HEADER OXIDOREDUCTASE 25-NOV-10 3PQ4
TITLE STRUCTURE OF I274C VARIANT OF E. COLI KATE[] - IMAGES 13-18
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATALASE HPII;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: HYDROXYPEROXIDASE II;
COMPND 5 EC: 1.11.1.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 GENE: B1732, JW1721, KATE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: UM255;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKS
KEYWDS CATALASE, I274C VARIANT, HEME ORIENTATION, X-RAY DAMAGE,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.LOEWEN,V.JHA,S.LOUIS,P.CHELIKANI,X.CARPENA,I.FITA
REVDAT 4 06-SEP-23 3PQ4 1 REMARK SEQADV LINK
REVDAT 3 08-NOV-17 3PQ4 1 REMARK
REVDAT 2 27-JUL-11 3PQ4 1 JRNL
REVDAT 1 22-DEC-10 3PQ4 0
JRNL AUTH V.JHA,S.LOUIS,P.CHELIKANI,X.CARPENA,L.J.DONALD,I.FITA,
JRNL AUTH 2 P.C.LOEWEN
JRNL TITL MODULATION OF HEME ORIENTATION AND BINDING BY A SINGLE
JRNL TITL 2 RESIDUE IN CATALASE HPII OF ESCHERICHIA COLI.
JRNL REF BIOCHEMISTRY V. 50 2101 2011
JRNL REFN ISSN 0006-2960
JRNL PMID 21332158
JRNL DOI 10.1021/BI200027V
REMARK 2
REMARK 2 RESOLUTION. 1.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 242617
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) : 0.144
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 12136
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) : 1.79
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.84
REMARK 3 REFLECTION IN BIN (WORKING SET) : 14740
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 772
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22936
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 356
REMARK 3 SOLVENT ATOMS : 3435
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.22000
REMARK 3 B22 (A**2) : -0.32000
REMARK 3 B33 (A**2) : 0.75000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.31000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.121
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.072
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.069
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24102 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 32898 ; 2.031 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2908 ; 6.504 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1181 ;36.300 ;23.853
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3780 ;14.236 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 177 ;14.531 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3447 ; 0.179 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18973 ; 0.012 ; 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): 14579 ; 1.097 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23575 ; 1.664 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9523 ; 2.701 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 9323 ; 3.952 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 28 A 753 4
REMARK 3 1 B 28 B 753 4
REMARK 3 1 C 28 C 753 4
REMARK 3 1 D 28 D 753 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 5705 ; 0.370 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 5705 ; 0.310 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 5705 ; 0.310 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 5705 ; 0.330 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 5705 ; 1.800 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 5705 ; 1.590 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 5705 ; 1.520 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 5705 ; 1.410 ; 2.000
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 : A -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6762 -9.3221 31.5426
REMARK 3 T TENSOR
REMARK 3 T11: 0.0058 T22: 0.0111
REMARK 3 T33: 0.0242 T12: 0.0035
REMARK 3 T13: 0.0084 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.0545 L22: 0.0434
REMARK 3 L33: 0.0357 L12: 0.0002
REMARK 3 L13: 0.0245 L23: -0.0204
REMARK 3 S TENSOR
REMARK 3 S11: -0.0054 S12: -0.0135 S13: -0.0233
REMARK 3 S21: 0.0055 S22: 0.0137 S23: 0.0186
REMARK 3 S31: -0.0005 S32: -0.0058 S33: -0.0083
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 : B -10 B 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6080 11.8541 -18.5900
REMARK 3 T TENSOR
REMARK 3 T11: 0.0283 T22: 0.0083
REMARK 3 T33: 0.0195 T12: -0.0055
REMARK 3 T13: -0.0130 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.0534 L22: 0.0918
REMARK 3 L33: 0.0331 L12: -0.0289
REMARK 3 L13: -0.0185 L23: -0.0119
REMARK 3 S TENSOR
REMARK 3 S11: 0.0038 S12: 0.0133 S13: 0.0242
REMARK 3 S21: -0.0439 S22: 0.0048 S23: 0.0091
REMARK 3 S31: -0.0003 S32: -0.0073 S33: -0.0086
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 : C -10 C 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4970 -12.0288 -19.6074
REMARK 3 T TENSOR
REMARK 3 T11: 0.0391 T22: 0.0073
REMARK 3 T33: 0.0087 T12: -0.0061
REMARK 3 T13: 0.0124 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 0.0393 L22: 0.0867
REMARK 3 L33: 0.0440 L12: 0.0101
REMARK 3 L13: -0.0101 L23: -0.0062
REMARK 3 S TENSOR
REMARK 3 S11: -0.0142 S12: 0.0035 S13: -0.0087
REMARK 3 S21: -0.0504 S22: 0.0105 S23: -0.0086
REMARK 3 S31: 0.0190 S32: 0.0092 S33: 0.0037
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 : D -10 D 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0685 9.4240 31.5616
REMARK 3 T TENSOR
REMARK 3 T11: 0.0064 T22: 0.0203
REMARK 3 T33: 0.0114 T12: -0.0001
REMARK 3 T13: -0.0042 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.0641 L22: 0.0508
REMARK 3 L33: 0.0355 L12: 0.0376
REMARK 3 L13: -0.0239 L23: 0.0082
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: -0.0186 S13: 0.0092
REMARK 3 S21: 0.0058 S22: -0.0023 S23: -0.0052
REMARK 3 S31: -0.0071 S32: 0.0191 S33: -0.0040
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 3PQ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000062682.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 33
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : DOUBLE MIRROR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 242816
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.794
REMARK 200 RESOLUTION RANGE LOW (A) : 35.193
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.15700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
REMARK 200 R SYM FOR SHELL (I) : 0.43000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 3P9Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG3350, 1.6 M LICL, 0.1 M TRIS,
REMARK 280 PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 66.51550
REMARK 290 SMTRY3 2 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: 57600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 79350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -301.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 A 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 HIS A 4
REMARK 465 ASN A 5
REMARK 465 GLU A 6
REMARK 465 LYS A 7
REMARK 465 ASN A 8
REMARK 465 PRO A 9
REMARK 465 HIS A 10
REMARK 465 GLN A 11
REMARK 465 HIS A 12
REMARK 465 GLN A 13
REMARK 465 SER A 14
REMARK 465 PRO A 15
REMARK 465 LEU A 16
REMARK 465 HIS A 17
REMARK 465 ASP A 18
REMARK 465 SER A 19
REMARK 465 SER A 20
REMARK 465 GLU A 21
REMARK 465 ALA A 22
REMARK 465 LYS A 23
REMARK 465 PRO A 24
REMARK 465 GLY A 25
REMARK 465 MET A 26
REMARK 465 ASP A 27
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLN B 3
REMARK 465 HIS B 4
REMARK 465 ASN B 5
REMARK 465 GLU B 6
REMARK 465 LYS B 7
REMARK 465 ASN B 8
REMARK 465 PRO B 9
REMARK 465 HIS B 10
REMARK 465 GLN B 11
REMARK 465 HIS B 12
REMARK 465 GLN B 13
REMARK 465 SER B 14
REMARK 465 PRO B 15
REMARK 465 LEU B 16
REMARK 465 HIS B 17
REMARK 465 ASP B 18
REMARK 465 SER B 19
REMARK 465 SER B 20
REMARK 465 GLU B 21
REMARK 465 ALA B 22
REMARK 465 LYS B 23
REMARK 465 PRO B 24
REMARK 465 GLY B 25
REMARK 465 MET B 26
REMARK 465 ASP B 27
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLN C 3
REMARK 465 HIS C 4
REMARK 465 ASN C 5
REMARK 465 GLU C 6
REMARK 465 LYS C 7
REMARK 465 ASN C 8
REMARK 465 PRO C 9
REMARK 465 HIS C 10
REMARK 465 GLN C 11
REMARK 465 HIS C 12
REMARK 465 GLN C 13
REMARK 465 SER C 14
REMARK 465 PRO C 15
REMARK 465 LEU C 16
REMARK 465 HIS C 17
REMARK 465 ASP C 18
REMARK 465 SER C 19
REMARK 465 SER C 20
REMARK 465 GLU C 21
REMARK 465 ALA C 22
REMARK 465 LYS C 23
REMARK 465 PRO C 24
REMARK 465 GLY C 25
REMARK 465 MET C 26
REMARK 465 ASP C 27
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 GLN D 3
REMARK 465 HIS D 4
REMARK 465 ASN D 5
REMARK 465 GLU D 6
REMARK 465 LYS D 7
REMARK 465 ASN D 8
REMARK 465 PRO D 9
REMARK 465 HIS D 10
REMARK 465 GLN D 11
REMARK 465 HIS D 12
REMARK 465 GLN D 13
REMARK 465 SER D 14
REMARK 465 PRO D 15
REMARK 465 LEU D 16
REMARK 465 HIS D 17
REMARK 465 ASP D 18
REMARK 465 SER D 19
REMARK 465 SER D 20
REMARK 465 GLU D 21
REMARK 465 ALA D 22
REMARK 465 LYS D 23
REMARK 465 PRO D 24
REMARK 465 GLY D 25
REMARK 465 MET D 26
REMARK 465 ASP D 27
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2305 O HOH A 3509 1.57
REMARK 500 O HOH D 1959 O HOH D 3443 1.78
REMARK 500 O HOH A 1712 O HOH A 3179 1.81
REMARK 500 O HOH D 1721 O HOH D 2639 1.82
REMARK 500 O HOH D 2813 O HOH D 3139 1.89
REMARK 500 OE2 GLU A 541 O HOH A 2550 1.91
REMARK 500 O HOH A 1111 O HOH A 3235 1.96
REMARK 500 O HOH B 2909 O HOH B 2958 2.00
REMARK 500 O HOH D 1982 O HOH D 2107 2.01
REMARK 500 OE2 GLU D 731 O HOH D 3028 2.06
REMARK 500 O HOH B 2689 O HOH D 3582 2.08
REMARK 500 O HOH C 2088 O HOH C 2444 2.08
REMARK 500 O HOH A 2377 O HOH A 3042 2.11
REMARK 500 O HOH A 1026 O HOH D 2541 2.13
REMARK 500 O HOH C 2207 O HOH C 2380 2.13
REMARK 500 O HOH B 2271 O HOH B 3063 2.14
REMARK 500 OE1 GLU D 639 O HOH D 2189 2.14
REMARK 500 O HOH D 845 O HOH D 2956 2.14
REMARK 500 O HOH A 774 O HOH A 2914 2.15
REMARK 500 O ASP C 725 O HOH C 2403 2.15
REMARK 500 O HOH A 2363 O HOH D 2782 2.15
REMARK 500 O HOH D 1303 O HOH D 1875 2.16
REMARK 500 OD2 ASP C 59 O HOH C 2529 2.16
REMARK 500 O HOH D 1120 O HOH D 2270 2.17
REMARK 500 O HOH D 1832 O HOH D 2497 2.17
REMARK 500 O HOH B 1082 O HOH B 3420 2.17
REMARK 500 O HOH C 2237 O HOH C 3449 2.18
REMARK 500 O HOH B 755 O HOH B 1087 2.18
REMARK 500 O HOH D 1714 O HOH D 2317 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH D 2178 O HOH D 2976 1655 2.00
REMARK 500 NZ LYS C 584 O HOH A 1624 1554 2.06
REMARK 500 O HOH A 3241 O HOH D 2457 2646 2.15
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 VAL A 603 CB VAL A 603 CG1 -0.138
REMARK 500 TYR A 684 CE2 TYR A 684 CD2 0.100
REMARK 500 PHE D 272 CZ PHE D 272 CE2 0.147
REMARK 500 GLU D 333 CD GLU D 333 OE2 -0.081
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 A 479 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 740 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 72 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 72 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 37 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP C 59 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP C 70 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG C 121 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ILE C 159 CB - CG1 - CD1 ANGL. DEV. = -17.8 DEGREES
REMARK 500 ARG C 636 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG C 636 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG D 377 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG D 488 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG D 495 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG D 521 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 LEU D 582 CB - CG - CD1 ANGL. DEV. = 12.6 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 SER A 75 -38.62 -166.47
REMARK 500 THR A 178 37.37 -91.53
REMARK 500 CYS A 274 -42.24 76.94
REMARK 500 ASP A 314 89.43 -152.35
REMARK 500 ASP A 446 -146.29 70.92
REMARK 500 LYS A 584 162.07 176.40
REMARK 500 ASP A 595 24.65 -155.44
REMARK 500 HIS A 739 -63.17 72.74
REMARK 500 SER B 75 -37.88 -161.04
REMARK 500 VAL B 169 -51.52 -120.82
REMARK 500 THR B 178 41.73 -86.99
REMARK 500 SER B 265 146.48 -170.61
REMARK 500 CYS B 274 -44.54 76.11
REMARK 500 ASP B 314 89.73 -153.11
REMARK 500 ASP B 330 57.95 -90.75
REMARK 500 ASN B 442 -166.97 -163.25
REMARK 500 ASP B 446 -149.60 70.11
REMARK 500 LYS B 584 165.41 176.60
REMARK 500 ARG B 612 94.98 -67.52
REMARK 500 ASP B 725 -172.56 -19.33
REMARK 500 HIS B 739 -62.06 78.54
REMARK 500 SER C 75 -36.20 -165.20
REMARK 500 THR C 178 34.70 -90.92
REMARK 500 CYS C 274 -48.72 75.92
REMARK 500 ASP C 314 89.55 -155.49
REMARK 500 ASN C 427 31.68 -93.67
REMARK 500 ASN C 442 -169.97 -164.29
REMARK 500 ASP C 446 -150.63 66.01
REMARK 500 LYS C 584 161.87 179.55
REMARK 500 ALA C 724 43.69 -81.87
REMARK 500 ASP C 725 -124.77 -154.58
REMARK 500 HIS C 739 -64.38 72.41
REMARK 500 SER D 75 -37.06 -162.95
REMARK 500 GLU D 106 2.55 -69.10
REMARK 500 THR D 178 38.13 -91.45
REMARK 500 CYS D 274 -44.69 82.09
REMARK 500 ASP D 314 84.70 -153.70
REMARK 500 ASP D 405 116.20 -36.69
REMARK 500 ASP D 446 -148.93 72.34
REMARK 500 ASP D 595 35.43 -145.88
REMARK 500 HIS D 739 -66.71 76.54
REMARK 500 VAL D 741 75.75 -105.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA C 724 ASP C 725 140.72
REMARK 500 ASP C 725 GLY C 726 -145.69
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 HDD A 760 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 415 OH
REMARK 620 2 HDD A 760 NA 94.9
REMARK 620 3 HDD A 760 NB 93.2 89.5
REMARK 620 4 HDD A 760 NC 89.2 175.9 89.7
REMARK 620 5 HDD A 760 ND 90.9 88.9 175.7 91.6
REMARK 620 6 HOH A3592 O 173.7 81.0 82.0 94.9 93.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HDE A 761 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 415 OH
REMARK 620 2 HDE A 761 NA 98.9
REMARK 620 3 HDE A 761 NB 95.5 89.0
REMARK 620 4 HDE A 761 NC 83.1 177.8 91.7
REMARK 620 5 HDE A 761 ND 86.0 90.9 178.4 88.4
REMARK 620 6 HOH A3592 O 151.9 108.9 88.9 69.0 89.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HDD B 760 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 415 OH
REMARK 620 2 HDD B 760 NA 94.4
REMARK 620 3 HDD B 760 NB 83.3 93.3
REMARK 620 4 HDD B 760 NC 89.3 176.3 86.8
REMARK 620 5 HDD B 760 ND 100.2 87.9 176.3 91.9
REMARK 620 6 HOH B3593 O 163.5 87.8 80.3 88.6 96.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HDE B 761 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 415 OH
REMARK 620 2 HDE B 761 NA 90.6
REMARK 620 3 HDE B 761 NB 94.4 89.0
REMARK 620 4 HDE B 761 NC 91.3 178.1 90.9
REMARK 620 5 HDE B 761 ND 86.8 90.5 178.8 89.5
REMARK 620 6 HOH B3593 O 175.8 93.4 84.4 84.7 94.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HDD C 760 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 415 OH
REMARK 620 2 HDD C 760 NA 89.6
REMARK 620 3 HDD C 760 NB 88.5 88.3
REMARK 620 4 HDD C 760 NC 94.0 176.4 92.1
REMARK 620 5 HDD C 760 ND 95.9 91.8 175.6 87.5
REMARK 620 6 HOH C3277 O 164.3 80.8 78.8 95.8 96.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HDE C 761 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 415 OH
REMARK 620 2 HDE C 761 NA 92.9
REMARK 620 3 HDE C 761 NB 96.6 87.9
REMARK 620 4 HDE C 761 NC 89.2 177.9 92.1
REMARK 620 5 HDE C 761 ND 84.9 91.7 178.5 88.3
REMARK 620 6 HOH C3277 O 168.3 98.3 87.3 79.6 91.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HDD D 760 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 415 OH
REMARK 620 2 HDD D 760 NA 94.7
REMARK 620 3 HDD D 760 NB 87.5 92.7
REMARK 620 4 HDD D 760 NC 88.6 176.6 88.3
REMARK 620 5 HDD D 760 ND 97.1 87.7 175.3 91.0
REMARK 620 6 HOH D3252 O 167.0 83.7 79.7 93.2 95.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HDE D 761 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 415 OH
REMARK 620 2 HDE D 761 NA 90.0
REMARK 620 3 HDE D 761 NB 94.8 87.3
REMARK 620 4 HDE D 761 NC 92.0 177.9 93.2
REMARK 620 5 HDE D 761 ND 86.5 91.9 178.4 87.7
REMARK 620 6 HOH D3252 O 170.8 98.9 87.6 79.0 91.3
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 HDD A 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD B 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD C 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD D 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDE A 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDE B 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDE C 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDE D 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S A 754
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S B 754
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S C 754
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S D 754
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P9P RELATED DB: PDB
REMARK 900 RELATED ID: 3P9Q RELATED DB: PDB
REMARK 900 RELATED ID: 3P9R RELATED DB: PDB
REMARK 900 RELATED ID: 3P9S RELATED DB: PDB
REMARK 900 RELATED ID: 3PQ2 RELATED DB: PDB
REMARK 900 RELATED ID: 3PQ3 RELATED DB: PDB
REMARK 900 RELATED ID: 3PQ5 RELATED DB: PDB
REMARK 900 RELATED ID: 3PQ6 RELATED DB: PDB
REMARK 900 RELATED ID: 3PQ7 RELATED DB: PDB
REMARK 900 RELATED ID: 3PQ8 RELATED DB: PDB
DBREF 3PQ4 A 1 753 UNP P21179 CATE_ECOLI 1 753
DBREF 3PQ4 B 1 753 UNP P21179 CATE_ECOLI 1 753
DBREF 3PQ4 C 1 753 UNP P21179 CATE_ECOLI 1 753
DBREF 3PQ4 D 1 753 UNP P21179 CATE_ECOLI 1 753
SEQADV 3PQ4 CYS A 274 UNP P21179 ILE 274 ENGINEERED MUTATION
SEQADV 3PQ4 ALA A 438 UNP P21179 CYS 438 ENGINEERED MUTATION
SEQADV 3PQ4 ALA A 669 UNP P21179 CYS 669 ENGINEERED MUTATION
SEQADV 3PQ4 CYS B 274 UNP P21179 ILE 274 ENGINEERED MUTATION
SEQADV 3PQ4 ALA B 438 UNP P21179 CYS 438 ENGINEERED MUTATION
SEQADV 3PQ4 ALA B 669 UNP P21179 CYS 669 ENGINEERED MUTATION
SEQADV 3PQ4 CYS C 274 UNP P21179 ILE 274 ENGINEERED MUTATION
SEQADV 3PQ4 ALA C 438 UNP P21179 CYS 438 ENGINEERED MUTATION
SEQADV 3PQ4 ALA C 669 UNP P21179 CYS 669 ENGINEERED MUTATION
SEQADV 3PQ4 CYS D 274 UNP P21179 ILE 274 ENGINEERED MUTATION
SEQADV 3PQ4 ALA D 438 UNP P21179 CYS 438 ENGINEERED MUTATION
SEQADV 3PQ4 ALA D 669 UNP P21179 CYS 669 ENGINEERED MUTATION
SEQRES 1 A 753 MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES 2 A 753 SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES 3 A 753 ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES 4 A 753 ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES 5 A 753 GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES 6 A 753 ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES 7 A 753 ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES 8 A 753 GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES 9 A 753 LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES 10 A 753 ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES 11 A 753 GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES 12 A 753 LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES 13 A 753 ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 14 A 753 GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES 15 A 753 ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES 16 A 753 PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES 17 A 753 GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES 18 A 753 LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES 19 A 753 ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES 20 A 753 GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES 21 A 753 GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES 22 A 753 CYS HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES 23 A 753 THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES 24 A 753 ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES 25 A 753 ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES 26 A 753 ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES 27 A 753 GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES 28 A 753 ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES 29 A 753 VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES 30 A 753 ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES 31 A 753 PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES 32 A 753 ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES 33 A 753 ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES 34 A 753 GLU ILE PRO ILE ASN ARG PRO THR ALA PRO TYR HIS ASN
SEQRES 35 A 753 PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES 36 A 753 ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES 37 A 753 TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES 38 A 753 PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES 39 A 753 ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES 40 A 753 PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES 41 A 753 ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES 42 A 753 VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES 43 A 753 LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES 44 A 753 LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES 45 A 753 ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES 46 A 753 PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES 47 A 753 LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES 48 A 753 ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES 49 A 753 ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES 50 A 753 GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES 51 A 753 ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES 52 A 753 ALA VAL ILE VAL PRO ALA GLY ASN ILE ALA ASP ILE ALA
SEQRES 53 A 753 ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES 54 A 753 LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES 55 A 753 LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES 56 A 753 GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES 57 A 753 MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES 58 A 753 TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES 1 B 753 MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES 2 B 753 SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES 3 B 753 ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES 4 B 753 ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES 5 B 753 GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES 6 B 753 ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES 7 B 753 ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES 8 B 753 GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES 9 B 753 LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES 10 B 753 ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES 11 B 753 GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES 12 B 753 LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES 13 B 753 ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 14 B 753 GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES 15 B 753 ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES 16 B 753 PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES 17 B 753 GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES 18 B 753 LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES 19 B 753 ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES 20 B 753 GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES 21 B 753 GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES 22 B 753 CYS HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES 23 B 753 THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES 24 B 753 ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES 25 B 753 ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES 26 B 753 ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES 27 B 753 GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES 28 B 753 ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES 29 B 753 VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES 30 B 753 ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES 31 B 753 PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES 32 B 753 ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES 33 B 753 ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES 34 B 753 GLU ILE PRO ILE ASN ARG PRO THR ALA PRO TYR HIS ASN
SEQRES 35 B 753 PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES 36 B 753 ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES 37 B 753 TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES 38 B 753 PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES 39 B 753 ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES 40 B 753 PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES 41 B 753 ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES 42 B 753 VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES 43 B 753 LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES 44 B 753 LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES 45 B 753 ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES 46 B 753 PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES 47 B 753 LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES 48 B 753 ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES 49 B 753 ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES 50 B 753 GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES 51 B 753 ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES 52 B 753 ALA VAL ILE VAL PRO ALA GLY ASN ILE ALA ASP ILE ALA
SEQRES 53 B 753 ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES 54 B 753 LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES 55 B 753 LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES 56 B 753 GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES 57 B 753 MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES 58 B 753 TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES 1 C 753 MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES 2 C 753 SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES 3 C 753 ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES 4 C 753 ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES 5 C 753 GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES 6 C 753 ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES 7 C 753 ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES 8 C 753 GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES 9 C 753 LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES 10 C 753 ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES 11 C 753 GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES 12 C 753 LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES 13 C 753 ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 14 C 753 GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES 15 C 753 ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES 16 C 753 PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES 17 C 753 GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES 18 C 753 LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES 19 C 753 ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES 20 C 753 GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES 21 C 753 GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES 22 C 753 CYS HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES 23 C 753 THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES 24 C 753 ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES 25 C 753 ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES 26 C 753 ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES 27 C 753 GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES 28 C 753 ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES 29 C 753 VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES 30 C 753 ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES 31 C 753 PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES 32 C 753 ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES 33 C 753 ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES 34 C 753 GLU ILE PRO ILE ASN ARG PRO THR ALA PRO TYR HIS ASN
SEQRES 35 C 753 PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES 36 C 753 ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES 37 C 753 TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES 38 C 753 PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES 39 C 753 ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES 40 C 753 PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES 41 C 753 ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES 42 C 753 VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES 43 C 753 LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES 44 C 753 LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES 45 C 753 ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES 46 C 753 PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES 47 C 753 LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES 48 C 753 ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES 49 C 753 ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES 50 C 753 GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES 51 C 753 ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES 52 C 753 ALA VAL ILE VAL PRO ALA GLY ASN ILE ALA ASP ILE ALA
SEQRES 53 C 753 ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES 54 C 753 LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES 55 C 753 LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES 56 C 753 GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES 57 C 753 MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES 58 C 753 TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES 1 D 753 MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES 2 D 753 SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES 3 D 753 ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES 4 D 753 ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES 5 D 753 GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES 6 D 753 ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES 7 D 753 ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES 8 D 753 GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES 9 D 753 LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES 10 D 753 ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES 11 D 753 GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES 12 D 753 LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES 13 D 753 ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 14 D 753 GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES 15 D 753 ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES 16 D 753 PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES 17 D 753 GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES 18 D 753 LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES 19 D 753 ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES 20 D 753 GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES 21 D 753 GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES 22 D 753 CYS HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES 23 D 753 THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES 24 D 753 ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES 25 D 753 ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES 26 D 753 ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES 27 D 753 GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES 28 D 753 ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES 29 D 753 VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES 30 D 753 ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES 31 D 753 PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES 32 D 753 ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES 33 D 753 ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES 34 D 753 GLU ILE PRO ILE ASN ARG PRO THR ALA PRO TYR HIS ASN
SEQRES 35 D 753 PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES 36 D 753 ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES 37 D 753 TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES 38 D 753 PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES 39 D 753 ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES 40 D 753 PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES 41 D 753 ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES 42 D 753 VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES 43 D 753 LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES 44 D 753 LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES 45 D 753 ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES 46 D 753 PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES 47 D 753 LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES 48 D 753 ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES 49 D 753 ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES 50 D 753 GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES 51 D 753 ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES 52 D 753 ALA VAL ILE VAL PRO ALA GLY ASN ILE ALA ASP ILE ALA
SEQRES 53 D 753 ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES 54 D 753 LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES 55 D 753 LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES 56 D 753 GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES 57 D 753 MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES 58 D 753 TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
HET HDD A 760 44
HET HDE A 761 44
HET H2S A 754 1
HET HDD B 760 44
HET HDE B 761 44
HET H2S B 754 1
HET HDD C 760 44
HET HDE C 761 44
HET H2S C 754 1
HET HDD D 760 44
HET HDE D 761 44
HET H2S D 754 1
HETNAM HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE
HETNAM HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S
HETNAM H2S HYDROSULFURIC ACID
HETSYN HDD HEME
HETSYN H2S HYDROGEN SULFIDE
FORMUL 5 HDD 4(C34 H32 FE N4 O5)
FORMUL 6 HDE 4(C34 H38 FE N4 O5)
FORMUL 7 H2S 4(H2 S)
FORMUL 17 HOH *3435(H2 O)
HELIX 1 1 PRO A 52 ALA A 57 1 6
HELIX 2 2 ASN A 62 LEU A 68 1 7
HELIX 3 3 ASP A 107 HIS A 119 1 13
HELIX 4 4 ALA A 150 SER A 154 5 5
HELIX 5 5 ASP A 210 HIS A 212 5 3
HELIX 6 6 LYS A 213 LYS A 222 1 10
HELIX 7 7 HIS A 236 GLN A 246 1 11
HELIX 8 8 THR A 249 SER A 258 1 10
HELIX 9 9 ASP A 259 ILE A 262 5 4
HELIX 10 10 SER A 265 MET A 269 5 5
HELIX 11 11 VAL A 303 ASP A 314 1 12
HELIX 12 12 ASP A 316 GLY A 329 1 14
HELIX 13 13 GLU A 344 GLU A 346 5 3
HELIX 14 14 ASN A 381 ASN A 386 1 6
HELIX 15 15 ASP A 405 THR A 418 1 14
HELIX 16 16 THR A 418 LEU A 423 1 6
HELIX 17 17 ASN A 427 ARG A 435 5 9
HELIX 18 18 SER A 498 GLY A 502 5 5
HELIX 19 19 TYR A 505 SER A 514 1 10
HELIX 20 20 THR A 516 LYS A 533 1 18
HELIX 21 21 ARG A 536 ASP A 551 1 16
HELIX 22 22 ASP A 551 LEU A 562 1 12
HELIX 23 23 THR A 567 ASN A 572 1 6
HELIX 24 24 ASP A 585 SER A 589 5 5
HELIX 25 25 ARG A 612 LYS A 626 1 15
HELIX 26 26 PRO A 658 VAL A 662 5 5
HELIX 27 27 ILE A 672 ASP A 677 1 6
HELIX 28 28 ASN A 678 HIS A 691 1 14
HELIX 29 29 ASP A 700 LYS A 709 5 10
HELIX 30 30 ASP A 725 ALA A 738 1 14
HELIX 31 31 VAL A 741 SER A 743 5 3
HELIX 32 32 ARG A 744 ASP A 749 1 6
HELIX 33 33 PRO B 52 ALA B 57 1 6
HELIX 34 34 ASN B 62 LEU B 68 1 7
HELIX 35 35 ASP B 107 HIS B 119 1 13
HELIX 36 36 ALA B 150 SER B 154 5 5
HELIX 37 37 ASP B 210 HIS B 212 5 3
HELIX 38 38 LYS B 213 LYS B 222 1 10
HELIX 39 39 HIS B 236 GLN B 246 1 11
HELIX 40 40 THR B 249 SER B 258 1 10
HELIX 41 41 ASP B 259 ILE B 262 5 4
HELIX 42 42 SER B 265 MET B 269 5 5
HELIX 43 43 VAL B 303 ASP B 314 1 12
HELIX 44 44 ASP B 316 GLY B 329 1 14
HELIX 45 45 GLU B 344 GLU B 346 5 3
HELIX 46 46 ASN B 381 ASN B 386 1 6
HELIX 47 47 ASP B 405 THR B 418 1 14
HELIX 48 48 THR B 418 LEU B 423 1 6
HELIX 49 49 ASN B 427 ARG B 435 5 9
HELIX 50 50 SER B 498 GLY B 502 5 5
HELIX 51 51 TYR B 505 GLN B 515 1 11
HELIX 52 52 THR B 516 LYS B 533 1 18
HELIX 53 53 ARG B 536 HIS B 549 1 14
HELIX 54 54 ASP B 551 LEU B 562 1 12
HELIX 55 55 THR B 567 ASN B 572 1 6
HELIX 56 56 ASP B 585 SER B 589 5 5
HELIX 57 57 ARG B 612 LYS B 626 1 15
HELIX 58 58 PRO B 658 VAL B 662 5 5
HELIX 59 59 ASN B 671 ILE B 675 5 5
HELIX 60 60 ASN B 678 HIS B 691 1 14
HELIX 61 61 ASP B 700 LYS B 709 5 10
HELIX 62 62 ASP B 725 ALA B 738 1 14
HELIX 63 63 VAL B 741 SER B 743 5 3
HELIX 64 64 ARG B 744 ASP B 749 1 6
HELIX 65 65 PRO C 52 ALA C 57 1 6
HELIX 66 66 ASN C 62 LEU C 68 1 7
HELIX 67 67 ASP C 107 HIS C 119 1 13
HELIX 68 68 ALA C 150 SER C 154 5 5
HELIX 69 69 ASP C 210 HIS C 212 5 3
HELIX 70 70 LYS C 213 LYS C 222 1 10
HELIX 71 71 HIS C 236 GLN C 246 1 11
HELIX 72 72 THR C 249 SER C 258 1 10
HELIX 73 73 ASP C 259 ILE C 262 5 4
HELIX 74 74 SER C 265 MET C 269 5 5
HELIX 75 75 VAL C 303 ASP C 314 1 12
HELIX 76 76 ASP C 316 GLY C 329 1 14
HELIX 77 77 GLU C 344 GLU C 346 5 3
HELIX 78 78 ASN C 381 ASN C 386 1 6
HELIX 79 79 ASP C 405 THR C 418 1 14
HELIX 80 80 THR C 418 LEU C 423 1 6
HELIX 81 81 ASN C 427 ARG C 435 5 9
HELIX 82 82 SER C 498 GLY C 502 5 5
HELIX 83 83 TYR C 505 SER C 514 1 10
HELIX 84 84 THR C 516 LYS C 533 1 18
HELIX 85 85 ARG C 536 HIS C 549 1 14
HELIX 86 86 ASP C 551 GLY C 563 1 13
HELIX 87 87 THR C 567 ASN C 572 1 6
HELIX 88 88 ASP C 585 SER C 589 5 5
HELIX 89 89 ARG C 612 LYS C 626 1 15
HELIX 90 90 PRO C 658 VAL C 662 5 5
HELIX 91 91 ASN C 671 ILE C 675 5 5
HELIX 92 92 ASN C 678 HIS C 691 1 14
HELIX 93 93 ASP C 700 ALA C 706 5 7
HELIX 94 94 SER C 727 ALA C 738 1 12
HELIX 95 95 VAL C 741 SER C 743 5 3
HELIX 96 96 ARG C 744 ASP C 749 1 6
HELIX 97 97 PRO D 52 ALA D 57 1 6
HELIX 98 98 ASN D 62 LEU D 68 1 7
HELIX 99 99 ASP D 107 HIS D 119 1 13
HELIX 100 100 ALA D 150 SER D 154 5 5
HELIX 101 101 ASP D 210 HIS D 212 5 3
HELIX 102 102 LYS D 213 LYS D 222 1 10
HELIX 103 103 HIS D 236 GLN D 246 1 11
HELIX 104 104 THR D 249 SER D 258 1 10
HELIX 105 105 ASP D 259 ILE D 262 5 4
HELIX 106 106 SER D 265 MET D 269 5 5
HELIX 107 107 VAL D 303 ASP D 314 1 12
HELIX 108 108 ASP D 316 GLY D 329 1 14
HELIX 109 109 GLU D 344 GLU D 346 5 3
HELIX 110 110 ASN D 381 ASN D 386 1 6
HELIX 111 111 ASP D 405 THR D 418 1 14
HELIX 112 112 THR D 418 LEU D 423 1 6
HELIX 113 113 ASN D 427 ARG D 435 5 9
HELIX 114 114 SER D 498 GLY D 502 5 5
HELIX 115 115 TYR D 505 GLN D 515 1 11
HELIX 116 116 THR D 516 LYS D 533 1 18
HELIX 117 117 ARG D 536 HIS D 549 1 14
HELIX 118 118 ASP D 551 LEU D 562 1 12
HELIX 119 119 THR D 567 ASN D 572 1 6
HELIX 120 120 ASP D 585 SER D 589 5 5
HELIX 121 121 ARG D 612 LYS D 626 1 15
HELIX 122 122 PRO D 658 VAL D 662 5 5
HELIX 123 123 ASN D 671 ILE D 675 5 5
HELIX 124 124 ASN D 678 HIS D 691 1 14
HELIX 125 125 ASP D 700 LYS D 703 5 4
HELIX 126 126 PHE D 704 LYS D 709 1 6
HELIX 127 127 SER D 727 ALA D 738 1 12
HELIX 128 128 VAL D 741 SER D 743 5 3
HELIX 129 129 ARG D 744 ASP D 749 1 6
SHEET 1 A 2 ARG A 72 LYS A 73 0
SHEET 2 A 2 ILE C 453 ASP C 454 1 O ILE C 453 N LYS A 73
SHEET 1 B 4 ARG A 96 ALA A 97 0
SHEET 2 B 4 ARG D 488 VAL D 494 -1 O VAL D 494 N ARG A 96
SHEET 3 B 4 ARG C 488 ARG C 495 -1 N VAL C 489 O GLY D 491
SHEET 4 B 4 LEU B 95 ALA B 97 -1 N ARG B 96 O VAL C 494
SHEET 1 C11 LEU A 400 ASP A 401 0
SHEET 2 C11 PHE A 277 ILE A 280 -1 N ARG A 278 O ASP A 401
SHEET 3 C11 ALA A 286 PRO A 295 -1 O THR A 287 N LEU A 279
SHEET 4 C11 GLU A 333 PRO A 342 -1 O GLU A 335 N LYS A 294
SHEET 5 C11 GLN A 368 ARG A 377 -1 O GLN A 368 N PHE A 338
SHEET 6 C11 GLY A 131 PRO A 140 -1 N HIS A 135 O ARG A 377
SHEET 7 C11 THR A 160 SER A 167 -1 O PHE A 166 N SER A 132
SHEET 8 C11 GLY A 184 THR A 191 -1 O LYS A 188 N PHE A 163
SHEET 9 C11 GLY A 194 ASN A 201 -1 O PHE A 196 N PHE A 189
SHEET 10 C11 GLY A 271 PHE A 272 -1 O PHE A 272 N ASN A 201
SHEET 11 C11 ALA A 286 PRO A 295 -1 O TRP A 293 N GLY A 271
SHEET 1 D 2 ILE A 453 ASP A 454 0
SHEET 2 D 2 ARG C 72 LYS C 73 1 O LYS C 73 N ILE A 453
SHEET 1 E 4 LEU C 95 ALA C 97 0
SHEET 2 E 4 ARG B 488 ARG B 495 -1 N VAL B 494 O ARG C 96
SHEET 3 E 4 ARG A 488 ARG A 495 -1 N VAL A 489 O GLY B 491
SHEET 4 E 4 LEU D 95 ALA D 97 -1 O ARG D 96 N VAL A 494
SHEET 1 F 6 ALA A 652 THR A 653 0
SHEET 2 F 6 HIS A 629 TYR A 634 1 N TYR A 634 O ALA A 652
SHEET 3 F 6 VAL A 602 LEU A 606 1 N ILE A 605 O LYS A 631
SHEET 4 F 6 ALA A 664 VAL A 667 1 O ILE A 666 N ALA A 604
SHEET 5 F 6 ILE A 695 ALA A 698 1 O ALA A 696 N VAL A 667
SHEET 6 F 6 ILE A 718 ALA A 721 1 O VAL A 719 N ILE A 695
SHEET 1 G 2 GLU A 639 THR A 641 0
SHEET 2 G 2 VAL A 647 PRO A 649 -1 O LEU A 648 N VAL A 640
SHEET 1 H 2 ARG B 72 LYS B 73 0
SHEET 2 H 2 ILE D 453 ASP D 454 1 O ILE D 453 N LYS B 73
SHEET 1 I11 LEU B 400 ASP B 401 0
SHEET 2 I11 PHE B 277 ILE B 280 -1 N ARG B 278 O ASP B 401
SHEET 3 I11 ALA B 286 PRO B 295 -1 O THR B 287 N LEU B 279
SHEET 4 I11 GLU B 333 PRO B 342 -1 O GLY B 337 N HIS B 292
SHEET 5 I11 GLN B 368 ARG B 377 -1 O GLN B 368 N PHE B 338
SHEET 6 I11 GLY B 131 PRO B 140 -1 N HIS B 135 O ARG B 377
SHEET 7 I11 THR B 160 SER B 167 -1 O PHE B 166 N SER B 132
SHEET 8 I11 GLY B 184 THR B 191 -1 O ALA B 186 N ARG B 165
SHEET 9 I11 GLY B 194 ASN B 201 -1 O PHE B 196 N PHE B 189
SHEET 10 I11 GLY B 271 PHE B 272 -1 O PHE B 272 N ASN B 201
SHEET 11 I11 ALA B 286 PRO B 295 -1 O TRP B 293 N GLY B 271
SHEET 1 J 2 ILE B 453 ASP B 454 0
SHEET 2 J 2 ARG D 72 LYS D 73 1 O LYS D 73 N ILE B 453
SHEET 1 K 6 ALA B 652 THR B 653 0
SHEET 2 K 6 HIS B 629 TYR B 634 1 N TYR B 634 O ALA B 652
SHEET 3 K 6 VAL B 602 LEU B 606 1 N ILE B 605 O LEU B 633
SHEET 4 K 6 ALA B 664 VAL B 667 1 O ILE B 666 N ALA B 604
SHEET 5 K 6 ILE B 695 ALA B 698 1 O ALA B 696 N VAL B 665
SHEET 6 K 6 ILE B 718 ALA B 721 1 O VAL B 719 N LEU B 697
SHEET 1 L 2 GLU B 639 THR B 641 0
SHEET 2 L 2 VAL B 647 PRO B 649 -1 O LEU B 648 N VAL B 640
SHEET 1 M11 LEU C 400 ASP C 401 0
SHEET 2 M11 PHE C 277 ILE C 280 -1 N ARG C 278 O ASP C 401
SHEET 3 M11 ALA C 286 PRO C 295 -1 O VAL C 289 N PHE C 277
SHEET 4 M11 GLU C 333 PRO C 342 -1 O GLU C 335 N LYS C 294
SHEET 5 M11 VAL C 367 ARG C 377 -1 O VAL C 370 N LEU C 336
SHEET 6 M11 GLY C 131 PRO C 140 -1 N HIS C 135 O ARG C 377
SHEET 7 M11 THR C 160 SER C 167 -1 O THR C 160 N PHE C 138
SHEET 8 M11 GLY C 184 THR C 191 -1 O LYS C 188 N PHE C 163
SHEET 9 M11 GLY C 194 ASN C 201 -1 O PHE C 196 N PHE C 189
SHEET 10 M11 GLY C 271 PHE C 272 -1 O PHE C 272 N ASN C 201
SHEET 11 M11 ALA C 286 PRO C 295 -1 O TRP C 293 N GLY C 271
SHEET 1 N 6 ALA C 652 THR C 653 0
SHEET 2 N 6 HIS C 629 TYR C 634 1 N TYR C 634 O ALA C 652
SHEET 3 N 6 VAL C 602 LEU C 606 1 N ILE C 605 O LYS C 631
SHEET 4 N 6 ALA C 664 VAL C 667 1 O ILE C 666 N ALA C 604
SHEET 5 N 6 ILE C 695 ALA C 698 1 O ALA C 696 N VAL C 667
SHEET 6 N 6 ILE C 718 ALA C 721 1 O VAL C 719 N LEU C 697
SHEET 1 O 2 GLU C 639 THR C 641 0
SHEET 2 O 2 VAL C 647 PRO C 649 -1 O LEU C 648 N VAL C 640
SHEET 1 P11 LEU D 400 ASP D 401 0
SHEET 2 P11 PHE D 277 ILE D 280 -1 N ARG D 278 O ASP D 401
SHEET 3 P11 ALA D 286 PRO D 295 -1 O VAL D 289 N PHE D 277
SHEET 4 P11 GLU D 333 PRO D 342 -1 O GLU D 335 N LYS D 294
SHEET 5 P11 GLN D 368 ARG D 377 -1 O MET D 373 N TYR D 334
SHEET 6 P11 GLY D 131 PRO D 140 -1 N HIS D 135 O ARG D 377
SHEET 7 P11 THR D 160 SER D 167 -1 O VAL D 164 N ALA D 134
SHEET 8 P11 GLY D 184 THR D 191 -1 O LYS D 188 N PHE D 163
SHEET 9 P11 GLY D 194 ASN D 201 -1 O PHE D 196 N PHE D 189
SHEET 10 P11 GLY D 271 PHE D 272 -1 O PHE D 272 N ASN D 201
SHEET 11 P11 ALA D 286 PRO D 295 -1 O TRP D 293 N GLY D 271
SHEET 1 Q 6 ALA D 652 THR D 653 0
SHEET 2 Q 6 HIS D 629 TYR D 634 1 N TYR D 634 O ALA D 652
SHEET 3 Q 6 VAL D 602 LEU D 606 1 N ILE D 605 O LEU D 633
SHEET 4 Q 6 ALA D 664 VAL D 667 1 O ILE D 666 N ALA D 604
SHEET 5 Q 6 ILE D 695 ALA D 698 1 O ALA D 696 N VAL D 667
SHEET 6 Q 6 ILE D 718 ALA D 721 1 O VAL D 719 N LEU D 697
SHEET 1 R 2 GLY D 638 THR D 641 0
SHEET 2 R 2 VAL D 647 ILE D 650 -1 O LEU D 648 N VAL D 640
LINK SG CYS A 274 CBCBHDE A 761 1555 1555 1.75
LINK ND1 HIS A 392 CB TYR A 415 1555 1555 1.63
LINK SG CYS B 274 CBCBHDE B 761 1555 1555 1.70
LINK ND1 HIS B 392 CB TYR B 415 1555 1555 1.59
LINK SG CYS C 274 CBCBHDE C 761 1555 1555 1.62
LINK ND1 HIS C 392 CB TYR C 415 1555 1555 1.60
LINK SG CYS D 274 CBCBHDE D 761 1555 1555 1.75
LINK ND1 HIS D 392 CB TYR D 415 1555 1555 1.55
LINK OH TYR A 415 FE AHDD A 760 1555 1555 1.84
LINK OH TYR A 415 FE BHDE A 761 1555 1555 2.17
LINK FE AHDD A 760 O HOH A3592 1555 1555 2.26
LINK FE BHDE A 761 O HOH A3592 1555 1555 2.05
LINK OH TYR B 415 FE AHDD B 760 1555 1555 1.82
LINK OH TYR B 415 FE BHDE B 761 1555 1555 2.17
LINK FE AHDD B 760 O HOH B3593 1555 1555 2.45
LINK FE BHDE B 761 O HOH B3593 1555 1555 2.06
LINK OH TYR C 415 FE AHDD C 760 1555 1555 1.91
LINK OH TYR C 415 FE BHDE C 761 1555 1555 2.24
LINK FE AHDD C 760 O HOH C3277 1555 1555 2.50
LINK FE BHDE C 761 O HOH C3277 1555 1555 2.15
LINK OH TYR D 415 FE AHDD D 760 1555 1555 1.91
LINK OH TYR D 415 FE BHDE D 761 1555 1555 2.24
LINK FE AHDD D 760 O HOH D3252 1555 1555 2.47
LINK FE BHDE D 761 O HOH D3252 1555 1555 2.13
CISPEP 1 ILE A 229 PRO A 230 0 2.03
CISPEP 2 GLU A 461 PRO A 462 0 -1.30
CISPEP 3 TRP A 469 PRO A 470 0 -4.65
CISPEP 4 ILE B 229 PRO B 230 0 5.06
CISPEP 5 GLU B 461 PRO B 462 0 0.05
CISPEP 6 TRP B 469 PRO B 470 0 -5.52
CISPEP 7 ILE C 229 PRO C 230 0 -2.98
CISPEP 8 GLU C 461 PRO C 462 0 5.30
CISPEP 9 TRP C 469 PRO C 470 0 -3.26
CISPEP 10 ILE D 229 PRO D 230 0 5.53
CISPEP 11 GLU D 461 PRO D 462 0 5.22
CISPEP 12 TRP D 469 PRO D 470 0 -5.23
SITE 1 AC1 24 ARG A 125 VAL A 127 HIS A 128 ARG A 165
SITE 2 AC1 24 GLY A 184 ALA A 186 VAL A 199 GLY A 200
SITE 3 AC1 24 ASN A 201 PHE A 206 PHE A 214 CYS A 274
SITE 4 AC1 24 HIS A 275 PHE A 391 LEU A 407 ARG A 411
SITE 5 AC1 24 SER A 414 TYR A 415 THR A 418 GLN A 419
SITE 6 AC1 24 H2S A 754 HOH A 792 HOH A 848 HOH A3592
SITE 1 AC2 24 ARG B 125 VAL B 127 HIS B 128 ARG B 165
SITE 2 AC2 24 GLY B 184 VAL B 199 GLY B 200 ASN B 201
SITE 3 AC2 24 PHE B 206 PHE B 214 CYS B 274 PHE B 391
SITE 4 AC2 24 LEU B 407 ARG B 411 SER B 414 TYR B 415
SITE 5 AC2 24 THR B 418 GLN B 419 ARG B 422 H2S B 754
SITE 6 AC2 24 HOH B 847 HOH B 895 HOH B 927 HOH B3593
SITE 1 AC3 23 ARG C 125 VAL C 127 HIS C 128 ARG C 165
SITE 2 AC3 23 GLY C 184 VAL C 199 GLY C 200 ASN C 201
SITE 3 AC3 23 PHE C 206 PHE C 214 CYS C 274 PHE C 391
SITE 4 AC3 23 LEU C 407 ARG C 411 SER C 414 TYR C 415
SITE 5 AC3 23 THR C 418 GLN C 419 H2S C 754 HOH C 871
SITE 6 AC3 23 HOH C 929 HOH C 964 HOH C3277
SITE 1 AC4 23 ARG D 125 VAL D 127 HIS D 128 ARG D 165
SITE 2 AC4 23 GLY D 184 VAL D 199 GLY D 200 ASN D 201
SITE 3 AC4 23 PHE D 214 CYS D 274 HIS D 275 PHE D 391
SITE 4 AC4 23 LEU D 407 ARG D 411 SER D 414 TYR D 415
SITE 5 AC4 23 THR D 418 GLN D 419 H2S D 754 HOH D1295
SITE 6 AC4 23 HOH D1353 HOH D1388 HOH D3252
SITE 1 AC5 21 ARG A 125 VAL A 127 HIS A 128 ARG A 165
SITE 2 AC5 21 VAL A 199 GLY A 200 ASN A 201 ALA A 211
SITE 3 AC5 21 PHE A 214 CYS A 274 PHE A 391 LEU A 407
SITE 4 AC5 21 ARG A 411 SER A 414 TYR A 415 THR A 418
SITE 5 AC5 21 GLN A 419 H2S A 754 HOH A 792 HOH A 848
SITE 6 AC5 21 HOH A3592
SITE 1 AC6 24 ARG B 125 VAL B 127 HIS B 128 ARG B 165
SITE 2 AC6 24 GLY B 184 ALA B 186 VAL B 199 GLY B 200
SITE 3 AC6 24 ASN B 201 ALA B 211 PHE B 214 CYS B 274
SITE 4 AC6 24 HIS B 275 PHE B 391 LEU B 407 ARG B 411
SITE 5 AC6 24 SER B 414 TYR B 415 THR B 418 GLN B 419
SITE 6 AC6 24 H2S B 754 HOH B 847 HOH B 895 HOH B3593
SITE 1 AC7 23 ARG C 125 VAL C 127 HIS C 128 ARG C 165
SITE 2 AC7 23 VAL C 199 GLY C 200 ASN C 201 ALA C 211
SITE 3 AC7 23 PHE C 214 CYS C 274 HIS C 275 PHE C 391
SITE 4 AC7 23 LEU C 407 ARG C 411 SER C 414 TYR C 415
SITE 5 AC7 23 THR C 418 GLN C 419 H2S C 754 HOH C 871
SITE 6 AC7 23 HOH C 929 HOH C1263 HOH C3277
SITE 1 AC8 22 ARG D 125 VAL D 127 HIS D 128 ARG D 165
SITE 2 AC8 22 GLY D 184 VAL D 199 GLY D 200 ASN D 201
SITE 3 AC8 22 ALA D 211 PHE D 214 CYS D 274 PHE D 391
SITE 4 AC8 22 LEU D 407 ARG D 411 SER D 414 TYR D 415
SITE 5 AC8 22 THR D 418 GLN D 419 H2S D 754 HOH D1295
SITE 6 AC8 22 HOH D1353 HOH D3252
SITE 1 AC9 4 CYS A 274 HDD A 760 HDE A 761 HOH A3466
SITE 1 BC1 4 PHE B 206 CYS B 274 HDD B 760 HDE B 761
SITE 1 BC2 5 PHE C 206 CYS C 274 HDD C 760 HDE C 761
SITE 2 BC2 5 HOH C3217
SITE 1 BC3 4 PHE D 206 CYS D 274 HDD D 760 HDE D 761
CRYST1 93.507 133.031 122.646 90.00 109.39 90.00 P 1 21 1 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 0.010694 0.000000 0.003764 0.00000
SCALE2 0.000000 0.007517 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008644 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
