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2gox.pdb
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6533 lines (6533 loc) · 517 KB
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HEADER CELL ADHESION/TOXIN 14-APR-06 2GOX
TITLE CRYSTAL STRUCTURE OF EFB-C / C3D COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COMPLEMENT C3;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: FRAGMENT OF ALPHA CHAIN: RESIDUES 996-1287;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: FIBRINOGEN-BINDING PROTEIN;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: C-TERMINAL DOMAIN: RESIDUES 101-165;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: C3;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT7-;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 11 ORGANISM_COMMON: BACTERIA;
SOURCE 12 STRAIN: MU50 / ATCC 700699;
SOURCE 13 GENE: EFB;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PT7HMT
KEYWDS PROTEIN-PROTEIN COMPLEX, CELL ADHESION/TOXIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HAMMEL,B.V.GEISBRECHT
REVDAT 3 18-SEP-07 2GOX 1 REMARK
REVDAT 2 04-SEP-07 2GOX 1 ATOM SEQADV DBREF
REVDAT 1 20-MAR-07 2GOX 0
JRNL AUTH M.HAMMEL,G.SFYROERA,D.RICKLIN,P.MAGOTTI,
JRNL AUTH 2 J.D.LAMBRIS,B.V.GEISBRECHT
JRNL TITL A STRUCTURAL BASIS FOR COMPLEMENT INHIBITION BY
JRNL TITL 2 STAPHYLOCOCCUS AUREUS.
JRNL REF NAT.IMMUNOL. V. 8 430 2007
JRNL REFN UK ISSN 1529-2908
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 49718
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2519
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3180
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 152
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 5991
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.97000
REMARK 3 B22 (A**2) : -0.97000
REMARK 3 B33 (A**2) : 1.93000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.207
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.185
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.430
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5780 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7825 ; 1.877 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 720 ; 6.477 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 259 ;38.304 ;25.058
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1027 ;18.533 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;18.584 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 886 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4323 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3165 ; 0.229 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4056 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 341 ; 0.176 ; 0.200
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): 35 ; 0.268 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.095 ; 0.200
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): 3733 ; 1.164 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5771 ; 1.867 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2385 ; 2.978 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2054 ; 4.370 ; 4.500
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 991 A 1287
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1920 -40.3390 0.4070
REMARK 3 T TENSOR
REMARK 3 T11: -0.0101 T22: -0.0672
REMARK 3 T33: 0.0030 T12: -0.0238
REMARK 3 T13: 0.0046 T23: 0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.4544 L22: 1.1803
REMARK 3 L33: 0.4127 L12: 0.3237
REMARK 3 L13: 0.0579 L23: -0.3352
REMARK 3 S TENSOR
REMARK 3 S11: 0.0714 S12: -0.0692 S13: -0.0063
REMARK 3 S21: -0.0138 S22: -0.0801 S23: -0.0786
REMARK 3 S31: -0.0405 S32: -0.0502 S33: 0.0087
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 : C 991 C 1287
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1120 -65.6480 13.3290
REMARK 3 T TENSOR
REMARK 3 T11: -0.0663 T22: -0.0095
REMARK 3 T33: -0.0017 T12: -0.0244
REMARK 3 T13: 0.0174 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 1.2829 L22: 0.4639
REMARK 3 L33: 0.3788 L12: 0.3198
REMARK 3 L13: -0.3561 L23: 0.0529
REMARK 3 S TENSOR
REMARK 3 S11: -0.0686 S12: -0.0163 S13: -0.0790
REMARK 3 S21: -0.0689 S22: 0.0663 S23: -0.0085
REMARK 3 S31: -0.0547 S32: -0.0427 S33: 0.0023
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 101 B 165
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3790 -37.5390 24.1960
REMARK 3 T TENSOR
REMARK 3 T11: 0.1234 T22: -0.0412
REMARK 3 T33: -0.0297 T12: -0.1891
REMARK 3 T13: -0.1484 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 8.2804 L22: 1.0356
REMARK 3 L33: 1.2715 L12: 1.8502
REMARK 3 L13: 0.6657 L23: 0.4528
REMARK 3 S TENSOR
REMARK 3 S11: 0.3709 S12: -0.5631 S13: 0.0632
REMARK 3 S21: 0.4694 S22: -0.3266 S23: -0.5110
REMARK 3 S31: -0.1512 S32: -0.2083 S33: -0.0443
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 101 D 165
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9280 -75.6720 -10.3790
REMARK 3 T TENSOR
REMARK 3 T11: -0.0175 T22: 0.1045
REMARK 3 T33: -0.0398 T12: -0.1668
REMARK 3 T13: 0.0294 T23: -0.1349
REMARK 3 L TENSOR
REMARK 3 L11: 1.4984 L22: 6.3736
REMARK 3 L33: 1.4692 L12: 1.5736
REMARK 3 L13: 1.1477 L23: 0.8523
REMARK 3 S TENSOR
REMARK 3 S11: -0.2246 S12: 0.4230 S13: -0.5442
REMARK 3 S21: -0.5034 S22: 0.3171 S23: 0.0230
REMARK 3 S31: -0.2350 S32: -0.1426 S33: -0.0925
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 ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2GOX COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB037379.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-2005
REMARK 200 TEMPERATURE (KELVIN) : 93.0
REMARK 200 PH : 7.40
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49761
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : 0.09200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.53200
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1C3D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% TACSIMATE PH 7.4, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 -Y,X,1/4+Z
REMARK 290 4555 Y,-X,3/4+Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.12100
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.56050
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 91.68150
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: DIMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 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 GLU A1035 CG CD OE1 OE2
REMARK 470 LYS A1036 CG CD CE NZ
REMARK 470 LYS B 123 CG CD CE NZ
REMARK 470 PHE B 142 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 160 CG CD CE NZ
REMARK 470 ARG B 165 CG CD NE CZ NH1 NH2
REMARK 470 GLU C1035 CG CD OE1 OE2
REMARK 470 LYS C1036 CG CD CE NZ
REMARK 470 ARG D 119 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 123 CG CD CE NZ
REMARK 470 PHE D 142 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 160 CG CD CE NZ
REMARK 470 ARG D 165 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 O HOH C 4 O HOH C 316 1.84
REMARK 500 OE1 GLN C 1152 O HOH C 247 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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS B 145 CD LYS B 145 CE 0.173
REMARK 500 LYS B 145 CE LYS B 145 NZ 0.158
REMARK 500 GLU C1153 CB GLU C1153 CG 0.114
REMARK 500 GLU C1221 CG GLU C1221 CD 0.107
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 PHE A1037 -29.17 -176.68
REMARK 500 LEU A1039 -39.16 -35.71
REMARK 500 SER A1064 -4.36 77.31
REMARK 500 GLU B 122 -34.00 -36.68
REMARK 500 LYS B 145 -39.44 -23.88
REMARK 500 ALA C1010 -148.70 -91.58
REMARK 500 LYS C1036 -98.78 -62.18
REMARK 500 PHE C1037 -60.53 -14.24
REMARK 500 LEU C1039 -29.83 -36.32
REMARK 500 SER C1064 -6.56 73.47
REMARK 500 GLU C1138 32.83 71.20
REMARK 500 LYS C1217 16.92 58.60
REMARK 500 ASP D 102 -41.50 -150.75
REMARK 500 LYS D 145 -40.91 -29.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GOM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EFB-C FROM STAPHYLOCOCCUS AUREUS: THE
REMARK 900 APO FORM OF THE BACTERIAL COMPONENT FOUND IN THE CURRENT
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 2NOJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EHP/C3D COMPLEX
DBREF 2GOX A 996 1287 UNP P01024 CO3_HUMAN 996 1287
DBREF 2GOX C 996 1287 UNP P01024 CO3_HUMAN 996 1287
DBREF 2GOX B 101 165 UNP P68799 FIB_STAAM 101 165
DBREF 2GOX D 101 165 UNP P68799 FIB_STAAM 101 165
SEQADV 2GOX GLY A 991 UNP P01024 EXPRESSION TAG
SEQADV 2GOX SER A 992 UNP P01024 EXPRESSION TAG
SEQADV 2GOX ARG A 993 UNP P01024 EXPRESSION TAG
SEQADV 2GOX SER A 994 UNP P01024 EXPRESSION TAG
SEQADV 2GOX THR A 995 UNP P01024 EXPRESSION TAG
SEQADV 2GOX ALA A 1010 UNP P01024 CYS 1010 ENGINEERED
SEQADV 2GOX GLY C 991 UNP P01024 EXPRESSION TAG
SEQADV 2GOX SER C 992 UNP P01024 EXPRESSION TAG
SEQADV 2GOX ARG C 993 UNP P01024 EXPRESSION TAG
SEQADV 2GOX SER C 994 UNP P01024 EXPRESSION TAG
SEQADV 2GOX THR C 995 UNP P01024 EXPRESSION TAG
SEQADV 2GOX ALA C 1010 UNP P01024 CYS 1010 ENGINEERED
SEQRES 1 A 297 GLY SER ARG SER THR ASP ALA GLU ARG LEU LYS HIS LEU
SEQRES 2 A 297 ILE VAL THR PRO SER GLY ALA GLY GLU GLN ASN MET ILE
SEQRES 3 A 297 GLY MET THR PRO THR VAL ILE ALA VAL HIS TYR LEU ASP
SEQRES 4 A 297 GLU THR GLU GLN TRP GLU LYS PHE GLY LEU GLU LYS ARG
SEQRES 5 A 297 GLN GLY ALA LEU GLU LEU ILE LYS LYS GLY TYR THR GLN
SEQRES 6 A 297 GLN LEU ALA PHE ARG GLN PRO SER SER ALA PHE ALA ALA
SEQRES 7 A 297 PHE VAL LYS ARG ALA PRO SER THR TRP LEU THR ALA TYR
SEQRES 8 A 297 VAL VAL LYS VAL PHE SER LEU ALA VAL ASN LEU ILE ALA
SEQRES 9 A 297 ILE ASP SER GLN VAL LEU CYS GLY ALA VAL LYS TRP LEU
SEQRES 10 A 297 ILE LEU GLU LYS GLN LYS PRO ASP GLY VAL PHE GLN GLU
SEQRES 11 A 297 ASP ALA PRO VAL ILE HIS GLN GLU MET ILE GLY GLY LEU
SEQRES 12 A 297 ARG ASN ASN ASN GLU LYS ASP MET ALA LEU THR ALA PHE
SEQRES 13 A 297 VAL LEU ILE SER LEU GLN GLU ALA LYS ASP ILE CYS GLU
SEQRES 14 A 297 GLU GLN VAL ASN SER LEU PRO GLY SER ILE THR LYS ALA
SEQRES 15 A 297 GLY ASP PHE LEU GLU ALA ASN TYR MET ASN LEU GLN ARG
SEQRES 16 A 297 SER TYR THR VAL ALA ILE ALA GLY TYR ALA LEU ALA GLN
SEQRES 17 A 297 MET GLY ARG LEU LYS GLY PRO LEU LEU ASN LYS PHE LEU
SEQRES 18 A 297 THR THR ALA LYS ASP LYS ASN ARG TRP GLU ASP PRO GLY
SEQRES 19 A 297 LYS GLN LEU TYR ASN VAL GLU ALA THR SER TYR ALA LEU
SEQRES 20 A 297 LEU ALA LEU LEU GLN LEU LYS ASP PHE ASP PHE VAL PRO
SEQRES 21 A 297 PRO VAL VAL ARG TRP LEU ASN GLU GLN ARG TYR TYR GLY
SEQRES 22 A 297 GLY GLY TYR GLY SER THR GLN ALA THR PHE MET VAL PHE
SEQRES 23 A 297 GLN ALA LEU ALA GLN TYR GLN LYS ASP ALA PRO
SEQRES 1 B 65 THR ASP ALA THR ILE LYS LYS GLU GLN LYS LEU ILE GLN
SEQRES 2 B 65 ALA GLN ASN LEU VAL ARG GLU PHE GLU LYS THR HIS THR
SEQRES 3 B 65 VAL SER ALA HIS ARG LYS ALA GLN LYS ALA VAL ASN LEU
SEQRES 4 B 65 VAL SER PHE GLU TYR LYS VAL LYS LYS MET VAL LEU GLN
SEQRES 5 B 65 GLU ARG ILE ASP ASN VAL LEU LYS GLN GLY LEU VAL ARG
SEQRES 1 C 297 GLY SER ARG SER THR ASP ALA GLU ARG LEU LYS HIS LEU
SEQRES 2 C 297 ILE VAL THR PRO SER GLY ALA GLY GLU GLN ASN MET ILE
SEQRES 3 C 297 GLY MET THR PRO THR VAL ILE ALA VAL HIS TYR LEU ASP
SEQRES 4 C 297 GLU THR GLU GLN TRP GLU LYS PHE GLY LEU GLU LYS ARG
SEQRES 5 C 297 GLN GLY ALA LEU GLU LEU ILE LYS LYS GLY TYR THR GLN
SEQRES 6 C 297 GLN LEU ALA PHE ARG GLN PRO SER SER ALA PHE ALA ALA
SEQRES 7 C 297 PHE VAL LYS ARG ALA PRO SER THR TRP LEU THR ALA TYR
SEQRES 8 C 297 VAL VAL LYS VAL PHE SER LEU ALA VAL ASN LEU ILE ALA
SEQRES 9 C 297 ILE ASP SER GLN VAL LEU CYS GLY ALA VAL LYS TRP LEU
SEQRES 10 C 297 ILE LEU GLU LYS GLN LYS PRO ASP GLY VAL PHE GLN GLU
SEQRES 11 C 297 ASP ALA PRO VAL ILE HIS GLN GLU MET ILE GLY GLY LEU
SEQRES 12 C 297 ARG ASN ASN ASN GLU LYS ASP MET ALA LEU THR ALA PHE
SEQRES 13 C 297 VAL LEU ILE SER LEU GLN GLU ALA LYS ASP ILE CYS GLU
SEQRES 14 C 297 GLU GLN VAL ASN SER LEU PRO GLY SER ILE THR LYS ALA
SEQRES 15 C 297 GLY ASP PHE LEU GLU ALA ASN TYR MET ASN LEU GLN ARG
SEQRES 16 C 297 SER TYR THR VAL ALA ILE ALA GLY TYR ALA LEU ALA GLN
SEQRES 17 C 297 MET GLY ARG LEU LYS GLY PRO LEU LEU ASN LYS PHE LEU
SEQRES 18 C 297 THR THR ALA LYS ASP LYS ASN ARG TRP GLU ASP PRO GLY
SEQRES 19 C 297 LYS GLN LEU TYR ASN VAL GLU ALA THR SER TYR ALA LEU
SEQRES 20 C 297 LEU ALA LEU LEU GLN LEU LYS ASP PHE ASP PHE VAL PRO
SEQRES 21 C 297 PRO VAL VAL ARG TRP LEU ASN GLU GLN ARG TYR TYR GLY
SEQRES 22 C 297 GLY GLY TYR GLY SER THR GLN ALA THR PHE MET VAL PHE
SEQRES 23 C 297 GLN ALA LEU ALA GLN TYR GLN LYS ASP ALA PRO
SEQRES 1 D 65 THR ASP ALA THR ILE LYS LYS GLU GLN LYS LEU ILE GLN
SEQRES 2 D 65 ALA GLN ASN LEU VAL ARG GLU PHE GLU LYS THR HIS THR
SEQRES 3 D 65 VAL SER ALA HIS ARG LYS ALA GLN LYS ALA VAL ASN LEU
SEQRES 4 D 65 VAL SER PHE GLU TYR LYS VAL LYS LYS MET VAL LEU GLN
SEQRES 5 D 65 GLU ARG ILE ASP ASN VAL LEU LYS GLN GLY LEU VAL ARG
FORMUL 5 HOH *317(H2 O)
HELIX 1 15 THR B 101 HIS B 125 1 25
HELIX 2 16 THR B 126 VAL B 140 1 15
HELIX 3 17 SER B 141 GLU B 143 5 3
HELIX 4 18 TYR B 144 GLY B 162 1 19
HELIX 5 36 ASP D 102 HIS D 125 1 24
HELIX 6 37 THR D 126 VAL D 140 1 15
HELIX 7 38 SER D 141 GLU D 143 5 3
HELIX 8 39 TYR D 144 GLY D 162 1 19
SSBOND 1 CYS A 1101 CYS A 1158 1555 1555 2.06
SSBOND 2 CYS C 1101 CYS C 1158 1555 1555 2.04
CRYST1 90.939 90.939 122.242 90.00 90.00 90.00 P 41 8
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 0.010996 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010996 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008180 0.00000
ATOM 1 N GLY A 991 7.296 -22.375 8.001 1.00 64.34 N
ATOM 2 CA GLY A 991 7.030 -23.809 8.376 1.00 64.21 C
ATOM 3 C GLY A 991 5.657 -24.278 7.916 1.00 63.80 C
ATOM 4 O GLY A 991 4.757 -23.450 7.652 1.00 63.85 O
ATOM 5 N SER A 992 5.513 -25.599 7.795 1.00 62.83 N
ATOM 6 CA SER A 992 4.238 -26.252 7.546 1.00 62.27 C
ATOM 7 C SER A 992 4.137 -27.194 8.694 1.00 62.22 C
ATOM 8 O SER A 992 5.150 -27.451 9.378 1.00 62.27 O
ATOM 9 CB SER A 992 4.254 -27.086 6.269 1.00 62.43 C
ATOM 10 OG SER A 992 4.666 -26.330 5.151 1.00 62.53 O
ATOM 11 N ARG A 993 2.927 -27.709 8.921 1.00 62.09 N
ATOM 12 CA ARG A 993 2.752 -28.843 9.835 1.00 61.81 C
ATOM 13 C ARG A 993 3.763 -29.996 9.496 1.00 60.27 C
ATOM 14 O ARG A 993 4.105 -30.270 8.328 1.00 59.17 O
ATOM 15 CB ARG A 993 1.286 -29.330 9.883 1.00 62.48 C
ATOM 16 CG ARG A 993 0.388 -28.604 10.930 1.00 67.79 C
ATOM 17 CD ARG A 993 -0.510 -27.443 10.357 1.00 76.16 C
ATOM 18 NE ARG A 993 0.252 -26.326 9.750 1.00 83.01 N
ATOM 19 CZ ARG A 993 0.282 -26.003 8.440 1.00 85.17 C
ATOM 20 NH1 ARG A 993 -0.428 -26.680 7.531 1.00 86.84 N
ATOM 21 NH2 ARG A 993 1.026 -24.978 8.031 1.00 85.03 N
ATOM 22 N SER A 994 4.283 -30.573 10.571 1.00 58.34 N
ATOM 23 CA SER A 994 5.013 -31.809 10.583 1.00 56.79 C
ATOM 24 C SER A 994 4.102 -32.958 10.097 1.00 55.02 C
ATOM 25 O SER A 994 2.904 -32.972 10.411 1.00 55.98 O
ATOM 26 CB SER A 994 5.439 -32.043 12.041 1.00 56.82 C
ATOM 27 OG SER A 994 6.340 -33.140 12.149 1.00 60.98 O
ATOM 28 N THR A 995 4.644 -33.918 9.345 1.00 51.99 N
ATOM 29 CA THR A 995 3.905 -35.171 9.026 1.00 49.79 C
ATOM 30 C THR A 995 3.605 -35.944 10.324 1.00 49.36 C
ATOM 31 O THR A 995 4.504 -36.201 11.119 1.00 47.99 O
ATOM 32 CB THR A 995 4.721 -36.096 8.067 1.00 49.07 C
ATOM 33 OG1 THR A 995 4.816 -35.484 6.774 1.00 46.82 O
ATOM 34 CG2 THR A 995 4.111 -37.483 7.974 1.00 46.51 C
ATOM 35 N ASP A 996 2.345 -36.284 10.543 1.00 48.90 N
ATOM 36 CA ASP A 996 1.952 -36.939 11.795 1.00 49.44 C
ATOM 37 C ASP A 996 2.615 -38.312 12.095 1.00 48.44 C
ATOM 38 O ASP A 996 2.476 -39.296 11.326 1.00 46.82 O
ATOM 39 CB ASP A 996 0.421 -37.039 11.866 1.00 50.05 C
ATOM 40 CG ASP A 996 -0.071 -37.777 13.119 1.00 54.69 C
ATOM 41 OD1 ASP A 996 0.500 -37.603 14.234 1.00 54.47 O
ATOM 42 OD2 ASP A 996 -1.044 -38.571 12.963 1.00 62.08 O
ATOM 43 N ALA A 997 3.278 -38.351 13.258 1.00 48.03 N
ATOM 44 CA ALA A 997 3.904 -39.549 13.840 1.00 48.54 C
ATOM 45 C ALA A 997 3.154 -40.819 13.656 1.00 49.62 C
ATOM 46 O ALA A 997 3.776 -41.854 13.385 1.00 49.92 O
ATOM 47 CB ALA A 997 4.189 -39.382 15.307 1.00 47.87 C
ATOM 48 N GLU A 998 1.838 -40.759 13.824 1.00 50.41 N
ATOM 49 CA GLU A 998 1.034 -41.955 13.692 1.00 52.61 C
ATOM 50 C GLU A 998 1.177 -42.588 12.296 1.00 52.14 C
ATOM 51 O GLU A 998 1.213 -43.805 12.170 1.00 52.39 O
ATOM 52 CB GLU A 998 -0.425 -41.673 14.039 1.00 52.74 C
ATOM 53 CG GLU A 998 -0.966 -42.669 15.069 1.00 58.08 C
ATOM 54 CD GLU A 998 -0.264 -42.594 16.452 1.00 62.07 C
ATOM 55 OE1 GLU A 998 -0.256 -41.487 17.059 1.00 63.81 O
ATOM 56 OE2 GLU A 998 0.261 -43.639 16.927 1.00 61.71 O
ATOM 57 N ARG A 999 1.296 -41.754 11.263 1.00 52.10 N
ATOM 58 CA ARG A 999 1.496 -42.257 9.890 1.00 51.49 C
ATOM 59 C ARG A 999 2.841 -42.997 9.756 1.00 49.96 C
ATOM 60 O ARG A 999 3.042 -43.715 8.789 1.00 48.40 O
ATOM 61 CB ARG A 999 1.472 -41.111 8.843 1.00 52.29 C
ATOM 62 CG ARG A 999 0.287 -40.140 8.890 1.00 55.57 C
ATOM 63 CD ARG A 999 -1.018 -40.886 8.843 1.00 61.67 C
ATOM 64 NE ARG A 999 -2.154 -39.986 8.623 1.00 65.49 N
ATOM 65 CZ ARG A 999 -3.369 -40.393 8.244 1.00 65.82 C
ATOM 66 NH1 ARG A 999 -3.607 -41.689 8.027 1.00 62.97 N
ATOM 67 NH2 ARG A 999 -4.349 -39.498 8.065 1.00 64.36 N
ATOM 68 N LEU A1000 3.759 -42.773 10.708 1.00 48.25 N
ATOM 69 CA LEU A1000 5.105 -43.372 10.638 1.00 47.14 C
ATOM 70 C LEU A1000 5.352 -44.645 11.461 1.00 45.65 C
ATOM 71 O LEU A1000 6.425 -45.216 11.343 1.00 45.09 O
ATOM 72 CB LEU A1000 6.193 -42.345 10.973 1.00 46.97 C
ATOM 73 CG LEU A1000 6.152 -40.971 10.314 1.00 46.24 C
ATOM 74 CD1 LEU A1000 7.552 -40.437 10.368 1.00 46.09 C
ATOM 75 CD2 LEU A1000 5.671 -41.076 8.888 1.00 49.34 C
ATOM 76 N LYS A1001 4.389 -45.084 12.274 1.00 44.17 N
ATOM 77 CA LYS A1001 4.620 -46.254 13.159 1.00 44.95 C
ATOM 78 C LYS A1001 5.089 -47.507 12.447 1.00 42.07 C
ATOM 79 O LYS A1001 5.967 -48.245 12.937 1.00 42.50 O
ATOM 80 CB LYS A1001 3.437 -46.577 14.078 1.00 44.73 C
ATOM 81 CG LYS A1001 2.013 -46.217 13.543 1.00 49.06 C
ATOM 82 CD LYS A1001 0.925 -46.629 14.557 1.00 50.16 C
ATOM 83 CE LYS A1001 1.585 -47.283 15.812 1.00 58.05 C
ATOM 84 NZ LYS A1001 2.562 -46.374 16.563 1.00 61.80 N
ATOM 85 N HIS A1002 4.572 -47.737 11.260 1.00 38.96 N
ATOM 86 CA HIS A1002 4.961 -48.931 10.583 1.00 36.28 C
ATOM 87 C HIS A1002 6.449 -48.935 10.130 1.00 34.70 C
ATOM 88 O HIS A1002 6.885 -49.916 9.588 1.00 33.42 O
ATOM 89 CB HIS A1002 4.065 -49.085 9.388 1.00 35.83 C
ATOM 90 CG HIS A1002 4.355 -48.089 8.322 1.00 35.74 C
ATOM 91 ND1 HIS A1002 3.842 -46.812 8.338 1.00 32.79 N
ATOM 92 CD2 HIS A1002 5.142 -48.173 7.219 1.00 35.64 C
ATOM 93 CE1 HIS A1002 4.282 -46.157 7.276 1.00 35.69 C
ATOM 94 NE2 HIS A1002 5.057 -46.967 6.572 1.00 34.49 N
ATOM 95 N LEU A1003 7.189 -47.833 10.305 1.00 32.69 N
ATOM 96 CA LEU A1003 8.590 -47.708 9.843 1.00 31.96 C
ATOM 97 C LEU A1003 9.592 -48.282 10.833 1.00 31.99 C
ATOM 98 O LEU A1003 10.822 -48.398 10.529 1.00 30.86 O
ATOM 99 CB LEU A1003 8.984 -46.247 9.463 1.00 31.09 C
ATOM 100 CG LEU A1003 8.128 -45.680 8.298 1.00 30.20 C
ATOM 101 CD1 LEU A1003 8.357 -44.124 8.102 1.00 32.70 C
ATOM 102 CD2 LEU A1003 8.328 -46.458 6.962 1.00 27.03 C
ATOM 103 N ILE A1004 9.083 -48.644 12.006 1.00 31.44 N
ATOM 104 CA ILE A1004 9.909 -49.257 13.057 1.00 32.44 C
ATOM 105 C ILE A1004 9.928 -50.763 12.892 1.00 34.00 C
ATOM 106 O ILE A1004 9.000 -51.499 13.326 1.00 35.73 O
ATOM 107 CB ILE A1004 9.456 -48.772 14.411 1.00 32.85 C
ATOM 108 CG1 ILE A1004 9.670 -47.229 14.468 1.00 34.45 C
ATOM 109 CG2 ILE A1004 10.230 -49.500 15.538 1.00 32.83 C
ATOM 110 CD1 ILE A1004 8.673 -46.513 15.449 1.00 40.50 C
ATOM 111 N VAL A1005 11.034 -51.223 12.319 1.00 33.44 N
ATOM 112 CA VAL A1005 11.121 -52.477 11.583 1.00 35.52 C
ATOM 113 C VAL A1005 12.343 -53.270 12.107 1.00 35.25 C
ATOM 114 O VAL A1005 13.326 -52.647 12.484 1.00 35.98 O
ATOM 115 CB VAL A1005 11.243 -52.104 10.081 1.00 34.38 C
ATOM 116 CG1 VAL A1005 12.138 -52.981 9.322 1.00 37.83 C
ATOM 117 CG2 VAL A1005 9.833 -51.999 9.463 1.00 36.32 C
ATOM 118 N THR A1006 12.281 -54.604 12.133 1.00 33.67 N
ATOM 119 CA THR A1006 13.458 -55.409 12.468 1.00 34.67 C
ATOM 120 C THR A1006 14.404 -55.493 11.244 1.00 35.59 C
ATOM 121 O THR A1006 13.930 -55.679 10.142 1.00 36.85 O
ATOM 122 CB THR A1006 13.034 -56.839 12.854 1.00 33.25 C
ATOM 123 OG1 THR A1006 12.232 -56.773 14.029 1.00 35.77 O
ATOM 124 CG2 THR A1006 14.248 -57.715 13.173 1.00 31.72 C
ATOM 125 N PRO A1007 15.720 -55.278 11.395 1.00 35.37 N
ATOM 126 CA PRO A1007 16.506 -55.567 10.147 1.00 35.27 C
ATOM 127 C PRO A1007 16.777 -57.048 10.074 1.00 34.92 C
ATOM 128 O PRO A1007 17.020 -57.661 11.111 1.00 35.47 O
ATOM 129 CB PRO A1007 17.837 -54.799 10.343 1.00 34.74 C
ATOM 130 CG PRO A1007 17.892 -54.414 11.762 1.00 35.89 C
ATOM 131 CD PRO A1007 16.562 -54.768 12.484 1.00 36.29 C
ATOM 132 N SER A1008 16.697 -57.637 8.901 1.00 33.59 N
ATOM 133 CA SER A1008 17.054 -59.028 8.765 1.00 34.40 C
ATOM 134 C SER A1008 17.615 -59.247 7.360 1.00 34.48 C
ATOM 135 O SER A1008 17.674 -58.321 6.515 1.00 34.63 O
ATOM 136 CB SER A1008 15.840 -59.976 9.003 1.00 35.26 C
ATOM 137 OG SER A1008 14.755 -59.618 8.178 1.00 34.36 O
ATOM 138 N GLY A1009 17.958 -60.492 7.092 1.00 32.37 N
ATOM 139 CA GLY A1009 18.624 -60.828 5.853 1.00 31.43 C
ATOM 140 C GLY A1009 20.107 -60.513 5.896 1.00 30.84 C
ATOM 141 O GLY A1009 20.753 -60.312 7.019 1.00 29.09 O
ATOM 142 N ALA A1010 20.659 -60.492 4.689 1.00 30.54 N
ATOM 143 CA ALA A1010 22.117 -60.366 4.478 1.00 31.87 C
ATOM 144 C ALA A1010 22.548 -58.895 4.234 1.00 31.02 C
ATOM 145 O ALA A1010 21.833 -57.992 4.583 1.00 31.20 O
ATOM 146 CB ALA A1010 22.559 -61.298 3.349 1.00 29.45 C
ATOM 147 N GLY A1011 23.733 -58.694 3.677 1.00 32.22 N
ATOM 148 CA GLY A1011 24.315 -57.372 3.348 1.00 31.13 C
ATOM 149 C GLY A1011 23.445 -56.243 2.792 1.00 30.49 C
ATOM 150 O GLY A1011 23.658 -55.030 3.095 1.00 29.11 O
ATOM 151 N GLU A1012 22.499 -56.622 1.962 1.00 28.87 N
ATOM 152 CA GLU A1012 21.642 -55.671 1.273 1.00 28.65 C
ATOM 153 C GLU A1012 20.381 -55.537 2.033 1.00 29.76 C
ATOM 154 O GLU A1012 19.930 -54.437 2.375 1.00 30.28 O
ATOM 155 CB GLU A1012 21.322 -56.195 -0.153 1.00 27.92 C
ATOM 156 CG GLU A1012 22.495 -56.076 -1.092 1.00 26.13 C
ATOM 157 CD GLU A1012 22.190 -56.549 -2.503 1.00 27.79 C
ATOM 158 OE1 GLU A1012 21.016 -56.570 -2.895 1.00 29.22 O
ATOM 159 OE2 GLU A1012 23.163 -56.891 -3.250 1.00 27.93 O
ATOM 160 N GLN A1013 19.764 -56.696 2.301 1.00 31.82 N
ATOM 161 CA GLN A1013 18.448 -56.673 2.858 1.00 32.14 C
ATOM 162 C GLN A1013 18.542 -56.152 4.328 1.00 31.03 C
ATOM 163 O GLN A1013 17.603 -55.575 4.828 1.00 29.82 O
ATOM 164 CB GLN A1013 17.934 -58.088 2.828 1.00 33.36 C
ATOM 165 CG GLN A1013 16.604 -58.203 3.525 1.00 38.56 C
ATOM 166 CD GLN A1013 15.505 -58.167 2.460 1.00 48.13 C
ATOM 167 OE1 GLN A1013 15.532 -59.034 1.508 1.00 49.98 O
ATOM 168 NE2 GLN A1013 14.578 -57.133 2.555 1.00 39.15 N
ATOM 169 N ASN A1014 19.663 -56.395 5.018 1.00 29.05 N
ATOM 170 CA ASN A1014 19.815 -55.792 6.324 1.00 30.28 C
ATOM 171 C ASN A1014 19.698 -54.229 6.221 1.00 30.31 C
ATOM 172 O ASN A1014 19.101 -53.584 7.098 1.00 29.90 O
ATOM 173 CB ASN A1014 21.141 -56.214 6.951 1.00 29.72 C
ATOM 174 CG ASN A1014 21.304 -55.700 8.397 1.00 33.02 C
ATOM 175 OD1 ASN A1014 20.604 -56.159 9.303 1.00 31.19 O
ATOM 176 ND2 ASN A1014 22.181 -54.716 8.597 1.00 26.64 N
ATOM 177 N MET A1015 20.166 -53.646 5.105 1.00 29.36 N
ATOM 178 CA MET A1015 20.069 -52.166 4.945 1.00 30.24 C
ATOM 179 C MET A1015 18.688 -51.728 4.539 1.00 29.97 C
ATOM 180 O MET A1015 18.278 -50.658 4.927 1.00 29.84 O
ATOM 181 CB MET A1015 21.152 -51.577 4.015 1.00 28.13 C
ATOM 182 CG MET A1015 22.621 -51.727 4.580 1.00 28.09 C
ATOM 183 SD MET A1015 22.837 -51.037 6.244 1.00 31.39 S
ATOM 184 CE MET A1015 22.638 -49.265 5.892 1.00 24.36 C
ATOM 185 N ILE A1016 17.966 -52.584 3.812 1.00 30.58 N
ATOM 186 CA ILE A1016 16.559 -52.333 3.523 1.00 31.94 C
ATOM 187 C ILE A1016 15.781 -52.254 4.863 1.00 33.03 C
ATOM 188 O ILE A1016 14.980 -51.326 5.052 1.00 33.14 O
ATOM 189 CB ILE A1016 15.963 -53.381 2.528 1.00 32.88 C
ATOM 190 CG1 ILE A1016 16.621 -53.264 1.152 1.00 33.26 C
ATOM 191 CG2 ILE A1016 14.425 -53.355 2.424 1.00 31.87 C
ATOM 192 CD1 ILE A1016 16.464 -54.532 0.237 1.00 29.75 C
ATOM 193 N GLY A1017 16.072 -53.160 5.816 1.00 33.33 N
ATOM 194 CA GLY A1017 15.434 -53.119 7.119 1.00 31.71 C
ATOM 195 C GLY A1017 15.833 -51.924 7.988 1.00 32.56 C
ATOM 196 O GLY A1017 14.989 -51.330 8.713 1.00 32.51 O
ATOM 197 N MET A1018 17.103 -51.537 7.907 1.00 31.95 N
ATOM 198 CA MET A1018 17.645 -50.486 8.746 1.00 34.24 C
ATOM 199 C MET A1018 17.132 -49.082 8.305 1.00 34.22 C
ATOM 200 O MET A1018 16.826 -48.215 9.137 1.00 33.64 O
ATOM 201 CB MET A1018 19.165 -50.543 8.659 1.00 34.04 C
ATOM 202 CG MET A1018 19.832 -50.090 9.878 1.00 35.51 C
ATOM 203 SD MET A1018 21.628 -50.062 9.734 1.00 39.07 S
ATOM 204 CE MET A1018 21.819 -48.832 11.020 1.00 33.80 C
ATOM 205 N THR A1019 17.045 -48.876 6.985 1.00 32.99 N
ATOM 206 CA THR A1019 16.599 -47.582 6.400 1.00 31.49 C
ATOM 207 C THR A1019 15.345 -46.887 7.116 1.00 31.72 C
ATOM 208 O THR A1019 15.444 -45.743 7.635 1.00 32.59 O
ATOM 209 CB THR A1019 16.353 -47.803 4.888 1.00 30.42 C
ATOM 210 OG1 THR A1019 17.620 -48.095 4.254 1.00 28.74 O
ATOM 211 CG2 THR A1019 15.592 -46.601 4.268 1.00 32.25 C
ATOM 212 N PRO A1020 14.173 -47.567 7.133 1.00 30.77 N
ATOM 213 CA PRO A1020 12.972 -46.921 7.666 1.00 30.70 C
ATOM 214 C PRO A1020 13.079 -46.511 9.140 1.00 31.29 C
ATOM 215 O PRO A1020 12.661 -45.426 9.520 1.00 31.75 O
ATOM 216 CB PRO A1020 11.876 -47.930 7.394 1.00 31.25 C
ATOM 217 CG PRO A1020 12.621 -49.215 7.399 1.00 32.37 C
ATOM 218 CD PRO A1020 13.913 -48.958 6.738 1.00 29.03 C
ATOM 219 N THR A1021 13.706 -47.321 9.961 1.00 32.51 N
ATOM 220 CA THR A1021 13.744 -47.026 11.402 1.00 32.92 C
ATOM 221 C THR A1021 14.767 -45.935 11.612 1.00 32.55 C
ATOM 222 O THR A1021 14.586 -45.061 12.449 1.00 32.73 O
ATOM 223 CB THR A1021 14.227 -48.240 12.159 1.00 30.84 C
ATOM 224 OG1 THR A1021 13.534 -49.349 11.626 1.00 34.14 O
ATOM 225 CG2 THR A1021 14.020 -48.097 13.654 1.00 33.28 C
ATOM 226 N VAL A1022 15.890 -46.039 10.909 1.00 33.01 N
ATOM 227 CA VAL A1022 16.823 -44.944 10.949 1.00 32.27 C
ATOM 228 C VAL A1022 16.120 -43.668 10.635 1.00 31.20 C
ATOM 229 O VAL A1022 16.152 -42.743 11.446 1.00 31.05 O
ATOM 230 CB VAL A1022 18.138 -45.176 10.147 1.00 32.64 C
ATOM 231 CG1 VAL A1022 18.927 -43.862 10.036 1.00 30.41 C
ATOM 232 CG2 VAL A1022 18.993 -46.201 10.895 1.00 31.55 C
ATOM 233 N ILE A1023 15.406 -43.619 9.515 1.00 31.72 N
ATOM 234 CA ILE A1023 14.928 -42.319 9.065 1.00 30.12 C
ATOM 235 C ILE A1023 13.722 -41.846 9.873 1.00 31.36 C
ATOM 236 O ILE A1023 13.503 -40.623 10.050 1.00 31.12 O
ATOM 237 CB ILE A1023 14.637 -42.282 7.545 1.00 30.96 C
ATOM 238 CG1 ILE A1023 14.715 -40.804 6.971 1.00 28.91 C
ATOM 239 CG2 ILE A1023 13.309 -42.941 7.217 1.00 29.17 C
ATOM 240 CD1 ILE A1023 16.093 -40.222 7.032 1.00 27.33 C
ATOM 241 N ALA A1024 12.887 -42.782 10.300 1.00 31.05 N
ATOM 242 CA ALA A1024 11.717 -42.433 11.126 1.00 32.31 C
ATOM 243 C ALA A1024 12.199 -41.821 12.437 1.00 33.44 C
ATOM 244 O ALA A1024 11.652 -40.811 12.843 1.00 33.88 O
ATOM 245 CB ALA A1024 10.855 -43.673 11.428 1.00 32.28 C
ATOM 246 N VAL A1025 13.225 -42.415 13.095 1.00 34.29 N
ATOM 247 CA VAL A1025 13.744 -41.782 14.336 1.00 35.84 C
ATOM 248 C VAL A1025 14.322 -40.402 14.067 1.00 36.99 C
ATOM 249 O VAL A1025 13.989 -39.417 14.791 1.00 38.93 O
ATOM 250 CB VAL A1025 14.739 -42.666 15.140 1.00 36.48 C
ATOM 251 CG1 VAL A1025 15.215 -41.909 16.423 1.00 36.86 C
ATOM 252 CG2 VAL A1025 14.092 -44.005 15.519 1.00 35.10 C
ATOM 253 N HIS A1026 15.171 -40.306 13.029 1.00 36.76 N
ATOM 254 CA HIS A1026 15.645 -38.997 12.529 1.00 36.20 C
ATOM 255 C HIS A1026 14.496 -38.011 12.380 1.00 36.42 C
ATOM 256 O HIS A1026 14.541 -36.924 12.928 1.00 36.42 O
ATOM 257 CB HIS A1026 16.337 -39.145 11.178 1.00 34.93 C
ATOM 258 CG HIS A1026 16.905 -37.865 10.630 1.00 34.13 C
ATOM 259 ND1 HIS A1026 18.097 -37.318 11.074 1.00 31.54 N
ATOM 260 CD2 HIS A1026 16.483 -37.066 9.619 1.00 32.14 C
ATOM 261 CE1 HIS A1026 18.379 -36.241 10.364 1.00 31.19 C
ATOM 262 NE2 HIS A1026 17.413 -36.058 9.479 1.00 31.30 N
ATOM 263 N TYR A1027 13.498 -38.356 11.569 1.00 36.78 N
ATOM 264 CA TYR A1027 12.369 -37.426 11.340 1.00 37.21 C
ATOM 265 C TYR A1027 11.604 -37.048 12.633 1.00 38.48 C
ATOM 266 O TYR A1027 11.279 -35.902 12.824 1.00 39.03 O
ATOM 267 CB TYR A1027 11.385 -37.977 10.340 1.00 35.68 C
ATOM 268 CG TYR A1027 10.293 -36.951 9.994 1.00 37.75 C
ATOM 269 CD1 TYR A1027 10.560 -35.832 9.177 1.00 34.34 C
ATOM 270 CD2 TYR A1027 8.979 -37.108 10.496 1.00 38.11 C
ATOM 271 CE1 TYR A1027 9.553 -34.895 8.887 1.00 31.98 C
ATOM 272 CE2 TYR A1027 7.974 -36.199 10.197 1.00 36.49 C
ATOM 273 CZ TYR A1027 8.260 -35.090 9.406 1.00 37.00 C
ATOM 274 OH TYR A1027 7.211 -34.228 9.140 1.00 33.46 O
ATOM 275 N LEU A1028 11.324 -38.006 13.498 1.00 39.59 N
ATOM 276 CA LEU A1028 10.579 -37.735 14.737 1.00 41.09 C
ATOM 277 C LEU A1028 11.354 -36.951 15.739 1.00 42.03 C
ATOM 278 O LEU A1028 10.767 -36.194 16.486 1.00 42.43 O
ATOM 279 CB LEU A1028 10.116 -39.041 15.406 1.00 40.85 C
ATOM 280 CG LEU A1028 9.003 -39.708 14.604 1.00 40.64 C
ATOM 281 CD1 LEU A1028 8.461 -40.876 15.428 1.00 43.95 C
ATOM 282 CD2 LEU A1028 7.927 -38.749 14.359 1.00 42.32 C
ATOM 283 N ASP A1029 12.673 -37.168 15.776 1.00 43.92 N
ATOM 284 CA ASP A1029 13.565 -36.439 16.673 1.00 43.86 C
ATOM 285 C ASP A1029 13.581 -34.988 16.263 1.00 45.37 C
ATOM 286 O ASP A1029 13.505 -34.070 17.100 1.00 44.89 O
ATOM 287 CB ASP A1029 14.975 -36.924 16.485 1.00 44.10 C
ATOM 288 CG ASP A1029 15.314 -38.075 17.358 1.00 43.40 C
ATOM 289 OD1 ASP A1029 14.414 -38.652 17.969 1.00 37.44 O
ATOM 290 OD2 ASP A1029 16.509 -38.409 17.378 1.00 43.20 O
ATOM 291 N GLU A1030 13.720 -34.776 14.958 1.00 45.84 N
ATOM 292 CA GLU A1030 13.760 -33.407 14.486 1.00 47.75 C
ATOM 293 C GLU A1030 12.449 -32.650 14.737 1.00 47.05 C
ATOM 294 O GLU A1030 12.472 -31.538 15.218 1.00 46.69 O
ATOM 295 CB GLU A1030 14.229 -33.317 13.036 1.00 47.66 C
ATOM 296 CG GLU A1030 15.321 -32.248 12.927 1.00 52.74 C
ATOM 297 CD GLU A1030 14.692 -30.900 12.878 1.00 55.27 C
ATOM 298 OE1 GLU A1030 13.557 -30.896 12.348 1.00 59.44 O
ATOM 299 OE2 GLU A1030 15.256 -29.886 13.340 1.00 53.75 O
ATOM 300 N THR A1031 11.312 -33.284 14.467 1.00 47.67 N
ATOM 301 CA THR A1031 10.031 -32.595 14.560 1.00 47.13 C
ATOM 302 C THR A1031 9.435 -32.749 15.954 1.00 48.88 C
ATOM 303 O THR A1031 8.295 -32.326 16.194 1.00 47.98 O
ATOM 304 CB THR A1031 9.055 -33.096 13.480 1.00 47.07 C
ATOM 305 OG1 THR A1031 8.852 -34.504 13.642 1.00 43.57 O
ATOM 306 CG2 THR A1031 9.612 -32.812 12.065 1.00 44.28 C
ATOM 307 N GLU A1032 10.201 -33.391 16.854 1.00 50.38 N
ATOM 308 CA GLU A1032 9.878 -33.404 18.281 1.00 52.15 C
ATOM 309 C GLU A1032 8.512 -34.021 18.586 1.00 52.08 C
ATOM 310 O GLU A1032 7.711 -33.390 19.235 1.00 52.66 O
ATOM 311 CB GLU A1032 9.920 -31.957 18.825 1.00 52.18 C
ATOM 312 CG GLU A1032 11.057 -31.681 19.784 1.00 56.26 C
ATOM 313 CD GLU A1032 11.647 -30.270 19.649 1.00 60.58 C
ATOM 314 OE1 GLU A1032 12.836 -30.091 20.020 1.00 61.83 O
ATOM 315 OE2 GLU A1032 10.951 -29.349 19.155 1.00 61.91 O
ATOM 316 N GLN A1033 8.239 -35.234 18.114 1.00 52.24 N
ATOM 317 CA GLN A1033 6.905 -35.824 18.247 1.00 51.89 C
ATOM 318 C GLN A1033 6.935 -36.991 19.218 1.00 53.07 C
ATOM 319 O GLN A1033 6.096 -37.862 19.187 1.00 53.62 O
ATOM 320 CB GLN A1033 6.356 -36.273 16.874 1.00 51.18 C
ATOM 321 CG GLN A1033 6.063 -35.138 15.939 1.00 49.15 C
ATOM 322 CD GLN A1033 5.340 -35.555 14.649 1.00 51.58 C
ATOM 323 OE1 GLN A1033 4.189 -36.054 14.668 1.00 45.14 O
ATOM 324 NE2 GLN A1033 6.008 -35.306 13.496 1.00 50.66 N
ATOM 325 N TRP A1034 7.927 -37.039 20.076 1.00 54.90 N
ATOM 326 CA TRP A1034 8.126 -38.270 20.799 1.00 56.71 C
ATOM 327 C TRP A1034 7.288 -38.311 22.069 1.00 59.51 C
ATOM 328 O TRP A1034 6.802 -39.400 22.451 1.00 59.85 O
ATOM 329 CB TRP A1034 9.593 -38.476 21.117 1.00 54.72 C
ATOM 330 CG TRP A1034 10.371 -39.048 19.989 1.00 53.17 C
ATOM 331 CD1 TRP A1034 11.343 -38.417 19.264 1.00 50.20 C
ATOM 332 CD2 TRP A1034 10.272 -40.388 19.461 1.00 50.93 C
ATOM 333 NE1 TRP A1034 11.852 -39.283 18.319 1.00 50.80 N
ATOM 334 CE2 TRP A1034 11.222 -40.495 18.420 1.00 50.08 C
ATOM 335 CE3 TRP A1034 9.491 -41.502 19.783 1.00 48.58 C
ATOM 336 CZ2 TRP A1034 11.404 -41.666 17.695 1.00 49.87 C
ATOM 337 CZ3 TRP A1034 9.651 -42.645 19.065 1.00 50.91 C
ATOM 338 CH2 TRP A1034 10.614 -42.731 18.020 1.00 51.53 C
ATOM 339 N GLU A1035 7.152 -37.138 22.715 1.00 62.57 N
ATOM 340 CA GLU A1035 6.304 -36.964 23.913 1.00 65.08 C
ATOM 341 C GLU A1035 4.873 -37.305 23.545 1.00 66.33 C
ATOM 342 O GLU A1035 4.282 -38.191 24.180 1.00 67.16 O
ATOM 343 CB GLU A1035 6.407 -35.520 24.530 1.00 65.54 C
ATOM 344 N LYS A1036 4.344 -36.658 22.497 1.00 67.21 N
ATOM 345 CA LYS A1036 2.996 -36.958 21.989 1.00 68.40 C
ATOM 346 C LYS A1036 2.971 -38.145 21.000 1.00 69.18 C
ATOM 347 O LYS A1036 2.417 -38.039 19.881 1.00 69.98 O
ATOM 348 CB LYS A1036 2.338 -35.691 21.368 1.00 68.43 C
ATOM 349 N PHE A1037 3.565 -39.272 21.409 1.00 69.14 N
ATOM 350 CA PHE A1037 3.596 -40.483 20.573 1.00 68.89 C
ATOM 351 C PHE A1037 4.251 -41.713 21.231 1.00 68.97 C
ATOM 352 O PHE A1037 3.917 -42.868 20.902 1.00 69.57 O
ATOM 353 CB PHE A1037 4.250 -40.206 19.225 1.00 68.34 C
ATOM 354 CG PHE A1037 4.660 -41.437 18.507 1.00 69.13 C
ATOM 355 CD1 PHE A1037 3.701 -42.311 17.982 1.00 70.38 C
ATOM 356 CD2 PHE A1037 6.007 -41.761 18.371 1.00 68.42 C
ATOM 357 CE1 PHE A1037 4.096 -43.479 17.319 1.00 70.21 C
ATOM 358 CE2 PHE A1037 6.401 -42.937 17.715 1.00 67.17 C
ATOM 359 CZ PHE A1037 5.459 -43.782 17.195 1.00 68.60 C
ATOM 360 N GLY A1038 5.204 -41.493 22.134 1.00 68.69 N
ATOM 361 CA GLY A1038 5.798 -42.629 22.832 1.00 67.46 C
ATOM 362 C GLY A1038 7.294 -42.562 22.986 1.00 66.40 C
ATOM 363 O GLY A1038 8.034 -43.369 22.427 1.00 66.65 O
ATOM 364 N LEU A1039 7.727 -41.605 23.784 1.00 65.48 N
ATOM 365 CA LEU A1039 9.119 -41.480 24.156 1.00 65.01 C
ATOM 366 C LEU A1039 9.831 -42.830 24.333 1.00 63.81 C
ATOM 367 O LEU A1039 10.972 -42.999 23.917 1.00 64.06 O
ATOM 368 CB LEU A1039 9.208 -40.671 25.429 1.00 65.07 C
ATOM 369 CG LEU A1039 10.144 -39.470 25.497 1.00 67.26 C
ATOM 370 CD1 LEU A1039 9.696 -38.592 26.680 1.00 66.59 C
ATOM 371 CD2 LEU A1039 11.612 -39.910 25.607 1.00 68.67 C
ATOM 372 N GLU A1040 9.137 -43.798 24.912 1.00 62.85 N
ATOM 373 CA GLU A1040 9.722 -45.112 25.204 1.00 61.39 C
ATOM 374 C GLU A1040 9.838 -46.047 23.972 1.00 59.50 C
ATOM 375 O GLU A1040 10.696 -46.931 23.950 1.00 58.32 O
ATOM 376 CB GLU A1040 9.001 -45.780 26.398 1.00 62.49 C
ATOM 377 CG GLU A1040 7.578 -45.203 26.752 1.00 65.53 C
ATOM 378 CD GLU A1040 6.502 -45.328 25.600 1.00 69.91 C
ATOM 379 OE1 GLU A1040 6.361 -46.397 24.930 1.00 68.67 O
ATOM 380 OE2 GLU A1040 5.763 -44.332 25.386 1.00 71.71 O
ATOM 381 N LYS A1041 8.991 -45.838 22.958 1.00 57.35 N
ATOM 382 CA LYS A1041 9.137 -46.539 21.672 1.00 56.42 C
ATOM 383 C LYS A1041 10.428 -46.081 20.974 1.00 54.12 C
ATOM 384 O LYS A1041 10.961 -46.814 20.139 1.00 53.72 O
ATOM 385 CB LYS A1041 7.947 -46.298 20.719 1.00 56.47 C
ATOM 386 CG LYS A1041 6.570 -46.136 21.388 1.00 59.36 C
ATOM 387 CD LYS A1041 5.432 -45.972 20.350 1.00 59.49 C
ATOM 388 CE LYS A1041 4.098 -46.665 20.790 1.00 61.67 C
ATOM 389 NZ LYS A1041 3.194 -46.881 19.576 1.00 61.44 N
ATOM 390 N ARG A1042 10.925 -44.880 21.315 1.00 51.55 N
ATOM 391 CA ARG A1042 12.201 -44.402 20.768 1.00 48.46 C
ATOM 392 C ARG A1042 13.331 -45.330 21.146 1.00 47.72 C
ATOM 393 O ARG A1042 14.154 -45.653 20.291 1.00 47.63 O
ATOM 394 CB ARG A1042 12.515 -42.948 21.159 1.00 48.35 C
ATOM 395 CG ARG A1042 13.631 -42.277 20.326 1.00 48.28 C
ATOM 396 CD ARG A1042 13.944 -40.812 20.750 1.00 46.81 C
ATOM 397 NE ARG A1042 15.118 -40.264 20.047 1.00 44.78 N
ATOM 398 CZ ARG A1042 16.379 -40.265 20.518 1.00 46.43 C
ATOM 399 NH1 ARG A1042 16.648 -40.779 21.725 1.00 41.32 N
ATOM 400 NH2 ARG A1042 17.395 -39.755 19.788 1.00 41.27 N
ATOM 401 N GLN A1043 13.350 -45.805 22.395 1.00 46.09 N
ATOM 402 CA GLN A1043 14.463 -46.613 22.854 1.00 45.19 C
ATOM 403 C GLN A1043 14.477 -47.946 22.135 1.00 44.25 C
ATOM 404 O GLN A1043 15.565 -48.513 21.774 1.00 43.85 O
ATOM 405 CB GLN A1043 14.427 -46.817 24.385 1.00 46.00 C
ATOM 406 CG GLN A1043 15.732 -47.460 24.940 1.00 48.62 C
ATOM 407 CD GLN A1043 17.016 -46.687 24.507 1.00 53.18 C
ATOM 408 OE1 GLN A1043 17.170 -45.508 24.816 1.00 55.13 O
ATOM 409 NE2 GLN A1043 17.913 -47.358 23.781 1.00 54.30 N
ATOM 410 N GLY A1044 13.258 -48.450 21.944 1.00 42.05 N
ATOM 411 CA GLY A1044 13.031 -49.638 21.142 1.00 40.56 C
ATOM 412 C GLY A1044 13.536 -49.472 19.718 1.00 38.23 C
ATOM 413 O GLY A1044 14.234 -50.338 19.211 1.00 38.38 O
ATOM 414 N ALA A1045 13.201 -48.370 19.063 1.00 38.35 N
ATOM 415 CA ALA A1045 13.777 -48.098 17.732 1.00 38.89 C
ATOM 416 C ALA A1045 15.321 -48.036 17.826 1.00 38.26 C
ATOM 417 O ALA A1045 16.014 -48.647 17.004 1.00 38.27 O
ATOM 418 CB ALA A1045 13.204 -46.845 17.146 1.00 38.81 C
ATOM 419 N LEU A1046 15.854 -47.402 18.878 1.00 37.69 N
ATOM 420 CA LEU A1046 17.325 -47.240 19.014 1.00 38.50 C
ATOM 421 C LEU A1046 17.996 -48.590 19.090 1.00 38.98 C
ATOM 422 O LEU A1046 19.058 -48.817 18.475 1.00 38.84 O
ATOM 423 CB LEU A1046 17.716 -46.415 20.250 1.00 38.31 C
ATOM 424 CG LEU A1046 18.077 -44.945 20.156 1.00 38.40 C
ATOM 425 CD1 LEU A1046 17.874 -44.332 18.759 1.00 38.80 C
ATOM 426 CD2 LEU A1046 17.389 -44.152 21.235 1.00 36.62 C
ATOM 427 N GLU A1047 17.354 -49.508 19.815 1.00 38.52 N
ATOM 428 CA GLU A1047 17.809 -50.884 19.844 1.00 38.52 C
ATOM 429 C GLU A1047 17.768 -51.609 18.517 1.00 36.68 C
ATOM 430 O GLU A1047 18.690 -52.361 18.169 1.00 36.60 O
ATOM 431 CB GLU A1047 16.938 -51.665 20.788 1.00 40.54 C
ATOM 432 CG GLU A1047 17.760 -52.618 21.458 1.00 47.74 C
ATOM 433 CD GLU A1047 18.590 -51.898 22.503 1.00 57.77 C
ATOM 434 OE1 GLU A1047 19.770 -52.319 22.729 1.00 60.65 O
ATOM 435 OE2 GLU A1047 18.041 -50.912 23.079 1.00 60.06 O
ATOM 436 N LEU A1048 16.697 -51.412 17.763 1.00 34.92 N
ATOM 437 CA LEU A1048 16.663 -51.980 16.410 1.00 34.62 C
ATOM 438 C LEU A1048 17.783 -51.477 15.454 1.00 35.54 C
ATOM 439 O LEU A1048 18.368 -52.256 14.652 1.00 36.12 O
ATOM 440 CB LEU A1048 15.269 -51.744 15.798 1.00 34.84 C
ATOM 441 CG LEU A1048 14.159 -52.558 16.524 1.00 35.76 C
ATOM 442 CD1 LEU A1048 12.758 -52.012 16.242 1.00 33.06 C
ATOM 443 CD2 LEU A1048 14.236 -54.119 16.249 1.00 28.76 C
ATOM 444 N ILE A1049 18.040 -50.166 15.526 1.00 35.21 N
ATOM 445 CA ILE A1049 19.111 -49.472 14.755 1.00 35.21 C
ATOM 446 C ILE A1049 20.516 -50.015 15.137 1.00 36.52 C
ATOM 447 O ILE A1049 21.305 -50.424 14.272 1.00 35.79 O
ATOM 448 CB ILE A1049 19.010 -47.907 14.989 1.00 34.17 C
ATOM 449 CG1 ILE A1049 17.636 -47.428 14.489 1.00 30.93 C
ATOM 450 CG2 ILE A1049 20.207 -47.159 14.265 1.00 34.57 C
ATOM 451 CD1 ILE A1049 17.288 -45.886 14.817 1.00 32.89 C
ATOM 452 N LYS A1050 20.761 -50.068 16.452 1.00 36.98 N
ATOM 453 CA LYS A1050 21.931 -50.686 17.042 1.00 38.92 C
ATOM 454 C LYS A1050 22.031 -52.092 16.423 1.00 37.38 C
ATOM 455 O LYS A1050 23.076 -52.485 15.866 1.00 37.96 O
ATOM 456 CB LYS A1050 21.691 -50.751 18.534 1.00 39.97 C
ATOM 457 CG LYS A1050 22.712 -50.282 19.604 1.00 44.42 C
ATOM 458 CD LYS A1050 21.790 -50.154 20.930 1.00 44.96 C
ATOM 459 CE LYS A1050 22.490 -50.153 22.322 1.00 51.41 C
ATOM 460 NZ LYS A1050 23.926 -50.715 22.371 1.00 55.25 N
ATOM 461 N LYS A1051 20.929 -52.833 16.457 1.00 35.75 N
ATOM 462 CA LYS A1051 20.885 -54.203 15.876 1.00 35.27 C
ATOM 463 C LYS A1051 21.190 -54.241 14.340 1.00 34.79 C
ATOM 464 O LYS A1051 21.909 -55.111 13.876 1.00 35.61 O
ATOM 465 CB LYS A1051 19.545 -54.891 16.249 1.00 34.09 C
ATOM 466 CG LYS A1051 19.392 -56.328 15.793 1.00 36.96 C
ATOM 467 CD LYS A1051 17.976 -56.779 16.045 1.00 41.17 C
ATOM 468 CE LYS A1051 17.867 -58.299 15.901 1.00 46.82 C