HEADER CHAPERONE 01-NOV-17 6BIE
TITLE MISREADING CHAPERONE-SUBSTRATE COMPLEXES FROM RANDOM NOISE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC CHAPERONE SPY;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 52-147;
COMPND 5 SYNONYM: SPHEROPLAST PROTEIN Y;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: SPY, B1743, JW1732;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WANG
REVDAT 6 04-OCT-23 6BIE 1 LINK
REVDAT 5 01-JAN-20 6BIE 1 REMARK
REVDAT 4 20-FEB-19 6BIE 1 REMARK
REVDAT 3 14-NOV-18 6BIE 1 JRNL
REVDAT 2 24-OCT-18 6BIE 1 JRNL
REVDAT 1 17-OCT-18 6BIE 0
JRNL AUTH J.WANG
JRNL TITL MISREADING CHAPERONE-SUBSTRATE COMPLEXES FROM RANDOM NOISE.
JRNL REF NAT. STRUCT. MOL. BIOL. V. 25 989 2018
JRNL REFN ESSN 1545-9985
JRNL PMID 30297779
JRNL DOI 10.1038/S41594-018-0144-3
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23687
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1267
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) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1697
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.3770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1608
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 224
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.12000
REMARK 3 B22 (A**2) : -0.12000
REMARK 3 B33 (A**2) : 0.24000
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): 0.168
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.128
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 : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1731 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1667 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2312 ; 1.322 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3895 ; 3.578 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 210 ; 6.036 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 94 ;38.542 ;24.894
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 382 ;14.991 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;13.703 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 239 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1900 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 339 ; 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): 807 ; 4.927 ; 4.898
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 806 ; 4.922 ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1016 ; 6.460 ; 7.304
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1017 ; 6.457 ;57.983
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 924 ; 5.895 ; 5.600
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 920 ; 5.908 ; 5.591
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1287 ; 7.061 ; 8.167
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2080 ; 8.542 ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2060 ; 8.373 ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1716 ; 1.859 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 59 ;39.447 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1744 ;28.693 ; 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 28 124 B 28 124 5610 0.16 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 : 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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6BIE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1000230900.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25052
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.769
REMARK 200 RESOLUTION RANGE LOW (A) : 64.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 8.20
REMARK 200 R MERGE FOR SHELL (I) : 1.34000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 5INA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3000, IMIDAZOLE, ZINC ACETATE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K, EVAPORATION,
REMARK 280 TEMPERATURE 273K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 129.08450
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 64.54225
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 193.62675
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 129.08450
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 193.62675
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 64.54225
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: DIMERIC
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -42.96000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -42.96000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -746.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 42.96000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 42.96000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 580.88025
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 42.96000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 42.96000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 580.88025
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 A 303 LIES ON A SPECIAL POSITION.
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 SER B 28 OG
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 HE2 HIS B 96 ZN ZN B 201 1.07
REMARK 500 HD1 HIS B 65 ZN ZN A 206 1.20
REMARK 500 HZ3 LYS B 90 O HOH B 301 1.51
REMARK 500 ZN ZN A 206 HN3 IMD A 216 1.54
REMARK 500 HZ2 LYS A 112 O HOH A 304 1.59
REMARK 500 OD2 ASP A 36 O HOH A 301 1.98
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 O HOH A 358 O HOH A 358 8557 0.69
REMARK 500 ZN ZN A 208 O HOH A 301 5457 1.47
REMARK 500 ZN ZN B 203 O HOH B 301 8557 1.62
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 LYS A 54 -156.25 -75.71
REMARK 500 PRO A 56 90.82 3.97
REMARK 500 PRO A 57 135.14 -29.35
REMARK 500 GLN B 52 -83.53 -43.95
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 ASP A 51 GLN A 52 -41.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 402 DISTANCE = 8.60 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 208 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 36 OD2
REMARK 620 2 GLU A 44 OE1 44.4
REMARK 620 3 GLU B 110 OE1 117.2 83.4
REMARK 620 4 GLU B 110 OE2 116.8 82.8 0.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 204 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 59 OE1
REMARK 620 2 GLU A 59 OE2 54.9
REMARK 620 3 ASP B 71 OD1 68.5 116.7
REMARK 620 4 ASP B 71 OD2 69.6 116.8 2.3
REMARK 620 5 HOH B 302 O 66.5 115.7 2.7 5.0
REMARK 620 6 HOH B 370 O 68.7 115.8 2.3 1.0 4.7
REMARK 620 7 HOH B 375 O 69.0 118.0 1.9 3.9 2.6 4.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 209 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 65 ND1
REMARK 620 2 IMD A 217 N3 116.4
REMARK 620 3 GLU B 120 OE2 93.6 106.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 204 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 66 OD1
REMARK 620 2 IMD A 216 N1 76.8
REMARK 620 3 ASP B 66 OD2 39.2 88.0
REMARK 620 4 HOH B 304 O 78.6 89.9 40.4
REMARK 620 5 HOH B 355 O 90.1 109.1 122.1 155.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 207 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 71 OD1
REMARK 620 2 ASP A 71 OD2 53.9
REMARK 620 3 ASP A 74 OD2 50.2 104.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 205 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 79 OE2
REMARK 620 2 HOH A 400 O 120.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 205 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 79 OE2
REMARK 620 2 HOH A 400 O 135.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 86 OE1
REMARK 620 2 IMD A 215 N1 98.5
REMARK 620 3 GLU B 79 OE2 71.6 164.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 96 ND1
REMARK 620 2 HOH A 373 O 103.9
REMARK 620 3 HOH A 385 O 109.5 126.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 96 NE2
REMARK 620 2 HOH A 393 O 94.8
REMARK 620 3 HOH A 401 O 142.0 100.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 206 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 120 OE2
REMARK 620 2 IMD A 216 N3 128.7
REMARK 620 3 HIS B 65 ND1 96.2 103.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 74 OD1
REMARK 620 2 ASP B 74 OD2 53.0
REMARK 620 3 HOH B 308 O 119.0 76.8
REMARK 620 4 HOH B 367 O 135.5 100.3 79.5
REMARK 620 5 HOH B 376 O 90.1 110.7 76.2 134.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 96 NE2
REMARK 620 2 THR B 124 OXT 111.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 96 ND1
REMARK 620 2 HOH B 327 O 130.2
REMARK 620 3 HOH B 362 O 93.0 96.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 205 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 98 OE2
REMARK 620 2 HOH B 315 O 68.9
REMARK 620 3 HOH B 318 O 109.6 178.4
REMARK 620 4 HOH B 325 O 91.7 89.8 89.6
REMARK 620 5 HOH B 354 O 89.1 90.2 90.4 179.1
REMARK 620 6 HOH B 387 O 159.4 90.6 90.9 89.8 89.3
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 ZN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 207
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IOG RELATED DB: PDB
REMARK 900 5IOG IS THE ORIGINAL DATA. THE CURRENT ENTRY IS AN ALTERNATIVE
REMARK 900 MODELING OF 5IOG. IN PARTICULAR, THERE IS NO EVIDENCE TO SUPPORT
REMARK 900 PRESENCE OF CASEIN SUBSTRATE.
DBREF 6BIE A 29 124 UNP P77754 SPY_ECOLI 52 147
DBREF 6BIE B 29 124 UNP P77754 SPY_ECOLI 52 147
SEQADV 6BIE SER A 28 UNP P77754 EXPRESSION TAG
SEQADV 6BIE SER B 28 UNP P77754 EXPRESSION TAG
SEQRES 1 A 97 SER PHE LYS ASP LEU ASN LEU THR ASP ALA GLN LYS GLN
SEQRES 2 A 97 GLN ILE ARG GLU ILE MET LYS GLY GLN ARG ASP GLN MET
SEQRES 3 A 97 LYS ARG PRO PRO LEU GLU GLU ARG ARG ALA MET HIS ASP
SEQRES 4 A 97 ILE ILE ALA SER ASP THR PHE ASP LYS VAL LYS ALA GLU
SEQRES 5 A 97 ALA GLN ILE ALA LYS MET GLU GLU GLN ARG LYS ALA ASN
SEQRES 6 A 97 MET LEU ALA HIS MET GLU THR GLN ASN LYS ILE TYR ASN
SEQRES 7 A 97 ILE LEU THR PRO GLU GLN LYS LYS GLN PHE ASN ALA ASN
SEQRES 8 A 97 PHE GLU LYS ARG LEU THR
SEQRES 1 B 97 SER PHE LYS ASP LEU ASN LEU THR ASP ALA GLN LYS GLN
SEQRES 2 B 97 GLN ILE ARG GLU ILE MET LYS GLY GLN ARG ASP GLN MET
SEQRES 3 B 97 LYS ARG PRO PRO LEU GLU GLU ARG ARG ALA MET HIS ASP
SEQRES 4 B 97 ILE ILE ALA SER ASP THR PHE ASP LYS VAL LYS ALA GLU
SEQRES 5 B 97 ALA GLN ILE ALA LYS MET GLU GLU GLN ARG LYS ALA ASN
SEQRES 6 B 97 MET LEU ALA HIS MET GLU THR GLN ASN LYS ILE TYR ASN
SEQRES 7 B 97 ILE LEU THR PRO GLU GLN LYS LYS GLN PHE ASN ALA ASN
SEQRES 8 B 97 PHE GLU LYS ARG LEU THR
HET ZN A 201 1
HET ZN A 202 1
HET ZN A 203 1
HET ZN A 204 1
HET ZN A 205 2
HET ZN A 206 1
HET ZN A 207 1
HET ZN A 208 1
HET ZN A 209 1
HET CL A 210 1
HET CL A 211 1
HET CL A 212 1
HET CL A 213 1
HET CL A 214 1
HET IMD A 215 9
HET IMD A 216 10
HET IMD A 217 9
HET ZN B 201 1
HET ZN B 202 1
HET ZN B 203 1
HET ZN B 204 1
HET MG B 205 1
HET CL B 206 1
HET CL B 207 1
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM IMD IMIDAZOLE
HETNAM MG MAGNESIUM ION
FORMUL 3 ZN 13(ZN 2+)
FORMUL 12 CL 7(CL 1-)
FORMUL 17 IMD 3(C3 H5 N2 1+)
FORMUL 24 MG MG 2+
FORMUL 27 HOH *224(H2 O)
HELIX 1 AA1 SER A 28 ASN A 33 5 6
HELIX 2 AA2 THR A 35 GLN A 49 1 15
HELIX 3 AA3 PRO A 57 ALA A 69 1 13
HELIX 4 AA4 ASP A 74 LYS A 84 1 11
HELIX 5 AA5 MET A 85 ASN A 105 1 21
HELIX 6 AA6 THR A 108 ARG A 122 1 15
HELIX 7 AA7 THR B 35 ASP B 51 1 17
HELIX 8 AA8 PRO B 57 ALA B 69 1 13
HELIX 9 AA9 ASP B 74 ASN B 105 1 32
HELIX 10 AB1 THR B 108 ARG B 122 1 15
LINK OD2 ASP A 36 ZN ZN A 208 1555 5457 2.46
LINK OE1 GLU A 44 ZN ZN A 208 1555 1555 1.77
LINK OE1 GLU A 59 ZN ZN B 204 1555 1565 2.59
LINK OE2 GLU A 59 ZN ZN B 204 1555 1565 2.10
LINK ND1 HIS A 65 ZN ZN A 209 1555 1555 2.13
LINK OD1 ASP A 66 ZN ZN A 204 1555 1555 2.00
LINK OD1 ASP A 71 ZN ZN A 207 1555 1555 2.67
LINK OD2 ASP A 71 ZN ZN A 207 1555 1555 1.83
LINK OD2 ASP A 74 ZN ZN A 207 1555 8667 2.01
LINK OE2AGLU A 79 ZN A ZN A 205 1555 1555 1.99
LINK OE2BGLU A 79 ZN B ZN A 205 1555 1555 2.01
LINK OE1 GLU A 86 ZN ZN A 201 1555 1555 1.96
LINK ND1 HIS A 96 ZN ZN A 202 1555 1555 1.86
LINK NE2 HIS A 96 ZN ZN A 203 1555 1555 2.14
LINK OE2 GLU A 120 ZN ZN A 206 1555 1555 1.84
LINK ZN ZN A 201 N1 IMD A 215 1555 1555 2.15
LINK ZN ZN A 201 OE2 GLU B 79 8557 1555 1.92
LINK ZN ZN A 202 O HOH A 373 1555 1555 2.42
LINK ZN ZN A 202 O HOH A 385 1555 1555 2.32
LINK ZN ZN A 203 O HOH A 393 1555 1555 2.69
LINK ZN ZN A 203 O HOH A 401 1555 1555 2.02
LINK ZN ZN A 204 N1 IMD A 216 1555 1565 2.43
LINK ZN ZN A 204 OD2 ASP B 66 1545 1555 1.98
LINK ZN ZN A 204 O HOH B 304 1555 1565 2.00
LINK ZN ZN A 204 O HOH B 355 1555 1565 2.20
LINK ZN A ZN A 205 O HOH A 400 1555 1555 2.60
LINK ZN B ZN A 205 O HOH A 400 1555 1555 2.33
LINK ZN ZN A 206 N3 IMD A 216 1555 1555 2.21
LINK ZN ZN A 206 ND1 HIS B 65 1555 1555 2.04
LINK ZN ZN A 208 OE1 GLU B 110 1665 1555 2.44
LINK ZN ZN A 208 OE2 GLU B 110 1665 1555 2.22
LINK ZN ZN A 209 N3 IMD A 217 1555 1555 1.96
LINK ZN ZN A 209 OE2 GLU B 120 1555 1555 2.06
LINK OD1 ASP B 71 ZN ZN B 204 1555 1555 2.60
LINK OD2 ASP B 71 ZN ZN B 204 1555 1555 1.98
LINK OD1 ASP B 74 ZN ZN B 203 1555 1555 2.67
LINK OD2 ASP B 74 ZN ZN B 203 1555 1555 2.15
LINK NE2 HIS B 96 ZN ZN B 201 1555 1555 1.88
LINK ND1 HIS B 96 ZN ZN B 202 1555 1555 1.97
LINK OE2 GLU B 98 MG MG B 205 1555 1555 2.45
LINK OXT THR B 124 ZN ZN B 201 1555 1555 1.91
LINK ZN ZN B 202 O HOH B 327 1555 1555 2.10
LINK ZN ZN B 202 O HOH B 362 1555 1555 2.32
LINK ZN ZN B 203 O HOH B 308 1555 1555 1.97
LINK ZN ZN B 203 O HOH B 367 1555 1555 2.08
LINK ZN ZN B 203 O HOH B 376 1555 1555 2.30
LINK ZN ZN B 204 O HOH B 302 1555 1555 2.36
LINK ZN ZN B 204 O HOH B 370 1555 1555 2.62
LINK ZN ZN B 204 O HOH B 375 1555 1555 2.24
LINK MG MG B 205 O HOH B 315 1555 1555 2.18
LINK MG MG B 205 O HOH B 318 1555 1555 2.18
LINK MG MG B 205 O HOH B 325 1555 1555 2.18
LINK MG MG B 205 O HOH B 354 1555 1555 2.18
LINK MG MG B 205 O HOH B 387 1555 1555 2.18
SITE 1 AC1 4 GLU A 86 CL A 211 IMD A 215 GLU B 79
SITE 1 AC2 4 HIS A 96 HOH A 318 HOH A 373 HOH A 385
SITE 1 AC3 4 HIS A 96 HOH A 393 HOH A 401 MET B 64
SITE 1 AC4 5 ASP A 66 IMD A 216 ASP B 66 HOH B 304
SITE 2 AC4 5 HOH B 355
SITE 1 AC5 6 LYS A 75 GLU A 79 HOH A 394 HOH A 400
SITE 2 AC5 6 LYS B 90 HOH B 385
SITE 1 AC6 4 GLU A 120 CL A 214 IMD A 216 HIS B 65
SITE 1 AC7 4 ASP A 71 ASP A 74 CL A 212 CL A 213
SITE 1 AC8 4 ASP A 36 GLU A 44 HOH A 301 GLU B 110
SITE 1 AC9 4 HIS A 65 CL A 210 IMD A 217 GLU B 120
SITE 1 AD1 6 ARG A 61 ARG A 62 ZN A 209 IMD A 217
SITE 2 AD1 6 PHE B 119 GLU B 120
SITE 1 AD2 5 GLU A 86 ZN A 201 IMD A 215 GLU B 79
SITE 2 AD2 5 HOH B 356
SITE 1 AD3 2 ASP A 71 ZN A 207
SITE 1 AD4 3 ASP A 71 ASP A 74 ZN A 207
SITE 1 AD5 6 PHE A 119 GLU A 120 ZN A 206 IMD A 216
SITE 2 AD5 6 ARG B 61 HIS B 65
SITE 1 AD6 7 ALA A 83 GLU A 86 ZN A 201 CL A 211
SITE 2 AD6 7 LYS B 75 VAL B 76 GLU B 79
SITE 1 AD7 10 HIS A 65 ASP A 66 GLU A 120 ZN A 204
SITE 2 AD7 10 ZN A 206 CL A 214 IMD A 217 ARG B 62
SITE 3 AD7 10 HIS B 65 ASP B 66
SITE 1 AD8 8 ARG A 62 HIS A 65 ZN A 209 CL A 210
SITE 2 AD8 8 IMD A 216 HIS B 65 ASP B 66 GLU B 120
SITE 1 AD9 4 HIS B 96 THR B 124 CL B 206 CL B 207
SITE 1 AE1 3 HIS B 96 HOH B 327 HOH B 362
SITE 1 AE2 5 ASP B 74 HOH B 301 HOH B 308 HOH B 367
SITE 2 AE2 5 HOH B 376
SITE 1 AE3 5 GLU A 59 ASP B 71 HOH B 302 HOH B 370
SITE 2 AE3 5 HOH B 375
SITE 1 AE4 6 GLU B 98 HOH B 315 HOH B 318 HOH B 325
SITE 2 AE4 6 HOH B 354 HOH B 387
SITE 1 AE5 3 HIS B 96 THR B 124 ZN B 201
SITE 1 AE6 7 ARG A 61 MET A 64 ILE A 68 HIS B 96
SITE 2 AE6 7 PHE B 119 THR B 124 ZN B 201
CRYST1 42.960 42.960 258.169 90.00 90.00 90.00 P 41 2 2 16
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 0.023277 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023277 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003873 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
