HEADER TRANSPORT PROTEIN 05-MAY-10 3MVZ
TITLE X-RAY STRUCTURE OF THE (HYDRO)PEROXO INTERMEDIATE NIKA/1-INT", AFTER
TITLE 2 MONOHYDROXYLATION OF THE IRON COMPLEX
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 3MVZ 1 REMARK LINK
REVDAT 1 09-FEB-11 3MVZ 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. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 105943
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5576
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7722
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE SET COUNT : 406
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7884
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 193
REMARK 3 SOLVENT ATOMS : 1089
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.20000
REMARK 3 B22 (A**2) : -0.50000
REMARK 3 B33 (A**2) : 0.71000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.103
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.063
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.856
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8316 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11304 ; 1.391 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1012 ; 6.096 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 379 ;37.683 ;24.670
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1336 ;13.423 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;15.290 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1222 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6380 ; 0.007 ; 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): 5076 ; 0.846 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8202 ; 1.361 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3240 ; 2.132 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3096 ; 3.446 ; 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 3MVZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059062.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-APR-09
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 : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9334
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105943
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 47.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
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 (%): 45.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM ACETATE, 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 43.36350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.27850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.14900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.27850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.36350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.14900
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 B 115 CG CD CE NZ
REMARK 470 LYS B 330 CG CD CE NZ
REMARK 470 GLU B 334 OE1
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 LYS A 115 NZ
REMARK 480 LYS A 171 CE NZ
REMARK 480 GLN B 309 CG CD OE1 NE2
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 593 O HOH A 902 2.13
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 377 CB GLU A 377 CG -0.129
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 -150.28 -113.40
REMARK 500 TRP A 49 -107.49 -138.57
REMARK 500 PHE A 139 45.25 -90.30
REMARK 500 LYS A 157 -101.91 -87.84
REMARK 500 GLN A 174 -64.70 -121.42
REMARK 500 ASN A 220 -155.04 -83.77
REMARK 500 ASP A 311 83.41 -162.01
REMARK 500 ASN A 336 73.94 44.19
REMARK 500 GLU A 377 151.10 -48.89
REMARK 500 SER A 415 33.03 -87.55
REMARK 500 TYR B 22 -145.09 -110.38
REMARK 500 TRP B 49 -108.44 -136.81
REMARK 500 TYR B 126 122.05 42.12
REMARK 500 PHE B 139 49.30 -92.97
REMARK 500 LYS B 157 -101.15 -91.16
REMARK 500 GLN B 174 -61.62 -136.74
REMARK 500 ASP B 311 86.02 -160.67
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 GLN B 288 -15.72
REMARK 500 GLN B 288 -16.32
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 511 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 BHN A 512 O6
REMARK 620 2 BHN A 512 O22 170.7
REMARK 620 3 BHN A 512 N11 105.1 73.9
REMARK 620 4 BHN A 512 N8 86.3 102.6 80.9
REMARK 620 5 BHN A 512 O20 104.4 81.4 137.5 71.2
REMARK 620 6 BHN A 512 O18 50.4 120.7 80.0 124.6 142.4
REMARK 620 7 PER A 513 O2 87.4 84.8 115.8 163.2 95.3 60.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 506 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 BHN B 507 O6
REMARK 620 2 BHN B 507 O22 170.0
REMARK 620 3 BHN B 507 O20 105.9 79.5
REMARK 620 4 BHN B 507 N11 107.8 72.3 134.4
REMARK 620 5 BHN B 507 N8 86.4 103.3 73.1 79.3
REMARK 620 6 BHN B 507 O18 52.4 118.5 144.9 80.7 124.6
REMARK 620 7 PER B 508 O2 84.3 86.9 95.1 117.8 162.3 59.0
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BHN A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PER A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BHN B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PER B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 512
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MVW RELATED DB: PDB
REMARK 900 RELATED ID: 3MVX RELATED DB: PDB
REMARK 900 RELATED ID: 3MVY RELATED DB: PDB
REMARK 900 RELATED ID: 3MW0 RELATED DB: PDB
REMARK 900 RELATED ID: 3MZ9 RELATED DB: PDB
REMARK 900 RELATED ID: 3MZB RELATED DB: PDB
DBREF 3MVZ A 1 502 UNP P33590 NIKA_ECOLI 23 524
DBREF 3MVZ 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 ACT A 503 4
HET ACT A 504 4
HET ACT A 505 4
HET ACT A 506 4
HET SO4 A 507 5
HET GOL A 508 6
HET GOL A 509 6
HET GOL A 510 6
HET FE A 511 1
HET BHN A 512 28
HET PER A 513 2
HET GOL A 514 6
HET GOL A 515 6
HET GOL A 516 6
HET GOL A 517 6
HET GOL A 518 6
HET GOL A 519 6
HET ACT A 520 4
HET GOL A 521 6
HET ACT A 522 4
HET ACT A 523 4
HET ACT B 503 4
HET ACT B 504 4
HET GOL B 505 6
HET FE B 506 1
HET BHN B 507 28
HET PER B 508 2
HET GOL B 509 6
HET GOL B 510 6
HET GOL B 511 6
HET GOL B 512 6
HETNAM ACT ACETATE ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM FE FE (III) ION
HETNAM BHN 2-[2-[CARBOXYMETHYL-[(2-HYDROXYPHENYL)
HETNAM 2 BHN METHYL]AMINO]ETHYL-[(2-HYDROXYPHENYL)
HETNAM 3 BHN METHYL]AMINO]ETHANOIC ACID
HETNAM PER PEROXIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN BHN N,N'-BIS(2-HYDROXYBENZYL)ETHYLENEDIAMINE-N,N'-DIACETIC
HETSYN 2 BHN ACID
FORMUL 3 ACT 9(C2 H3 O2 1-)
FORMUL 7 SO4 O4 S 2-
FORMUL 8 GOL 15(C3 H8 O3)
FORMUL 11 FE 2(FE 3+)
FORMUL 12 BHN 2(C20 H24 N2 O6)
FORMUL 13 PER 2(O2 2-)
FORMUL 34 HOH *1089(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 VAL A 273 1 12
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 GLN A 366 1 17
HELIX 13 13 GLU A 377 GLY A 388 1 12
HELIX 14 14 PRO A 404 MET A 411 1 8
HELIX 15 15 HIS A 416 GLN A 423 1 8
HELIX 16 16 ASP A 427 ALA A 440 1 14
HELIX 17 17 ASP A 443 GLU A 461 1 19
HELIX 18 18 PRO A 478 GLY A 481 5 4
HELIX 19 19 PRO A 493 ILE A 497 5 5
HELIX 20 20 GLN B 26 TYR B 34 1 9
HELIX 21 21 ASP B 80 ASP B 93 1 14
HELIX 22 22 ASN B 94 ALA B 99 5 6
HELIX 23 23 LEU B 101 GLN B 106 1 6
HELIX 24 24 PRO B 128 ALA B 134 1 7
HELIX 25 25 ALA B 143 SER B 145 5 3
HELIX 26 26 ASP B 201 THR B 211 1 11
HELIX 27 27 PRO B 225 GLN B 234 1 10
HELIX 28 28 GLU B 262 VAL B 273 1 12
HELIX 29 29 ASN B 274 LEU B 283 1 10
HELIX 30 30 ASP B 311 ALA B 322 1 12
HELIX 31 31 ASP B 350 GLN B 366 1 17
HELIX 32 32 GLU B 377 GLY B 388 1 12
HELIX 33 33 PRO B 404 MET B 411 1 8
HELIX 34 34 HIS B 416 GLN B 422 1 7
HELIX 35 35 ASP B 427 THR B 441 1 15
HELIX 36 36 ASP B 443 GLU B 461 1 19
HELIX 37 37 PRO B 478 GLY B 481 5 4
HELIX 38 38 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 ILE A 166 O VAL A 179
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 LYS A 111 O GLN A 119
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 MET A 473 SER A 476 -1 O MET A 473 N GLY A 219
SHEET 3 E 3 HIS A 239 LEU A 242 -1 N HIS A 239 O SER A 476
SHEET 1 F 6 GLN A 288 VAL A 289 0
SHEET 2 F 6 TYR A 464 ILE A 470 -1 O TYR A 469 N GLN A 288
SHEET 3 F 6 GLU A 247 LEU A 253 -1 N VAL A 249 O SER A 468
SHEET 4 F 6 MET A 392 ARG A 396 -1 O ILE A 393 N ALA A 252
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 VAL B 108 O THR B 121
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 TYR B 464 SER B 476 -1 O MET B 473 N GLY B 219
SHEET 3 L 3 GLN B 288 VAL B 289 -1 N GLN B 288 O TYR B 469
SHEET 1 M 6 LEU B 216 GLY B 219 0
SHEET 2 M 6 TYR B 464 SER B 476 -1 O MET B 473 N GLY B 219
SHEET 3 M 6 HIS B 239 LEU B 253 -1 N ILE B 246 O ILE B 470
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
SHEET 1 N 2 GLU B 334 LYS B 335 0
SHEET 2 N 2 GLN B 338 PRO B 339 -1 O GLN B 338 N LYS B 335
LINK FE FE A 511 O6 BHN A 512 1555 1555 1.94
LINK FE FE A 511 O22 BHN A 512 1555 1555 2.10
LINK FE FE A 511 N11 BHN A 512 1555 1555 2.14
LINK FE FE A 511 N8 BHN A 512 1555 1555 2.25
LINK FE FE A 511 O20 BHN A 512 1555 1555 2.26
LINK FE FE A 511 O18 BHN A 512 1555 1555 2.68
LINK FE FE A 511 O2 PER A 513 1555 1555 2.22
LINK FE FE B 506 O6 BHN B 507 1555 1555 1.88
LINK FE FE B 506 O22 BHN B 507 1555 1555 2.13
LINK FE FE B 506 O20 BHN B 507 1555 1555 2.22
LINK FE FE B 506 N11 BHN B 507 1555 1555 2.26
LINK FE FE B 506 N8 BHN B 507 1555 1555 2.29
LINK FE FE B 506 O18 BHN B 507 1555 1555 2.78
LINK FE FE B 506 O2 PER B 508 1555 1555 2.33
CISPEP 1 THR A 23 PRO A 24 0 11.59
CISPEP 2 ARG A 137 PRO A 138 0 5.54
CISPEP 3 ALA A 258 PRO A 259 0 -1.32
CISPEP 4 ALA A 328 GLY A 329 0 6.82
CISPEP 5 ALA A 400 PRO A 401 0 1.68
CISPEP 6 ASP A 403 PRO A 404 0 3.00
CISPEP 7 THR B 23 PRO B 24 0 11.66
CISPEP 8 ARG B 137 PRO B 138 0 9.03
CISPEP 9 ALA B 258 PRO B 259 0 -4.55
CISPEP 10 ALA B 328 GLY B 329 0 -8.57
CISPEP 11 ALA B 400 PRO B 401 0 0.27
CISPEP 12 ASP B 403 PRO B 404 0 2.11
SITE 1 AC1 4 LYS A 52 ARG A 68 ASP A 69 HOH A 622
SITE 1 AC2 3 ASN A 261 LEU A 263 HOH A 727
SITE 1 AC3 5 ASN A 235 ALA A 237 PHE A 419 GLN A 423
SITE 2 AC3 5 HOH A 914
SITE 1 AC4 2 ASN A 482 GLN A 496
SITE 1 AC5 6 ARG A 384 HOH A 854 HOH A 861 LEU B 430
SITE 2 AC5 6 ARG B 457 HOH B 568
SITE 1 AC6 5 LEU A 167 GLN A 168 HOH A 660 THR B 211
SITE 2 AC6 5 ASP B 213
SITE 1 AC7 2 ASN A 149 LYS A 157
SITE 1 AC8 9 GLN A 361 ASP A 370 VAL A 371 SER A 372
SITE 2 AC8 9 LEU A 373 ASN B 149 LYS B 157 HOH B 582
SITE 3 AC8 9 HOH B 782
SITE 1 AC9 2 BHN A 512 PER A 513
SITE 1 BC1 13 TYR A 22 MET A 27 ARG A 97 TRP A 100
SITE 2 BC1 13 ARG A 137 TRP A 398 HIS A 416 THR A 490
SITE 3 BC1 13 FE A 511 PER A 513 HOH A 607 HOH A 676
SITE 4 BC1 13 HOH A 720
SITE 1 BC2 3 ARG A 137 FE A 511 BHN A 512
SITE 1 BC3 6 ASN A 220 GLU A 247 THR A 490 GOL A 521
SITE 2 BC3 6 HOH A 548 HOH A 928
SITE 1 BC4 9 ARG A 89 LEU A 92 ARG A 95 ILE A 107
SITE 2 BC4 9 VAL A 108 ASP A 109 VAL A 110 ASN A 281
SITE 3 BC4 9 HOH A 728
SITE 1 BC5 6 GLU A 102 ASN A 105 LYS A 123 THR A 228
SITE 2 BC5 6 ARG A 231 HOH A 584
SITE 1 BC6 8 VAL A 273 ASN A 274 LYS A 275 LYS A 276
SITE 2 BC6 8 GLN A 309 TYR A 310 HOH A 922 HOH A1120
SITE 1 BC7 8 GLU A 82 ARG A 89 PRO A 144 PHE A 147
SITE 2 BC7 8 HIS A 150 HOH A 763 HOH A 959 HOH A1203
SITE 1 BC8 6 ASN A 302 GLY A 304 HOH A 900 PHE B 229
SITE 2 BC8 6 ALA B 230 SER B 233
SITE 1 BC9 3 THR A 23 GLN A 26 HOH A 646
SITE 1 CC1 6 TRP A 10 GLY A 219 ASN A 220 GLY A 222
SITE 2 CC1 6 LEU A 223 GOL A 514
SITE 1 CC2 4 ASP A 331 ARG A 365 HOH A1105 LYS B 148
SITE 1 CC3 3 THR A 441 HIS A 442 ASP A 443
SITE 1 CC4 6 THR B 23 GLN B 26 GLU B 378 PER B 508
SITE 2 CC4 6 HOH B 626 HOH B 697
SITE 1 CC5 4 VAL B 273 LYS B 275 LYS B 276 TYR B 310
SITE 1 CC6 7 TRP B 10 PRO B 11 GLY B 219 ASN B 220
SITE 2 CC6 7 GLY B 222 LEU B 223 GOL B 509
SITE 1 CC7 2 BHN B 507 PER B 508
SITE 1 CC8 11 TYR B 22 MET B 27 ARG B 97 TRP B 100
SITE 2 CC8 11 ARG B 137 TRP B 398 THR B 490 FE B 506
SITE 3 CC8 11 PER B 508 HOH B 635 HOH B1202
SITE 1 CC9 4 ARG B 137 ACT B 503 FE B 506 BHN B 507
SITE 1 DC1 8 ASN B 220 GLU B 247 ARG B 396 MET B 472
SITE 2 DC1 8 ALA B 489 THR B 490 GOL B 505 HOH B 577
SITE 1 DC2 8 LEU A 21 TYR A 22 THR A 23 ARG A 97
SITE 2 DC2 8 HOH A 644 HOH A 748 LYS B 314 HOH B 657
SITE 1 DC3 9 ASP A 43 PRO A 299 GLN B 241 ASN B 482
SITE 2 DC3 9 ILE B 483 PRO B 484 TYR B 485 HOH B 526
SITE 3 DC3 9 HOH B 695
SITE 1 DC4 8 GLU B 221 VAL B 249 SER B 353 MET B 356
SITE 2 DC4 8 PHE B 394 ARG B 396 HOH B 848 HOH B1114
CRYST1 86.727 94.298 124.557 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 0.011530 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010605 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008028 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
