HEADER OXIDOREDUCTASE 10-JUN-15 5A4M
TITLE MECHANISM OF HYDROGEN ACTIVATION BY NIFE-HYDROGENASES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROGENASE-1 LARGE CHAIN;
COMPND 3 CHAIN: L, M;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 46-311;
COMPND 5 SYNONYM: HYD1, MEMBRANE-BOUND HYDROGENASE 1 LARGE SUBUNIT, NIFE
COMPND 6 HYDROGENASE;
COMPND 7 EC: 1.12.99.6;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HYDROGENASE-1 SMALL CHAIN;
COMPND 10 CHAIN: S, T;
COMPND 11 FRAGMENT: UNP RESIDUES 1-582;
COMPND 12 SYNONYM: HYD1, MEMBRANE-BOUND HYDROGENASE 1 SMALL SUBUNIT, NIFE
COMPND 13 HYDROGENASE;
COMPND 14 EC: 1.12.99.6
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI STR. K-12 SUBSTR. MC4100;
SOURCE 3 ORGANISM_TAXID: 1403831;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI STR. K-12 SUBSTR. MC4100;
SOURCE 6 ORGANISM_TAXID: 1403831
KEYWDS OXIDOREDUCTASE, HYDROGEN ACTIVATION, NIFE HYDROGENASE, FES CLUSTERS,
KEYWDS 2 CATALYSIS, TRANSMEMBRANE DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.EVANS,E.J.BROOKE,S.A.M.WEHLIN,E.NOMEROTSKAIA,F.SERGENT,S.B.CARR,
AUTHOR 2 S.E.V.PHILIPS,F.A.ARMSTRONG
REVDAT 4 10-JAN-24 5A4M 1 REMARK LINK
REVDAT 3 13-JAN-16 5A4M 1 JRNL
REVDAT 2 09-DEC-15 5A4M 1 JRNL
REVDAT 1 25-NOV-15 5A4M 0
JRNL AUTH R.M.EVANS,E.J.BROOKE,S.A.WEHLIN,E.NOMEROTSKAIA,F.SARGENT,
JRNL AUTH 2 S.B.CARR,S.E.PHILLIPS,F.A.ARMSTRONG
JRNL TITL MECHANISM OF HYDROGEN ACTIVATION BY [NIFE] HYDROGENASES.
JRNL REF NAT.CHEM.BIOL. V. 12 46 2016
JRNL REFN ISSN 1552-4450
JRNL PMID 26619250
JRNL DOI 10.1038/NCHEMBIO.1976
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0123
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) : 91.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 172419
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) : 0.136
REMARK 3 R VALUE (WORKING SET) : 0.134
REMARK 3 FREE R VALUE : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 8979
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) : 12544
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 627
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13133
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 1492
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 1.32000
REMARK 3 B33 (A**2) : -1.31000
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): 0.084
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.083
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.065
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.862
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13749 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 12762 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18715 ; 2.256 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 29361 ; 1.585 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1733 ; 6.105 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 633 ;34.904 ;23.934
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2176 ;12.526 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 90 ;17.443 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2005 ; 0.175 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15719 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3235 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 9730 ; 0.278 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 25298 ; 0.232 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 13788 ; 0.186 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 13044 ; 0.099 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 680 ; 0.169 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 22 ; 0.262 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.112 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 89 ; 0.310 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 65 ; 0.175 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.143 ; 0.200
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): 6800 ; 1.058 ; 1.644
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6799 ; 1.058 ; 1.644
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8508 ; 1.547 ; 2.461
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6949 ; 2.094 ; 1.886
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10140 ; 4.135 ; 2.765
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 5 S 265
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1660 9.7130 18.1910
REMARK 3 T TENSOR
REMARK 3 T11: 0.0215 T22: 0.0140
REMARK 3 T33: 0.0138 T12: 0.0041
REMARK 3 T13: -0.0068 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.0795 L22: 0.0575
REMARK 3 L33: 0.2109 L12: 0.0445
REMARK 3 L13: 0.0411 L23: 0.0362
REMARK 3 S TENSOR
REMARK 3 S11: -0.0139 S12: -0.0095 S13: 0.0167
REMARK 3 S21: -0.0033 S22: 0.0062 S23: -0.0070
REMARK 3 S31: -0.0101 S32: -0.0364 S33: 0.0077
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 2 L 582
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7650 -5.4570 25.7330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0203 T22: 0.0188
REMARK 3 T33: 0.0119 T12: 0.0131
REMARK 3 T13: -0.0028 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.1104 L22: 0.0697
REMARK 3 L33: 0.2270 L12: 0.0350
REMARK 3 L13: -0.0126 L23: 0.0049
REMARK 3 S TENSOR
REMARK 3 S11: -0.0177 S12: -0.0250 S13: -0.0038
REMARK 3 S21: 0.0076 S22: 0.0042 S23: -0.0225
REMARK 3 S31: 0.0567 S32: 0.0434 S33: 0.0134
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 5 T 265
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8680 -8.7910 -19.6690
REMARK 3 T TENSOR
REMARK 3 T11: 0.0363 T22: 0.0146
REMARK 3 T33: 0.0132 T12: -0.0029
REMARK 3 T13: 0.0101 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.0858 L22: 0.0552
REMARK 3 L33: 0.2117 L12: -0.0470
REMARK 3 L13: -0.0396 L23: -0.0356
REMARK 3 S TENSOR
REMARK 3 S11: -0.0124 S12: 0.0077 S13: -0.0115
REMARK 3 S21: -0.0182 S22: 0.0019 S23: -0.0035
REMARK 3 S31: 0.0562 S32: -0.0372 S33: 0.0105
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 2 M 582
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4430 9.4480 -27.4420
REMARK 3 T TENSOR
REMARK 3 T11: 0.0237 T22: 0.0184
REMARK 3 T33: 0.0092 T12: 0.0005
REMARK 3 T13: 0.0104 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.1017 L22: 0.0623
REMARK 3 L33: 0.2139 L12: -0.0461
REMARK 3 L13: 0.0038 L23: 0.0160
REMARK 3 S TENSOR
REMARK 3 S11: -0.0091 S12: 0.0155 S13: 0.0073
REMARK 3 S21: -0.0237 S22: -0.0045 S23: -0.0183
REMARK 3 S31: -0.0241 S32: 0.0227 S33: 0.0137
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 5A4M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1290063998.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 181455
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 46.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
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) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 1.04000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3USC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NA/K TARTRATE, 20% (W/V) PEG
REMARK 280 3350, PH 7.2
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 46.83550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.45550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.58100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 91.45550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.83550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.58100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 23810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -281.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, M, S, T
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 L 1
REMARK 465 MET M 1
REMARK 465 LEU S 1
REMARK 465 GLU S 2
REMARK 465 ASN S 3
REMARK 465 GLY S 267
REMARK 465 SER S 268
REMARK 465 PHE S 269
REMARK 465 TYR S 270
REMARK 465 SER S 271
REMARK 465 ARG S 272
REMARK 465 HIS S 273
REMARK 465 HIS S 274
REMARK 465 HIS S 275
REMARK 465 HIS S 276
REMARK 465 HIS S 277
REMARK 465 HIS S 278
REMARK 465 LEU T 1
REMARK 465 GLU T 2
REMARK 465 ASN T 3
REMARK 465 LYS T 4
REMARK 465 GLY T 267
REMARK 465 SER T 268
REMARK 465 PHE T 269
REMARK 465 TYR T 270
REMARK 465 SER T 271
REMARK 465 ARG T 272
REMARK 465 HIS T 273
REMARK 465 HIS T 274
REMARK 465 HIS T 275
REMARK 465 HIS T 276
REMARK 465 HIS T 277
REMARK 465 HIS T 278
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 ARG S 266 CG CD NE CZ NH1 NH2
REMARK 470 ARG T 266 CG CD NE CZ NH1 NH2
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 ARG S 168 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 SG CYS L 576 O HOH L 2106 1.83
REMARK 500 O HOH M 2287 O HOH T 2161 1.84
REMARK 500 NH2 ARG T 168 O HOH L 2511 1.95
REMARK 500 OE2 GLU M 208 O HOH M 2192 2.00
REMARK 500 O HOH L 2472 O HOH L 2489 2.03
REMARK 500 O HOH M 2111 O HOH M 2113 2.07
REMARK 500 N PRO T 5 O HOH T 2002 2.09
REMARK 500 S2 SF3 S 404 O HOH S 2009 2.10
REMARK 500 O HOH S 2008 O HOH S 2009 2.11
REMARK 500 O HOH T 2008 O HOH T 2009 2.12
REMARK 500 O HOH S 2135 O HOH T 2130 2.13
REMARK 500 SG CYS S 20 O HOH S 2009 2.14
REMARK 500 SG CYS T 20 O HOH T 2009 2.15
REMARK 500 O HOH M 2208 O HOH M 2209 2.17
REMARK 500 NH1 ARG T 234 O HOH T 2156 2.18
REMARK 500 NH2 ARG S 234 O HOH S 2177 2.18
REMARK 500 OD1 ASP L 269 O HOH L 2319 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU L 245 CD GLU L 245 OE2 0.078
REMARK 500 GLU M 73 CD GLU M 73 OE1 0.071
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 L 26 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP L 269 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 MET L 275 CG - SD - CE ANGL. DEV. = 11.8 DEGREES
REMARK 500 ASP L 338 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG L 363 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG L 363 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP L 574 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 CYS L 576 CA - CB - SG ANGL. DEV. = -13.5 DEGREES
REMARK 500 ARG M 32 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP M 269 CB - CG - OD1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ASP M 338 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG M 363 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG M 519 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG M 519 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP M 574 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP M 574 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 CYS M 576 CA - CB - SG ANGL. DEV. = -14.2 DEGREES
REMARK 500 ARG S 93 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG S 168 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG S 168 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG S 193 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG S 193 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP S 197 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP S 197 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG S 234 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG S 234 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG T 93 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG T 168 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG T 193 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG T 193 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG T 260 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG T 260 NE - CZ - NH2 ANGL. DEV. = -5.7 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 CYS L 79 46.93 -85.50
REMARK 500 LEU L 126 -60.80 -101.27
REMARK 500 SER L 158 11.59 -147.79
REMARK 500 HIS L 229 64.98 63.59
REMARK 500 LYS L 299 -63.28 -126.75
REMARK 500 PHE L 307 64.74 67.23
REMARK 500 GLN L 344 -89.81 -93.89
REMARK 500 ASN L 375 78.90 -152.24
REMARK 500 ASN L 385 82.84 -150.94
REMARK 500 GLU L 393 -136.29 -129.16
REMARK 500 TYR L 395 16.65 -140.85
REMARK 500 PRO L 563 42.88 -75.23
REMARK 500 CYS M 79 46.31 -85.71
REMARK 500 SER M 158 10.63 -142.98
REMARK 500 HIS M 229 67.05 61.95
REMARK 500 LYS M 299 -61.81 -127.14
REMARK 500 PHE M 307 64.93 64.96
REMARK 500 GLN M 344 -89.27 -92.20
REMARK 500 ASN M 375 79.66 -151.03
REMARK 500 ASN M 385 79.16 -151.35
REMARK 500 GLU M 393 -139.60 -126.28
REMARK 500 TYR M 395 21.19 -146.10
REMARK 500 PRO M 563 41.46 -81.82
REMARK 500 THR S 18 8.20 81.22
REMARK 500 HIS S 29 110.92 -162.59
REMARK 500 ASP S 45 106.88 -169.72
REMARK 500 TRP S 118 -31.66 -137.77
REMARK 500 CYS S 120 -150.19 57.20
REMARK 500 ASN S 228 -177.09 -172.98
REMARK 500 SER S 232 -64.46 -120.25
REMARK 500 ARG S 234 -176.79 66.21
REMARK 500 THR T 18 13.67 80.94
REMARK 500 HIS T 29 107.39 -165.43
REMARK 500 ASP T 45 108.59 -166.59
REMARK 500 ASP T 45 107.58 -166.20
REMARK 500 TRP T 118 -30.92 -139.49
REMARK 500 CYS T 120 -150.62 56.84
REMARK 500 LYS T 189 27.27 -140.61
REMARK 500 SER T 232 -61.52 -120.06
REMARK 500 SER T 232 -60.93 -120.64
REMARK 500 ARG T 234 -176.20 68.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH L2206 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH T2173 DISTANCE = 6.51 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU L 57 OE2
REMARK 620 2 CYS L 528 O 91.9
REMARK 620 3 HIS L 582 NE2 88.1 86.9
REMARK 620 4 HOH L2075 O 89.8 177.2 91.0
REMARK 620 5 HOH L2076 O 87.3 90.6 174.7 91.7
REMARK 620 6 HOH L2396 O 178.5 86.7 91.1 91.6 93.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NFV L 601 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 76 SG
REMARK 620 2 NFV L 601 O4 162.6
REMARK 620 3 CYS L 79 SG 109.3 70.0
REMARK 620 4 CYS L 576 SG 84.4 97.4 166.2
REMARK 620 5 CYS L 579 SG 110.4 86.2 72.6 101.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NFV L 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 79 SG
REMARK 620 2 NFV L 601 C2 168.7
REMARK 620 3 NFV L 601 O4 79.2 90.9
REMARK 620 4 NFV L 601 C1 101.2 90.0 160.1
REMARK 620 5 NFV L 601 C3 94.8 88.4 78.1 82.1
REMARK 620 6 CYS L 579 SG 82.2 93.6 96.7 103.1 174.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF3 S 404 FE7
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH L2282 O
REMARK 620 2 SF3 S 404 S2 162.9
REMARK 620 3 CYS S 17 SG 69.9 124.0
REMARK 620 4 CYS S 19 SG 66.7 99.4 98.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG M 604 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU M 57 OE2
REMARK 620 2 CYS M 528 O 91.8
REMARK 620 3 HIS M 582 NE2 87.3 86.7
REMARK 620 4 HOH M2068 O 89.1 175.9 89.3
REMARK 620 5 HOH M2069 O 89.4 91.8 176.3 92.2
REMARK 620 6 HOH M2390 O 177.7 87.6 90.4 91.4 92.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NFV M 603 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 76 SG
REMARK 620 2 NFV M 603 O4 163.6
REMARK 620 3 CYS M 79 SG 108.0 71.3
REMARK 620 4 CYS M 576 SG 82.8 99.8 168.3
REMARK 620 5 CYS M 579 SG 108.5 87.0 71.6 100.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NFV M 603 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 79 SG
REMARK 620 2 NFV M 603 C2 168.3
REMARK 620 3 NFV M 603 O4 80.7 88.9
REMARK 620 4 NFV M 603 C1 99.1 92.5 159.4
REMARK 620 5 NFV M 603 C3 96.2 86.5 76.8 82.8
REMARK 620 6 CYS M 579 SG 82.2 94.3 98.7 101.6 175.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF3 T 404 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH M2265 O
REMARK 620 2 SF3 T 404 S2 166.8
REMARK 620 3 SF3 T 404 S3 79.0 107.5
REMARK 620 4 CYS T 17 SG 65.2 121.9 105.6
REMARK 620 5 CYS T 19 SG 68.4 99.0 126.9 97.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF3 S 404 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 19 SG
REMARK 620 2 SF3 S 404 S2 101.7
REMARK 620 3 SF3 S 404 S3 78.4 69.7
REMARK 620 4 CYS S 20 SG 126.0 114.3 78.2
REMARK 620 5 HOH S2009 O 143.7 57.3 66.8 57.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF3 S 404 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 115 SG
REMARK 620 2 SF3 S 404 S1 98.1
REMARK 620 3 SF3 S 404 S2 113.3 108.9
REMARK 620 4 SF3 S 404 S3 112.0 104.4 117.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF3 S 404 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 120 SG
REMARK 620 2 SF3 S 404 S1 114.8
REMARK 620 3 SF3 S 404 S3 115.8 102.3
REMARK 620 4 CYS S 149 SG 101.3 108.4 114.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 401 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS S 187 ND1
REMARK 620 2 SF4 S 401 S1 120.1
REMARK 620 3 SF4 S 401 S2 115.9 99.9
REMARK 620 4 SF4 S 401 S4 109.1 104.1 106.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 401 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 190 SG
REMARK 620 2 SF4 S 401 S2 108.2
REMARK 620 3 SF4 S 401 S3 121.2 104.4
REMARK 620 4 SF4 S 401 S4 112.2 106.8 102.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 401 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 215 SG
REMARK 620 2 SF4 S 401 S1 104.2
REMARK 620 3 SF4 S 401 S3 120.9 102.1
REMARK 620 4 SF4 S 401 S4 118.4 104.7 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S 401 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 221 SG
REMARK 620 2 SF4 S 401 S1 114.5
REMARK 620 3 SF4 S 401 S2 111.8 101.2
REMARK 620 4 SF4 S 401 S3 118.0 103.1 106.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S S 402 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 230 SG
REMARK 620 2 F3S S 402 S2 104.4
REMARK 620 3 F3S S 402 S3 117.0 103.7
REMARK 620 4 F3S S 402 S4 113.0 116.1 102.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S S 402 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 249 SG
REMARK 620 2 F3S S 402 S1 108.4
REMARK 620 3 F3S S 402 S3 112.2 103.7
REMARK 620 4 F3S S 402 S4 113.0 117.2 101.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S S 402 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 252 SG
REMARK 620 2 F3S S 402 S1 107.9
REMARK 620 3 F3S S 402 S2 108.3 115.4
REMARK 620 4 F3S S 402 S3 116.8 105.0 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF3 T 404 FE7
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 19 SG
REMARK 620 2 SF3 T 404 S2 97.7
REMARK 620 3 CYS T 20 SG 121.6 116.8
REMARK 620 4 HOH T2009 O 138.7 61.8 55.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF3 T 404 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 115 SG
REMARK 620 2 SF3 T 404 S1 113.1
REMARK 620 3 SF3 T 404 S2 114.9 118.3
REMARK 620 4 SF3 T 404 S3 96.1 103.3 107.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF3 T 404 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 120 SG
REMARK 620 2 SF3 T 404 S1 116.5
REMARK 620 3 SF3 T 404 S3 113.1 101.6
REMARK 620 4 CYS T 149 SG 101.9 115.0 109.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 401 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS T 187 ND1
REMARK 620 2 SF4 T 401 S1 119.0
REMARK 620 3 SF4 T 401 S2 116.9 100.8
REMARK 620 4 SF4 T 401 S4 107.6 104.3 107.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 401 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 190 SG
REMARK 620 2 SF4 T 401 S2 108.1
REMARK 620 3 SF4 T 401 S3 120.3 104.3
REMARK 620 4 SF4 T 401 S4 112.7 107.2 103.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 401 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 215 SG
REMARK 620 2 SF4 T 401 S1 104.3
REMARK 620 3 SF4 T 401 S3 119.8 103.0
REMARK 620 4 SF4 T 401 S4 119.3 104.0 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 T 401 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 221 SG
REMARK 620 2 SF4 T 401 S1 114.7
REMARK 620 3 SF4 T 401 S2 110.9 101.9
REMARK 620 4 SF4 T 401 S3 117.9 103.4 106.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S T 402 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 230 SG
REMARK 620 2 F3S T 402 S2 104.4
REMARK 620 3 F3S T 402 S3 117.0 102.9
REMARK 620 4 F3S T 402 S4 114.9 115.6 101.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S T 402 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 249 SG
REMARK 620 2 F3S T 402 S1 110.0
REMARK 620 3 F3S T 402 S3 113.1 102.5
REMARK 620 4 F3S T 402 S4 113.0 116.1 101.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S T 402 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 252 SG
REMARK 620 2 F3S T 402 S1 107.8
REMARK 620 3 F3S T 402 S2 109.6 114.6
REMARK 620 4 F3S T 402 S3 117.9 104.2 103.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NFV L 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NFV M 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG M 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 S 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S S 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF3 S 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL S 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 T 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S T 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF3 T 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL T 409
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5A4F RELATED DB: PDB
REMARK 900 THE MECHANISM OF HYDROGEN ACTIVATION BY NIFE- HYDROGENASES.
REMARK 900 RELATED ID: 5A4I RELATED DB: PDB
REMARK 900 MECHANISM OF HYDROGEN ACTIVATION BY NIFE-HYDROGENASES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 TRANSMEMBRANE DOMAIN DELETED
DBREF 5A4M L 1 582 UNP P0ACD8 MBHL_ECOLI 1 582
DBREF 5A4M M 1 582 UNP P0ACD8 MBHL_ECOLI 1 582
DBREF 5A4M S 1 266 UNP P69739 MBHS_ECOLI 46 311
DBREF 5A4M T 1 266 UNP P69739 MBHS_ECOLI 46 311
SEQADV 5A4M GLY S 267 UNP P69739 EXPRESSION TAG
SEQADV 5A4M SER S 268 UNP P69739 EXPRESSION TAG
SEQADV 5A4M PHE S 269 UNP P69739 EXPRESSION TAG
SEQADV 5A4M TYR S 270 UNP P69739 EXPRESSION TAG
SEQADV 5A4M SER S 271 UNP P69739 EXPRESSION TAG
SEQADV 5A4M ARG S 272 UNP P69739 EXPRESSION TAG
SEQADV 5A4M HIS S 273 UNP P69739 EXPRESSION TAG
SEQADV 5A4M HIS S 274 UNP P69739 EXPRESSION TAG
SEQADV 5A4M HIS S 275 UNP P69739 EXPRESSION TAG
SEQADV 5A4M HIS S 276 UNP P69739 EXPRESSION TAG
SEQADV 5A4M HIS S 277 UNP P69739 EXPRESSION TAG
SEQADV 5A4M HIS S 278 UNP P69739 EXPRESSION TAG
SEQADV 5A4M GLY T 267 UNP P69739 EXPRESSION TAG
SEQADV 5A4M SER T 268 UNP P69739 EXPRESSION TAG
SEQADV 5A4M PHE T 269 UNP P69739 EXPRESSION TAG
SEQADV 5A4M TYR T 270 UNP P69739 EXPRESSION TAG
SEQADV 5A4M SER T 271 UNP P69739 EXPRESSION TAG
SEQADV 5A4M ARG T 272 UNP P69739 EXPRESSION TAG
SEQADV 5A4M HIS T 273 UNP P69739 EXPRESSION TAG
SEQADV 5A4M HIS T 274 UNP P69739 EXPRESSION TAG
SEQADV 5A4M HIS T 275 UNP P69739 EXPRESSION TAG
SEQADV 5A4M HIS T 276 UNP P69739 EXPRESSION TAG
SEQADV 5A4M HIS T 277 UNP P69739 EXPRESSION TAG
SEQADV 5A4M HIS T 278 UNP P69739 EXPRESSION TAG
SEQRES 1 L 582 MET SER THR GLN TYR GLU THR GLN GLY TYR THR ILE ASN
SEQRES 2 L 582 ASN ALA GLY ARG ARG LEU VAL VAL ASP PRO ILE THR ARG
SEQRES 3 L 582 ILE GLU GLY HIS MET ARG CYS GLU VAL ASN ILE ASN ASP
SEQRES 4 L 582 GLN ASN VAL ILE THR ASN ALA VAL SER CYS GLY THR MET
SEQRES 5 L 582 PHE ARG GLY LEU GLU ILE ILE LEU GLN GLY ARG ASP PRO
SEQRES 6 L 582 ARG ASP ALA TRP ALA PHE VAL GLU ARG ILE CYS GLY VAL
SEQRES 7 L 582 CYS THR GLY VAL HIS ALA LEU ALA SER VAL TYR ALA ILE
SEQRES 8 L 582 GLU ASP ALA ILE GLY ILE LYS VAL PRO ASP ASN ALA ASN
SEQRES 9 L 582 ILE ILE ARG ASN ILE MET LEU ALA THR LEU TRP CYS HIS
SEQRES 10 L 582 ASP HIS LEU VAL HIS PHE TYR GLN LEU ALA GLY MET ASP
SEQRES 11 L 582 TRP ILE ASP VAL LEU ASP ALA LEU LYS ALA ASP PRO ARG
SEQRES 12 L 582 LYS THR SER GLU LEU ALA GLN SER LEU SER SER TRP PRO
SEQRES 13 L 582 LYS SER SER PRO GLY TYR PHE PHE ASP VAL GLN ASN ARG
SEQRES 14 L 582 LEU LYS LYS PHE VAL GLU GLY GLY GLN LEU GLY ILE PHE
SEQRES 15 L 582 ARG ASN GLY TYR TRP GLY HIS PRO GLN TYR LYS LEU PRO
SEQRES 16 L 582 PRO GLU ALA ASN LEU MET GLY PHE ALA HIS TYR LEU GLU
SEQRES 17 L 582 ALA LEU ASP PHE GLN ARG GLU ILE VAL LYS ILE HIS ALA
SEQRES 18 L 582 VAL PHE GLY GLY LYS ASN PRO HIS PRO ASN TRP ILE VAL
SEQRES 19 L 582 GLY GLY MET PRO CYS ALA ILE ASN ILE ASP GLU SER GLY
SEQRES 20 L 582 ALA VAL GLY ALA VAL ASN MET GLU ARG LEU ASN LEU VAL
SEQRES 21 L 582 GLN SER ILE ILE THR ARG THR ALA ASP PHE ILE ASN ASN
SEQRES 22 L 582 VAL MET ILE PRO ASP ALA LEU ALA ILE GLY GLN PHE ASN
SEQRES 23 L 582 LYS PRO TRP SER GLU ILE GLY THR GLY LEU SER ASP LYS
SEQRES 24 L 582 CYS VAL LEU SER TYR GLY ALA PHE PRO ASP ILE ALA ASN
SEQRES 25 L 582 ASP PHE GLY GLU LYS SER LEU LEU MET PRO GLY GLY ALA
SEQRES 26 L 582 VAL ILE ASN GLY ASP PHE ASN ASN VAL LEU PRO VAL ASP
SEQRES 27 L 582 LEU VAL ASP PRO GLN GLN VAL GLN GLU PHE VAL ASP HIS
SEQRES 28 L 582 ALA TRP TYR ARG TYR PRO ASN ASP GLN VAL GLY ARG HIS
SEQRES 29 L 582 PRO PHE ASP GLY ILE THR ASP PRO TRP TYR ASN PRO GLY
SEQRES 30 L 582 ASP VAL LYS GLY SER ASP THR ASN ILE GLN GLN LEU ASN
SEQRES 31 L 582 GLU GLN GLU ARG TYR SER TRP ILE LYS ALA PRO ARG TRP
SEQRES 32 L 582 ARG GLY ASN ALA MET GLU VAL GLY PRO LEU ALA ARG THR
SEQRES 33 L 582 LEU ILE ALA TYR HIS LYS GLY ASP ALA ALA THR VAL GLU
SEQRES 34 L 582 SER VAL ASP ARG MET MET SER ALA LEU ASN LEU PRO LEU
SEQRES 35 L 582 SER GLY ILE GLN SER THR LEU GLY ARG ILE LEU CYS ARG
SEQRES 36 L 582 ALA HIS GLU ALA GLN TRP ALA ALA GLY LYS LEU GLN TYR
SEQRES 37 L 582 PHE PHE ASP LYS LEU MET THR ASN LEU LYS ASN GLY ASN
SEQRES 38 L 582 LEU ALA THR ALA SER THR GLU LYS TRP GLU PRO ALA THR
SEQRES 39 L 582 TRP PRO THR GLU CYS ARG GLY VAL GLY PHE THR GLU ALA
SEQRES 40 L 582 PRO ARG GLY ALA LEU GLY HIS TRP ALA ALA ILE ARG ASP
SEQRES 41 L 582 GLY LYS ILE ASP LEU TYR GLN CYS VAL VAL PRO THR THR
SEQRES 42 L 582 TRP ASN ALA SER PRO ARG ASP PRO LYS GLY GLN ILE GLY
SEQRES 43 L 582 ALA TYR GLU ALA ALA LEU MET ASN THR LYS MET ALA ILE
SEQRES 44 L 582 PRO GLU GLN PRO LEU GLU ILE LEU ARG THR LEU HIS SER
SEQRES 45 L 582 PHE ASP PRO CYS LEU ALA CYS SER THR HIS
SEQRES 1 M 582 MET SER THR GLN TYR GLU THR GLN GLY TYR THR ILE ASN
SEQRES 2 M 582 ASN ALA GLY ARG ARG LEU VAL VAL ASP PRO ILE THR ARG
SEQRES 3 M 582 ILE GLU GLY HIS MET ARG CYS GLU VAL ASN ILE ASN ASP
SEQRES 4 M 582 GLN ASN VAL ILE THR ASN ALA VAL SER CYS GLY THR MET
SEQRES 5 M 582 PHE ARG GLY LEU GLU ILE ILE LEU GLN GLY ARG ASP PRO
SEQRES 6 M 582 ARG ASP ALA TRP ALA PHE VAL GLU ARG ILE CYS GLY VAL
SEQRES 7 M 582 CYS THR GLY VAL HIS ALA LEU ALA SER VAL TYR ALA ILE
SEQRES 8 M 582 GLU ASP ALA ILE GLY ILE LYS VAL PRO ASP ASN ALA ASN
SEQRES 9 M 582 ILE ILE ARG ASN ILE MET LEU ALA THR LEU TRP CYS HIS
SEQRES 10 M 582 ASP HIS LEU VAL HIS PHE TYR GLN LEU ALA GLY MET ASP
SEQRES 11 M 582 TRP ILE ASP VAL LEU ASP ALA LEU LYS ALA ASP PRO ARG
SEQRES 12 M 582 LYS THR SER GLU LEU ALA GLN SER LEU SER SER TRP PRO
SEQRES 13 M 582 LYS SER SER PRO GLY TYR PHE PHE ASP VAL GLN ASN ARG
SEQRES 14 M 582 LEU LYS LYS PHE VAL GLU GLY GLY GLN LEU GLY ILE PHE
SEQRES 15 M 582 ARG ASN GLY TYR TRP GLY HIS PRO GLN TYR LYS LEU PRO
SEQRES 16 M 582 PRO GLU ALA ASN LEU MET GLY PHE ALA HIS TYR LEU GLU
SEQRES 17 M 582 ALA LEU ASP PHE GLN ARG GLU ILE VAL LYS ILE HIS ALA
SEQRES 18 M 582 VAL PHE GLY GLY LYS ASN PRO HIS PRO ASN TRP ILE VAL
SEQRES 19 M 582 GLY GLY MET PRO CYS ALA ILE ASN ILE ASP GLU SER GLY
SEQRES 20 M 582 ALA VAL GLY ALA VAL ASN MET GLU ARG LEU ASN LEU VAL
SEQRES 21 M 582 GLN SER ILE ILE THR ARG THR ALA ASP PHE ILE ASN ASN
SEQRES 22 M 582 VAL MET ILE PRO ASP ALA LEU ALA ILE GLY GLN PHE ASN
SEQRES 23 M 582 LYS PRO TRP SER GLU ILE GLY THR GLY LEU SER ASP LYS
SEQRES 24 M 582 CYS VAL LEU SER TYR GLY ALA PHE PRO ASP ILE ALA ASN
SEQRES 25 M 582 ASP PHE GLY GLU LYS SER LEU LEU MET PRO GLY GLY ALA
SEQRES 26 M 582 VAL ILE ASN GLY ASP PHE ASN ASN VAL LEU PRO VAL ASP
SEQRES 27 M 582 LEU VAL ASP PRO GLN GLN VAL GLN GLU PHE VAL ASP HIS
SEQRES 28 M 582 ALA TRP TYR ARG TYR PRO ASN ASP GLN VAL GLY ARG HIS
SEQRES 29 M 582 PRO PHE ASP GLY ILE THR ASP PRO TRP TYR ASN PRO GLY
SEQRES 30 M 582 ASP VAL LYS GLY SER ASP THR ASN ILE GLN GLN LEU ASN
SEQRES 31 M 582 GLU GLN GLU ARG TYR SER TRP ILE LYS ALA PRO ARG TRP
SEQRES 32 M 582 ARG GLY ASN ALA MET GLU VAL GLY PRO LEU ALA ARG THR
SEQRES 33 M 582 LEU ILE ALA TYR HIS LYS GLY ASP ALA ALA THR VAL GLU
SEQRES 34 M 582 SER VAL ASP ARG MET MET SER ALA LEU ASN LEU PRO LEU
SEQRES 35 M 582 SER GLY ILE GLN SER THR LEU GLY ARG ILE LEU CYS ARG
SEQRES 36 M 582 ALA HIS GLU ALA GLN TRP ALA ALA GLY LYS LEU GLN TYR
SEQRES 37 M 582 PHE PHE ASP LYS LEU MET THR ASN LEU LYS ASN GLY ASN
SEQRES 38 M 582 LEU ALA THR ALA SER THR GLU LYS TRP GLU PRO ALA THR
SEQRES 39 M 582 TRP PRO THR GLU CYS ARG GLY VAL GLY PHE THR GLU ALA
SEQRES 40 M 582 PRO ARG GLY ALA LEU GLY HIS TRP ALA ALA ILE ARG ASP
SEQRES 41 M 582 GLY LYS ILE ASP LEU TYR GLN CYS VAL VAL PRO THR THR
SEQRES 42 M 582 TRP ASN ALA SER PRO ARG ASP PRO LYS GLY GLN ILE GLY
SEQRES 43 M 582 ALA TYR GLU ALA ALA LEU MET ASN THR LYS MET ALA ILE
SEQRES 44 M 582 PRO GLU GLN PRO LEU GLU ILE LEU ARG THR LEU HIS SER
SEQRES 45 M 582 PHE ASP PRO CYS LEU ALA CYS SER THR HIS
SEQRES 1 S 278 LEU GLU ASN LYS PRO ARG ILE PRO VAL VAL TRP ILE HIS
SEQRES 2 S 278 GLY LEU GLU CYS THR CYS CYS THR GLU SER PHE ILE ARG
SEQRES 3 S 278 SER ALA HIS PRO LEU ALA LYS ASP VAL ILE LEU SER LEU
SEQRES 4 S 278 ILE SER LEU ASP TYR ASP ASP THR LEU MET ALA ALA ALA
SEQRES 5 S 278 GLY THR GLN ALA GLU GLU VAL PHE GLU ASP ILE ILE THR
SEQRES 6 S 278 GLN TYR ASN GLY LYS TYR ILE LEU ALA VAL GLU GLY ASN
SEQRES 7 S 278 PRO PRO LEU GLY GLU GLN GLY MET PHE CYS ILE SER SER
SEQRES 8 S 278 GLY ARG PRO PHE ILE GLU LYS LEU LYS ARG ALA ALA ALA
SEQRES 9 S 278 GLY ALA SER ALA ILE ILE ALA TRP GLY THR CYS ALA SER
SEQRES 10 S 278 TRP GLY CYS VAL GLN ALA ALA ARG PRO ASN PRO THR GLN
SEQRES 11 S 278 ALA THR PRO ILE ASP LYS VAL ILE THR ASP LYS PRO ILE
SEQRES 12 S 278 ILE LYS VAL PRO GLY CYS PRO PRO ILE PRO ASP VAL MET
SEQRES 13 S 278 SER ALA ILE ILE THR TYR MET VAL THR PHE ASP ARG LEU
SEQRES 14 S 278 PRO ASP VAL ASP ARG MET GLY ARG PRO LEU MET PHE TYR
SEQRES 15 S 278 GLY GLN ARG ILE HIS ASP LYS CYS TYR ARG ARG ALA HIS
SEQRES 16 S 278 PHE ASP ALA GLY GLU PHE VAL GLN SER TRP ASP ASP ASP
SEQRES 17 S 278 ALA ALA ARG LYS GLY TYR CYS LEU TYR LYS MET GLY CYS
SEQRES 18 S 278 LYS GLY PRO THR THR TYR ASN ALA CYS SER SER THR ARG
SEQRES 19 S 278 TRP ASN ASP GLY VAL SER PHE PRO ILE GLN SER GLY HIS
SEQRES 20 S 278 GLY CYS LEU GLY CYS ALA GLU ASN GLY PHE TRP ASP ARG
SEQRES 21 S 278 GLY SER PHE TYR SER ARG GLY SER PHE TYR SER ARG HIS
SEQRES 22 S 278 HIS HIS HIS HIS HIS
SEQRES 1 T 278 LEU GLU ASN LYS PRO ARG ILE PRO VAL VAL TRP ILE HIS
SEQRES 2 T 278 GLY LEU GLU CYS THR CYS CYS THR GLU SER PHE ILE ARG
SEQRES 3 T 278 SER ALA HIS PRO LEU ALA LYS ASP VAL ILE LEU SER LEU
SEQRES 4 T 278 ILE SER LEU ASP TYR ASP ASP THR LEU MET ALA ALA ALA
SEQRES 5 T 278 GLY THR GLN ALA GLU GLU VAL PHE GLU ASP ILE ILE THR
SEQRES 6 T 278 GLN TYR ASN GLY LYS TYR ILE LEU ALA VAL GLU GLY ASN
SEQRES 7 T 278 PRO PRO LEU GLY GLU GLN GLY MET PHE CYS ILE SER SER
SEQRES 8 T 278 GLY ARG PRO PHE ILE GLU LYS LEU LYS ARG ALA ALA ALA
SEQRES 9 T 278 GLY ALA SER ALA ILE ILE ALA TRP GLY THR CYS ALA SER
SEQRES 10 T 278 TRP GLY CYS VAL GLN ALA ALA ARG PRO ASN PRO THR GLN
SEQRES 11 T 278 ALA THR PRO ILE ASP LYS VAL ILE THR ASP LYS PRO ILE
SEQRES 12 T 278 ILE LYS VAL PRO GLY CYS PRO PRO ILE PRO ASP VAL MET
SEQRES 13 T 278 SER ALA ILE ILE THR TYR MET VAL THR PHE ASP ARG LEU
SEQRES 14 T 278 PRO ASP VAL ASP ARG MET GLY ARG PRO LEU MET PHE TYR
SEQRES 15 T 278 GLY GLN ARG ILE HIS ASP LYS CYS TYR ARG ARG ALA HIS
SEQRES 16 T 278 PHE ASP ALA GLY GLU PHE VAL GLN SER TRP ASP ASP ASP
SEQRES 17 T 278 ALA ALA ARG LYS GLY TYR CYS LEU TYR LYS MET GLY CYS
SEQRES 18 T 278 LYS GLY PRO THR THR TYR ASN ALA CYS SER SER THR ARG
SEQRES 19 T 278 TRP ASN ASP GLY VAL SER PHE PRO ILE GLN SER GLY HIS
SEQRES 20 T 278 GLY CYS LEU GLY CYS ALA GLU ASN GLY PHE TRP ASP ARG
SEQRES 21 T 278 GLY SER PHE TYR SER ARG GLY SER PHE TYR SER ARG HIS
SEQRES 22 T 278 HIS HIS HIS HIS HIS
HET NFV L 601 9
HET MG L 602 1
HET NFV M 603 9
HET MG M 604 1
HET SF4 S 401 8
HET F3S S 402 7
HET SF3 S 404 7
HET CL S 408 1
HET SF4 T 401 8
HET F3S T 402 7
HET SF3 T 404 7
HET CL T 409 1
HETNAM NFV NI-FE OXIDIZED ACTIVE CENTER
HETNAM MG MAGNESIUM ION
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM F3S FE3-S4 CLUSTER
HETNAM SF3 FE4-S3 CLUSTER
HETNAM CL CHLORIDE ION
FORMUL 5 NFV 2(C3 FE N2 NI O2)
FORMUL 6 MG 2(MG 2+)
FORMUL 9 SF4 2(FE4 S4)
FORMUL 10 F3S 2(FE3 S4)
FORMUL 11 SF3 2(FE4 S3)
FORMUL 12 CL 2(CL 1-)
FORMUL 17 HOH *1492(H2 O)
HELIX 1 1 GLY L 55 LEU L 60 1 6
HELIX 2 2 ASP L 64 ARG L 66 5 3
HELIX 3 3 ASP L 67 ARG L 74 1 8
HELIX 4 4 GLY L 81 GLY L 96 1 16
HELIX 5 5 PRO L 100 LEU L 126 1 27
HELIX 6 6 ALA L 127 TRP L 131 5 5
HELIX 7 7 VAL L 134 ALA L 140 5 7
HELIX 8 8 ASP L 141 SER L 153 1 13
HELIX 9 9 SER L 159 GLY L 176 1 18
HELIX 10 10 LEU L 179 ARG L 183 5 5
HELIX 11 11 PRO L 195 GLY L 225 1 31
HELIX 12 12 GLY L 247 ALA L 251 5 5
HELIX 13 13 ASN L 253 VAL L 274 1 22
HELIX 14 14 VAL L 274 ASN L 286 1 13
HELIX 15 15 LYS L 287 ILE L 292 5 6
HELIX 16 16 THR L 294 LYS L 299 5 6
HELIX 17 17 HIS L 364 GLY L 368 5 5
HELIX 18 18 GLY L 411 LYS L 422 1 12
HELIX 19 19 ASP L 424 LEU L 438 1 15
HELIX 20 20 PRO L 441 GLN L 446 5 6
HELIX 21 21 SER L 447 ASN L 479 1 33
HELIX 22 22 GLU L 491 TRP L 495 5 5
HELIX 23 23 VAL L 530 ALA L 536 1 7
HELIX 24 24 GLY L 546 MET L 553 1 8
HELIX 25 25 PRO L 563 PHE L 573 1 11
HELIX 26 26 CYS L 576 HIS L 582 1 7
HELIX 27 27 GLY M 55 LEU M 60 1 6
HELIX 28 28 ASP M 64 ARG M 66 5 3
HELIX 29 29 ASP M 67 ARG M 74 1 8
HELIX 30 30 GLY M 81 GLY M 96 1 16
HELIX 31 31 PRO M 100 LEU M 126 1 27
HELIX 32 32 ALA M 127 TRP M 131 5 5
HELIX 33 33 VAL M 134 ALA M 140 5 7
HELIX 34 34 ASP M 141 SER M 153 1 13
HELIX 35 35 SER M 159 GLY M 176 1 18
HELIX 36 36 LEU M 179 ARG M 183 5 5
HELIX 37 37 PRO M 195 GLY M 225 1 31
HELIX 38 38 GLY M 247 ALA M 251 5 5
HELIX 39 39 ASN M 253 VAL M 274 1 22
HELIX 40 40 VAL M 274 ASN M 286 1 13
HELIX 41 41 LYS M 287 ILE M 292 5 6
HELIX 42 42 THR M 294 LYS M 299 5 6
HELIX 43 43 HIS M 364 GLY M 368 5 5
HELIX 44 44 GLY M 411 GLY M 423 1 13
HELIX 45 45 ASP M 424 LEU M 438 1 15
HELIX 46 46 PRO M 441 GLN M 446 5 6
HELIX 47 47 SER M 447 ASN M 479 1 33
HELIX 48 48 GLU M 491 TRP M 495 5 5
HELIX 49 49 VAL M 530 ALA M 536 1 7
HELIX 50 50 GLY M 546 MET M 553 1 8
HELIX 51 51 PRO M 563 PHE M 573 1 11
HELIX 52 52 CYS M 576 HIS M 582 1 7
HELIX 53 53 THR S 18 ARG S 26 1 9
HELIX 54 54 LEU S 31 LEU S 39 1 9
HELIX 55 55 ALA S 52 TYR S 67 1 16
HELIX 56 56 LEU S 81 MET S 86 5 6
HELIX 57 57 PHE S 95 GLY S 105 1 11
HELIX 58 58 GLY S 113 TRP S 118 1 6
HELIX 59 59 CYS S 120 ALA S 124 5 5
HELIX 60 60 PRO S 133 VAL S 137 5 5
HELIX 61 61 ILE S 152 ASP S 167 1 16
HELIX 62 62 PRO S 178 GLY S 183 1 6
HELIX 63 63 ILE S 186 CYS S 190 5 5
HELIX 64 64 ARG S 192 GLY S 199 1 8
HELIX 65 65 ALA S 209 GLY S 213 5 5
HELIX 66 66 LEU S 216 GLY S 220 5 5
HELIX 67 67 LYS S 222 THR S 226 5 5
HELIX 68 68 GLY S 256 ARG S 260 5 5
HELIX 69 69 THR T 18 ARG T 26 1 9
HELIX 70 70 LEU T 31 LEU T 39 1 9
HELIX 71 71 ALA T 52 TYR T 67 1 16
HELIX 72 72 LEU T 81 MET T 86 5 6
HELIX 73 73 PHE T 95 GLY T 105 1 11
HELIX 74 74 GLY T 113 TRP T 118 1 6
HELIX 75 75 GLY T 119 ALA T 124 1 6
HELIX 76 76 PRO T 133 VAL T 137 5 5
HELIX 77 77 ILE T 152 ASP T 167 1 16
HELIX 78 78 PRO T 178 GLY T 183 1 6
HELIX 79 79 ILE T 186 CYS T 190 5 5
HELIX 80 80 ARG T 192 GLY T 199 1 8
HELIX 81 81 ASP T 207 LYS T 212 1 6
HELIX 82 82 LEU T 216 GLY T 220 5 5
HELIX 83 83 LYS T 222 THR T 226 5 5
HELIX 84 84 GLY T 256 ARG T 260 5 5
SHEET 1 LA 2 GLN L 4 THR L 7 0
SHEET 2 LA 2 TYR L 10 ASN L 13 -1 O TYR L 10 N THR L 7
SHEET 1 LB 3 ARG L 17 VAL L 21 0
SHEET 2 LB 3 MET L 31 ILE L 37 -1 O CYS L 33 N VAL L 21
SHEET 3 LB 3 ILE L 43 GLY L 50 -1 N THR L 44 O ASN L 36
SHEET 1 LC 2 VAL L 301 SER L 303 0
SHEET 2 LC 2 GLY L 324 VAL L 326 -1 O GLY L 324 N SER L 303
SHEET 1 LD 2 ALA L 306 PRO L 308 0
SHEET 2 LD 2 LEU L 319 MET L 321 -1 N LEU L 320 O PHE L 307
SHEET 1 LE 2 VAL L 345 PHE L 348 0
SHEET 2 LE 2 ALA L 400 TRP L 403 -1 O ALA L 400 N PHE L 348
SHEET 1 LF 3 GLU L 498 ALA L 507 0
SHEET 2 LF 3 GLY L 510 ARG L 519 -1 O GLY L 510 N ALA L 507
SHEET 3 LF 3 LYS L 522 VAL L 529 -1 O LYS L 522 N ARG L 519
SHEET 1 MA 2 GLN M 4 THR M 7 0
SHEET 2 MA 2 TYR M 10 ASN M 13 -1 O TYR M 10 N THR M 7
SHEET 1 MB 3 ARG M 17 VAL M 21 0
SHEET 2 MB 3 MET M 31 ILE M 37 -1 O CYS M 33 N VAL M 21
SHEET 3 MB 3 ILE M 43 GLY M 50 -1 N THR M 44 O ASN M 36
SHEET 1 MC 2 VAL M 301 SER M 303 0
SHEET 2 MC 2 GLY M 324 VAL M 326 -1 O GLY M 324 N SER M 303
SHEET 1 MD 2 ALA M 306 PRO M 308 0
SHEET 2 MD 2 LEU M 319 MET M 321 -1 N LEU M 320 O PHE M 307
SHEET 1 ME 2 VAL M 345 PHE M 348 0
SHEET 2 ME 2 ALA M 400 TRP M 403 -1 O ALA M 400 N PHE M 348
SHEET 1 MF 2 LYS M 380 SER M 382 0
SHEET 2 MF 2 ASN M 385 GLN M 388 -1 O ASN M 385 N SER M 382
SHEET 1 MG 3 GLU M 498 ALA M 507 0
SHEET 2 MG 3 GLY M 510 ARG M 519 -1 O GLY M 510 N ALA M 507
SHEET 3 MG 3 LYS M 522 VAL M 529 -1 O LYS M 522 N ARG M 519
SHEET 1 SA 5 ILE S 40 ASP S 45 0
SHEET 2 SA 5 ILE S 7 HIS S 13 1 O ILE S 7 N SER S 41
SHEET 3 SA 5 TYR S 71 GLU S 76 1 O ILE S 72 N VAL S 10
SHEET 4 SA 5 ALA S 106 TRP S 112 1 N SER S 107 O TYR S 71
SHEET 5 SA 5 ILE S 143 VAL S 146 1 O ILE S 144 N ALA S 111
SHEET 1 SB 2 ILE S 89 SER S 90 0
SHEET 2 SB 2 ARG S 93 PRO S 94 -1 O ARG S 93 N SER S 90
SHEET 1 TA 5 ILE T 40 ASP T 45 0
SHEET 2 TA 5 ILE T 7 HIS T 13 1 O ILE T 7 N SER T 41
SHEET 3 TA 5 TYR T 71 GLU T 76 1 O ILE T 72 N VAL T 10
SHEET 4 TA 5 ALA T 106 TRP T 112 1 N SER T 107 O TYR T 71
SHEET 5 TA 5 ILE T 143 VAL T 146 1 O ILE T 144 N ALA T 111
SHEET 1 TB 2 ILE T 89 SER T 90 0
SHEET 2 TB 2 ARG T 93 PRO T 94 -1 O ARG T 93 N SER T 90
SSBOND 1 CYS M 79 CYS M 579 1555 1555 2.98
LINK OE2 GLU L 57 MG MG L 602 1555 1555 2.17
LINK SG CYS L 76 NI NFV L 601 1555 1555 2.29
LINK SG CYS L 79 NI NFV L 601 1555 1555 2.59
LINK SG CYS L 79 FE NFV L 601 1555 1555 2.31
LINK O CYS L 528 MG MG L 602 1555 1555 2.14
LINK SG CYS L 576 NI NFV L 601 1555 1555 2.23
LINK SG CYS L 579 FE NFV L 601 1555 1555 2.26
LINK SG CYS L 579 NI NFV L 601 1555 1555 2.48
LINK NE2 HIS L 582 MG MG L 602 1555 1555 2.26
LINK MG MG L 602 O HOH L2075 1555 1555 2.12
LINK MG MG L 602 O HOH L2076 1555 1555 2.09
LINK MG MG L 602 O HOH L2396 1555 1555 2.05
LINK O HOH L2282 FE7 SF3 S 404 1555 1555 1.88
LINK OE2 GLU M 57 MG MG M 604 1555 1555 2.18
LINK SG CYS M 76 NI NFV M 603 1555 1555 2.31
LINK SG CYS M 79 FE NFV M 603 1555 1555 2.29
LINK SG CYS M 79 NI NFV M 603 1555 1555 2.58
LINK O CYS M 528 MG MG M 604 1555 1555 2.13
LINK SG CYS M 576 NI NFV M 603 1555 1555 2.23
LINK SG CYS M 579 FE NFV M 603 1555 1555 2.24
LINK SG CYS M 579 NI NFV M 603 1555 1555 2.51
LINK NE2 HIS M 582 MG MG M 604 1555 1555 2.27
LINK MG MG M 604 O HOH M2068 1555 1555 2.15
LINK MG MG M 604 O HOH M2069 1555 1555 2.03
LINK MG MG M 604 O HOH M2390 1555 1555 2.10
LINK O HOH M2265 FE4 SF3 T 404 1555 1555 1.97
LINK SG CYS S 17 FE7 SF3 S 404 1555 1555 2.45
LINK SG CYS S 19 FE4 SF3 S 404 1555 1555 2.33
LINK SG CYS S 19 FE7 SF3 S 404 1555 1555 2.41
LINK SG CYS S 20 FE4 SF3 S 404 1555 1555 2.34
LINK SG CYS S 115 FE1 SF3 S 404 1555 1555 2.35
LINK SG CYS S 120 FE3 SF3 S 404 1555 1555 2.33
LINK SG CYS S 149 FE3 SF3 S 404 1555 1555 2.29
LINK ND1 HIS S 187 FE3 SF4 S 401 1555 1555 1.94
LINK SG CYS S 190 FE1 SF4 S 401 1555 1555 2.29
LINK SG CYS S 215 FE2 SF4 S 401 1555 1555 2.28
LINK SG CYS S 221 FE4 SF4 S 401 1555 1555 2.32
LINK SG CYS S 230 FE4 F3S S 402 1555 1555 2.31
LINK SG CYS S 249 FE3 F3S S 402 1555 1555 2.34
LINK SG CYS S 252 FE1 F3S S 402 1555 1555 2.29
LINK FE4 SF3 S 404 O HOH S2009 1555 1555 2.08
LINK SG CYS T 17 FE4 SF3 T 404 1555 1555 2.43
LINK SG CYS T 19 FE7 SF3 T 404 1555 1555 2.45
LINK SG CYS T 19 FE4 SF3 T 404 1555 1555 2.42
LINK SG CYS T 20 FE7 SF3 T 404 1555 1555 2.37
LINK SG CYS T 115 FE1 SF3 T 404 1555 1555 2.34
LINK SG CYS T 120 FE3 SF3 T 404 1555 1555 2.33
LINK SG CYS T 149 FE3 SF3 T 404 1555 1555 2.26
LINK ND1 HIS T 187 FE3 SF4 T 401 1555 1555 1.98
LINK SG CYS T 190 FE1 SF4 T 401 1555 1555 2.31
LINK SG CYS T 215 FE2 SF4 T 401 1555 1555 2.28
LINK SG CYS T 221 FE4 SF4 T 401 1555 1555 2.30
LINK SG CYS T 230 FE4 F3S T 402 1555 1555 2.30
LINK SG CYS T 249 FE3 F3S T 402 1555 1555 2.31
LINK SG CYS T 252 FE1 F3S T 402 1555 1555 2.29
LINK FE7 SF3 T 404 O HOH T2009 1555 1555 2.20
CISPEP 1 ASP L 22 PRO L 23 0 10.16
CISPEP 2 ASN L 227 PRO L 228 0 7.11
CISPEP 3 ASP M 22 PRO M 23 0 11.95
CISPEP 4 ASN M 227 PRO M 228 0 4.67
CISPEP 5 HIS S 29 PRO S 30 0 -9.47
CISPEP 6 ARG S 125 PRO S 126 0 4.23
CISPEP 7 CYS S 149 PRO S 150 0 -10.24
CISPEP 8 HIS T 29 PRO T 30 0 -6.40
CISPEP 9 ARG T 125 PRO T 126 0 5.36
CISPEP 10 CYS T 149 PRO T 150 0 -5.76
SITE 1 AC1 14 CYS L 76 CYS L 79 VAL L 82 HIS L 83
SITE 2 AC1 14 ALA L 507 PRO L 508 ARG L 509 LEU L 512
SITE 3 AC1 14 VAL L 530 PRO L 531 THR L 532 CYS L 576
SITE 4 AC1 14 CYS L 579 HOH L2106
SITE 1 AC2 6 GLU L 57 CYS L 528 HIS L 582 HOH L2075
SITE 2 AC2 6 HOH L2076 HOH L2396
SITE 1 AC3 13 CYS M 76 CYS M 79 VAL M 82 HIS M 83
SITE 2 AC3 13 ALA M 507 PRO M 508 ARG M 509 LEU M 512
SITE 3 AC3 13 VAL M 530 PRO M 531 THR M 532 CYS M 576
SITE 4 AC3 13 CYS M 579
SITE 1 AC4 6 GLU M 57 CYS M 528 HIS M 582 HOH M2068
SITE 2 AC4 6 HOH M2069 HOH M2390
SITE 1 AC5 6 HIS S 187 CYS S 190 ARG S 193 CYS S 215
SITE 2 AC5 6 LEU S 216 CYS S 221
SITE 1 AC6 8 LYS L 226 THR S 226 ASN S 228 CYS S 230
SITE 2 AC6 8 TRP S 235 CYS S 249 LEU S 250 CYS S 252
SITE 1 AC7 10 HOH L2282 CYS S 17 CYS S 19 CYS S 20
SITE 2 AC7 10 THR S 114 CYS S 115 CYS S 120 GLY S 148
SITE 3 AC7 10 CYS S 149 HOH S2009
SITE 1 AC8 4 TRP S 118 CYS S 120 GLY S 256 HOH S2083
SITE 1 AC9 6 HIS T 187 CYS T 190 ARG T 193 CYS T 215
SITE 2 AC9 6 LEU T 216 CYS T 221
SITE 1 BC1 7 LYS M 226 ASN T 228 CYS T 230 TRP T 235
SITE 2 BC1 7 CYS T 249 LEU T 250 CYS T 252
SITE 1 BC2 10 HOH M2265 CYS T 17 CYS T 19 CYS T 20
SITE 2 BC2 10 THR T 114 CYS T 115 CYS T 120 GLY T 148
SITE 3 BC2 10 CYS T 149 HOH T2009
SITE 1 BC3 3 CYS T 120 GLY T 256 HOH T2074
CRYST1 93.671 97.162 182.911 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 0.010676 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010292 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005467 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
