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3245 lines (3245 loc) · 257 KB
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HEADER MEMBRANE PROTEIN 21-SEP-12 3VY8
TITLE CRYSTAL STRUCTURE OF PORB FROM NEISSERIA MENINGITIDIS IN COMPLEX WITH
TITLE 2 CESIUM ION, SPACE GROUP P63
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OUTER MEMBRANE PROTEIN;
COMPND 3 CHAIN: X;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;
SOURCE 3 ORGANISM_TAXID: 487;
SOURCE 4 STRAIN: W135;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS BETA-BARREL, PORIN, CHANNEL, OUTER MEMBRANE PROTEIN, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.KATTNER,J.ZAUCHA,F.JAENECKE,U.ZACHARIAE,M.TANABE
REVDAT 2 09-OCT-13 3VY8 1 JRNL
REVDAT 1 02-JAN-13 3VY8 0
JRNL AUTH C.KATTNER,J.ZAUCHA,F.JAENECKE,U.ZACHARIAE,M.TANABE
JRNL TITL IDENTIFICATION OF A CATION TRANSPORT PATHWAY IN NEISSERIA
JRNL TITL 2 MENINGITIDIS PORB.
JRNL REF PROTEINS V. 81 830 2013
JRNL REFN ISSN 0887-3585
JRNL PMID 23255122
JRNL DOI 10.1002/PROT.24241
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 16.500
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 21933
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1091
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.12
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1117
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.3750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2593
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 93
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.10000
REMARK 3 B22 (A**2) : 0.10000
REMARK 3 B33 (A**2) : -0.16000
REMARK 3 B12 (A**2) : 0.05000
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): 0.226
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.194
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2673 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3609 ; 1.914 ; 1.920
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 344 ; 7.722 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 128 ;38.337 ;24.375
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 433 ;18.300 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;19.440 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 376 ; 0.137 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2081 ; 0.009 ; 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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3VY8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-SEP-12.
REMARK 100 THE RCSB ID CODE IS RCSB095649.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23050
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.670
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.8
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REGID BODY REFINEMENT
REMARK 200 STARTING MODEL: 3A2R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% JEFFAMINE M600, 50MM CSCL, 0.1M
REMARK 280 MES, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 0.00000
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 0.00000
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 53.20750
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 53.20750
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 53.20750
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: X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -295.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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 BIOMT1 2 -0.500000 -0.866025 0.000000 83.20100
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 41.60050
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 72.05418
REMARK 350 BIOMT3 3 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 HOH X 504 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 MET X -13
REMARK 465 ALA X -12
REMARK 465 SER X -11
REMARK 465 MET X -10
REMARK 465 THR X -9
REMARK 465 GLY X -8
REMARK 465 GLY X -7
REMARK 465 GLN X -6
REMARK 465 GLN X -5
REMARK 465 MET X -4
REMARK 465 GLY X -3
REMARK 465 ARG X -2
REMARK 465 ASP X -1
REMARK 465 LEU X 0
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 CH2 TRP X 318 CE LYS X 320 1.92
REMARK 500 CZ2 TRP X 318 CE LYS X 320 2.02
REMARK 500 O HOH X 511 O HOH X 560 2.14
REMARK 500 O ASP X 160 O LYS X 163 2.18
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 GLU X 246 CD GLU X 246 OE2 0.078
REMARK 500 HIS X 255 CG HIS X 255 CD2 0.061
REMARK 500 TYR X 266 CZ TYR X 266 CE2 0.091
REMARK 500 HIS X 339 CG HIS X 339 CD2 0.056
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 LEU X 61 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 LYS X 161 CB - CA - C ANGL. DEV. = -13.1 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 ALA X 65 58.60 -149.28
REMARK 500 ALA X 228 164.17 176.34
REMARK 500 PHE X 268 79.37 -110.27
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 CS X 403 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH X 586 O
REMARK 620 2 HOH X 568 O 157.2
REMARK 620 3 HOH X 565 O 67.1 93.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS X 402 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG X 130 O
REMARK 620 2 GLU X 131 OE2 64.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS X 401 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY X 125 O
REMARK 620 2 GLU X 128 O 79.1
REMARK 620 3 HOH X 554 O 60.0 139.1
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS X 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS X 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS X 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VY9 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN DOES NOT CURRENTLY
REMARK 999 EXIST.
DBREF 3VY8 X -13 341 PDB 3VY8 3VY8 -13 341
SEQRES 1 X 355 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG ASP
SEQRES 2 X 355 LEU GLN VAL THR LEU TYR GLY THR ILE LYS ALA GLY VAL
SEQRES 3 X 355 GLU VAL SER ARG VAL LYS ASP ALA GLY THR TYR LYS ALA
SEQRES 4 X 355 GLN GLY GLY LYS SER LYS THR ALA THR GLN ILE ALA ASP
SEQRES 5 X 355 PHE GLY SER LYS ILE GLY PHE LYS GLY GLN GLU ASP LEU
SEQRES 6 X 355 GLY ASN GLY MET LYS ALA ILE TRP GLN LEU GLU GLN LYS
SEQRES 7 X 355 ALA SER ILE ALA GLY THR ASN SER GLY TRP GLY ASN ARG
SEQRES 8 X 355 GLN SER PHE ILE GLY LEU LYS GLY GLY PHE GLY THR VAL
SEQRES 9 X 355 ARG ALA GLY ASN LEU ASN THR VAL LEU LYS ASP SER GLY
SEQRES 10 X 355 ASP ASN VAL ASN ALA TRP GLU SER GLY SER ASN THR GLU
SEQRES 11 X 355 ASP VAL LEU GLY LEU GLY THR ILE GLY ARG VAL GLU SER
SEQRES 12 X 355 ARG GLU ILE SER VAL ARG TYR ASP SER PRO VAL PHE ALA
SEQRES 13 X 355 GLY PHE SER GLY SER VAL GLN TYR VAL PRO ARG ASP ASN
SEQRES 14 X 355 ALA ASN ASP VAL ASP LYS TYR LYS HIS THR LYS SER SER
SEQRES 15 X 355 ARG GLU SER TYR HIS ALA GLY LEU LYS TYR GLU ASN ALA
SEQRES 16 X 355 GLY PHE PHE GLY GLN TYR ALA GLY SER PHE ALA LYS TYR
SEQRES 17 X 355 ALA ASP LEU ASN THR ASP ALA GLU ARG VAL ALA VAL ASN
SEQRES 18 X 355 THR ALA ASN ALA HIS PRO VAL LYS ASP TYR GLN VAL HIS
SEQRES 19 X 355 ARG VAL VAL ALA GLY TYR ASP ALA ASN ASP LEU TYR VAL
SEQRES 20 X 355 SER VAL ALA GLY GLN TYR GLU ALA ALA LYS ASN ASN GLU
SEQRES 21 X 355 VAL GLY SER ILE LYS GLY LYS LYS HIS GLU GLN THR GLN
SEQRES 22 X 355 VAL ALA ALA THR ALA ALA TYR ARG PHE GLY ASN VAL THR
SEQRES 23 X 355 PRO ARG VAL SER TYR ALA HIS GLY PHE LYS ALA LYS VAL
SEQRES 24 X 355 ASN GLY VAL LYS ASP ALA ASN TYR GLN TYR ASP GLN VAL
SEQRES 25 X 355 ILE VAL GLY ALA ASP TYR ASP PHE SER LYS ARG THR SER
SEQRES 26 X 355 ALA LEU VAL SER ALA GLY TRP LEU LYS GLN GLY LYS GLY
SEQRES 27 X 355 ALA GLY LYS VAL GLU GLN THR ALA SER MET VAL GLY LEU
SEQRES 28 X 355 ARG HIS LYS PHE
HET CS X 401 1
HET CS X 402 1
HET CS X 403 1
HETNAM CS CESIUM ION
FORMUL 2 CS 3(CS 1+)
FORMUL 5 HOH *93(H2 O)
HELIX 1 1 THR X 97 GLY X 103 1 7
HELIX 2 2 ASP X 104 VAL X 106 5 3
HELIX 3 3 GLY X 112 GLU X 116 5 5
HELIX 4 4 THR X 123 GLU X 128 5 6
HELIX 5 5 PRO X 152 ASN X 157 1 6
HELIX 6 6 ALA X 291 TYR X 293 5 3
SHEET 1 A18 ALA X 33 ASP X 38 0
SHEET 2 A18 VAL X 2 ASP X 19 -1 N SER X 15 O ALA X 33
SHEET 3 A18 VAL X 328 PHE X 341 -1 O GLU X 329 N LYS X 18
SHEET 4 A18 THR X 310 GLN X 321 -1 N GLY X 317 O ALA X 332
SHEET 5 A18 TYR X 295 ASP X 305 -1 N TYR X 304 O ALA X 312
SHEET 6 A18 VAL X 271 GLY X 280 -1 N ARG X 274 O GLY X 301
SHEET 7 A18 LYS X 254 TYR X 266 -1 N ALA X 262 O TYR X 277
SHEET 8 A18 LEU X 231 ASN X 244 -1 N ALA X 242 O HIS X 255
SHEET 9 A18 HIS X 212 ALA X 228 -1 N VAL X 222 O GLY X 237
SHEET 10 A18 PHE X 183 LEU X 197 -1 N ALA X 192 O TYR X 217
SHEET 11 A18 SER X 171 ASN X 180 -1 N LEU X 176 O TYR X 187
SHEET 12 A18 PHE X 144 VAL X 151 -1 N SER X 145 O LYS X 177
SHEET 13 A18 ARG X 130 ASP X 137 -1 N TYR X 136 O VAL X 148
SHEET 14 A18 GLY X 88 ASN X 96 -1 N THR X 89 O ASP X 137
SHEET 15 A18 ARG X 77 GLY X 85 -1 N LEU X 83 O VAL X 90
SHEET 16 A18 LYS X 56 LYS X 64 -1 N LYS X 56 O LYS X 84
SHEET 17 A18 LYS X 42 ASP X 50 -1 N PHE X 45 O LEU X 61
SHEET 18 A18 VAL X 2 ASP X 19 -1 N THR X 3 O LYS X 46
SHEET 1 B 2 ALA X 283 VAL X 285 0
SHEET 2 B 2 VAL X 288 ASP X 290 -1 O ASP X 290 N ALA X 283
LINK CS CS X 403 O HOH X 586 1555 1555 2.56
LINK CS CS X 403 O HOH X 568 1555 1555 2.65
LINK CS CS X 403 O HOH X 565 1555 1555 2.93
LINK O ARG X 130 CS CS X 402 1555 1555 3.04
LINK O GLY X 125 CS CS X 401 1555 1555 3.16
LINK O GLU X 128 CS CS X 401 1555 1555 3.19
LINK CS CS X 401 O HOH X 554 1555 1555 3.19
LINK OE2 GLU X 131 CS CS X 402 1555 1555 3.42
SITE 1 AC1 2 GLY X 125 GLU X 128
SITE 1 AC2 2 ARG X 130 GLU X 131
SITE 1 AC3 3 HOH X 565 HOH X 568 HOH X 586
CRYST1 83.201 83.201 106.415 90.00 90.00 120.00 P 63 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012019 0.006939 0.000000 0.00000
SCALE2 0.000000 0.013878 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009397 0.00000
ATOM 1 N GLN X 1 44.092 13.218 -4.339 1.00 79.91 N
ATOM 2 CA GLN X 1 42.858 14.021 -4.042 1.00 79.21 C
ATOM 3 C GLN X 1 42.536 14.180 -2.518 1.00 70.43 C
ATOM 4 O GLN X 1 42.530 13.214 -1.766 1.00 68.28 O
ATOM 5 CB GLN X 1 41.673 13.434 -4.817 1.00 82.68 C
ATOM 6 CG GLN X 1 40.331 14.069 -4.505 1.00 83.67 C
ATOM 7 CD GLN X 1 39.247 13.022 -4.314 1.00102.28 C
ATOM 8 OE1 GLN X 1 39.508 11.808 -4.421 1.00102.32 O
ATOM 9 NE2 GLN X 1 38.016 13.479 -4.024 1.00 95.46 N
ATOM 10 N VAL X 2 42.300 15.430 -2.110 1.00 67.73 N
ATOM 11 CA VAL X 2 42.117 15.864 -0.731 1.00 59.75 C
ATOM 12 C VAL X 2 40.924 16.825 -0.694 1.00 61.28 C
ATOM 13 O VAL X 2 40.942 17.835 -1.409 1.00 52.03 O
ATOM 14 CB VAL X 2 43.349 16.666 -0.243 1.00 64.24 C
ATOM 15 CG1 VAL X 2 43.031 17.371 1.077 1.00 63.43 C
ATOM 16 CG2 VAL X 2 44.579 15.769 -0.095 1.00 57.36 C
ATOM 17 N THR X 3 39.881 16.513 0.089 1.00 48.27 N
ATOM 18 CA THR X 3 38.727 17.375 0.060 1.00 44.70 C
ATOM 19 C THR X 3 38.390 18.011 1.414 1.00 46.73 C
ATOM 20 O THR X 3 38.533 17.385 2.491 1.00 40.51 O
ATOM 21 CB THR X 3 37.474 16.721 -0.645 1.00 48.93 C
ATOM 22 OG1 THR X 3 36.460 16.378 0.292 1.00 47.66 O
ATOM 23 CG2 THR X 3 37.815 15.493 -1.455 1.00 51.02 C
ATOM 24 N LEU X 4 37.946 19.269 1.334 1.00 38.92 N
ATOM 25 CA LEU X 4 37.375 19.984 2.439 1.00 39.14 C
ATOM 26 C LEU X 4 35.847 19.922 2.390 1.00 40.14 C
ATOM 27 O LEU X 4 35.258 20.077 1.344 1.00 40.62 O
ATOM 28 CB LEU X 4 37.843 21.427 2.408 1.00 43.33 C
ATOM 29 CG LEU X 4 37.001 22.422 3.191 1.00 46.69 C
ATOM 30 CD1 LEU X 4 37.132 22.140 4.671 1.00 48.26 C
ATOM 31 CD2 LEU X 4 37.473 23.836 2.888 1.00 52.80 C
ATOM 32 N TYR X 5 35.215 19.694 3.532 1.00 36.58 N
ATOM 33 CA TYR X 5 33.788 19.479 3.600 1.00 32.60 C
ATOM 34 C TYR X 5 33.286 19.897 4.964 1.00 33.43 C
ATOM 35 O TYR X 5 34.082 20.147 5.880 1.00 36.50 O
ATOM 36 CB TYR X 5 33.397 18.039 3.285 1.00 31.42 C
ATOM 37 CG TYR X 5 33.811 17.130 4.379 1.00 32.02 C
ATOM 38 CD1 TYR X 5 35.158 16.636 4.433 1.00 32.12 C
ATOM 39 CD2 TYR X 5 32.930 16.794 5.400 1.00 32.48 C
ATOM 40 CE1 TYR X 5 35.567 15.759 5.438 1.00 31.76 C
ATOM 41 CE2 TYR X 5 33.319 15.927 6.420 1.00 35.98 C
ATOM 42 CZ TYR X 5 34.667 15.419 6.425 1.00 36.33 C
ATOM 43 OH TYR X 5 35.106 14.612 7.445 1.00 36.73 O
ATOM 44 N GLY X 6 31.971 19.999 5.124 1.00 31.34 N
ATOM 45 CA GLY X 6 31.427 20.325 6.416 1.00 35.15 C
ATOM 46 C GLY X 6 29.939 20.674 6.361 1.00 34.57 C
ATOM 47 O GLY X 6 29.319 20.623 5.323 1.00 32.18 O
ATOM 48 N THR X 7 29.383 21.014 7.506 1.00 31.12 N
ATOM 49 CA THR X 7 28.032 21.486 7.560 1.00 34.22 C
ATOM 50 C THR X 7 28.006 22.642 8.548 1.00 34.74 C
ATOM 51 O THR X 7 28.525 22.496 9.663 1.00 35.74 O
ATOM 52 CB THR X 7 27.083 20.379 8.074 1.00 32.58 C
ATOM 53 OG1 THR X 7 27.149 19.325 7.173 1.00 30.63 O
ATOM 54 CG2 THR X 7 25.610 20.841 7.977 1.00 29.69 C
ATOM 55 N ILE X 8 27.452 23.783 8.129 1.00 33.30 N
ATOM 56 CA ILE X 8 27.226 24.876 9.061 1.00 29.54 C
ATOM 57 C ILE X 8 25.702 24.885 9.359 1.00 33.71 C
ATOM 58 O ILE X 8 24.915 24.955 8.440 1.00 31.29 O
ATOM 59 CB ILE X 8 27.603 26.239 8.440 1.00 31.42 C
ATOM 60 CG1 ILE X 8 29.050 26.289 7.851 1.00 37.08 C
ATOM 61 CG2 ILE X 8 27.453 27.337 9.465 1.00 27.95 C
ATOM 62 CD1 ILE X 8 30.112 26.009 8.895 1.00 34.74 C
ATOM 63 N LYS X 9 25.277 24.842 10.615 1.00 33.94 N
ATOM 64 CA LYS X 9 23.845 24.742 10.884 1.00 31.21 C
ATOM 65 C LYS X 9 23.532 25.368 12.213 1.00 32.36 C
ATOM 66 O LYS X 9 24.286 25.229 13.180 1.00 36.12 O
ATOM 67 CB LYS X 9 23.356 23.273 10.793 1.00 33.63 C
ATOM 68 CG LYS X 9 24.122 22.253 11.649 1.00 30.06 C
ATOM 69 CD LYS X 9 23.453 20.870 11.580 1.00 33.63 C
ATOM 70 CE LYS X 9 24.453 19.784 12.037 1.00 34.32 C
ATOM 71 NZ LYS X 9 23.989 18.427 11.631 1.00 37.64 N
ATOM 72 N ALA X 10 22.420 26.103 12.271 1.00 28.70 N
ATOM 73 CA ALA X 10 22.096 26.869 13.443 1.00 29.79 C
ATOM 74 C ALA X 10 20.657 27.338 13.360 1.00 32.24 C
ATOM 75 O ALA X 10 20.067 27.336 12.305 1.00 33.15 O
ATOM 76 CB ALA X 10 23.028 28.096 13.530 1.00 30.06 C
ATOM 77 N GLY X 11 20.124 27.815 14.478 1.00 37.74 N
ATOM 78 CA GLY X 11 18.782 28.370 14.508 1.00 38.68 C
ATOM 79 C GLY X 11 18.486 29.060 15.816 1.00 42.00 C
ATOM 80 O GLY X 11 19.398 29.363 16.656 1.00 35.32 O
ATOM 81 N VAL X 12 17.194 29.380 15.964 1.00 37.64 N
ATOM 82 CA VAL X 12 16.707 29.815 17.234 1.00 35.10 C
ATOM 83 C VAL X 12 15.735 28.847 17.825 1.00 34.96 C
ATOM 84 O VAL X 12 14.822 28.437 17.152 1.00 35.24 O
ATOM 85 CB VAL X 12 16.229 31.289 17.216 1.00 39.42 C
ATOM 86 CG1 VAL X 12 16.729 31.980 15.980 1.00 41.27 C
ATOM 87 CG2 VAL X 12 14.747 31.451 17.398 1.00 48.61 C
ATOM 88 N GLU X 13 15.982 28.474 19.093 1.00 38.42 N
ATOM 89 CA GLU X 13 15.212 27.487 19.808 1.00 42.60 C
ATOM 90 C GLU X 13 14.431 28.195 20.928 1.00 48.77 C
ATOM 91 O GLU X 13 14.968 29.076 21.635 1.00 40.03 O
ATOM 92 CB GLU X 13 16.087 26.408 20.446 1.00 41.87 C
ATOM 93 CG GLU X 13 17.287 25.908 19.679 1.00 44.42 C
ATOM 94 CD GLU X 13 18.172 24.966 20.499 1.00 45.44 C
ATOM 95 OE1 GLU X 13 18.251 23.812 20.062 1.00 47.21 O
ATOM 96 OE2 GLU X 13 18.749 25.323 21.590 1.00 46.13 O
ATOM 97 N VAL X 14 13.169 27.792 21.071 1.00 42.10 N
ATOM 98 CA VAL X 14 12.337 28.253 22.178 1.00 43.20 C
ATOM 99 C VAL X 14 12.010 27.009 23.005 1.00 42.87 C
ATOM 100 O VAL X 14 11.597 25.982 22.456 1.00 41.67 O
ATOM 101 CB VAL X 14 11.113 29.045 21.619 1.00 45.81 C
ATOM 102 CG1 VAL X 14 10.084 29.397 22.662 1.00 40.48 C
ATOM 103 CG2 VAL X 14 11.625 30.266 20.897 1.00 46.22 C
ATOM 104 N SER X 15 12.272 27.075 24.311 1.00 42.53 N
ATOM 105 CA SER X 15 12.088 25.918 25.182 1.00 44.19 C
ATOM 106 C SER X 15 11.597 26.324 26.578 1.00 43.18 C
ATOM 107 O SER X 15 11.958 27.376 27.125 1.00 38.51 O
ATOM 108 CB SER X 15 13.391 25.116 25.342 1.00 41.31 C
ATOM 109 OG SER X 15 14.321 25.934 26.035 1.00 45.29 O
ATOM 110 N ARG X 16 10.826 25.397 27.145 1.00 46.55 N
ATOM 111 CA ARG X 16 10.264 25.479 28.469 1.00 51.70 C
ATOM 112 C ARG X 16 10.312 24.103 29.104 1.00 47.53 C
ATOM 113 O ARG X 16 10.141 23.089 28.431 1.00 51.81 O
ATOM 114 CB ARG X 16 8.812 25.934 28.368 1.00 53.94 C
ATOM 115 CG ARG X 16 8.110 26.114 29.701 1.00 68.28 C
ATOM 116 CD ARG X 16 6.673 26.514 29.434 1.00 73.16 C
ATOM 117 NE ARG X 16 6.487 27.953 29.565 1.00 82.09 N
ATOM 118 CZ ARG X 16 5.847 28.538 30.582 1.00 94.71 C
ATOM 119 NH1 ARG X 16 5.315 27.806 31.564 1.00 88.00 N
ATOM 120 NH2 ARG X 16 5.728 29.864 30.616 1.00 92.45 N
ATOM 121 N VAL X 17 10.479 24.079 30.415 1.00 48.12 N
ATOM 122 CA VAL X 17 10.558 22.841 31.168 1.00 54.25 C
ATOM 123 C VAL X 17 9.512 22.919 32.265 1.00 59.71 C
ATOM 124 O VAL X 17 9.301 23.978 32.861 1.00 54.33 O
ATOM 125 CB VAL X 17 11.974 22.612 31.783 1.00 50.75 C
ATOM 126 CG1 VAL X 17 11.963 21.391 32.705 1.00 50.09 C
ATOM 127 CG2 VAL X 17 13.039 22.479 30.662 1.00 43.18 C
ATOM 128 N LYS X 18 8.845 21.790 32.496 1.00 62.14 N
ATOM 129 CA LYS X 18 7.834 21.657 33.536 1.00 62.53 C
ATOM 130 C LYS X 18 8.397 20.620 34.484 1.00 59.35 C
ATOM 131 O LYS X 18 8.369 19.424 34.212 1.00 60.88 O
ATOM 132 CB LYS X 18 6.478 21.237 32.936 1.00 57.16 C
ATOM 133 CG LYS X 18 5.285 21.452 33.844 1.00 60.82 C
ATOM 134 CD LYS X 18 4.015 20.748 33.330 1.00 65.06 C
ATOM 135 CE LYS X 18 2.997 20.477 34.448 1.00 64.59 C
ATOM 136 NZ LYS X 18 1.711 19.951 33.919 1.00 61.73 N
ATOM 137 N ASP X 19 8.967 21.100 35.583 1.00 64.62 N
ATOM 138 CA ASP X 19 9.600 20.235 36.590 1.00 65.16 C
ATOM 139 C ASP X 19 9.210 20.823 37.951 1.00 72.97 C
ATOM 140 O ASP X 19 9.658 21.939 38.317 1.00 69.58 O
ATOM 141 CB ASP X 19 11.102 20.184 36.375 1.00 58.64 C
ATOM 142 CG ASP X 19 11.814 19.435 37.453 1.00 65.20 C
ATOM 143 OD1 ASP X 19 11.146 18.858 38.333 1.00 70.25 O
ATOM 144 OD2 ASP X 19 13.058 19.403 37.415 1.00 72.97 O
ATOM 145 N ALA X 20 8.395 20.052 38.689 1.00 73.01 N
ATOM 146 CA ALA X 20 7.844 20.454 39.991 1.00 70.85 C
ATOM 147 C ALA X 20 8.981 20.631 40.985 1.00 75.71 C
ATOM 148 O ALA X 20 9.039 21.653 41.676 1.00 74.77 O
ATOM 149 CB ALA X 20 6.824 19.441 40.504 1.00 68.05 C
ATOM 150 N GLY X 21 9.896 19.654 41.019 1.00 69.43 N
ATOM 151 CA GLY X 21 11.076 19.687 41.892 1.00 70.67 C
ATOM 152 C GLY X 21 11.958 20.920 41.795 1.00 70.18 C
ATOM 153 O GLY X 21 12.338 21.496 42.813 1.00 72.59 O
ATOM 154 N THR X 22 12.294 21.339 40.581 1.00 73.12 N
ATOM 155 CA THR X 22 13.299 22.387 40.422 1.00 73.60 C
ATOM 156 C THR X 22 12.706 23.787 40.252 1.00 74.91 C
ATOM 157 O THR X 22 13.410 24.772 40.494 1.00 75.76 O
ATOM 158 CB THR X 22 14.349 22.049 39.328 1.00 70.68 C
ATOM 159 OG1 THR X 22 13.685 21.830 38.086 1.00 71.88 O
ATOM 160 CG2 THR X 22 15.117 20.771 39.686 1.00 74.55 C
ATOM 161 N TYR X 23 11.429 23.893 39.860 1.00 78.48 N
ATOM 162 CA TYR X 23 10.818 25.228 39.642 1.00 77.69 C
ATOM 163 C TYR X 23 9.676 25.530 40.575 1.00 82.80 C
ATOM 164 O TYR X 23 8.679 24.805 40.595 1.00 85.94 O
ATOM 165 CB TYR X 23 10.364 25.434 38.192 1.00 70.75 C
ATOM 166 CG TYR X 23 11.484 25.223 37.224 1.00 66.01 C
ATOM 167 CD1 TYR X 23 12.493 26.200 37.061 1.00 60.68 C
ATOM 168 CD2 TYR X 23 11.578 24.022 36.511 1.00 56.93 C
ATOM 169 CE1 TYR X 23 13.554 25.987 36.188 1.00 61.66 C
ATOM 170 CE2 TYR X 23 12.627 23.796 35.637 1.00 57.78 C
ATOM 171 CZ TYR X 23 13.608 24.774 35.470 1.00 59.26 C
ATOM 172 OH TYR X 23 14.643 24.531 34.603 1.00 59.52 O
ATOM 173 N LYS X 24 9.826 26.620 41.328 1.00 94.26 N
ATOM 174 CA LYS X 24 8.801 27.066 42.283 1.00 99.85 C
ATOM 175 C LYS X 24 7.671 27.845 41.577 1.00103.25 C
ATOM 176 O LYS X 24 6.526 27.808 42.023 1.00100.44 O
ATOM 177 CB LYS X 24 9.422 27.839 43.479 1.00 93.88 C
ATOM 178 CG LYS X 24 9.149 29.348 43.568 1.00103.21 C
ATOM 179 CD LYS X 24 9.221 29.833 45.023 1.00105.83 C
ATOM 180 CE LYS X 24 8.486 31.152 45.276 1.00106.40 C
ATOM 181 NZ LYS X 24 9.348 32.359 45.061 1.00115.13 N
ATOM 182 N ALA X 25 7.998 28.516 40.468 1.00108.67 N
ATOM 183 CA ALA X 25 7.017 29.270 39.674 1.00107.96 C
ATOM 184 C ALA X 25 5.793 28.414 39.289 1.00106.23 C
ATOM 185 O ALA X 25 5.898 27.188 39.206 1.00109.02 O
ATOM 186 CB ALA X 25 7.688 29.889 38.448 1.00110.53 C
ATOM 187 N GLN X 26 4.648 29.070 39.055 1.00109.51 N
ATOM 188 CA GLN X 26 3.311 28.415 39.038 1.00103.07 C
ATOM 189 C GLN X 26 3.111 27.190 38.111 1.00111.16 C
ATOM 190 O GLN X 26 3.218 27.289 36.873 1.00104.51 O
ATOM 191 CB GLN X 26 2.180 29.449 38.843 1.00107.50 C
ATOM 192 CG GLN X 26 2.321 30.359 37.618 1.00113.82 C
ATOM 193 CD GLN X 26 1.071 31.195 37.325 1.00113.22 C
ATOM 194 OE1 GLN X 26 -0.024 30.661 37.108 1.00111.34 O
ATOM 195 NE2 GLN X 26 1.238 32.513 37.295 1.00 97.57 N
ATOM 196 N GLY X 27 2.798 26.048 38.735 1.00108.57 N
ATOM 197 CA GLY X 27 2.556 24.775 38.034 1.00106.55 C
ATOM 198 C GLY X 27 3.793 23.894 37.879 1.00102.43 C
ATOM 199 O GLY X 27 3.720 22.822 37.269 1.00 95.95 O
ATOM 200 N GLY X 28 4.922 24.339 38.443 1.00 98.16 N
ATOM 201 CA GLY X 28 6.231 23.691 38.240 1.00 85.84 C
ATOM 202 C GLY X 28 6.900 24.080 36.921 1.00 71.45 C
ATOM 203 O GLY X 28 7.846 23.451 36.494 1.00 76.07 O
ATOM 204 N LYS X 29 6.406 25.137 36.298 1.00 66.20 N
ATOM 205 CA LYS X 29 6.861 25.617 34.995 1.00 68.57 C
ATOM 206 C LYS X 29 8.031 26.593 35.083 1.00 66.44 C
ATOM 207 O LYS X 29 7.998 27.538 35.872 1.00 61.60 O
ATOM 208 CB LYS X 29 5.691 26.296 34.274 1.00 71.84 C
ATOM 209 CG LYS X 29 4.681 25.316 33.705 1.00 73.37 C
ATOM 210 CD LYS X 29 3.327 25.973 33.496 1.00 80.59 C
ATOM 211 CE LYS X 29 2.217 24.918 33.429 1.00 89.80 C
ATOM 212 NZ LYS X 29 0.843 25.472 33.661 1.00 80.38 N
ATOM 213 N SER X 30 9.075 26.344 34.280 1.00 66.02 N
ATOM 214 CA SER X 30 10.194 27.285 34.133 1.00 59.79 C
ATOM 215 C SER X 30 9.684 28.501 33.366 1.00 56.66 C
ATOM 216 O SER X 30 8.522 28.546 32.925 1.00 55.33 O
ATOM 217 CB SER X 30 11.329 26.648 33.336 1.00 55.77 C
ATOM 218 OG SER X 30 10.937 26.474 31.977 1.00 51.60 O
ATOM 219 N LYS X 31 10.543 29.492 33.201 1.00 52.66 N
ATOM 220 CA LYS X 31 10.262 30.522 32.201 1.00 58.27 C
ATOM 221 C LYS X 31 10.571 29.951 30.802 1.00 50.60 C
ATOM 222 O LYS X 31 11.194 28.881 30.676 1.00 45.91 O
ATOM 223 CB LYS X 31 11.044 31.803 32.530 1.00 64.68 C
ATOM 224 CG LYS X 31 10.264 32.730 33.478 1.00 69.25 C
ATOM 225 CD LYS X 31 10.612 32.512 34.951 1.00 81.02 C
ATOM 226 CE LYS X 31 9.688 33.266 35.931 1.00 68.80 C
ATOM 227 NZ LYS X 31 9.716 34.747 35.755 1.00 74.23 N
ATOM 228 N THR X 32 10.122 30.636 29.762 1.00 50.97 N
ATOM 229 CA THR X 32 10.415 30.246 28.380 1.00 52.41 C
ATOM 230 C THR X 32 11.792 30.795 27.951 1.00 50.74 C
ATOM 231 O THR X 32 12.044 31.978 28.031 1.00 48.55 O
ATOM 232 CB THR X 32 9.288 30.700 27.433 1.00 49.68 C
ATOM 233 OG1 THR X 32 8.090 30.031 27.799 1.00 51.53 O
ATOM 234 CG2 THR X 32 9.576 30.316 26.007 1.00 54.17 C
ATOM 235 N ALA X 33 12.678 29.911 27.514 1.00 51.85 N
ATOM 236 CA ALA X 33 14.001 30.314 27.073 1.00 45.28 C
ATOM 237 C ALA X 33 14.011 30.456 25.546 1.00 45.68 C
ATOM 238 O ALA X 33 13.412 29.608 24.825 1.00 38.31 O
ATOM 239 CB ALA X 33 15.020 29.285 27.563 1.00 49.78 C
ATOM 240 N THR X 34 14.644 31.546 25.062 1.00 43.34 N
ATOM 241 CA THR X 34 14.790 31.828 23.603 1.00 46.10 C
ATOM 242 C THR X 34 16.252 32.041 23.256 1.00 40.85 C
ATOM 243 O THR X 34 16.872 33.019 23.706 1.00 40.61 O
ATOM 244 CB THR X 34 13.968 33.035 23.070 1.00 43.89 C
ATOM 245 OG1 THR X 34 12.610 32.927 23.514 1.00 56.15 O
ATOM 246 CG2 THR X 34 14.002 33.068 21.520 1.00 42.65 C
ATOM 247 N GLN X 35 16.775 31.150 22.422 1.00 38.51 N
ATOM 248 CA GLN X 35 18.225 31.085 22.200 1.00 44.87 C
ATOM 249 C GLN X 35 18.576 30.836 20.788 1.00 40.17 C
ATOM 250 O GLN X 35 18.047 29.905 20.198 1.00 36.94 O
ATOM 251 CB GLN X 35 18.862 29.932 22.958 1.00 41.51 C
ATOM 252 CG GLN X 35 19.126 30.263 24.371 1.00 48.86 C
ATOM 253 CD GLN X 35 20.087 29.286 25.008 1.00 48.57 C
ATOM 254 OE1 GLN X 35 19.998 28.055 24.796 1.00 44.84 O
ATOM 255 NE2 GLN X 35 21.014 29.823 25.809 1.00 43.74 N
ATOM 256 N ILE X 36 19.446 31.700 20.268 1.00 33.93 N
ATOM 257 CA ILE X 36 20.267 31.397 19.120 1.00 35.98 C
ATOM 258 C ILE X 36 21.183 30.207 19.515 1.00 36.87 C
ATOM 259 O ILE X 36 21.848 30.239 20.534 1.00 33.13 O
ATOM 260 CB ILE X 36 21.118 32.615 18.715 1.00 34.45 C
ATOM 261 CG1 ILE X 36 20.237 33.763 18.258 1.00 33.44 C
ATOM 262 CG2 ILE X 36 22.043 32.274 17.540 1.00 37.46 C
ATOM 263 CD1 ILE X 36 20.988 35.090 18.060 1.00 34.81 C
ATOM 264 N ALA X 37 21.171 29.141 18.728 1.00 37.85 N
ATOM 265 CA ALA X 37 21.999 28.012 19.037 1.00 35.59 C
ATOM 266 C ALA X 37 22.644 27.380 17.787 1.00 36.78 C
ATOM 267 O ALA X 37 21.973 27.135 16.816 1.00 35.05 O
ATOM 268 CB ALA X 37 21.198 26.958 19.795 1.00 37.77 C
ATOM 269 N ASP X 38 23.919 27.009 17.881 1.00 28.78 N
ATOM 270 CA ASP X 38 24.511 26.165 16.832 1.00 31.38 C
ATOM 271 C ASP X 38 23.918 24.749 16.961 1.00 31.14 C
ATOM 272 O ASP X 38 23.786 24.219 18.068 1.00 29.59 O
ATOM 273 CB ASP X 38 26.025 26.032 17.097 1.00 28.94 C
ATOM 274 CG ASP X 38 26.706 25.295 16.009 1.00 29.73 C
ATOM 275 OD1 ASP X 38 26.980 25.902 14.948 1.00 32.23 O
ATOM 276 OD2 ASP X 38 27.013 24.102 16.166 1.00 32.13 O
ATOM 277 N PHE X 39 23.662 24.142 15.819 1.00 29.69 N
ATOM 278 CA PHE X 39 23.073 22.800 15.747 1.00 31.19 C
ATOM 279 C PHE X 39 24.121 21.736 15.545 1.00 32.79 C
ATOM 280 O PHE X 39 23.776 20.623 15.250 1.00 31.71 O
ATOM 281 CB PHE X 39 22.055 22.761 14.644 1.00 28.95 C
ATOM 282 CG PHE X 39 20.805 23.582 14.943 1.00 33.32 C
ATOM 283 CD1 PHE X 39 20.664 24.227 16.149 1.00 28.69 C
ATOM 284 CD2 PHE X 39 19.728 23.624 14.027 1.00 37.99 C
ATOM 285 CE1 PHE X 39 19.527 24.974 16.456 1.00 33.43 C
ATOM 286 CE2 PHE X 39 18.562 24.331 14.355 1.00 45.36 C
ATOM 287 CZ PHE X 39 18.471 25.003 15.581 1.00 36.07 C
ATOM 288 N GLY X 40 25.416 22.069 15.676 1.00 33.02 N
ATOM 289 CA GLY X 40 26.426 21.008 15.504 1.00 31.68 C
ATOM 290 C GLY X 40 27.262 21.177 14.237 1.00 32.32 C
ATOM 291 O GLY X 40 27.691 20.207 13.619 1.00 30.31 O
ATOM 292 N SER X 41 27.593 22.433 13.935 1.00 28.46 N
ATOM 293 CA SER X 41 28.339 22.764 12.767 1.00 28.55 C
ATOM 294 C SER X 41 29.685 22.009 12.881 1.00 29.01 C
ATOM 295 O SER X 41 30.145 21.796 13.941 1.00 28.00 O
ATOM 296 CB SER X 41 28.619 24.279 12.756 1.00 25.91 C
ATOM 297 OG SER X 41 27.326 24.913 12.535 1.00 34.05 O
ATOM 298 N LYS X 42 30.245 21.616 11.761 1.00 28.90 N
ATOM 299 CA LYS X 42 31.456 20.794 11.752 1.00 35.01 C
ATOM 300 C LYS X 42 32.212 21.044 10.478 1.00 34.97 C
ATOM 301 O LYS X 42 31.684 21.519 9.457 1.00 33.07 O
ATOM 302 CB LYS X 42 31.127 19.325 11.853 1.00 38.33 C
ATOM 303 CG LYS X 42 29.882 18.941 11.062 1.00 41.13 C
ATOM 304 CD LYS X 42 30.055 17.566 10.467 1.00 48.63 C
ATOM 305 CE LYS X 42 28.823 17.130 9.681 1.00 53.40 C
ATOM 306 NZ LYS X 42 27.729 16.810 10.627 1.00 54.94 N
ATOM 307 N ILE X 43 33.484 20.726 10.548 1.00 37.26 N
ATOM 308 CA ILE X 43 34.354 20.914 9.433 1.00 34.54 C
ATOM 309 C ILE X 43 35.356 19.777 9.394 1.00 36.29 C
ATOM 310 O ILE X 43 35.854 19.345 10.421 1.00 37.19 O
ATOM 311 CB ILE X 43 35.078 22.281 9.456 1.00 35.11 C
ATOM 312 CG1 ILE X 43 35.759 22.525 8.103 1.00 36.06 C
ATOM 313 CG2 ILE X 43 36.086 22.402 10.610 1.00 32.81 C
ATOM 314 CD1 ILE X 43 36.292 23.962 7.907 1.00 39.17 C
ATOM 315 N GLY X 44 35.592 19.268 8.186 1.00 39.26 N
ATOM 316 CA GLY X 44 36.466 18.126 7.958 1.00 35.54 C
ATOM 317 C GLY X 44 37.413 18.265 6.772 1.00 41.10 C
ATOM 318 O GLY X 44 37.200 19.098 5.858 1.00 37.11 O
ATOM 319 N PHE X 45 38.448 17.416 6.805 1.00 37.44 N
ATOM 320 CA PHE X 45 39.403 17.228 5.735 1.00 38.54 C
ATOM 321 C PHE X 45 39.538 15.715 5.522 1.00 40.31 C
ATOM 322 O PHE X 45 39.730 14.981 6.479 1.00 40.85 O
ATOM 323 CB PHE X 45 40.747 17.838 6.089 1.00 36.94 C
ATOM 324 CG PHE X 45 40.663 19.267 6.491 1.00 40.87 C
ATOM 325 CD1 PHE X 45 40.429 19.630 7.821 1.00 37.56 C
ATOM 326 CD2 PHE X 45 40.812 20.271 5.541 1.00 40.70 C
ATOM 327 CE1 PHE X 45 40.322 20.984 8.177 1.00 37.13 C
ATOM 328 CE2 PHE X 45 40.739 21.613 5.904 1.00 40.37 C
ATOM 329 CZ PHE X 45 40.522 21.962 7.229 1.00 41.25 C
ATOM 330 N LYS X 46 39.422 15.260 4.276 1.00 38.78 N
ATOM 331 CA LYS X 46 39.583 13.825 3.958 1.00 38.85 C
ATOM 332 C LYS X 46 40.221 13.665 2.608 1.00 42.86 C
ATOM 333 O LYS X 46 40.230 14.610 1.782 1.00 38.93 O
ATOM 334 CB LYS X 46 38.261 13.055 3.968 1.00 35.38 C
ATOM 335 CG LYS X 46 37.290 13.565 2.919 1.00 43.00 C
ATOM 336 CD LYS X 46 35.929 12.910 3.050 1.00 45.76 C
ATOM 337 CE LYS X 46 34.958 13.530 2.090 1.00 45.61 C
ATOM 338 NZ LYS X 46 33.714 12.762 2.301 1.00 56.02 N
ATOM 339 N GLY X 47 40.742 12.462 2.369 1.00 37.93 N
ATOM 340 CA GLY X 47 41.463 12.206 1.149 1.00 37.38 C
ATOM 341 C GLY X 47 41.514 10.707 0.927 1.00 41.01 C
ATOM 342 O GLY X 47 41.190 9.926 1.829 1.00 36.00 O
ATOM 343 N GLN X 48 41.938 10.318 -0.268 1.00 39.67 N
ATOM 344 CA GLN X 48 42.149 8.910 -0.619 1.00 41.23 C
ATOM 345 C GLN X 48 43.223 8.886 -1.668 1.00 43.32 C
ATOM 346 O GLN X 48 43.391 9.870 -2.395 1.00 45.13 O
ATOM 347 CB GLN X 48 40.903 8.273 -1.246 1.00 42.18 C
ATOM 348 CG GLN X 48 40.481 8.906 -2.569 1.00 48.36 C
ATOM 349 CD GLN X 48 39.269 8.216 -3.133 1.00 60.35 C
ATOM 350 OE1 GLN X 48 38.167 8.323 -2.588 1.00 66.30 O
ATOM 351 NE2 GLN X 48 39.461 7.480 -4.214 1.00 64.06 N
ATOM 352 N GLU X 49 43.930 7.762 -1.766 1.00 38.55 N
ATOM 353 CA GLU X 49 44.937 7.597 -2.789 1.00 43.36 C
ATOM 354 C GLU X 49 44.881 6.170 -3.334 1.00 41.50 C
ATOM 355 O GLU X 49 44.979 5.224 -2.556 1.00 41.33 O
ATOM 356 CB GLU X 49 46.362 7.857 -2.236 1.00 44.47 C
ATOM 357 CG GLU X 49 47.442 7.570 -3.289 1.00 44.85 C
ATOM 358 CD GLU X 49 48.882 7.740 -2.795 1.00 43.90 C
ATOM 359 OE1 GLU X 49 49.234 7.380 -1.655 1.00 43.18 O
ATOM 360 OE2 GLU X 49 49.681 8.222 -3.587 1.00 47.81 O
ATOM 361 N ASP X 50 44.789 6.039 -4.661 1.00 40.17 N
ATOM 362 CA ASP X 50 44.767 4.736 -5.294 1.00 44.79 C
ATOM 363 C ASP X 50 46.171 4.153 -5.159 1.00 44.46 C
ATOM 364 O ASP X 50 47.163 4.766 -5.510 1.00 42.54 O
ATOM 365 CB ASP X 50 44.256 4.860 -6.751 1.00 53.14 C
ATOM 366 CG ASP X 50 44.500 3.604 -7.623 1.00 54.78 C
ATOM 367 OD1 ASP X 50 44.347 2.439 -7.170 1.00 63.85 O
ATOM 368 OD2 ASP X 50 44.831 3.801 -8.823 1.00 66.73 O
ATOM 369 N LEU X 51 46.229 2.980 -4.566 1.00 43.36 N
ATOM 370 CA LEU X 51 47.489 2.280 -4.420 1.00 45.80 C
ATOM 371 C LEU X 51 47.765 1.268 -5.568 1.00 52.13 C
ATOM 372 O LEU X 51 48.783 0.553 -5.516 1.00 46.49 O
ATOM 373 CB LEU X 51 47.549 1.610 -3.046 1.00 46.06 C
ATOM 374 CG LEU X 51 47.365 2.584 -1.862 1.00 49.54 C
ATOM 375 CD1 LEU X 51 47.450 1.784 -0.572 1.00 44.14 C
ATOM 376 CD2 LEU X 51 48.362 3.752 -1.876 1.00 42.79 C
ATOM 377 N GLY X 52 46.876 1.242 -6.577 1.00 47.99 N
ATOM 378 CA GLY X 52 47.113 0.497 -7.808 1.00 59.00 C
ATOM 379 C GLY X 52 46.326 -0.792 -8.132 1.00 72.00 C
ATOM 380 O GLY X 52 46.189 -1.160 -9.325 1.00 70.57 O
ATOM 381 N ASN X 53 45.814 -1.483 -7.109 1.00 71.18 N
ATOM 382 CA ASN X 53 45.295 -2.851 -7.297 1.00 70.32 C
ATOM 383 C ASN X 53 43.810 -2.999 -6.984 1.00 69.52 C
ATOM 384 O ASN X 53 43.360 -4.095 -6.641 1.00 70.22 O
ATOM 385 CB ASN X 53 46.151 -3.810 -6.457 1.00 73.18 C
ATOM 386 CG ASN X 53 47.392 -3.127 -5.912 1.00 86.11 C
ATOM 387 OD1 ASN X 53 48.070 -2.413 -6.648 1.00 89.32 O
ATOM 388 ND2 ASN X 53 47.668 -3.292 -4.610 1.00 85.16 N
ATOM 389 N GLY X 54 43.047 -1.908 -7.079 1.00 63.63 N
ATOM 390 CA GLY X 54 41.730 -1.870 -6.446 1.00 61.78 C
ATOM 391 C GLY X 54 41.870 -1.539 -4.947 1.00 63.28 C
ATOM 392 O GLY X 54 40.881 -1.553 -4.212 1.00 71.35 O
ATOM 393 N MET X 55 43.086 -1.234 -4.491 1.00 56.02 N
ATOM 394 CA MET X 55 43.319 -0.749 -3.127 1.00 52.59 C
ATOM 395 C MET X 55 43.515 0.773 -3.005 1.00 48.67 C
ATOM 396 O MET X 55 44.192 1.413 -3.812 1.00 51.04 O
ATOM 397 CB MET X 55 44.510 -1.491 -2.558 1.00 54.94 C
ATOM 398 CG MET X 55 44.764 -1.289 -1.079 1.00 62.13 C
ATOM 399 SD MET X 55 45.051 -2.836 -0.188 1.00 72.94 S
ATOM 400 CE MET X 55 46.143 -3.682 -1.352 1.00 63.53 C
ATOM 401 N LYS X 56 42.960 1.349 -1.955 1.00 46.23 N
ATOM 402 CA LYS X 56 43.105 2.771 -1.689 1.00 44.03 C
ATOM 403 C LYS X 56 43.533 3.036 -0.268 1.00 39.44 C
ATOM 404 O LYS X 56 43.086 2.355 0.623 1.00 37.80 O
ATOM 405 CB LYS X 56 41.768 3.456 -1.939 1.00 45.81 C
ATOM 406 CG LYS X 56 41.219 3.254 -3.342 1.00 57.02 C
ATOM 407 CD LYS X 56 40.192 4.336 -3.688 1.00 69.30 C
ATOM 408 CE LYS X 56 38.767 3.938 -3.331 1.00 76.04 C
ATOM 409 NZ LYS X 56 37.784 4.656 -4.206 1.00 80.11 N
ATOM 410 N ALA X 57 44.410 4.020 -0.040 1.00 39.38 N
ATOM 411 CA ALA X 57 44.585 4.599 1.310 1.00 36.49 C
ATOM 412 C ALA X 57 43.424 5.566 1.532 1.00 36.08 C
ATOM 413 O ALA X 57 43.046 6.254 0.590 1.00 33.42 O
ATOM 414 CB ALA X 57 45.876 5.356 1.379 1.00 40.01 C
ATOM 415 N ILE X 58 42.869 5.605 2.758 1.00 35.93 N
ATOM 416 CA ILE X 58 41.851 6.600 3.122 1.00 38.57 C
ATOM 417 C ILE X 58 42.181 7.261 4.436 1.00 37.77 C
ATOM 418 O ILE X 58 42.730 6.609 5.291 1.00 42.57 O
ATOM 419 CB ILE X 58 40.409 6.010 3.097 1.00 31.65 C
ATOM 420 CG1 ILE X 58 40.246 4.935 4.157 1.00 36.39 C
ATOM 421 CG2 ILE X 58 40.146 5.415 1.688 1.00 37.17 C
ATOM 422 CD1 ILE X 58 38.847 4.318 4.161 1.00 37.17 C
ATOM 423 N TRP X 59 41.781 8.520 4.609 1.00 33.72 N
ATOM 424 CA TRP X 59 41.934 9.194 5.880 1.00 36.68 C
ATOM 425 C TRP X 59 40.919 10.283 5.963 1.00 37.68 C
ATOM 426 O TRP X 59 40.374 10.687 4.955 1.00 32.48 O
ATOM 427 CB TRP X 59 43.303 9.809 6.031 1.00 34.67 C
ATOM 428 CG TRP X 59 43.555 10.914 5.026 1.00 36.09 C
ATOM 429 CD1 TRP X 59 43.986 10.775 3.711 1.00 38.00 C
ATOM 430 CD2 TRP X 59 43.375 12.342 5.220 1.00 33.26 C
ATOM 431 NE1 TRP X 59 44.132 11.996 3.106 1.00 34.06 N
ATOM 432 CE2 TRP X 59 43.782 12.979 3.976 1.00 34.86 C
ATOM 433 CE3 TRP X 59 42.977 13.133 6.275 1.00 34.46 C
ATOM 434 CZ2 TRP X 59 43.729 14.340 3.809 1.00 31.67 C
ATOM 435 CZ3 TRP X 59 42.967 14.504 6.094 1.00 35.56 C
ATOM 436 CH2 TRP X 59 43.344 15.086 4.893 1.00 33.93 C
ATOM 437 N GLN X 60 40.707 10.779 7.177 1.00 36.23 N
ATOM 438 CA GLN X 60 39.728 11.822 7.434 1.00 37.49 C
ATOM 439 C GLN X 60 40.083 12.420 8.762 1.00 37.82 C
ATOM 440 O GLN X 60 40.519 11.707 9.682 1.00 37.79 O
ATOM 441 CB GLN X 60 38.284 11.234 7.460 1.00 33.57 C
ATOM 442 CG GLN X 60 37.288 12.194 8.038 1.00 34.07 C
ATOM 443 CD GLN X 60 35.832 11.791 7.735 1.00 36.19 C
ATOM 444 OE1 GLN X 60 35.444 11.704 6.570 1.00 33.64 O
ATOM 445 NE2 GLN X 60 35.017 11.635 8.774 1.00 26.81 N
ATOM 446 N LEU X 61 39.973 13.741 8.834 1.00 32.10 N
ATOM 447 CA LEU X 61 40.149 14.458 10.060 1.00 33.68 C
ATOM 448 C LEU X 61 38.930 15.412 10.170 1.00 34.35 C
ATOM 449 O LEU X 61 38.841 16.383 9.440 1.00 33.34 O
ATOM 450 CB LEU X 61 41.427 15.306 9.953 1.00 35.24 C
ATOM 451 CG LEU X 61 42.691 15.302 10.824 1.00 42.53 C
ATOM 452 CD1 LEU X 61 43.460 16.662 10.641 1.00 41.30 C
ATOM 453 CD2 LEU X 61 42.400 15.033 12.296 1.00 36.85 C
ATOM 454 N GLU X 62 37.994 15.098 11.048 1.00 32.89 N
ATOM 455 CA GLU X 62 36.809 15.887 11.208 1.00 33.30 C
ATOM 456 C GLU X 62 36.733 16.492 12.600 1.00 34.10 C
ATOM 457 O GLU X 62 37.121 15.843 13.574 1.00 29.17 O
ATOM 458 CB GLU X 62 35.574 15.005 10.944 1.00 30.12 C
ATOM 459 CG GLU X 62 34.371 15.854 10.582 1.00 32.75 C
ATOM 460 CD GLU X 62 33.162 15.011 10.205 1.00 34.64 C
ATOM 461 OE1 GLU X 62 33.234 14.284 9.188 1.00 37.65 O
ATOM 462 OE2 GLU X 62 32.201 15.048 10.965 1.00 38.57 O
ATOM 463 N GLN X 63 36.155 17.701 12.717 1.00 31.90 N
ATOM 464 CA GLN X 63 36.191 18.453 13.993 1.00 35.78 C
ATOM 465 C GLN X 63 34.837 19.100 14.221 1.00 30.42 C
ATOM 466 O GLN X 63 34.259 19.549 13.278 1.00 29.91 O
ATOM 467 CB GLN X 63 37.110 19.742 13.833 1.00 33.94 C
ATOM 468 CG GLN X 63 38.562 19.627 13.553 1.00 36.00 C
ATOM 469 CD GLN X 63 38.979 18.688 12.463 1.00 32.68 C
ATOM 470 OE1 GLN X 63 38.741 18.913 11.252 1.00 35.05 O
ATOM 471 NE2 GLN X 63 39.675 17.674 12.866 1.00 31.40 N
ATOM 472 N LYS X 64 34.463 19.304 15.474 1.00 30.29 N
ATOM 473 CA LYS X 64 33.378 20.229 15.866 1.00 32.67 C
ATOM 474 C LYS X 64 33.793 21.649 15.608 1.00 34.63 C
ATOM 475 O LYS X 64 34.979 22.018 15.881 1.00 33.78 O
ATOM 476 CB LYS X 64 33.050 20.088 17.347 1.00 32.29 C
ATOM 477 CG LYS X 64 32.591 18.661 17.706 1.00 36.90 C
ATOM 478 CD LYS X 64 32.284 18.528 19.202 1.00 41.85 C
ATOM 479 CE LYS X 64 32.444 17.063 19.654 1.00 45.40 C
ATOM 480 NZ LYS X 64 32.207 16.941 21.105 1.00 49.27 N
ATOM 481 N ALA X 65 32.874 22.457 15.046 1.00 31.32 N
ATOM 482 CA ALA X 65 33.290 23.851 14.709 1.00 33.45 C
ATOM 483 C ALA X 65 32.075 24.753 14.833 1.00 31.85 C
ATOM 484 O ALA X 65 31.673 25.355 13.877 1.00 30.62 O