HEADER LIGASE 23-APR-17 5NRH
TITLE CRYSTAL STRUCTURE OF BURKHOLDERIA PSEUDOMALLEI D-ALANINE-D-ALANINE
TITLE 2 LIGASE IN COMPLEX WITH AMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: D-ALA-D-ALA LIGASE,D-ALANYLALANINE SYNTHETASE;
COMPND 5 EC: 6.3.2.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI;
SOURCE 3 ORGANISM_TAXID: 28450;
SOURCE 4 GENE: DDL, BURPS1106A_3548;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS LIGASE, COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.DIAZ-SAEZ,W.N.HUNTER
REVDAT 1 30-MAY-18 5NRH 0
JRNL AUTH L.DIAZ-SAEZ,W.N.HUNTER
JRNL TITL CHARACTERISATION OF BURKHOLDERIA PSEUDOMALLEI
JRNL TITL 2 D-ALANINE-D-ALANINE LIGASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 133936
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) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7097
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) : 1.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9734
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 482
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4672
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 785
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.98000
REMARK 3 B22 (A**2) : 0.64000
REMARK 3 B33 (A**2) : 0.33000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.52000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.052
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.053
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.042
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.286
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5124 ; 0.022 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4908 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6976 ; 2.247 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11383 ; 1.444 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 648 ; 7.711 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 233 ;30.341 ;23.348
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 859 ;13.802 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;20.523 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 789 ; 0.184 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5695 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1060 ; 0.005 ; 0.020
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): 2518 ; 3.726 ; 2.225
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2517 ; 3.716 ; 2.222
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3154 ; 4.581 ; 3.357
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3155 ; 4.583 ; 3.359
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2606 ; 5.385 ; 2.425
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2607 ; 5.386 ; 2.425
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3807 ; 6.253 ; 3.543
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5971 ; 7.277 ;28.885
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5972 ; 7.276 ;28.887
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 10032 ; 4.711 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 497 ;42.426 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 10205 ;19.534 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 4 311 B 4 311 18826 0.13 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5NRH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004599.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.917410
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 141049
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 70.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: SEE PUBLICATION
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 TO 0.3 M LI2SO4, 0.1 M BIS-TRIS
REMARK 280 PH 5.5 AND 15-30% (W/V) PEG 3350, RATIO PROTEIN:RESERVOIR 1:1,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 30.57500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 3
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASN A 224 CB CG OD1 ND2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 834 O HOH A 1081 2.10
REMARK 500 O HOH A 1246 O HOH B 1096 2.13
REMARK 500 O HOH B 887 O HOH B 1069 2.17
REMARK 500 OE1 GLU A 152 O HOH A 801 2.18
REMARK 500 O HOH A 1126 O HOH A 1144 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE2 HIS A 218 O HOH A 1246 2647 2.15
REMARK 500 ND2 ASN B 224 O HOH B 1037 2756 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 239 CD GLU A 239 OE1 0.126
REMARK 500 GLU A 239 CD GLU A 239 OE2 0.068
REMARK 500 LEU B 15 C LEU B 15 O 0.134
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 52 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 52 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP A 103 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 SER A 151 CA - C - N ANGL. DEV. = 16.7 DEGREES
REMARK 500 GLU A 152 C - N - CA ANGL. DEV. = 16.4 DEGREES
REMARK 500 ASP A 165 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASN A 224 CB - CA - C ANGL. DEV. = 14.1 DEGREES
REMARK 500 PHE A 250 CB - CA - C ANGL. DEV. = -12.4 DEGREES
REMARK 500 PHE A 250 N - CA - CB ANGL. DEV. = -10.9 DEGREES
REMARK 500 ASP A 251 CB - CG - OD1 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ASP A 251 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 284 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 284 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG B 38 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 38 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ILE B 42 CG1 - CB - CG2 ANGL. DEV. = -14.6 DEGREES
REMARK 500 PRO B 53 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 ARG B 106 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 106 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG B 133 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 244 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP B 251 CB - CG - OD1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 ASP B 251 CB - CG - OD2 ANGL. DEV. = -6.4 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 SER A 151 146.49 148.09
REMARK 500 GLU A 152 -161.29 -167.11
REMARK 500 SER A 155 -66.60 69.67
REMARK 500 ALA A 199 -136.21 49.86
REMARK 500 ASP A 257 61.73 -67.61
REMARK 500 ASP A 257 -27.30 53.04
REMARK 500 TRP A 258 116.03 -172.46
REMARK 500 ALA B 199 -133.86 52.72
REMARK 500 ASP B 257 -40.39 72.31
REMARK 500 MET B 282 33.13 -140.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 150 SER A 151 107.46
REMARK 500 SER A 151 GLU A 152 50.97
REMARK 500 THR A 256 ASP A 257 -129.28
REMARK 500 THR A 256 ASP A 257 112.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY A 190 11.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1253 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A1254 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A1255 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A1256 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A1257 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A1258 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A1259 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A1260 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH A1261 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH A1262 DISTANCE = 7.08 ANGSTROMS
REMARK 525 HOH A1263 DISTANCE = 7.28 ANGSTROMS
REMARK 525 HOH A1264 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH A1265 DISTANCE = 8.16 ANGSTROMS
REMARK 525 HOH B1111 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH B1112 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B1113 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH B1114 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH B1115 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH B1116 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH B1117 DISTANCE = 7.47 ANGSTROMS
REMARK 525 HOH B1118 DISTANCE = 7.87 ANGSTROMS
REMARK 525 HOH B1119 DISTANCE = 8.77 ANGSTROMS
REMARK 525 HOH B1120 DISTANCE = 9.20 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 809 O
REMARK 620 2 HOH A 947 O 88.4
REMARK 620 3 HOH A1070 O 164.8 88.4
REMARK 620 4 HOH A1094 O 82.8 164.8 96.8
REMARK 620 5 HOH A1170 O 79.8 75.2 85.1 91.1
REMARK 620 6 HOH A 809 O 42.8 103.8 152.0 77.9 122.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 701
DBREF 5NRH A 1 312 UNP A3NZL3 DDL_BURP0 1 312
DBREF 5NRH B 1 312 UNP A3NZL3 DDL_BURP0 1 312
SEQRES 1 A 312 MET SER GLY ILE ASP PRO LYS ARG PHE GLY LYS VAL ALA
SEQRES 2 A 312 VAL LEU LEU GLY GLY ASP SER ALA GLU ARG GLU VAL SER
SEQRES 3 A 312 LEU ASN SER GLY ARG LEU VAL LEU GLN GLY LEU ARG ASP
SEQRES 4 A 312 ALA GLY ILE ASP ALA HIS PRO PHE ASP PRO ALA GLN ARG
SEQRES 5 A 312 PRO LEU ALA ALA LEU LYS ASP GLU GLY PHE VAL ARG ALA
SEQRES 6 A 312 PHE ASN ALA LEU HIS GLY GLY TYR GLY GLU ASN GLY GLN
SEQRES 7 A 312 ILE GLN GLY ALA LEU ASP PHE TYR GLY ILE ARG TYR THR
SEQRES 8 A 312 GLY SER GLY VAL LEU GLY SER ALA LEU GLY LEU ASP LYS
SEQRES 9 A 312 PHE ARG THR LYS LEU VAL TRP GLN GLN THR GLY ILE PRO
SEQRES 10 A 312 THR PRO PRO PHE GLU THR VAL MET ARG GLY ASP ASP TYR
SEQRES 11 A 312 ALA ALA ARG ALA GLN ASP ILE VAL ALA LYS LEU GLY VAL
SEQRES 12 A 312 PRO LEU PHE VAL LYS PRO ALA SER GLU GLY SER SER VAL
SEQRES 13 A 312 ALA VAL GLU LYS VAL LYS SER ALA ASP ALA LEU PRO ALA
SEQRES 14 A 312 ALA LEU GLU GLU ALA ALA LYS HIS ASP LYS ILE VAL ILE
SEQRES 15 A 312 VAL GLU LYS SER ILE GLU GLY GLY GLY GLU TYR THR ALA
SEQRES 16 A 312 CYS ILE ALA ALA ASP LEU ASP LEU PRO LEU ILE ARG ILE
SEQRES 17 A 312 VAL PRO ALA GLY GLU PHE TYR ASP TYR HIS ALA LYS TYR
SEQRES 18 A 312 ILE ALA ASN ASP THR GLN TYR LEU ILE PRO CYS GLY LEU
SEQRES 19 A 312 ASP ALA ALA LYS GLU ALA GLU PHE LYS ARG ILE ALA ARG
SEQRES 20 A 312 ARG ALA PHE ASP VAL LEU GLY CYS THR ASP TRP GLY ARG
SEQRES 21 A 312 ALA ASP PHE MET LEU ASP ALA ALA GLY ASN PRO TYR PHE
SEQRES 22 A 312 LEU GLU VAL ASN THR ALA PRO GLY MET THR ASP HIS SER
SEQRES 23 A 312 LEU PRO PRO LYS ALA ALA ARG ALA VAL GLY ILE GLY TYR
SEQRES 24 A 312 SER GLU LEU VAL VAL LYS VAL LEU SER LEU THR LEU ASP
SEQRES 1 B 312 MET SER GLY ILE ASP PRO LYS ARG PHE GLY LYS VAL ALA
SEQRES 2 B 312 VAL LEU LEU GLY GLY ASP SER ALA GLU ARG GLU VAL SER
SEQRES 3 B 312 LEU ASN SER GLY ARG LEU VAL LEU GLN GLY LEU ARG ASP
SEQRES 4 B 312 ALA GLY ILE ASP ALA HIS PRO PHE ASP PRO ALA GLN ARG
SEQRES 5 B 312 PRO LEU ALA ALA LEU LYS ASP GLU GLY PHE VAL ARG ALA
SEQRES 6 B 312 PHE ASN ALA LEU HIS GLY GLY TYR GLY GLU ASN GLY GLN
SEQRES 7 B 312 ILE GLN GLY ALA LEU ASP PHE TYR GLY ILE ARG TYR THR
SEQRES 8 B 312 GLY SER GLY VAL LEU GLY SER ALA LEU GLY LEU ASP LYS
SEQRES 9 B 312 PHE ARG THR LYS LEU VAL TRP GLN GLN THR GLY ILE PRO
SEQRES 10 B 312 THR PRO PRO PHE GLU THR VAL MET ARG GLY ASP ASP TYR
SEQRES 11 B 312 ALA ALA ARG ALA GLN ASP ILE VAL ALA LYS LEU GLY VAL
SEQRES 12 B 312 PRO LEU PHE VAL LYS PRO ALA SER GLU GLY SER SER VAL
SEQRES 13 B 312 ALA VAL GLU LYS VAL LYS SER ALA ASP ALA LEU PRO ALA
SEQRES 14 B 312 ALA LEU GLU GLU ALA ALA LYS HIS ASP LYS ILE VAL ILE
SEQRES 15 B 312 VAL GLU LYS SER ILE GLU GLY GLY GLY GLU TYR THR ALA
SEQRES 16 B 312 CYS ILE ALA ALA ASP LEU ASP LEU PRO LEU ILE ARG ILE
SEQRES 17 B 312 VAL PRO ALA GLY GLU PHE TYR ASP TYR HIS ALA LYS TYR
SEQRES 18 B 312 ILE ALA ASN ASP THR GLN TYR LEU ILE PRO CYS GLY LEU
SEQRES 19 B 312 ASP ALA ALA LYS GLU ALA GLU PHE LYS ARG ILE ALA ARG
SEQRES 20 B 312 ARG ALA PHE ASP VAL LEU GLY CYS THR ASP TRP GLY ARG
SEQRES 21 B 312 ALA ASP PHE MET LEU ASP ALA ALA GLY ASN PRO TYR PHE
SEQRES 22 B 312 LEU GLU VAL ASN THR ALA PRO GLY MET THR ASP HIS SER
SEQRES 23 B 312 LEU PRO PRO LYS ALA ALA ARG ALA VAL GLY ILE GLY TYR
SEQRES 24 B 312 SER GLU LEU VAL VAL LYS VAL LEU SER LEU THR LEU ASP
HET AMP A 700 23
HET MG A 701 1
HET SO4 A 702 5
HET EDO A 703 4
HET EDO A 704 4
HET EDO A 705 4
HET AMP B 700 23
HET SO4 B 701 5
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 AMP 2(C10 H14 N5 O7 P)
FORMUL 4 MG MG 2+
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 6 EDO 3(C2 H6 O2)
FORMUL 11 HOH *785(H2 O)
HELIX 1 AA1 ASP A 5 PHE A 9 5 5
HELIX 2 AA2 GLU A 22 ALA A 40 1 19
HELIX 3 AA3 ALA A 55 GLU A 60 1 6
HELIX 4 AA4 GLY A 71 GLU A 75 5 5
HELIX 5 AA5 GLY A 77 TYR A 86 1 10
HELIX 6 AA6 GLY A 94 LEU A 102 1 9
HELIX 7 AA7 ASP A 103 GLY A 115 1 13
HELIX 8 AA8 ASP A 129 GLY A 142 1 14
HELIX 9 AA9 SER A 163 ASP A 165 5 3
HELIX 10 AB1 ALA A 166 ASP A 178 1 13
HELIX 11 AB2 ASP A 216 ILE A 222 1 7
HELIX 12 AB3 ASP A 235 LEU A 253 1 19
HELIX 13 AB4 SER A 286 ALA A 294 1 9
HELIX 14 AB5 GLY A 298 LEU A 309 1 12
HELIX 15 AB6 ASP B 5 PHE B 9 5 5
HELIX 16 AB7 GLU B 22 ALA B 40 1 19
HELIX 17 AB8 ALA B 55 GLU B 60 1 6
HELIX 18 AB9 GLY B 71 GLU B 75 5 5
HELIX 19 AC1 GLY B 77 TYR B 86 1 10
HELIX 20 AC2 GLY B 94 ASP B 103 1 10
HELIX 21 AC3 ASP B 103 THR B 114 1 12
HELIX 22 AC4 ASP B 129 GLY B 142 1 14
HELIX 23 AC5 GLU B 152 VAL B 156 5 5
HELIX 24 AC6 SER B 163 ASP B 165 5 3
HELIX 25 AC7 ALA B 166 LYS B 176 1 11
HELIX 26 AC8 ASP B 216 ILE B 222 1 7
HELIX 27 AC9 ASP B 235 VAL B 252 1 18
HELIX 28 AD1 SER B 286 VAL B 295 1 10
HELIX 29 AD2 GLY B 298 LEU B 309 1 12
SHEET 1 AA1 4 ASP A 43 PHE A 47 0
SHEET 2 AA1 4 LYS A 11 LEU A 15 1 N VAL A 12 O ASP A 43
SHEET 3 AA1 4 ARG A 64 ASN A 67 1 O PHE A 66 N ALA A 13
SHEET 4 AA1 4 ARG A 89 TYR A 90 1 O ARG A 89 N ALA A 65
SHEET 1 AA2 4 PHE A 121 MET A 125 0
SHEET 2 AA2 4 ILE A 180 LYS A 185 -1 O VAL A 183 N GLU A 122
SHEET 3 AA2 4 LEU A 145 PRO A 149 -1 N LYS A 148 O ILE A 182
SHEET 4 AA2 4 GLU A 159 VAL A 161 -1 O VAL A 161 N LEU A 145
SHEET 1 AA3 5 GLN A 227 LEU A 229 0
SHEET 2 AA3 5 ILE A 206 VAL A 209 -1 N ARG A 207 O LEU A 229
SHEET 3 AA3 5 GLY A 189 ALA A 198 -1 N GLU A 192 O ILE A 208
SHEET 4 AA3 5 TRP A 258 ASP A 266 -1 O GLY A 259 N ILE A 197
SHEET 5 AA3 5 PRO A 271 ASN A 277 -1 O LEU A 274 N ASP A 262
SHEET 1 AA4 4 ASP B 43 PHE B 47 0
SHEET 2 AA4 4 LYS B 11 LEU B 15 1 N VAL B 12 O ASP B 43
SHEET 3 AA4 4 ARG B 64 ASN B 67 1 O PHE B 66 N ALA B 13
SHEET 4 AA4 4 ARG B 89 TYR B 90 1 O ARG B 89 N ALA B 65
SHEET 1 AA5 4 PHE B 121 MET B 125 0
SHEET 2 AA5 4 ILE B 180 LYS B 185 -1 O VAL B 183 N GLU B 122
SHEET 3 AA5 4 LEU B 145 PRO B 149 -1 N PHE B 146 O GLU B 184
SHEET 4 AA5 4 GLU B 159 VAL B 161 -1 O VAL B 161 N LEU B 145
SHEET 1 AA6 5 GLN B 227 LEU B 229 0
SHEET 2 AA6 5 ILE B 206 VAL B 209 -1 N VAL B 209 O GLN B 227
SHEET 3 AA6 5 GLY B 189 ALA B 198 -1 N GLU B 192 O ILE B 208
SHEET 4 AA6 5 TRP B 258 ASP B 266 -1 O GLY B 259 N ILE B 197
SHEET 5 AA6 5 PRO B 271 ASN B 277 -1 O LEU B 274 N ASP B 262
LINK MG MG A 701 O BHOH A 809 1555 1555 2.17
LINK MG MG A 701 O HOH A 947 1555 1555 1.99
LINK MG MG A 701 O HOH A1070 1555 1555 1.94
LINK MG MG A 701 O HOH A1094 1555 1555 2.20
LINK MG MG A 701 O HOH A1170 1555 1555 2.04
LINK MG MG A 701 O AHOH A 809 1555 1555 2.94
CISPEP 1 VAL A 143 PRO A 144 0 -2.66
CISPEP 2 SER A 151 GLU A 152 0 15.18
CISPEP 3 ILE A 230 PRO A 231 0 3.49
CISPEP 4 VAL B 143 PRO B 144 0 -0.38
CISPEP 5 ILE B 230 PRO B 231 0 -5.62
SITE 1 AC1 15 LYS A 104 PHE A 146 LYS A 148 GLU A 184
SITE 2 AC1 15 LYS A 185 SER A 186 ILE A 187 GLU A 192
SITE 3 AC1 15 PHE A 214 TYR A 215 GLU A 275 HOH A 804
SITE 4 AC1 15 HOH A 842 HOH A 920 HOH A 951
SITE 1 AC2 6 HIS A 70 HOH A 809 HOH A 947 HOH A1070
SITE 2 AC2 6 HOH A1094 HOH A1170
SITE 1 AC3 7 ARG A 293 GLY A 298 TYR A 299 HOH A 818
SITE 2 AC3 7 HOH A 819 HOH A1003 ARG B 293
SITE 1 AC4 4 GLU A 24 ARG A 31 HOH A 826 HOH A 949
SITE 1 AC5 4 LEU A 201 ASP A 202 VAL A 295 HOH A 856
SITE 1 AC6 8 ALA A 219 LYS A 220 ALA A 223 ASN A 224
SITE 2 AC6 8 ASP A 225 THR A 226 TYR A 228 HOH A 973
SITE 1 AC7 16 LYS B 104 PHE B 146 LYS B 148 SER B 155
SITE 2 AC7 16 GLU B 184 LYS B 185 SER B 186 ILE B 187
SITE 3 AC7 16 GLU B 192 PHE B 214 TYR B 215 LEU B 274
SITE 4 AC7 16 GLU B 275 HOH B 852 HOH B 912 HOH B 949
SITE 1 AC8 8 HIS B 70 TYR B 221 ARG B 260 ASN B 277
SITE 2 AC8 8 PRO B 280 GLY B 281 HOH B 827 HOH B 950
CRYST1 69.648 61.150 70.079 90.00 90.17 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014358 0.000000 0.000043 0.00000
SCALE2 0.000000 0.016353 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014270 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
