HEADER OXIDOREDUCTASE 11-MAY-13 4KO1
TITLE HIGH X-RAY DOSE STRUCTURE OF H2-ACTIVATED ANAEROBICALLY PURIFIED DM.
TITLE 2 BACULATUM [NIFESE]-HYDROGENASE AFTER CRYSTALLIZATION UNDER AIR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC [NIFESE] HYDROGENASE SMALL SUBUNIT;
COMPND 3 CHAIN: S, T;
COMPND 4 SYNONYM: NIFESE HYDROGENLYASE SMALL CHAIN;
COMPND 5 EC: 1.12.99.6;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: NICKEL-DEPENDENT HYDROGENASE LARGE SUBUNIT;
COMPND 8 CHAIN: L, M;
COMPND 9 EC: 1.18.99.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOMICROBIUM BACULATUM;
SOURCE 3 ORGANISM_TAXID: 899;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: DESULFOMICROBIUM BACULATUM;
SOURCE 6 ORGANISM_TAXID: 525897;
SOURCE 7 STRAIN: DSM 4028 / VKM B-1378
KEYWDS NIFESE-SITE, O2-RESISTANCE, H2-CLEAVAGE/PRODUCTION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VOLBEDA,C.CAVAZZA,J.C.FONTECILLA-CAMPS
REVDAT 6 20-SEP-23 4KO1 1 REMARK LINK
REVDAT 5 06-AUG-14 4KO1 1 HET HETNAM FORMUL LINK
REVDAT 4 09-APR-14 4KO1 1 REMARK SEQRES HET MODRES
REVDAT 4 2 1 HETNAM FORMUL HELIX LINK
REVDAT 4 3 1 SITE HETATM
REVDAT 3 24-JUL-13 4KO1 1 JRNL
REVDAT 2 17-JUL-13 4KO1 1 JRNL
REVDAT 1 10-JUL-13 4KO1 0
JRNL AUTH A.VOLBEDA,P.AMARA,M.IANNELLO,A.L.DE LACEY,C.CAVAZZA,
JRNL AUTH 2 J.C.FONTECILLA-CAMPS
JRNL TITL STRUCTURAL FOUNDATIONS FOR THE O2 RESISTANCE OF
JRNL TITL 2 DESULFOMICROBIUM BACULATUM [NIFESE]-HYDROGENASE.
JRNL REF CHEM.COMMUN.(CAMB.) V. 49 7061 2013
JRNL REFN ISSN 1359-7345
JRNL PMID 23811828
JRNL DOI 10.1039/C3CC43619E
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.GARCIN,X.VERNEDE,E.C.HATCHIKIAN,A.VOLBEDA,M.FREY,
REMARK 1 AUTH 2 J.C.FONTECILLA-CAMPS
REMARK 1 TITL THE CRYSTAL STRUCTURE OF A REDUCED [NIFESE] HYDROGENASE
REMARK 1 TITL 2 PROVIDES AN IMAGE OF THE ACTIVATED CATALYTIC CENTER.
REMARK 1 REF STRUCTURE V. 7 557 1999
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 10378275
REMARK 2
REMARK 2 RESOLUTION. 1.55 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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 196199
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) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 10443
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9023
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 56.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE SET COUNT : 455
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11916
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 97
REMARK 3 SOLVENT ATOMS : 1770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.09000
REMARK 3 B22 (A**2) : -0.54000
REMARK 3 B33 (A**2) : 0.63000
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): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.080
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.507
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12706 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17249 ; 1.263 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1562 ; 5.539 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 567 ;36.176 ;24.409
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2157 ;11.409 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 65 ;17.242 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1906 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9571 ; 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): 7758 ; 2.019 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12606 ; 3.019 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4948 ; 4.265 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4560 ; 6.047 ; 5.000
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): 12706 ; 2.217 ; 3.000
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 : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 4KO1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079578.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9500
REMARK 200 MONOCHROMATOR : TWO CRYSTALS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 206663
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 61.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.62800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.030
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 4KL8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 4000, 0.2M CACL2, 0.1M
REMARK 280 TRIS/HCL, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 53.11500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.17000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.45500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.17000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.11500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.45500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -137.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, L
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -144.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, M
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET S 1
REMARK 465 THR S 2
REMARK 465 GLU S 3
REMARK 465 GLY S 4
REMARK 465 MET L 0
REMARK 465 SER L 1
REMARK 465 GLN L 2
REMARK 465 ALA L 3
REMARK 465 ALA L 4
REMARK 465 THR L 5
REMARK 465 PRO L 6
REMARK 465 ALA L 7
REMARK 465 ALA L 8
REMARK 465 ASP L 9
REMARK 465 MET T 1
REMARK 465 THR T 2
REMARK 465 GLU T 3
REMARK 465 GLY T 4
REMARK 465 MET M 0
REMARK 465 SER M 1
REMARK 465 GLN M 2
REMARK 465 ALA M 3
REMARK 465 ALA M 4
REMARK 465 THR M 5
REMARK 465 PRO M 6
REMARK 465 ALA M 7
REMARK 465 ALA M 8
REMARK 465 ASP M 9
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 ASN S 71 31.29 -146.81
REMARK 500 ASP S 96 -166.48 -54.58
REMARK 500 ASN S 184 88.00 -153.42
REMARK 500 ARG S 250 -167.99 56.19
REMARK 500 ALA S 262 -106.12 -161.23
REMARK 500 TYR L 125 -33.81 -132.71
REMARK 500 ASP L 130 48.33 -86.62
REMARK 500 HIS L 188 79.08 73.63
REMARK 500 GLU L 223 -59.25 -121.41
REMARK 500 TYR L 235 54.91 -107.81
REMARK 500 PHE L 254 76.60 66.79
REMARK 500 ASN L 310 87.66 -152.31
REMARK 500 ALA L 447 -81.33 22.12
REMARK 500 HIS T 46 113.37 -162.44
REMARK 500 ASN T 71 23.61 -141.25
REMARK 500 ASN T 184 73.98 -150.31
REMARK 500 ARG T 250 -160.64 58.18
REMARK 500 ALA T 262 -108.26 -159.99
REMARK 500 TYR M 125 -31.65 -135.23
REMARK 500 ASN M 140 77.62 -112.79
REMARK 500 ASP M 150 96.90 -68.89
REMARK 500 HIS M 188 79.07 76.33
REMARK 500 GLU M 223 -57.71 -126.47
REMARK 500 TYR M 235 54.81 -106.51
REMARK 500 PHE M 254 75.78 66.47
REMARK 500 ALA M 447 -82.68 21.05
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 SF4 S 303 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 18 SG
REMARK 620 2 SF4 S 303 S1 121.5
REMARK 620 3 SF4 S 303 S2 114.2 104.9
REMARK 620 4 SF4 S 303 S3 102.0 107.4 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 303 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 21 SG
REMARK 620 2 SF4 S 303 S1 114.0
REMARK 620 3 SF4 S 303 S3 122.4 107.9
REMARK 620 4 SF4 S 303 S4 105.8 102.9 101.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 303 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 126 SG
REMARK 620 2 SF4 S 303 S1 130.0
REMARK 620 3 SF4 S 303 S2 98.1 104.2
REMARK 620 4 SF4 S 303 S4 111.7 102.4 109.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA S 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU S 152 O
REMARK 620 2 HOH S 455 O 82.2
REMARK 620 3 HOH S 456 O 87.4 81.5
REMARK 620 4 HOH S 458 O 94.0 154.0 72.6
REMARK 620 5 HOH S 472 O 83.4 139.8 135.0 64.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 303 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 164 SG
REMARK 620 2 SF4 S 303 S2 100.9
REMARK 620 3 SF4 S 303 S3 125.2 105.0
REMARK 620 4 SF4 S 303 S4 114.8 108.6 101.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 301 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS S 208 ND1
REMARK 620 2 SF4 S 301 S1 119.6
REMARK 620 3 SF4 S 301 S2 116.2 102.5
REMARK 620 4 SF4 S 301 S4 102.7 107.4 107.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 301 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 211 SG
REMARK 620 2 SF4 S 301 S1 108.7
REMARK 620 3 SF4 S 301 S3 119.7 105.8
REMARK 620 4 SF4 S 301 S4 112.0 107.4 102.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 301 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 231 SG
REMARK 620 2 SF4 S 301 S2 102.2
REMARK 620 3 SF4 S 301 S3 119.9 103.1
REMARK 620 4 SF4 S 301 S4 118.6 108.2 103.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 301 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 237 SG
REMARK 620 2 SF4 S 301 S1 109.4
REMARK 620 3 SF4 S 301 S2 116.2 103.4
REMARK 620 4 SF4 S 301 S3 118.2 105.1 103.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 302 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 246 SG
REMARK 620 2 SF4 S 302 S1 122.8
REMARK 620 3 SF4 S 302 S3 105.4 102.0
REMARK 620 4 SF4 S 302 S4 115.6 103.9 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 302 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 258 SG
REMARK 620 2 SF4 S 302 S2 114.2
REMARK 620 3 SF4 S 302 S3 116.4 104.3
REMARK 620 4 SF4 S 302 S4 110.7 105.7 104.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 302 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 264 SG
REMARK 620 2 SF4 S 302 S1 116.3
REMARK 620 3 SF4 S 302 S2 112.6 103.3
REMARK 620 4 SF4 S 302 S4 113.6 104.7 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 302 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 267 SG
REMARK 620 2 SF4 S 302 S1 122.1
REMARK 620 3 SF4 S 302 S2 113.9 104.3
REMARK 620 4 SF4 S 302 S3 106.8 103.2 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA S 307 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH S 539 O
REMARK 620 2 HOH S 634 O 96.5
REMARK 620 3 HOH S 652 O 70.2 86.9
REMARK 620 4 HOH S 754 O 76.8 172.5 87.6
REMARK 620 5 HOH L 897 O 72.2 88.1 141.2 93.0
REMARK 620 6 HOH L1085 O 151.9 83.8 137.7 103.6 79.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA L 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU L 51 OE1
REMARK 620 2 ILE L 444 O 93.9
REMARK 620 3 HIS L 498 NE2 87.8 85.7
REMARK 620 4 HOH L 608 O 171.9 94.1 93.8
REMARK 620 5 HOH L 609 O 89.3 91.6 175.9 89.4
REMARK 620 6 HOH L 610 O 89.1 171.2 86.1 83.1 96.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI L 502 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 70 SG
REMARK 620 2 CYS L 73 SG 101.6
REMARK 620 3 SEC L 492 SE 85.4 171.7
REMARK 620 4 CYS L 495 SG 115.1 75.9 97.1
REMARK 620 5 HOH L 607 O 151.9 87.2 88.8 92.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI L 502 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 70 SG
REMARK 620 2 CYS L 73 SG 99.3
REMARK 620 3 SEC L 492 SE 108.5 151.5
REMARK 620 4 HOH L 607 O 164.0 87.1 64.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FCO L 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 73 SG
REMARK 620 2 FCO L 501 C1 165.5
REMARK 620 3 FCO L 501 C2 95.0 88.9
REMARK 620 4 FCO L 501 C3 102.5 91.0 95.9
REMARK 620 5 CYS L 495 SG 81.7 92.4 171.1 92.9
REMARK 620 6 HOH L 607 O 84.3 82.8 79.0 172.0 92.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 303 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 18 SG
REMARK 620 2 SF4 T 303 S1 122.4
REMARK 620 3 SF4 T 303 S2 113.5 104.1
REMARK 620 4 SF4 T 303 S3 101.8 107.7 106.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 303 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 21 SG
REMARK 620 2 SF4 T 303 S1 114.1
REMARK 620 3 SF4 T 303 S3 122.0 107.5
REMARK 620 4 SF4 T 303 S4 105.9 102.6 102.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 303 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 126 SG
REMARK 620 2 SF4 T 303 S1 131.1
REMARK 620 3 SF4 T 303 S2 97.9 103.6
REMARK 620 4 SF4 T 303 S4 110.5 102.5 110.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 303 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 164 SG
REMARK 620 2 SF4 T 303 S2 100.8
REMARK 620 3 SF4 T 303 S3 125.1 105.1
REMARK 620 4 SF4 T 303 S4 114.5 108.2 102.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA T 306 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP T 195 O
REMARK 620 2 ASP T 196 OD1 77.8
REMARK 620 3 HOH T 484 O 56.6 124.6
REMARK 620 4 HOH T 591 O 127.8 80.7 102.3
REMARK 620 5 HOH T 725 O 162.3 114.0 118.5 68.9
REMARK 620 6 HOH T 731 O 107.2 175.0 59.9 96.3 61.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 301 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS T 208 ND1
REMARK 620 2 SF4 T 301 S1 120.6
REMARK 620 3 SF4 T 301 S2 117.9 102.5
REMARK 620 4 SF4 T 301 S4 100.4 107.6 106.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 301 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 211 SG
REMARK 620 2 SF4 T 301 S1 109.7
REMARK 620 3 SF4 T 301 S3 117.0 105.6
REMARK 620 4 SF4 T 301 S4 112.3 107.3 104.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 301 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 231 SG
REMARK 620 2 SF4 T 301 S2 102.9
REMARK 620 3 SF4 T 301 S3 119.3 103.6
REMARK 620 4 SF4 T 301 S4 117.8 107.1 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 301 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 237 SG
REMARK 620 2 SF4 T 301 S1 110.8
REMARK 620 3 SF4 T 301 S2 115.8 103.2
REMARK 620 4 SF4 T 301 S3 115.3 106.4 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 302 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 246 SG
REMARK 620 2 SF4 T 302 S1 121.4
REMARK 620 3 SF4 T 302 S3 105.4 102.9
REMARK 620 4 SF4 T 302 S4 115.9 104.5 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 302 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 258 SG
REMARK 620 2 SF4 T 302 S2 113.9
REMARK 620 3 SF4 T 302 S3 115.4 104.4
REMARK 620 4 SF4 T 302 S4 111.6 105.2 105.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 302 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 264 SG
REMARK 620 2 SF4 T 302 S1 116.6
REMARK 620 3 SF4 T 302 S2 112.1 103.7
REMARK 620 4 SF4 T 302 S4 113.7 104.1 105.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 302 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 267 SG
REMARK 620 2 SF4 T 302 S1 121.9
REMARK 620 3 SF4 T 302 S2 113.2 104.3
REMARK 620 4 SF4 T 302 S3 107.6 103.4 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA T 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP T 271 OD2
REMARK 620 2 GLY T 275 O 82.2
REMARK 620 3 HOH T 407 O 71.9 153.5
REMARK 620 4 HOH T 478 O 81.0 71.9 97.9
REMARK 620 5 HOH T 508 O 141.4 63.5 142.8 102.9
REMARK 620 6 HOH T 728 O 145.6 128.8 75.2 94.0 73.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA T 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH T 515 O
REMARK 620 2 HOH T 537 O 150.3
REMARK 620 3 HOH T 547 O 85.0 86.5
REMARK 620 4 HOH T 556 O 81.6 69.2 83.5
REMARK 620 5 HOH T 589 O 91.7 96.9 176.5 97.0
REMARK 620 6 HOH M 612 O 71.8 136.1 87.2 152.5 90.8
REMARK 620 7 HOH M 617 O 142.7 67.0 105.2 134.6 76.9 72.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA M 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU M 51 OE1
REMARK 620 2 ILE M 444 O 92.5
REMARK 620 3 HIS M 498 NE2 86.3 85.1
REMARK 620 4 HOH M 623 O 171.6 95.9 94.1
REMARK 620 5 HOH M 624 O 86.9 97.9 172.7 92.2
REMARK 620 6 HOH M 625 O 87.1 171.7 86.6 84.6 90.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI M 502 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 70 SG
REMARK 620 2 CYS M 73 SG 100.6
REMARK 620 3 SEC M 492 SE 86.0 170.9
REMARK 620 4 CYS M 495 SG 114.1 75.2 96.5
REMARK 620 5 HOH M 622 O 152.6 86.1 90.9 93.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI M 502 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 70 SG
REMARK 620 2 CYS M 73 SG 99.3
REMARK 620 3 SEC M 492 SE 108.8 151.4
REMARK 620 4 HOH M 622 O 165.6 86.9 64.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FCO M 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 73 SG
REMARK 620 2 FCO M 501 C1 165.6
REMARK 620 3 FCO M 501 C2 94.8 89.0
REMARK 620 4 FCO M 501 C3 102.4 91.1 95.7
REMARK 620 5 CYS M 495 SG 81.0 93.4 171.7 92.1
REMARK 620 6 HOH M 622 O 83.7 83.6 77.1 171.1 95.3
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 SF4 S 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 S 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 S 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA S 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL S 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL S 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA S 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FCO L 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI L 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S L 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 T 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 T 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 T 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA T 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA T 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA T 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FCO M 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI M 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA M 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S M 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL M 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL M 506
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CC1 RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF A REDUCED [NIFESE]-HYDROGENASE PROVIDES AN
REMARK 900 IMAGE OF THE ACTIVATED CATALYTIC CENTER
REMARK 900 RELATED ID: 4KL8 RELATED DB: PDB
REMARK 900 RELATED ID: 4KN9 RELATED DB: PDB
REMARK 900 RELATED ID: 4KO2 RELATED DB: PDB
REMARK 900 RELATED ID: 4KO3 RELATED DB: PDB
REMARK 900 RELATED ID: 4KO4 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE IS A SELENOCYSTEINE AT POSITIONS L 492 AND M 492. TWO MINOR
REMARK 999 CONFORMATIONS OF THE NIFESE SITE CALLED D AND Q ARE ONLY PARTIALLY
REMARK 999 RESOLVED.
DBREF 4KO1 S 1 283 UNP P13063 PHSS_DESBA 33 315
DBREF 4KO1 L 0 498 UNP C7LN88 C7LN88_DESBD 1 499
DBREF 4KO1 T 1 283 UNP P13063 PHSS_DESBA 33 315
DBREF 4KO1 M 0 498 UNP C7LN88 C7LN88_DESBD 1 499
SEQRES 1 S 283 MET THR GLU GLY ALA LYS LYS ALA PRO VAL ILE TRP VAL
SEQRES 2 S 283 GLN GLY GLN GLY CYS THR GLY CYS SER VAL SER LEU LEU
SEQRES 3 S 283 ASN ALA VAL HIS PRO ARG ILE LYS GLU ILE LEU LEU ASP
SEQRES 4 S 283 VAL ILE SER LEU GLU PHE HIS PRO THR VAL MET ALA SER
SEQRES 5 S 283 GLU GLY GLU MET ALA LEU ALA HIS MET TYR GLU ILE ALA
SEQRES 6 S 283 GLU LYS PHE ASN GLY ASN PHE PHE LEU LEU VAL GLU GLY
SEQRES 7 S 283 ALA ILE PRO THR ALA LYS GLU GLY ARG TYR CYS ILE VAL
SEQRES 8 S 283 GLY GLU THR LEU ASP ALA LYS GLY HIS HIS HIS GLU VAL
SEQRES 9 S 283 THR MET MET GLU LEU ILE ARG ASP LEU ALA PRO LYS SER
SEQRES 10 S 283 LEU ALA THR VAL ALA VAL GLY THR CYS SER ALA TYR GLY
SEQRES 11 S 283 GLY ILE PRO ALA ALA GLU GLY ASN VAL THR GLY SER LYS
SEQRES 12 S 283 SER VAL ARG ASP PHE PHE ALA ASP GLU LYS ILE GLU LYS
SEQRES 13 S 283 LEU LEU VAL ASN VAL PRO GLY CYS PRO PRO HIS PRO ASP
SEQRES 14 S 283 TRP MET VAL GLY THR LEU VAL ALA ALA TRP SER HIS VAL
SEQRES 15 S 283 LEU ASN PRO THR GLU HIS PRO LEU PRO GLU LEU ASP ASP
SEQRES 16 S 283 ASP GLY ARG PRO LEU LEU PHE PHE GLY ASP ASN ILE HIS
SEQRES 17 S 283 GLU ASN CYS PRO TYR LEU ASP LYS TYR ASP ASN SER GLU
SEQRES 18 S 283 PHE ALA GLU THR PHE THR LYS PRO GLY CYS LYS ALA GLU
SEQRES 19 S 283 LEU GLY CYS LYS GLY PRO SER THR TYR ALA ASP CYS ALA
SEQRES 20 S 283 LYS ARG ARG TRP ASN ASN GLY ILE ASN TRP CYS VAL GLU
SEQRES 21 S 283 ASN ALA VAL CYS ILE GLY CYS VAL GLU PRO ASP PHE PRO
SEQRES 22 S 283 ASP GLY LYS SER PRO PHE TYR VAL ALA GLU
SEQRES 1 L 499 MET SER GLN ALA ALA THR PRO ALA ALA ASP GLY LYS VAL
SEQRES 2 L 499 LYS ILE SER ILE ASP PRO LEU THR ARG VAL GLU GLY HIS
SEQRES 3 L 499 LEU LYS ILE GLU VAL GLU VAL LYS ASP GLY LYS VAL VAL
SEQRES 4 L 499 ASP ALA LYS CYS SER GLY GLY MET PHE ARG GLY PHE GLU
SEQRES 5 L 499 GLN ILE LEU ARG GLY ARG ASP PRO ARG ASP SER SER GLN
SEQRES 6 L 499 ILE VAL GLN ARG ILE CYS GLY VAL CYS PRO THR ALA HIS
SEQRES 7 L 499 CYS THR ALA SER VAL MET ALA GLN ASP ASP ALA PHE GLY
SEQRES 8 L 499 VAL LYS VAL THR THR ASN GLY ARG ILE THR ARG ASN LEU
SEQRES 9 L 499 ILE PHE GLY ALA ASN TYR LEU GLN SER HIS ILE LEU HIS
SEQRES 10 L 499 PHE TYR HIS LEU ALA ALA LEU ASP TYR VAL LYS GLY PRO
SEQRES 11 L 499 ASP VAL SER PRO PHE VAL PRO ARG TYR ALA ASN ALA ASP
SEQRES 12 L 499 LEU LEU THR ASP ARG ILE LYS ASP GLY ALA LYS ALA ASP
SEQRES 13 L 499 ALA THR ASN THR TYR GLY LEU ASN GLN TYR LEU LYS ALA
SEQRES 14 L 499 LEU GLU ILE ARG ARG ILE CYS HIS GLU MET VAL ALA MET
SEQRES 15 L 499 PHE GLY GLY ARG MET PRO HIS VAL GLN GLY MET VAL VAL
SEQRES 16 L 499 GLY GLY ALA THR GLU ILE PRO THR ALA ASP LYS VAL ALA
SEQRES 17 L 499 GLU TYR ALA ALA ARG PHE LYS GLU VAL GLN LYS PHE VAL
SEQRES 18 L 499 ILE GLU GLU TYR LEU PRO LEU ILE TYR THR LEU GLY SER
SEQRES 19 L 499 VAL TYR THR ASP LEU PHE GLU THR GLY ILE GLY TRP LYS
SEQRES 20 L 499 ASN VAL ILE ALA PHE GLY VAL PHE PRO GLU ASP ASP ASP
SEQRES 21 L 499 TYR LYS THR PHE LEU LEU LYS PRO GLY VAL TYR ILE ASP
SEQRES 22 L 499 GLY LYS ASP GLU GLU PHE ASP SER LYS LEU VAL LYS GLU
SEQRES 23 L 499 TYR VAL GLY HIS SER PHE PHE ASP HIS SER ALA PRO GLY
SEQRES 24 L 499 GLY LEU HIS TYR SER VAL GLY GLU THR ASN PRO ASN PRO
SEQRES 25 L 499 ASP LYS PRO GLY ALA TYR SER PHE VAL LYS ALA PRO ARG
SEQRES 26 L 499 TYR LYS ASP LYS PRO CYS GLU VAL GLY PRO LEU ALA ARG
SEQRES 27 L 499 MET TRP VAL GLN ASN PRO GLU LEU SER PRO VAL GLY GLN
SEQRES 28 L 499 LYS LEU LEU LYS GLU LEU TYR GLY ILE GLU ALA LYS ASN
SEQRES 29 L 499 PHE ARG ASP LEU GLY ASP LYS ALA PHE SER ILE MET GLY
SEQRES 30 L 499 ARG HIS VAL ALA ARG ALA GLU GLU THR TRP LEU THR ALA
SEQRES 31 L 499 VAL ALA VAL GLU LYS TRP LEU LYS GLN VAL GLN PRO GLY
SEQRES 32 L 499 ALA GLU THR TYR VAL LYS SER GLU ILE PRO ASP ALA ALA
SEQRES 33 L 499 GLU GLY THR GLY PHE THR GLU ALA PRO ARG GLY ALA LEU
SEQRES 34 L 499 LEU HIS TYR LEU LYS ILE LYS ASP LYS LYS ILE GLU ASN
SEQRES 35 L 499 TYR GLN ILE VAL SER ALA THR LEU TRP ASN ALA ASN PRO
SEQRES 36 L 499 ARG ASP ASP MET GLY GLN ARG GLY PRO ILE GLU GLU ALA
SEQRES 37 L 499 LEU ILE GLY VAL PRO VAL PRO ASP ILE LYS ASN PRO VAL
SEQRES 38 L 499 ASN VAL GLY ARG LEU VAL ARG SER TYR ASP PRO SEC LEU
SEQRES 39 L 499 GLY CYS ALA VAL HIS
SEQRES 1 T 283 MET THR GLU GLY ALA LYS LYS ALA PRO VAL ILE TRP VAL
SEQRES 2 T 283 GLN GLY GLN GLY CYS THR GLY CYS SER VAL SER LEU LEU
SEQRES 3 T 283 ASN ALA VAL HIS PRO ARG ILE LYS GLU ILE LEU LEU ASP
SEQRES 4 T 283 VAL ILE SER LEU GLU PHE HIS PRO THR VAL MET ALA SER
SEQRES 5 T 283 GLU GLY GLU MET ALA LEU ALA HIS MET TYR GLU ILE ALA
SEQRES 6 T 283 GLU LYS PHE ASN GLY ASN PHE PHE LEU LEU VAL GLU GLY
SEQRES 7 T 283 ALA ILE PRO THR ALA LYS GLU GLY ARG TYR CYS ILE VAL
SEQRES 8 T 283 GLY GLU THR LEU ASP ALA LYS GLY HIS HIS HIS GLU VAL
SEQRES 9 T 283 THR MET MET GLU LEU ILE ARG ASP LEU ALA PRO LYS SER
SEQRES 10 T 283 LEU ALA THR VAL ALA VAL GLY THR CYS SER ALA TYR GLY
SEQRES 11 T 283 GLY ILE PRO ALA ALA GLU GLY ASN VAL THR GLY SER LYS
SEQRES 12 T 283 SER VAL ARG ASP PHE PHE ALA ASP GLU LYS ILE GLU LYS
SEQRES 13 T 283 LEU LEU VAL ASN VAL PRO GLY CYS PRO PRO HIS PRO ASP
SEQRES 14 T 283 TRP MET VAL GLY THR LEU VAL ALA ALA TRP SER HIS VAL
SEQRES 15 T 283 LEU ASN PRO THR GLU HIS PRO LEU PRO GLU LEU ASP ASP
SEQRES 16 T 283 ASP GLY ARG PRO LEU LEU PHE PHE GLY ASP ASN ILE HIS
SEQRES 17 T 283 GLU ASN CYS PRO TYR LEU ASP LYS TYR ASP ASN SER GLU
SEQRES 18 T 283 PHE ALA GLU THR PHE THR LYS PRO GLY CYS LYS ALA GLU
SEQRES 19 T 283 LEU GLY CYS LYS GLY PRO SER THR TYR ALA ASP CYS ALA
SEQRES 20 T 283 LYS ARG ARG TRP ASN ASN GLY ILE ASN TRP CYS VAL GLU
SEQRES 21 T 283 ASN ALA VAL CYS ILE GLY CYS VAL GLU PRO ASP PHE PRO
SEQRES 22 T 283 ASP GLY LYS SER PRO PHE TYR VAL ALA GLU
SEQRES 1 M 499 MET SER GLN ALA ALA THR PRO ALA ALA ASP GLY LYS VAL
SEQRES 2 M 499 LYS ILE SER ILE ASP PRO LEU THR ARG VAL GLU GLY HIS
SEQRES 3 M 499 LEU LYS ILE GLU VAL GLU VAL LYS ASP GLY LYS VAL VAL
SEQRES 4 M 499 ASP ALA LYS CYS SER GLY GLY MET PHE ARG GLY PHE GLU
SEQRES 5 M 499 GLN ILE LEU ARG GLY ARG ASP PRO ARG ASP SER SER GLN
SEQRES 6 M 499 ILE VAL GLN ARG ILE CYS GLY VAL CYS PRO THR ALA HIS
SEQRES 7 M 499 CYS THR ALA SER VAL MET ALA GLN ASP ASP ALA PHE GLY
SEQRES 8 M 499 VAL LYS VAL THR THR ASN GLY ARG ILE THR ARG ASN LEU
SEQRES 9 M 499 ILE PHE GLY ALA ASN TYR LEU GLN SER HIS ILE LEU HIS
SEQRES 10 M 499 PHE TYR HIS LEU ALA ALA LEU ASP TYR VAL LYS GLY PRO
SEQRES 11 M 499 ASP VAL SER PRO PHE VAL PRO ARG TYR ALA ASN ALA ASP
SEQRES 12 M 499 LEU LEU THR ASP ARG ILE LYS ASP GLY ALA LYS ALA ASP
SEQRES 13 M 499 ALA THR ASN THR TYR GLY LEU ASN GLN TYR LEU LYS ALA
SEQRES 14 M 499 LEU GLU ILE ARG ARG ILE CYS HIS GLU MET VAL ALA MET
SEQRES 15 M 499 PHE GLY GLY ARG MET PRO HIS VAL GLN GLY MET VAL VAL
SEQRES 16 M 499 GLY GLY ALA THR GLU ILE PRO THR ALA ASP LYS VAL ALA
SEQRES 17 M 499 GLU TYR ALA ALA ARG PHE LYS GLU VAL GLN LYS PHE VAL
SEQRES 18 M 499 ILE GLU GLU TYR LEU PRO LEU ILE TYR THR LEU GLY SER
SEQRES 19 M 499 VAL TYR THR ASP LEU PHE GLU THR GLY ILE GLY TRP LYS
SEQRES 20 M 499 ASN VAL ILE ALA PHE GLY VAL PHE PRO GLU ASP ASP ASP
SEQRES 21 M 499 TYR LYS THR PHE LEU LEU LYS PRO GLY VAL TYR ILE ASP
SEQRES 22 M 499 GLY LYS ASP GLU GLU PHE ASP SER LYS LEU VAL LYS GLU
SEQRES 23 M 499 TYR VAL GLY HIS SER PHE PHE ASP HIS SER ALA PRO GLY
SEQRES 24 M 499 GLY LEU HIS TYR SER VAL GLY GLU THR ASN PRO ASN PRO
SEQRES 25 M 499 ASP LYS PRO GLY ALA TYR SER PHE VAL LYS ALA PRO ARG
SEQRES 26 M 499 TYR LYS ASP LYS PRO CYS GLU VAL GLY PRO LEU ALA ARG
SEQRES 27 M 499 MET TRP VAL GLN ASN PRO GLU LEU SER PRO VAL GLY GLN
SEQRES 28 M 499 LYS LEU LEU LYS GLU LEU TYR GLY ILE GLU ALA LYS ASN
SEQRES 29 M 499 PHE ARG ASP LEU GLY ASP LYS ALA PHE SER ILE MET GLY
SEQRES 30 M 499 ARG HIS VAL ALA ARG ALA GLU GLU THR TRP LEU THR ALA
SEQRES 31 M 499 VAL ALA VAL GLU LYS TRP LEU LYS GLN VAL GLN PRO GLY
SEQRES 32 M 499 ALA GLU THR TYR VAL LYS SER GLU ILE PRO ASP ALA ALA
SEQRES 33 M 499 GLU GLY THR GLY PHE THR GLU ALA PRO ARG GLY ALA LEU
SEQRES 34 M 499 LEU HIS TYR LEU LYS ILE LYS ASP LYS LYS ILE GLU ASN
SEQRES 35 M 499 TYR GLN ILE VAL SER ALA THR LEU TRP ASN ALA ASN PRO
SEQRES 36 M 499 ARG ASP ASP MET GLY GLN ARG GLY PRO ILE GLU GLU ALA
SEQRES 37 M 499 LEU ILE GLY VAL PRO VAL PRO ASP ILE LYS ASN PRO VAL
SEQRES 38 M 499 ASN VAL GLY ARG LEU VAL ARG SER TYR ASP PRO SEC LEU
SEQRES 39 M 499 GLY CYS ALA VAL HIS
HET SF4 S 301 8
HET SF4 S 302 8
HET SF4 S 303 8
HET CA S 304 1
HET GOL S 305 6
HET GOL S 306 6
HET CA S 307 1
HET FCO L 501 7
HET NI L 502 3
HET CA L 503 1
HET H2S L 504 1
HET SF4 T 301 8
HET SF4 T 302 8
HET SF4 T 303 8
HET CA T 304 1
HET CA T 305 1
HET CA T 306 1
HET FCO M 501 7
HET NI M 502 3
HET CA M 503 1
HET H2S M 504 1
HET GOL M 505 6
HET GOL M 506 6
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETNAM FCO CARBONMONOXIDE-(DICYANO) IRON
HETNAM NI NICKEL (II) ION
HETNAM H2S HYDROSULFURIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN H2S HYDROGEN SULFIDE
FORMUL 5 SF4 6(FE4 S4)
FORMUL 8 CA 7(CA 2+)
FORMUL 9 GOL 4(C3 H8 O3)
FORMUL 12 FCO 2(C3 FE N2 O)
FORMUL 13 NI 2(NI 2+)
FORMUL 15 H2S 2(H2 S)
FORMUL 28 HOH *1770(H2 O)
HELIX 1 1 THR S 19 ASN S 27 1 9
HELIX 2 2 ARG S 32 VAL S 40 1 9
HELIX 3 3 GLU S 53 PHE S 68 1 16
HELIX 4 4 ALA S 83 ARG S 87 5 5
HELIX 5 5 MET S 106 ALA S 114 1 9
HELIX 6 6 PRO S 115 SER S 117 5 3
HELIX 7 7 GLY S 124 GLY S 130 1 7
HELIX 8 8 GLY S 131 ALA S 135 5 5
HELIX 9 9 SER S 144 LYS S 153 1 10
HELIX 10 10 HIS S 167 ASN S 184 1 18
HELIX 11 11 PRO S 199 GLY S 204 1 6
HELIX 12 12 ILE S 207 CYS S 211 5 5
HELIX 13 13 TYR S 213 ASN S 219 1 7
HELIX 14 14 LYS S 232 GLY S 236 5 5
HELIX 15 15 LYS S 238 THR S 242 5 5
HELIX 16 16 ASP S 245 ARG S 250 1 6
HELIX 17 17 TRP S 257 ALA S 262 1 6
HELIX 18 18 PRO S 273 SER S 277 5 5
HELIX 19 19 GLY L 49 LEU L 54 1 6
HELIX 20 20 ASP L 58 ARG L 60 5 3
HELIX 21 21 ASP L 61 VAL L 66 1 6
HELIX 22 22 GLN L 67 CYS L 70 5 4
HELIX 23 23 CYS L 73 GLY L 90 1 18
HELIX 24 24 THR L 94 LEU L 120 1 27
HELIX 25 25 ALA L 121 TYR L 125 5 5
HELIX 26 26 LEU L 143 ILE L 148 1 6
HELIX 27 27 ASP L 150 GLY L 184 1 35
HELIX 28 28 THR L 202 GLU L 223 1 22
HELIX 29 29 GLU L 223 TYR L 235 1 13
HELIX 30 30 THR L 236 GLU L 240 5 5
HELIX 31 31 ASP L 279 LYS L 281 5 3
HELIX 32 32 HIS L 301 GLY L 305 5 5
HELIX 33 33 GLY L 333 ASN L 342 1 10
HELIX 34 34 SER L 346 GLY L 358 1 13
HELIX 35 35 ASN L 363 PHE L 372 5 10
HELIX 36 36 SER L 373 VAL L 399 1 27
HELIX 37 37 SER L 446 ALA L 452 1 7
HELIX 38 38 GLY L 462 ILE L 469 1 8
HELIX 39 39 PRO L 479 TYR L 489 1 11
HELIX 40 40 SEC L 492 HIS L 498 1 7
HELIX 41 41 THR T 19 ASN T 27 1 9
HELIX 42 42 ARG T 32 VAL T 40 1 9
HELIX 43 43 GLU T 53 PHE T 68 1 16
HELIX 44 44 ALA T 83 ARG T 87 5 5
HELIX 45 45 MET T 106 ALA T 114 1 9
HELIX 46 46 PRO T 115 SER T 117 5 3
HELIX 47 47 GLY T 124 GLY T 130 1 7
HELIX 48 48 GLY T 131 ALA T 135 5 5
HELIX 49 49 SER T 144 LYS T 153 1 10
HELIX 50 50 HIS T 167 ASN T 184 1 18
HELIX 51 51 PRO T 199 GLY T 204 1 6
HELIX 52 52 ILE T 207 CYS T 211 5 5
HELIX 53 53 TYR T 213 ASN T 219 1 7
HELIX 54 54 LYS T 232 GLY T 236 5 5
HELIX 55 55 LYS T 238 THR T 242 5 5
HELIX 56 56 ASP T 245 ARG T 250 1 6
HELIX 57 57 TRP T 257 ALA T 262 1 6
HELIX 58 58 PRO T 273 SER T 277 5 5
HELIX 59 59 GLY M 49 ARG M 55 1 7
HELIX 60 60 ASP M 58 ARG M 60 5 3
HELIX 61 61 ASP M 61 VAL M 66 1 6
HELIX 62 62 GLN M 67 CYS M 70 5 4
HELIX 63 63 CYS M 73 GLY M 90 1 18
HELIX 64 64 THR M 94 LEU M 120 1 27
HELIX 65 65 ALA M 121 TYR M 125 5 5
HELIX 66 66 LEU M 143 ILE M 148 1 6
HELIX 67 67 ASP M 150 GLY M 184 1 35
HELIX 68 68 THR M 202 GLU M 223 1 22
HELIX 69 69 GLU M 223 TYR M 235 1 13
HELIX 70 70 THR M 236 GLU M 240 5 5
HELIX 71 71 ASP M 279 LYS M 281 5 3
HELIX 72 72 HIS M 301 GLY M 305 5 5
HELIX 73 73 GLY M 333 ASN M 342 1 10
HELIX 74 74 SER M 346 GLY M 358 1 13
HELIX 75 75 ASN M 363 PHE M 372 5 10
HELIX 76 76 SER M 373 VAL M 399 1 27
HELIX 77 77 SER M 446 ALA M 452 1 7
HELIX 78 78 GLY M 462 ILE M 469 1 8
HELIX 79 79 PRO M 479 TYR M 489 1 11
HELIX 80 80 SEC M 492 HIS M 498 1 7
SHEET 1 A 5 ILE S 41 PHE S 45 0
SHEET 2 A 5 ALA S 8 GLN S 14 1 N TRP S 12 O PHE S 45
SHEET 3 A 5 PHE S 73 GLU S 77 1 O LEU S 75 N VAL S 13
SHEET 4 A 5 ALA S 119 VAL S 123 1 O VAL S 121 N LEU S 74
SHEET 5 A 5 LEU S 158 VAL S 161 1 O VAL S 161 N ALA S 122
SHEET 1 B 2 ILE S 80 PRO S 81 0
SHEET 2 B 2 SER S 142 LYS S 143 -1 O LYS S 143 N ILE S 80
SHEET 1 C 2 ILE S 90 LEU S 95 0
SHEET 2 C 2 HIS S 101 THR S 105 -1 O HIS S 102 N THR S 94
SHEET 1 D 3 VAL L 12 ILE L 16 0
SHEET 2 D 3 LEU L 26 LYS L 33 -1 O ILE L 28 N ILE L 16
SHEET 3 D 3 LYS L 36 GLY L 44 -1 O VAL L 38 N GLU L 31
SHEET 1 E 2 MET L 192 VAL L 193 0
SHEET 2 E 2 GLY L 196 ALA L 197 -1 O GLY L 196 N VAL L 193
SHEET 1 F 3 VAL L 248 ALA L 250 0
SHEET 2 F 3 GLY L 268 ILE L 271 -1 O TYR L 270 N VAL L 248
SHEET 3 F 3 LYS L 274 GLU L 276 -1 O GLU L 276 N VAL L 269
SHEET 1 G 2 VAL L 253 PRO L 255 0
SHEET 2 G 2 PHE L 263 LEU L 265 -1 O LEU L 265 N VAL L 253
SHEET 1 H 2 VAL L 283 TYR L 286 0
SHEET 2 H 2 ALA L 322 TYR L 325 -1 O ARG L 324 N LYS L 284
SHEET 1 I 3 ALA L 415 ALA L 423 0
SHEET 2 I 3 GLY L 426 LYS L 435 -1 O ILE L 434 N ALA L 415
SHEET 3 I 3 LYS L 438 VAL L 445 -1 O GLN L 443 N TYR L 431
SHEET 1 J 5 ILE T 41 PHE T 45 0
SHEET 2 J 5 ALA T 8 GLN T 14 1 N TRP T 12 O PHE T 45
SHEET 3 J 5 PHE T 73 GLU T 77 1 O PHE T 73 N PRO T 9
SHEET 4 J 5 ALA T 119 VAL T 123 1 O VAL T 121 N LEU T 74
SHEET 5 J 5 LEU T 158 VAL T 161 1 O VAL T 161 N ALA T 122
SHEET 1 K 2 ILE T 80 PRO T 81 0
SHEET 2 K 2 SER T 142 LYS T 143 -1 O LYS T 143 N ILE T 80
SHEET 1 L 2 ILE T 90 LEU T 95 0
SHEET 2 L 2 HIS T 101 THR T 105 -1 O VAL T 104 N GLY T 92
SHEET 1 M 3 VAL M 12 ILE M 16 0
SHEET 2 M 3 LEU M 26 LYS M 33 -1 O ILE M 28 N ILE M 16
SHEET 3 M 3 LYS M 36 GLY M 44 -1 O VAL M 38 N GLU M 31
SHEET 1 N 2 MET M 192 VAL M 193 0
SHEET 2 N 2 GLY M 196 ALA M 197 -1 O GLY M 196 N VAL M 193
SHEET 1 O 3 VAL M 248 ALA M 250 0
SHEET 2 O 3 GLY M 268 ILE M 271 -1 O TYR M 270 N VAL M 248
SHEET 3 O 3 LYS M 274 GLU M 276 -1 O GLU M 276 N VAL M 269
SHEET 1 P 2 VAL M 253 PRO M 255 0
SHEET 2 P 2 PHE M 263 LEU M 265 -1 O LEU M 265 N VAL M 253
SHEET 1 Q 2 VAL M 283 TYR M 286 0
SHEET 2 Q 2 ALA M 322 TYR M 325 -1 O ARG M 324 N LYS M 284
SHEET 1 R 3 ALA M 414 ALA M 423 0
SHEET 2 R 3 GLY M 426 LYS M 435 -1 O ILE M 434 N ALA M 415
SHEET 3 R 3 LYS M 438 VAL M 445 -1 O GLU M 440 N LYS M 433
LINK SG CYS S 18 FE4 SF4 S 303 1555 1555 2.27
LINK SG CYS S 21 FE2 SF4 S 303 1555 1555 2.29
LINK SG CYS S 126 FE3 SF4 S 303 1555 1555 2.29
LINK O GLU S 152 CA CA S 304 1555 1555 2.32
LINK SG CYS S 164 FE1 SF4 S 303 1555 1555 2.29
LINK ND1 HIS S 208 FE3 SF4 S 301 1555 1555 2.07
LINK SG CYS S 211 FE2 SF4 S 301 1555 1555 2.29
LINK SG CYS S 231 FE1 SF4 S 301 1555 1555 2.28
LINK SG CYS S 237 FE4 SF4 S 301 1555 1555 2.32
LINK SG CYS S 246 FE2 SF4 S 302 1555 1555 2.29
LINK SG CYS S 258 FE1 SF4 S 302 1555 1555 2.27
LINK SG CYS S 264 FE3 SF4 S 302 1555 1555 2.29
LINK SG CYS S 267 FE4 SF4 S 302 1555 1555 2.28
LINK CA CA S 304 O HOH S 455 1555 1555 2.43
LINK CA CA S 304 O HOH S 456 1555 1555 2.41
LINK CA CA S 304 O HOH S 458 1555 1555 2.41
LINK CA CA S 304 O HOH S 472 1555 1555 2.51
LINK CA CA S 307 O HOH S 539 1555 1555 2.50
LINK CA CA S 307 O HOH S 634 1555 1555 2.32
LINK CA CA S 307 O HOH S 652 1555 1555 2.37
LINK CA CA S 307 O HOH S 754 1555 1555 2.67
LINK CA CA S 307 O HOH L 897 1555 1555 2.36
LINK CA CA S 307 O HOH L1085 1555 1555 2.41
LINK OE1 GLU L 51 CA CA L 503 1555 1555 2.36
LINK SG CYS L 70 NI N NI L 502 1555 1555 2.17
LINK SG CYS L 70 NI Q NI L 502 1555 1555 2.18
LINK SG CYS L 73 FE FCO L 501 1555 1555 2.27
LINK SG CYS L 73 NI N NI L 502 1555 1555 2.37
LINK SG CYS L 73 NI Q NI L 502 1555 1555 2.43
LINK O ILE L 444 CA CA L 503 1555 1555 2.36
LINK SE NSEC L 492 NI N NI L 502 1555 1555 2.31
LINK SE QSEC L 492 NI Q NI L 502 1555 1555 2.41
LINK SG CYS L 495 FE FCO L 501 1555 1555 2.33
LINK SG CYS L 495 NI D NI L 502 1555 1555 2.26
LINK SG CYS L 495 NI N NI L 502 1555 1555 2.52
LINK NE2 HIS L 498 CA CA L 503 1555 1555 2.45
LINK FE FCO L 501 O HOH L 607 1555 1555 2.07
LINK NI Q NI L 502 O HOH L 607 1555 1555 1.72
LINK NI N NI L 502 O HOH L 607 1555 1555 1.81
LINK CA CA L 503 O HOH L 608 1555 1555 2.33
LINK CA CA L 503 O HOH L 609 1555 1555 2.32
LINK CA CA L 503 O HOH L 610 1555 1555 2.23
LINK SG CYS T 18 FE4 SF4 T 303 1555 1555 2.27
LINK SG CYS T 21 FE2 SF4 T 303 1555 1555 2.29
LINK SG CYS T 126 FE3 SF4 T 303 1555 1555 2.27
LINK SG CYS T 164 FE1 SF4 T 303 1555 1555 2.28
LINK O ASP T 195 CA CA T 306 1555 1555 2.92
LINK OD1 ASP T 196 CA CA T 306 1555 1555 2.97
LINK ND1 HIS T 208 FE3 SF4 T 301 1555 1555 2.13
LINK SG CYS T 211 FE2 SF4 T 301 1555 1555 2.28
LINK SG CYS T 231 FE1 SF4 T 301 1555 1555 2.29
LINK SG CYS T 237 FE4 SF4 T 301 1555 1555 2.32
LINK SG CYS T 246 FE2 SF4 T 302 1555 1555 2.29
LINK SG CYS T 258 FE1 SF4 T 302 1555 1555 2.28
LINK SG CYS T 264 FE3 SF4 T 302 1555 1555 2.30
LINK SG CYS T 267 FE4 SF4 T 302 1555 1555 2.30
LINK OD2 ASP T 271 CA CA T 305 1555 1555 2.35
LINK O GLY T 275 CA CA T 305 1555 1555 2.82
LINK CA CA T 304 O HOH T 515 1555 1555 2.45
LINK CA CA T 304 O HOH T 537 1555 1555 2.32
LINK CA CA T 304 O HOH T 547 1555 1555 2.36
LINK CA CA T 304 O HOH T 556 1555 1555 2.26
LINK CA CA T 304 O HOH T 589 1555 1555 2.26
LINK CA CA T 304 O HOH M 612 1555 1555 2.45
LINK CA CA T 304 O HOH M 617 1555 1555 2.48
LINK CA CA T 305 O HOH T 407 1555 1555 2.39
LINK CA CA T 305 O HOH T 478 1555 1555 2.58
LINK CA CA T 305 O HOH T 508 1555 1555 2.24
LINK CA CA T 305 O HOH T 728 1555 1555 2.42
LINK CA CA T 306 O HOH T 484 1555 1555 2.34
LINK CA CA T 306 O HOH T 591 1555 1555 2.74
LINK CA CA T 306 O HOH T 725 1555 1555 2.36
LINK CA CA T 306 O HOH T 731 1555 1555 2.70
LINK OE1 GLU M 51 CA CA M 503 1555 1555 2.41
LINK SG CYS M 70 NI N NI M 502 1555 1555 2.18
LINK SG CYS M 70 NI Q NI M 502 1555 1555 2.19
LINK SG CYS M 73 FE FCO M 501 1555 1555 2.28
LINK SG CYS M 73 NI N NI M 502 1555 1555 2.34
LINK SG CYS M 73 NI Q NI M 502 1555 1555 2.38
LINK O ILE M 444 CA CA M 503 1555 1555 2.37
LINK SE NSEC M 492 NI N NI M 502 1555 1555 2.31
LINK SE QSEC M 492 NI Q NI M 502 1555 1555 2.44
LINK SG CYS M 495 FE FCO M 501 1555 1555 2.31
LINK SG CYS M 495 NI D NI M 502 1555 1555 2.29
LINK SG CYS M 495 NI N NI M 502 1555 1555 2.53
LINK NE2 HIS M 498 CA CA M 503 1555 1555 2.46
LINK FE FCO M 501 O HOH M 622 1555 1555 2.02
LINK NI Q NI M 502 O HOH M 622 1555 1555 1.74
LINK NI N NI M 502 O HOH M 622 1555 1555 1.83
LINK CA CA M 503 O HOH M 623 1555 1555 2.25
LINK CA CA M 503 O HOH M 624 1555 1555 2.22
LINK CA CA M 503 O HOH M 625 1555 1555 2.26
CISPEP 1 HIS S 30 PRO S 31 0 8.25
CISPEP 2 CYS S 164 PRO S 165 0 -0.77
CISPEP 3 PHE S 272 PRO S 273 0 4.32
CISPEP 4 SER S 277 PRO S 278 0 -2.69
CISPEP 5 ASP L 17 PRO L 18 0 8.05
CISPEP 6 SER L 132 PRO L 133 0 8.86
CISPEP 7 VAL L 135 PRO L 136 0 1.38
CISPEP 8 MET L 186 PRO L 187 0 -4.06
CISPEP 9 HIS T 30 PRO T 31 0 3.99
CISPEP 10 CYS T 164 PRO T 165 0 -0.54
CISPEP 11 PHE T 272 PRO T 273 0 4.95
CISPEP 12 SER T 277 PRO T 278 0 -4.15
CISPEP 13 ASP M 17 PRO M 18 0 6.26
CISPEP 14 SER M 132 PRO M 133 0 8.15
CISPEP 15 VAL M 135 PRO M 136 0 0.30
CISPEP 16 MET M 186 PRO M 187 0 -6.50
SITE 1 AC1 6 HIS S 208 CYS S 211 CYS S 231 LYS S 232
SITE 2 AC1 6 CYS S 237 VAL S 259
SITE 1 AC2 8 ARG L 185 THR S 242 CYS S 246 TRP S 251
SITE 2 AC2 8 CYS S 258 CYS S 264 ILE S 265 CYS S 267
SITE 1 AC3 10 ARG L 68 HIS L 188 CYS S 18 CYS S 21
SITE 2 AC3 10 GLY S 124 THR S 125 CYS S 126 GLY S 163
SITE 3 AC3 10 CYS S 164 PRO S 165
SITE 1 AC4 6 ASP L 87 GLU S 152 HOH S 455 HOH S 456
SITE 2 AC4 6 HOH S 458 HOH S 472
SITE 1 AC5 7 ASP M 39 ARG M 455 HOH M 992 HIS S 30
SITE 2 AC5 7 ARG S 32 HOH S 520 HOH S 567
SITE 1 AC6 7 ASP L 413 HOH L 946 ASP S 112 LYS S 116
SITE 2 AC6 7 HOH S 548 HOH S 558 HOH S 675
SITE 1 AC7 6 HOH L 897 HOH L1085 HOH S 539 HOH S 634
SITE 2 AC7 6 HOH S 652 HOH S 754
SITE 1 AC8 11 CYS L 73 HIS L 77 ALA L 423 PRO L 424
SITE 2 AC8 11 ARG L 425 ALA L 447 THR L 448 SEC L 492
SITE 3 AC8 11 CYS L 495 NI L 502 HOH L 607
SITE 1 AC9 6 CYS L 70 CYS L 73 SEC L 492 CYS L 495
SITE 2 AC9 6 FCO L 501 HOH L 607
SITE 1 BC1 6 GLU L 51 ILE L 444 HIS L 498 HOH L 608
SITE 2 BC1 6 HOH L 609 HOH L 610
SITE 1 BC2 6 CYS L 73 THR L 75 ALA L 76 PHE L 105
SITE 2 BC2 6 ASN L 108 PRO L 424
SITE 1 BC3 10 HIS T 208 CYS T 211 TYR T 213 LEU T 214
SITE 2 BC3 10 CYS T 231 LYS T 232 ALA T 233 CYS T 237
SITE 3 BC3 10 GLY T 239 VAL T 259
SITE 1 BC4 8 ARG M 185 THR T 242 CYS T 246 TRP T 251
SITE 2 BC4 8 CYS T 258 CYS T 264 ILE T 265 CYS T 267
SITE 1 BC5 11 ARG M 68 HIS M 188 GLY T 17 CYS T 18
SITE 2 BC5 11 CYS T 21 GLY T 124 THR T 125 CYS T 126
SITE 3 BC5 11 GLY T 163 CYS T 164 PRO T 165
SITE 1 BC6 7 HOH M 612 HOH M 617 HOH T 515 HOH T 537
SITE 2 BC6 7 HOH T 547 HOH T 556 HOH T 589
SITE 1 BC7 7 HOH L 852 ASP T 271 GLY T 275 HOH T 407
SITE 2 BC7 7 HOH T 478 HOH T 508 HOH T 728
SITE 1 BC8 6 ASP T 195 ASP T 196 HOH T 484 HOH T 591
SITE 2 BC8 6 HOH T 725 HOH T 731
SITE 1 BC9 11 CYS M 73 HIS M 77 ALA M 423 PRO M 424
SITE 2 BC9 11 ARG M 425 ALA M 447 THR M 448 SEC M 492
SITE 3 BC9 11 CYS M 495 NI M 502 HOH M 622
SITE 1 CC1 6 CYS M 70 CYS M 73 SEC M 492 CYS M 495
SITE 2 CC1 6 FCO M 501 HOH M 622
SITE 1 CC2 6 GLU M 51 ILE M 444 HIS M 498 HOH M 623
SITE 2 CC2 6 HOH M 624 HOH M 625
SITE 1 CC3 6 CYS M 73 THR M 75 ALA M 76 PHE M 105
SITE 2 CC3 6 ASN M 108 PRO M 424
SITE 1 CC4 6 ASP M 39 ARG M 455 GLY M 459 HOH M 661
SITE 2 CC4 6 HOH M 858 GLU S 35
SITE 1 CC5 2 THR M 157 TYR M 160
CRYST1 106.230 108.910 136.340 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 0.009414 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009182 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007335 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
