 34.597 -2.596 19.196 1.00123.36 N
ANISOU 134 N TYR A 28 18482 7190 21198 3423 444 4990 N
ATOM 135 CA TYR A 28 35.954 -2.112 18.998 1.00122.42 C
ANISOU 135 CA TYR A 28 18140 7258 21113 3817 469 4956 C