HEADER TRANSPORT PROTEIN 05-MAY-10 3MW0
TITLE X-RAY STRUCTURE OF THE DOUBLY HYDROXYLATED IRON COMPLEX-NIKA SPECIES,
TITLE 2 NIKA1/O2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NICKEL-BINDING PERIPLASMIC PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NIKA;
COMPND 5 EC: 3.6.3.24;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: NIKA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS PROTEIN-BOUND IRON COMPLEX, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CAVAZZA,C.BOCHOT,P.ROUSSELOT-PAILLEY,P.CARPENTIER,M.V.CHERRIER,
AUTHOR 2 L.MARTIN,C.MARCHI-DELAPIERRE,J.C.FONTECILLA-CAMPS,S.MENAGE
REVDAT 2 01-NOV-23 3MW0 1 REMARK LINK
REVDAT 1 09-FEB-11 3MW0 0
JRNL AUTH C.CAVAZZA,C.BOCHOT,P.ROUSSELOT-PAILLEY,P.CARPENTIER,
JRNL AUTH 2 M.V.CHERRIER,L.MARTIN,C.MARCHI-DELAPIERRE,
JRNL AUTH 3 J.C.FONTECILLA-CAMPS,S.MENAGE
JRNL TITL CRYSTALLOGRAPHIC SNAPSHOTS OF THE REACTION OF AROMATIC C-H
JRNL TITL 2 WITH O(2) CATALYSED BY A PROTEIN-BOUND IRON COMPLEX
JRNL REF NAT.CHEM. V. 2 1069 2010
JRNL REFN ISSN 1755-4330
JRNL PMID 21107372
JRNL DOI 10.1038/NCHEM.841
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 45153
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2377
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3296
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE SET COUNT : 173
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7869
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 477
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.25000
REMARK 3 B22 (A**2) : -0.43000
REMARK 3 B33 (A**2) : 0.17000
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): 0.349
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.247
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.160
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.506
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8130 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11076 ; 1.320 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 993 ; 6.120 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 371 ;37.978 ;24.717
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1307 ;16.403 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;14.627 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1211 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6256 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5006 ; 0.607 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8098 ; 1.175 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3124 ; 1.827 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2978 ; 3.068 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3MW0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000059063.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 4.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46496
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 47.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.700
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: PDB ENTRY 1ZLQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULFATE, 0.1M SODIUM
REMARK 280 ACETATE, PH 4.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 43.49150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.55250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.25550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.55250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.49150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.25550
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 ALA A 1
REMARK 465 VAL A 500
REMARK 465 LYS A 501
REMARK 465 PRO A 502
REMARK 465 ALA B 1
REMARK 465 ALA B 2
REMARK 465 VAL B 500
REMARK 465 LYS B 501
REMARK 465 PRO B 502
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 LYS A 192 CD CE NZ
REMARK 470 GLU A 479 CG CD OE1 OE2
REMARK 470 LYS B 111 CD CE NZ
REMARK 470 LYS B 115 CG CD CE NZ
REMARK 470 ALA B 125 CB
REMARK 470 LYS B 188 CB CG CD CE NZ
REMARK 470 ASP B 213 OD2
REMARK 470 GLU B 334 OE1
REMARK 470 GLY B 337 O
REMARK 470 ARG B 341 CD
REMARK 470 GLU B 377 CG CD OE1 OE2
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 GLU A 358 CD OE1 OE2
REMARK 480 ASP A 387 CG OD1 OD2
REMARK 480 ARG B 386 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 DISTANCE
REMARK 500 CB GLU A 58 O ASP A 59 1.66
REMARK 500 O18 BHR B 503 FE FE B 505 1.69
REMARK 500 CB GLU A 58 CB ASP A 59 1.74
REMARK 500 O HOH B 661 O HOH B 688 2.18
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 700 O HOH A 770 3555 1.96
REMARK 500 OD2 ASP A 387 OD2 ASP B 460 3545 2.09
REMARK 500 O HOH A 654 O HOH A 671 3545 2.10
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 B 389 NE - CZ - NH1 ANGL. DEV. = 4.7 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 TYR A 22 -130.71 -110.72
REMARK 500 TRP A 49 -103.45 -135.05
REMARK 500 GLU A 58 -127.63 38.89
REMARK 500 ASP A 59 80.00 64.55
REMARK 500 HIS A 150 18.29 59.63
REMARK 500 LYS A 157 -102.05 -95.01
REMARK 500 GLN A 174 -62.78 -124.81
REMARK 500 ASN A 220 -158.94 -90.38
REMARK 500 THR A 292 142.55 -172.76
REMARK 500 ASP A 311 86.29 -157.52
REMARK 500 ALA A 328 -111.70 -11.62
REMARK 500 SER A 415 33.48 -98.48
REMARK 500 THR B 8 -162.58 -127.33
REMARK 500 TYR B 22 -132.49 -105.04
REMARK 500 TRP B 49 -94.09 -130.75
REMARK 500 LYS B 157 -94.11 -94.78
REMARK 500 GLN B 174 -65.06 -125.02
REMARK 500 ILE B 279 -4.10 -57.76
REMARK 500 ASP B 311 87.45 -167.13
REMARK 500 SER B 415 7.31 81.26
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 GLU A 495 10.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 503 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 BHR A 504 O18
REMARK 620 2 BHR A 504 O6 104.9
REMARK 620 3 BHR A 504 N8 162.1 86.6
REMARK 620 4 BHR A 504 N11 88.0 162.5 83.9
REMARK 620 5 BHR A 504 O20 87.2 102.7 76.8 89.4
REMARK 620 6 BHR A 504 O23 95.9 94.2 96.9 72.5 161.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 505 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 BHR B 503 O6
REMARK 620 2 BHR B 503 O23 88.2
REMARK 620 3 BHR B 503 N11 165.5 79.0
REMARK 620 4 BHR B 503 O21 100.0 165.7 91.2
REMARK 620 5 BHR B 503 N8 92.5 94.9 81.9 73.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BHR A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTD A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BHR B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTD B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MVW RELATED DB: PDB
REMARK 900 RELATED ID: 3MVY RELATED DB: PDB
REMARK 900 RELATED ID: 3MVX RELATED DB: PDB
REMARK 900 RELATED ID: 3MVZ RELATED DB: PDB
DBREF 3MW0 A 1 502 UNP P33590 NIKA_ECOLI 23 524
DBREF 3MW0 B 1 502 UNP P33590 NIKA_ECOLI 23 524
SEQRES 1 A 502 ALA ALA PRO ASP GLU ILE THR THR ALA TRP PRO VAL ASN
SEQRES 2 A 502 VAL GLY PRO LEU ASN PRO HIS LEU TYR THR PRO ASN GLN
SEQRES 3 A 502 MET PHE ALA GLN SER MET VAL TYR GLU PRO LEU VAL LYS
SEQRES 4 A 502 TYR GLN ALA ASP GLY SER VAL ILE PRO TRP LEU ALA LYS
SEQRES 5 A 502 SER TRP THR HIS SER GLU ASP GLY LYS THR TRP THR PHE
SEQRES 6 A 502 THR LEU ARG ASP ASP VAL LYS PHE SER ASN GLY GLU PRO
SEQRES 7 A 502 PHE ASP ALA GLU ALA ALA ALA GLU ASN PHE ARG ALA VAL
SEQRES 8 A 502 LEU ASP ASN ARG GLN ARG HIS ALA TRP LEU GLU LEU ALA
SEQRES 9 A 502 ASN GLN ILE VAL ASP VAL LYS ALA LEU SER LYS THR GLU
SEQRES 10 A 502 LEU GLN ILE THR LEU LYS SER ALA TYR TYR PRO PHE LEU
SEQRES 11 A 502 GLN GLU LEU ALA LEU PRO ARG PRO PHE ARG PHE ILE ALA
SEQRES 12 A 502 PRO SER GLN PHE LYS ASN HIS GLU THR MET ASN GLY ILE
SEQRES 13 A 502 LYS ALA PRO ILE GLY THR GLY PRO TRP ILE LEU GLN GLU
SEQRES 14 A 502 SER LYS LEU ASN GLN TYR ASP VAL PHE VAL ARG ASN GLU
SEQRES 15 A 502 ASN TYR TRP GLY GLU LYS PRO ALA ILE LYS LYS ILE THR
SEQRES 16 A 502 PHE ASN VAL ILE PRO ASP PRO THR THR ARG ALA VAL ALA
SEQRES 17 A 502 PHE GLU THR GLY ASP ILE ASP LEU LEU TYR GLY ASN GLU
SEQRES 18 A 502 GLY LEU LEU PRO LEU ASP THR PHE ALA ARG PHE SER GLN
SEQRES 19 A 502 ASN PRO ALA TYR HIS THR GLN LEU SER GLN PRO ILE GLU
SEQRES 20 A 502 THR VAL MET LEU ALA LEU ASN THR ALA LYS ALA PRO THR
SEQRES 21 A 502 ASN GLU LEU ALA VAL ARG GLU ALA LEU ASN TYR ALA VAL
SEQRES 22 A 502 ASN LYS LYS SER LEU ILE ASP ASN ALA LEU TYR GLY THR
SEQRES 23 A 502 GLN GLN VAL ALA ASP THR LEU PHE ALA PRO SER VAL PRO
SEQRES 24 A 502 TYR ALA ASN LEU GLY LEU LYS PRO SER GLN TYR ASP PRO
SEQRES 25 A 502 GLN LYS ALA LYS ALA LEU LEU GLU LYS ALA GLY TRP THR
SEQRES 26 A 502 LEU PRO ALA GLY LYS ASP ILE ARG GLU LYS ASN GLY GLN
SEQRES 27 A 502 PRO LEU ARG ILE GLU LEU SER PHE ILE GLY THR ASP ALA
SEQRES 28 A 502 LEU SER LYS SER MET ALA GLU ILE ILE GLN ALA ASP MET
SEQRES 29 A 502 ARG GLN ILE GLY ALA ASP VAL SER LEU ILE GLY GLU GLU
SEQRES 30 A 502 GLU SER SER ILE TYR ALA ARG GLN ARG ASP GLY ARG PHE
SEQRES 31 A 502 GLY MET ILE PHE HIS ARG THR TRP GLY ALA PRO TYR ASP
SEQRES 32 A 502 PRO HIS ALA PHE LEU SER SER MET ARG VAL PRO SER HIS
SEQRES 33 A 502 ALA ASP PHE GLN ALA GLN GLN GLY LEU ALA ASP LYS PRO
SEQRES 34 A 502 LEU ILE ASP LYS GLU ILE GLY GLU VAL LEU ALA THR HIS
SEQRES 35 A 502 ASP GLU THR GLN ARG GLN ALA LEU TYR ARG ASP ILE LEU
SEQRES 36 A 502 THR ARG LEU HIS ASP GLU ALA VAL TYR LEU PRO ILE SER
SEQRES 37 A 502 TYR ILE SER MET MET VAL VAL SER LYS PRO GLU LEU GLY
SEQRES 38 A 502 ASN ILE PRO TYR ALA PRO ILE ALA THR GLU ILE PRO PHE
SEQRES 39 A 502 GLU GLN ILE LYS PRO VAL LYS PRO
SEQRES 1 B 502 ALA ALA PRO ASP GLU ILE THR THR ALA TRP PRO VAL ASN
SEQRES 2 B 502 VAL GLY PRO LEU ASN PRO HIS LEU TYR THR PRO ASN GLN
SEQRES 3 B 502 MET PHE ALA GLN SER MET VAL TYR GLU PRO LEU VAL LYS
SEQRES 4 B 502 TYR GLN ALA ASP GLY SER VAL ILE PRO TRP LEU ALA LYS
SEQRES 5 B 502 SER TRP THR HIS SER GLU ASP GLY LYS THR TRP THR PHE
SEQRES 6 B 502 THR LEU ARG ASP ASP VAL LYS PHE SER ASN GLY GLU PRO
SEQRES 7 B 502 PHE ASP ALA GLU ALA ALA ALA GLU ASN PHE ARG ALA VAL
SEQRES 8 B 502 LEU ASP ASN ARG GLN ARG HIS ALA TRP LEU GLU LEU ALA
SEQRES 9 B 502 ASN GLN ILE VAL ASP VAL LYS ALA LEU SER LYS THR GLU
SEQRES 10 B 502 LEU GLN ILE THR LEU LYS SER ALA TYR TYR PRO PHE LEU
SEQRES 11 B 502 GLN GLU LEU ALA LEU PRO ARG PRO PHE ARG PHE ILE ALA
SEQRES 12 B 502 PRO SER GLN PHE LYS ASN HIS GLU THR MET ASN GLY ILE
SEQRES 13 B 502 LYS ALA PRO ILE GLY THR GLY PRO TRP ILE LEU GLN GLU
SEQRES 14 B 502 SER LYS LEU ASN GLN TYR ASP VAL PHE VAL ARG ASN GLU
SEQRES 15 B 502 ASN TYR TRP GLY GLU LYS PRO ALA ILE LYS LYS ILE THR
SEQRES 16 B 502 PHE ASN VAL ILE PRO ASP PRO THR THR ARG ALA VAL ALA
SEQRES 17 B 502 PHE GLU THR GLY ASP ILE ASP LEU LEU TYR GLY ASN GLU
SEQRES 18 B 502 GLY LEU LEU PRO LEU ASP THR PHE ALA ARG PHE SER GLN
SEQRES 19 B 502 ASN PRO ALA TYR HIS THR GLN LEU SER GLN PRO ILE GLU
SEQRES 20 B 502 THR VAL MET LEU ALA LEU ASN THR ALA LYS ALA PRO THR
SEQRES 21 B 502 ASN GLU LEU ALA VAL ARG GLU ALA LEU ASN TYR ALA VAL
SEQRES 22 B 502 ASN LYS LYS SER LEU ILE ASP ASN ALA LEU TYR GLY THR
SEQRES 23 B 502 GLN GLN VAL ALA ASP THR LEU PHE ALA PRO SER VAL PRO
SEQRES 24 B 502 TYR ALA ASN LEU GLY LEU LYS PRO SER GLN TYR ASP PRO
SEQRES 25 B 502 GLN LYS ALA LYS ALA LEU LEU GLU LYS ALA GLY TRP THR
SEQRES 26 B 502 LEU PRO ALA GLY LYS ASP ILE ARG GLU LYS ASN GLY GLN
SEQRES 27 B 502 PRO LEU ARG ILE GLU LEU SER PHE ILE GLY THR ASP ALA
SEQRES 28 B 502 LEU SER LYS SER MET ALA GLU ILE ILE GLN ALA ASP MET
SEQRES 29 B 502 ARG GLN ILE GLY ALA ASP VAL SER LEU ILE GLY GLU GLU
SEQRES 30 B 502 GLU SER SER ILE TYR ALA ARG GLN ARG ASP GLY ARG PHE
SEQRES 31 B 502 GLY MET ILE PHE HIS ARG THR TRP GLY ALA PRO TYR ASP
SEQRES 32 B 502 PRO HIS ALA PHE LEU SER SER MET ARG VAL PRO SER HIS
SEQRES 33 B 502 ALA ASP PHE GLN ALA GLN GLN GLY LEU ALA ASP LYS PRO
SEQRES 34 B 502 LEU ILE ASP LYS GLU ILE GLY GLU VAL LEU ALA THR HIS
SEQRES 35 B 502 ASP GLU THR GLN ARG GLN ALA LEU TYR ARG ASP ILE LEU
SEQRES 36 B 502 THR ARG LEU HIS ASP GLU ALA VAL TYR LEU PRO ILE SER
SEQRES 37 B 502 TYR ILE SER MET MET VAL VAL SER LYS PRO GLU LEU GLY
SEQRES 38 B 502 ASN ILE PRO TYR ALA PRO ILE ALA THR GLU ILE PRO PHE
SEQRES 39 B 502 GLU GLN ILE LYS PRO VAL LYS PRO
HET FE A 503 1
HET BHR A 504 29
HET DTD A 505 8
HET BHR B 503 29
HET DTD B 504 8
HET FE B 505 1
HETNAM FE FE (III) ION
HETNAM BHR 2-[2-[CARBOXYMETHYL-[(2-HYDROXYPHENYL)
HETNAM 2 BHR METHYL]AMINO]ETHYL-[(2,3-DIHYDROXYPHENYL)
HETNAM 3 BHR METHYL]AMINO]ETHANOIC ACID
HETNAM DTD DITHIANE DIOL
FORMUL 3 FE 2(FE 3+)
FORMUL 4 BHR 2(C20 H24 N2 O7)
FORMUL 5 DTD 2(C4 H8 O2 S2)
FORMUL 9 HOH *477(H2 O)
HELIX 1 1 GLN A 26 TYR A 34 1 9
HELIX 2 2 ASP A 80 ASP A 93 1 14
HELIX 3 3 ASN A 94 ALA A 99 5 6
HELIX 4 4 LEU A 101 GLN A 106 1 6
HELIX 5 5 PRO A 128 ALA A 134 1 7
HELIX 6 6 ALA A 143 SER A 145 5 3
HELIX 7 7 ASP A 201 THR A 211 1 11
HELIX 8 8 PRO A 225 ASN A 235 1 11
HELIX 9 9 GLU A 262 ASN A 270 1 9
HELIX 10 10 ASN A 274 LEU A 283 1 10
HELIX 11 11 ASP A 311 ALA A 322 1 12
HELIX 12 12 ASP A 350 ILE A 367 1 18
HELIX 13 13 GLU A 377 GLY A 388 1 12
HELIX 14 14 PRO A 404 SER A 410 1 7
HELIX 15 15 MET A 411 VAL A 413 5 3
HELIX 16 16 HIS A 416 GLN A 423 1 8
HELIX 17 17 ASP A 427 THR A 441 1 15
HELIX 18 18 ASP A 443 GLU A 461 1 19
HELIX 19 19 PRO A 478 GLY A 481 5 4
HELIX 20 20 PRO A 493 ILE A 497 5 5
HELIX 21 21 GLN B 26 TYR B 34 1 9
HELIX 22 22 ASP B 80 ASP B 93 1 14
HELIX 23 23 ASN B 94 ALA B 99 5 6
HELIX 24 24 LEU B 101 GLN B 106 1 6
HELIX 25 25 PRO B 128 ALA B 134 1 7
HELIX 26 26 ALA B 143 SER B 145 5 3
HELIX 27 27 ASP B 201 THR B 211 1 11
HELIX 28 28 PRO B 225 GLN B 234 1 10
HELIX 29 29 GLU B 262 VAL B 273 1 12
HELIX 30 30 ASN B 274 ALA B 282 1 9
HELIX 31 31 ASP B 311 ALA B 322 1 12
HELIX 32 32 ASP B 350 GLN B 366 1 17
HELIX 33 33 GLU B 377 GLY B 388 1 12
HELIX 34 34 PRO B 404 MET B 411 1 8
HELIX 35 35 HIS B 416 GLN B 422 1 7
HELIX 36 36 ASP B 427 THR B 441 1 15
HELIX 37 37 ASP B 443 GLU B 461 1 19
HELIX 38 38 PRO B 478 GLY B 481 5 4
HELIX 39 39 PRO B 493 ILE B 497 5 5
SHEET 1 A 4 GLU A 5 TRP A 10 0
SHEET 2 A 4 LYS A 193 VAL A 198 1 O THR A 195 N THR A 8
SHEET 3 A 4 TYR A 175 ARG A 180 -1 N ASP A 176 O PHE A 196
SHEET 4 A 4 TRP A 165 LYS A 171 -1 N LYS A 171 O TYR A 175
SHEET 1 B 2 VAL A 38 TYR A 40 0
SHEET 2 B 2 VAL A 46 PRO A 48 -1 O ILE A 47 N LYS A 39
SHEET 1 C 4 ALA A 51 HIS A 56 0
SHEET 2 C 4 THR A 62 LEU A 67 -1 O THR A 66 N SER A 53
SHEET 3 C 4 GLU A 117 LEU A 122 -1 O LEU A 118 N PHE A 65
SHEET 4 C 4 ILE A 107 ALA A 112 -1 N VAL A 108 O THR A 121
SHEET 1 D 2 PHE A 147 LYS A 148 0
SHEET 2 D 2 GLU A 151 ILE A 156 -1 O GLU A 151 N LYS A 148
SHEET 1 E 3 LEU A 216 GLY A 219 0
SHEET 2 E 3 TYR A 464 SER A 476 -1 O MET A 473 N GLY A 219
SHEET 3 E 3 GLN A 288 VAL A 289 -1 N GLN A 288 O TYR A 469
SHEET 1 F 6 LEU A 216 GLY A 219 0
SHEET 2 F 6 TYR A 464 SER A 476 -1 O MET A 473 N GLY A 219
SHEET 3 F 6 HIS A 239 LEU A 253 -1 N HIS A 239 O SER A 476
SHEET 4 F 6 MET A 392 ARG A 396 -1 O HIS A 395 N MET A 250
SHEET 5 F 6 ARG A 341 ILE A 347 1 N GLU A 343 O MET A 392
SHEET 6 F 6 ASP A 370 GLU A 376 1 O SER A 372 N LEU A 344
SHEET 1 G 2 GLU A 334 LYS A 335 0
SHEET 2 G 2 GLN A 338 PRO A 339 -1 O GLN A 338 N LYS A 335
SHEET 1 H 4 GLU B 5 TRP B 10 0
SHEET 2 H 4 LYS B 193 VAL B 198 1 O THR B 195 N THR B 8
SHEET 3 H 4 TYR B 175 ARG B 180 -1 N ASP B 176 O PHE B 196
SHEET 4 H 4 TRP B 165 LYS B 171 -1 N LYS B 171 O TYR B 175
SHEET 1 I 2 VAL B 38 TYR B 40 0
SHEET 2 I 2 VAL B 46 PRO B 48 -1 O ILE B 47 N LYS B 39
SHEET 1 J 4 ALA B 51 HIS B 56 0
SHEET 2 J 4 THR B 62 LEU B 67 -1 O THR B 66 N SER B 53
SHEET 3 J 4 GLU B 117 LEU B 122 -1 O ILE B 120 N TRP B 63
SHEET 4 J 4 ILE B 107 ALA B 112 -1 N LYS B 111 O GLN B 119
SHEET 1 K 2 PHE B 147 LYS B 148 0
SHEET 2 K 2 GLU B 151 ILE B 156 -1 O GLU B 151 N LYS B 148
SHEET 1 L 3 LEU B 216 GLY B 219 0
SHEET 2 L 3 MET B 473 SER B 476 -1 O MET B 473 N GLY B 219
SHEET 3 L 3 HIS B 239 LEU B 242 -1 N HIS B 239 O SER B 476
SHEET 1 M 6 GLN B 288 VAL B 289 0
SHEET 2 M 6 TYR B 464 ILE B 470 -1 O TYR B 469 N GLN B 288
SHEET 3 M 6 GLU B 247 LEU B 253 -1 N VAL B 249 O SER B 468
SHEET 4 M 6 MET B 392 ARG B 396 -1 O HIS B 395 N MET B 250
SHEET 5 M 6 ARG B 341 ILE B 347 1 N GLU B 343 O MET B 392
SHEET 6 M 6 ASP B 370 GLU B 376 1 O SER B 372 N LEU B 344
LINK FE FE A 503 O18 BHR A 504 1555 1555 1.77
LINK FE FE A 503 O6 BHR A 504 1555 1555 1.86
LINK FE FE A 503 N8 BHR A 504 1555 1555 2.16
LINK FE FE A 503 N11 BHR A 504 1555 1555 2.23
LINK FE FE A 503 O20 BHR A 504 1555 1555 2.23
LINK FE FE A 503 O23 BHR A 504 1555 1555 2.37
LINK O6 BHR B 503 FE FE B 505 1555 1555 1.92
LINK O23 BHR B 503 FE FE B 505 1555 1555 2.06
LINK N11 BHR B 503 FE FE B 505 1555 1555 2.18
LINK O21 BHR B 503 FE FE B 505 1555 1555 2.20
LINK N8 BHR B 503 FE FE B 505 1555 1555 2.22
CISPEP 1 THR A 23 PRO A 24 0 5.00
CISPEP 2 GLU A 58 ASP A 59 0 4.75
CISPEP 3 ARG A 137 PRO A 138 0 3.46
CISPEP 4 ALA A 258 PRO A 259 0 -4.06
CISPEP 5 ALA A 400 PRO A 401 0 3.97
CISPEP 6 ASP A 403 PRO A 404 0 4.80
CISPEP 7 THR B 23 PRO B 24 0 5.87
CISPEP 8 ARG B 137 PRO B 138 0 7.69
CISPEP 9 ALA B 258 PRO B 259 0 -5.67
CISPEP 10 ALA B 328 GLY B 329 0 -3.09
CISPEP 11 ALA B 400 PRO B 401 0 -1.29
CISPEP 12 ASP B 403 PRO B 404 0 2.51
SITE 1 AC1 1 BHR A 504
SITE 1 AC2 10 TYR A 22 THR A 23 MET A 27 TRP A 100
SITE 2 AC2 10 ARG A 137 TRP A 398 HIS A 416 THR A 490
SITE 3 AC2 10 FE A 503 HOH A 543
SITE 1 AC3 5 TRP A 10 PRO A 11 ARG A 205 GLY A 219
SITE 2 AC3 5 ASN A 220
SITE 1 AC4 9 TYR B 22 MET B 27 TRP B 100 ARG B 137
SITE 2 AC4 9 TRP B 398 THR B 490 FE B 505 HOH B 551
SITE 3 AC4 9 HOH B 587
SITE 1 AC5 2 PRO B 11 ASN B 220
SITE 1 AC6 1 BHR B 503
CRYST1 86.983 94.511 125.105 90.00 90.00 90.00 P 21 21 21 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 0.011497 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010581 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007993 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
