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Chemical substance (7) PDB-CCD (7) Chemical reaction (1) KEGG ENZYME (1) Protein sequence (4) UniProt (1) SWISS-PROT (1) PDBSTR (2) Protein domain (7) InterPro (6) PROSITE (1) Literature (1) PubMed (1) All databases (20)
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HEADER OXIDOREDUCTASE 21-JUN-10 3NLI
TITLE STRUCTURE OF ENDOTHELIAL NITRIC OXIDE SYNTHASE N368D MUTANT HEME
TITLE 2 DOMAIN COMPLEXED WITH 6-{{(3'R,4'R)-3'-[2"-(3'''-
TITLE 3 FLUOROPHENETHYLAMINO)ETHOXY]PYRROLIDIN-4'-YL}METHYL}-4-METHYLPYRIDIN-
TITLE 4 2-AMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, ENDOTHELIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 39-482;
COMPND 5 SYNONYM: ENDOTHELIAL NOS, ENOS, EC-NOS, NOS TYPE III, NOSIII,
COMPND 6 CONSTITUTIVE NOS, CNOS;
COMPND 7 EC: 1.14.13.39;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS NITRIC OXIDE SYNTHASE, HEME ENZYME, SUBSTRATE INHIBITOR,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.L.DELKER,H.LI,T.L.POULOS
REVDAT 4 21-FEB-24 3NLI 1 REMARK SEQADV LINK
REVDAT 3 17-JUL-19 3NLI 1 REMARK
REVDAT 2 24-NOV-10 3NLI 1 JRNL
REVDAT 1 03-NOV-10 3NLI 0
JRNL AUTH H.JI,S.L.DELKER,H.LI,P.MARTASEK,L.J.ROMAN,T.L.POULOS,
JRNL AUTH 2 R.B.SILVERMAN
JRNL TITL EXPLORATION OF THE ACTIVE SITE OF NEURONAL NITRIC OXIDE
JRNL TITL 2 SYNTHASE BY THE DESIGN AND SYNTHESIS OF PYRROLIDINOMETHYL
JRNL TITL 3 2-AMINOPYRIDINE DERIVATIVES.
JRNL REF J.MED.CHEM. V. 53 7804 2010
JRNL REFN ISSN 0022-2623
JRNL PMID 20958055
JRNL DOI 10.1021/JM100947X
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0089
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 64937
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3409
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) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4626
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 242
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6415
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 201
REMARK 3 SOLVENT ATOMS : 626
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.137
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.308
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6822 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9316 ; 1.313 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 806 ; 5.581 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 320 ;35.086 ;23.375
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1043 ;15.270 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;19.708 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 974 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5318 ; 0.005 ; 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): 4042 ; 0.511 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6525 ; 0.998 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2780 ; 1.650 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2791 ; 2.702 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
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 67 A 482
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9270 10.2680 32.1980
REMARK 3 T TENSOR
REMARK 3 T11: 0.0395 T22: 0.0448
REMARK 3 T33: 0.0294 T12: -0.0280
REMARK 3 T13: 0.0021 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.6274 L22: 0.9615
REMARK 3 L33: 1.2372 L12: -0.2217
REMARK 3 L13: -0.3141 L23: 0.1578
REMARK 3 S TENSOR
REMARK 3 S11: 0.0208 S12: 0.0137 S13: 0.0255
REMARK 3 S21: -0.1009 S22: 0.0237 S23: -0.1347
REMARK 3 S31: -0.0493 S32: 0.1088 S33: -0.0445
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 69 B 482
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9480 6.2000 67.8040
REMARK 3 T TENSOR
REMARK 3 T11: 0.0145 T22: 0.0524
REMARK 3 T33: 0.0228 T12: -0.0104
REMARK 3 T13: -0.0011 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.6795 L22: 0.8305
REMARK 3 L33: 1.4322 L12: -0.1445
REMARK 3 L13: 0.1617 L23: -0.5126
REMARK 3 S TENSOR
REMARK 3 S11: 0.0217 S12: -0.1021 S13: -0.0707
REMARK 3 S21: 0.0567 S22: 0.0478 S23: 0.0369
REMARK 3 S31: 0.0186 S32: -0.0503 S33: -0.0695
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3NLI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059978.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68424
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : 0.07700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.73000
REMARK 200 R SYM FOR SHELL (I) : 0.73000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.860
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 9-12% PEG 3350, 0.2M MAGNESIUM
REMARK 280 ACETATE, 0.1M SODIUM CACODYLATE, 0.005M TCEP-HCL, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 278K
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 28.97950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.31400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.39850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.31400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.97950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.39850
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -128.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 39
REMARK 465 ARG A 40
REMARK 465 ALA A 41
REMARK 465 PRO A 42
REMARK 465 ALA A 43
REMARK 465 PRO A 44
REMARK 465 ALA A 45
REMARK 465 THR A 46
REMARK 465 PRO A 47
REMARK 465 HIS A 48
REMARK 465 ALA A 49
REMARK 465 PRO A 50
REMARK 465 ASP A 51
REMARK 465 HIS A 52
REMARK 465 SER A 53
REMARK 465 PRO A 54
REMARK 465 ALA A 55
REMARK 465 PRO A 56
REMARK 465 ASN A 57
REMARK 465 SER A 58
REMARK 465 PRO A 59
REMARK 465 THR A 60
REMARK 465 LEU A 61
REMARK 465 THR A 62
REMARK 465 ARG A 63
REMARK 465 PRO A 64
REMARK 465 PRO A 65
REMARK 465 GLU A 66
REMARK 465 LYS A 110
REMARK 465 LEU A 111
REMARK 465 GLN A 112
REMARK 465 THR A 113
REMARK 465 ARG A 114
REMARK 465 PRO A 115
REMARK 465 SER A 116
REMARK 465 PRO A 117
REMARK 465 GLY A 118
REMARK 465 PRO A 119
REMARK 465 PRO A 120
REMARK 465 PRO A 121
REMARK 465 SER B 39
REMARK 465 ARG B 40
REMARK 465 ALA B 41
REMARK 465 PRO B 42
REMARK 465 ALA B 43
REMARK 465 PRO B 44
REMARK 465 ALA B 45
REMARK 465 THR B 46
REMARK 465 PRO B 47
REMARK 465 HIS B 48
REMARK 465 ALA B 49
REMARK 465 PRO B 50
REMARK 465 ASP B 51
REMARK 465 HIS B 52
REMARK 465 SER B 53
REMARK 465 PRO B 54
REMARK 465 ALA B 55
REMARK 465 PRO B 56
REMARK 465 ASN B 57
REMARK 465 SER B 58
REMARK 465 PRO B 59
REMARK 465 THR B 60
REMARK 465 LEU B 61
REMARK 465 THR B 62
REMARK 465 ARG B 63
REMARK 465 PRO B 64
REMARK 465 PRO B 65
REMARK 465 GLU B 66
REMARK 465 GLY B 67
REMARK 465 PRO B 68
REMARK 465 LYS B 110
REMARK 465 LEU B 111
REMARK 465 GLN B 112
REMARK 465 THR B 113
REMARK 465 ARG B 114
REMARK 465 PRO B 115
REMARK 465 SER B 116
REMARK 465 PRO B 117
REMARK 465 GLY B 118
REMARK 465 PRO B 119
REMARK 465 PRO B 120
REMARK 465 PRO B 121
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 ND1 HIS A 410 O HOH A 1267 2.07
REMARK 500 O LEU B 107 O HOH B 1216 2.17
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 ASN A 285 31.48 -144.25
REMARK 500 ALA A 353 68.84 -155.95
REMARK 500 ARG A 374 -134.58 -118.06
REMARK 500 ASN B 285 22.97 -145.56
REMARK 500 ALA B 353 67.59 -157.89
REMARK 500 ARG B 374 -135.30 -120.02
REMARK 500 ASP B 480 128.71 -39.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CAD A 950
REMARK 610 CAD B 950
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 ZN A 900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 96 SG
REMARK 620 2 CYS A 101 SG 109.5
REMARK 620 3 CYS B 96 SG 117.9 106.1
REMARK 620 4 CYS B 101 SG 106.6 106.6 109.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 186 SG
REMARK 620 2 HEM A 500 NA 102.0
REMARK 620 3 HEM A 500 NB 98.5 86.3
REMARK 620 4 HEM A 500 NC 98.0 159.8 87.8
REMARK 620 5 HEM A 500 ND 102.2 90.3 159.2 88.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 186 SG
REMARK 620 2 HEM B 500 NA 101.5
REMARK 620 3 HEM B 500 NB 99.9 87.3
REMARK 620 4 HEM B 500 NC 98.0 160.5 88.1
REMARK 620 5 HEM B 500 ND 101.4 88.5 158.7 89.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 880
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JRR A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAD A 950
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 880
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JRR B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAD B 950
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NLD RELATED DB: PDB
REMARK 900 RELATED ID: 3NLE RELATED DB: PDB
REMARK 900 RELATED ID: 3NLF RELATED DB: PDB
REMARK 900 RELATED ID: 3NLG RELATED DB: PDB
REMARK 900 RELATED ID: 3NLH RELATED DB: PDB
REMARK 900 RELATED ID: 3NLJ RELATED DB: PDB
REMARK 900 RELATED ID: 3NLK RELATED DB: PDB
REMARK 900 RELATED ID: 3NLM RELATED DB: PDB
REMARK 900 RELATED ID: 3NLN RELATED DB: PDB
REMARK 900 RELATED ID: 3NLO RELATED DB: PDB
REMARK 900 RELATED ID: 3NLP RELATED DB: PDB
REMARK 900 RELATED ID: 3NLQ RELATED DB: PDB
REMARK 900 RELATED ID: 3NLR RELATED DB: PDB
REMARK 900 RELATED ID: 3NLT RELATED DB: PDB
REMARK 900 RELATED ID: 3NLU RELATED DB: PDB
REMARK 900 RELATED ID: 3NLV RELATED DB: PDB
REMARK 900 RELATED ID: 3NLW RELATED DB: PDB
REMARK 900 RELATED ID: 3NLX RELATED DB: PDB
REMARK 900 RELATED ID: 3NLY RELATED DB: PDB
REMARK 900 RELATED ID: 3NLZ RELATED DB: PDB
REMARK 900 RELATED ID: 3NM0 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CYS TO ARG CONFLICT IN UNP ENTRY P29473
DBREF 3NLI A 39 482 UNP P29473 NOS3_BOVIN 39 482
DBREF 3NLI B 39 482 UNP P29473 NOS3_BOVIN 39 482
SEQADV 3NLI ARG A 100 UNP P29473 CYS 100 SEE REMARK 999
SEQADV 3NLI ASP A 368 UNP P29473 ASN 368 ENGINEERED MUTATION
SEQADV 3NLI ARG B 100 UNP P29473 CYS 100 SEE REMARK 999
SEQADV 3NLI ASP B 368 UNP P29473 ASN 368 ENGINEERED MUTATION
SEQRES 1 A 444 SER ARG ALA PRO ALA PRO ALA THR PRO HIS ALA PRO ASP
SEQRES 2 A 444 HIS SER PRO ALA PRO ASN SER PRO THR LEU THR ARG PRO
SEQRES 3 A 444 PRO GLU GLY PRO LYS PHE PRO ARG VAL LYS ASN TRP GLU
SEQRES 4 A 444 LEU GLY SER ILE THR TYR ASP THR LEU CYS ALA GLN SER
SEQRES 5 A 444 GLN GLN ASP GLY PRO CYS THR PRO ARG ARG CYS LEU GLY
SEQRES 6 A 444 SER LEU VAL LEU PRO ARG LYS LEU GLN THR ARG PRO SER
SEQRES 7 A 444 PRO GLY PRO PRO PRO ALA GLU GLN LEU LEU SER GLN ALA
SEQRES 8 A 444 ARG ASP PHE ILE ASN GLN TYR TYR SER SER ILE LYS ARG
SEQRES 9 A 444 SER GLY SER GLN ALA HIS GLU GLU ARG LEU GLN GLU VAL
SEQRES 10 A 444 GLU ALA GLU VAL ALA SER THR GLY THR TYR HIS LEU ARG
SEQRES 11 A 444 GLU SER GLU LEU VAL PHE GLY ALA LYS GLN ALA TRP ARG
SEQRES 12 A 444 ASN ALA PRO ARG CYS VAL GLY ARG ILE GLN TRP GLY LYS
SEQRES 13 A 444 LEU GLN VAL PHE ASP ALA ARG ASP CYS SER SER ALA GLN
SEQRES 14 A 444 GLU MET PHE THR TYR ILE CYS ASN HIS ILE LYS TYR ALA
SEQRES 15 A 444 THR ASN ARG GLY ASN LEU ARG SER ALA ILE THR VAL PHE
SEQRES 16 A 444 PRO GLN ARG ALA PRO GLY ARG GLY ASP PHE ARG ILE TRP
SEQRES 17 A 444 ASN SER GLN LEU VAL ARG TYR ALA GLY TYR ARG GLN GLN
SEQRES 18 A 444 ASP GLY SER VAL ARG GLY ASP PRO ALA ASN VAL GLU ILE
SEQRES 19 A 444 THR GLU LEU CYS ILE GLN HIS GLY TRP THR PRO GLY ASN
SEQRES 20 A 444 GLY ARG PHE ASP VAL LEU PRO LEU LEU LEU GLN ALA PRO
SEQRES 21 A 444 ASP GLU ALA PRO GLU LEU PHE VAL LEU PRO PRO GLU LEU
SEQRES 22 A 444 VAL LEU GLU VAL PRO LEU GLU HIS PRO THR LEU GLU TRP
SEQRES 23 A 444 PHE ALA ALA LEU GLY LEU ARG TRP TYR ALA LEU PRO ALA
SEQRES 24 A 444 VAL SER ASN MET LEU LEU GLU ILE GLY GLY LEU GLU PHE
SEQRES 25 A 444 SER ALA ALA PRO PHE SER GLY TRP TYR MET SER THR GLU
SEQRES 26 A 444 ILE GLY THR ARG ASP LEU CYS ASP PRO HIS ARG TYR ASN
SEQRES 27 A 444 ILE LEU GLU ASP VAL ALA VAL CYS MET ASP LEU ASP THR
SEQRES 28 A 444 ARG THR THR SER SER LEU TRP LYS ASP LYS ALA ALA VAL
SEQRES 29 A 444 GLU ILE ASN LEU ALA VAL LEU HIS SER PHE GLN LEU ALA
SEQRES 30 A 444 LYS VAL THR ILE VAL ASP HIS HIS ALA ALA THR VAL SER
SEQRES 31 A 444 PHE MET LYS HIS LEU ASP ASN GLU GLN LYS ALA ARG GLY
SEQRES 32 A 444 GLY CYS PRO ALA ASP TRP ALA TRP ILE VAL PRO PRO ILE
SEQRES 33 A 444 SER GLY SER LEU THR PRO VAL PHE HIS GLN GLU MET VAL
SEQRES 34 A 444 ASN TYR ILE LEU SER PRO ALA PHE ARG TYR GLN PRO ASP
SEQRES 35 A 444 PRO TRP
SEQRES 1 B 444 SER ARG ALA PRO ALA PRO ALA THR PRO HIS ALA PRO ASP
SEQRES 2 B 444 HIS SER PRO ALA PRO ASN SER PRO THR LEU THR ARG PRO
SEQRES 3 B 444 PRO GLU GLY PRO LYS PHE PRO ARG VAL LYS ASN TRP GLU
SEQRES 4 B 444 LEU GLY SER ILE THR TYR ASP THR LEU CYS ALA GLN SER
SEQRES 5 B 444 GLN GLN ASP GLY PRO CYS THR PRO ARG ARG CYS LEU GLY
SEQRES 6 B 444 SER LEU VAL LEU PRO ARG LYS LEU GLN THR ARG PRO SER
SEQRES 7 B 444 PRO GLY PRO PRO PRO ALA GLU GLN LEU LEU SER GLN ALA
SEQRES 8 B 444 ARG ASP PHE ILE ASN GLN TYR TYR SER SER ILE LYS ARG
SEQRES 9 B 444 SER GLY SER GLN ALA HIS GLU GLU ARG LEU GLN GLU VAL
SEQRES 10 B 444 GLU ALA GLU VAL ALA SER THR GLY THR TYR HIS LEU ARG
SEQRES 11 B 444 GLU SER GLU LEU VAL PHE GLY ALA LYS GLN ALA TRP ARG
SEQRES 12 B 444 ASN ALA PRO ARG CYS VAL GLY ARG ILE GLN TRP GLY LYS
SEQRES 13 B 444 LEU GLN VAL PHE ASP ALA ARG ASP CYS SER SER ALA GLN
SEQRES 14 B 444 GLU MET PHE THR TYR ILE CYS ASN HIS ILE LYS TYR ALA
SEQRES 15 B 444 THR ASN ARG GLY ASN LEU ARG SER ALA ILE THR VAL PHE
SEQRES 16 B 444 PRO GLN ARG ALA PRO GLY ARG GLY ASP PHE ARG ILE TRP
SEQRES 17 B 444 ASN SER GLN LEU VAL ARG TYR ALA GLY TYR ARG GLN GLN
SEQRES 18 B 444 ASP GLY SER VAL ARG GLY ASP PRO ALA ASN VAL GLU ILE
SEQRES 19 B 444 THR GLU LEU CYS ILE GLN HIS GLY TRP THR PRO GLY ASN
SEQRES 20 B 444 GLY ARG PHE ASP VAL LEU PRO LEU LEU LEU GLN ALA PRO
SEQRES 21 B 444 ASP GLU ALA PRO GLU LEU PHE VAL LEU PRO PRO GLU LEU
SEQRES 22 B 444 VAL LEU GLU VAL PRO LEU GLU HIS PRO THR LEU GLU TRP
SEQRES 23 B 444 PHE ALA ALA LEU GLY LEU ARG TRP TYR ALA LEU PRO ALA
SEQRES 24 B 444 VAL SER ASN MET LEU LEU GLU ILE GLY GLY LEU GLU PHE
SEQRES 25 B 444 SER ALA ALA PRO PHE SER GLY TRP TYR MET SER THR GLU
SEQRES 26 B 444 ILE GLY THR ARG ASP LEU CYS ASP PRO HIS ARG TYR ASN
SEQRES 27 B 444 ILE LEU GLU ASP VAL ALA VAL CYS MET ASP LEU ASP THR
SEQRES 28 B 444 ARG THR THR SER SER LEU TRP LYS ASP LYS ALA ALA VAL
SEQRES 29 B 444 GLU ILE ASN LEU ALA VAL LEU HIS SER PHE GLN LEU ALA
SEQRES 30 B 444 LYS VAL THR ILE VAL ASP HIS HIS ALA ALA THR VAL SER
SEQRES 31 B 444 PHE MET LYS HIS LEU ASP ASN GLU GLN LYS ALA ARG GLY
SEQRES 32 B 444 GLY CYS PRO ALA ASP TRP ALA TRP ILE VAL PRO PRO ILE
SEQRES 33 B 444 SER GLY SER LEU THR PRO VAL PHE HIS GLN GLU MET VAL
SEQRES 34 B 444 ASN TYR ILE LEU SER PRO ALA PHE ARG TYR GLN PRO ASP
SEQRES 35 B 444 PRO TRP
HET HEM A 500 43
HET H4B A 600 17
HET ACT A 860 4
HET GOL A 880 6
HET JRR A 800 27
HET CAD A 950 3
HET ZN A 900 1
HET HEM B 500 43
HET H4B B 600 17
HET ACT B 860 4
HET GOL B 880 6
HET JRR B 800 27
HET CAD B 950 3
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
HETNAM JRR 6-{[(3R,4R)-4-(2-{[2-(3-FLUOROPHENYL)
HETNAM 2 JRR ETHYL]AMINO}ETHOXY)PYRROLIDIN-3-YL]METHYL}-4-
HETNAM 3 JRR METHYLPYRIDIN-2-AMINE
HETNAM CAD CACODYLIC ACID
HETNAM ZN ZINC ION
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN CAD HYDROXYDIMETHYLARSINE OXIDE
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 H4B 2(C9 H15 N5 O3)
FORMUL 5 ACT 2(C2 H3 O2 1-)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 7 JRR 2(C21 H29 F N4 O)
FORMUL 8 CAD 2(C2 H7 AS O2)
FORMUL 9 ZN ZN 2+
FORMUL 16 HOH *626(H2 O)
HELIX 1 1 THR A 85 SER A 90 5 6
HELIX 2 2 ALA A 122 ILE A 140 1 19
HELIX 3 3 SER A 145 GLY A 163 1 19
HELIX 4 4 ARG A 168 ALA A 183 1 16
HELIX 5 5 GLY A 188 TRP A 192 5 5
HELIX 6 6 SER A 205 ASN A 222 1 18
HELIX 7 7 ARG A 223 ASN A 225 5 3
HELIX 8 8 ASN A 269 HIS A 279 1 11
HELIX 9 9 PRO A 308 VAL A 312 5 5
HELIX 10 10 PHE A 325 GLY A 329 5 5
HELIX 11 11 SER A 361 THR A 366 1 6
HELIX 12 12 THR A 366 ASP A 371 1 6
HELIX 13 13 ILE A 377 MET A 385 1 9
HELIX 14 14 THR A 391 SER A 394 5 4
HELIX 15 15 LEU A 395 ALA A 415 1 21
HELIX 16 16 ASP A 421 GLY A 441 1 21
HELIX 17 17 ASP A 446 VAL A 451 1 6
HELIX 18 18 SER A 455 GLN A 464 5 10
HELIX 19 19 THR B 85 SER B 90 5 6
HELIX 20 20 ALA B 122 ILE B 140 1 19
HELIX 21 21 SER B 145 GLY B 163 1 19
HELIX 22 22 ARG B 168 ALA B 183 1 16
HELIX 23 23 GLY B 188 TRP B 192 5 5
HELIX 24 24 SER B 205 ASN B 222 1 18
HELIX 25 25 ARG B 223 ASN B 225 5 3
HELIX 26 26 ASN B 269 HIS B 279 1 11
HELIX 27 27 PRO B 308 VAL B 312 5 5
HELIX 28 28 LEU B 322 GLY B 329 5 8
HELIX 29 29 SER B 361 THR B 366 1 6
HELIX 30 30 THR B 366 ASP B 371 1 6
HELIX 31 31 ILE B 377 MET B 385 1 9
HELIX 32 32 THR B 391 SER B 394 5 4
HELIX 33 33 LEU B 395 ALA B 415 1 21
HELIX 34 34 ASP B 421 GLY B 441 1 21
HELIX 35 35 ASP B 446 VAL B 451 1 6
HELIX 36 36 SER B 455 GLN B 464 5 10
SHEET 1 A 2 ARG A 72 LYS A 74 0
SHEET 2 A 2 ILE A 81 TYR A 83 -1 O THR A 82 N VAL A 73
SHEET 1 B 4 GLN A 196 ASP A 199 0
SHEET 2 B 4 ALA A 229 VAL A 232 1 O ILE A 230 N PHE A 198
SHEET 3 B 4 PHE A 355 SER A 356 -1 O SER A 356 N ALA A 229
SHEET 4 B 4 ALA A 337 VAL A 338 -1 N VAL A 338 O PHE A 355
SHEET 1 C 3 ARG A 244 ILE A 245 0
SHEET 2 C 3 LEU A 293 GLN A 296 -1 O GLN A 296 N ARG A 244
SHEET 3 C 3 GLU A 303 PHE A 305 -1 O PHE A 305 N LEU A 293
SHEET 1 D 2 GLY A 255 ARG A 257 0
SHEET 2 D 2 VAL A 263 GLY A 265 -1 O ARG A 264 N TYR A 256
SHEET 1 E 2 GLU A 314 PRO A 316 0
SHEET 2 E 2 ARG A 331 TYR A 333 -1 O TRP A 332 N VAL A 315
SHEET 1 F 3 LEU A 348 PHE A 350 0
SHEET 2 F 3 MET A 341 ILE A 345 -1 N LEU A 343 O PHE A 350
SHEET 3 F 3 ALA A 474 TYR A 477 -1 O ARG A 476 N LEU A 342
SHEET 1 G 2 TYR A 359 MET A 360 0
SHEET 2 G 2 ILE A 419 VAL A 420 1 O VAL A 420 N TYR A 359
SHEET 1 H 2 ARG B 72 LYS B 74 0
SHEET 2 H 2 ILE B 81 TYR B 83 -1 O THR B 82 N VAL B 73
SHEET 1 I 4 GLN B 196 ASP B 199 0
SHEET 2 I 4 ALA B 229 VAL B 232 1 O ILE B 230 N PHE B 198
SHEET 3 I 4 PHE B 355 SER B 356 -1 O SER B 356 N ALA B 229
SHEET 4 I 4 ALA B 337 VAL B 338 -1 N VAL B 338 O PHE B 355
SHEET 1 J 3 ARG B 244 ILE B 245 0
SHEET 2 J 3 LEU B 293 GLN B 296 -1 O GLN B 296 N ARG B 244
SHEET 3 J 3 GLU B 303 PHE B 305 -1 O PHE B 305 N LEU B 293
SHEET 1 K 2 GLY B 255 ARG B 257 0
SHEET 2 K 2 VAL B 263 GLY B 265 -1 O ARG B 264 N TYR B 256
SHEET 1 L 2 GLU B 314 PRO B 316 0
SHEET 2 L 2 ARG B 331 TYR B 333 -1 O TRP B 332 N VAL B 315
SHEET 1 M 3 LEU B 348 PHE B 350 0
SHEET 2 M 3 MET B 341 ILE B 345 -1 N LEU B 343 O PHE B 350
SHEET 3 M 3 ALA B 474 TYR B 477 -1 O ARG B 476 N LEU B 342
SHEET 1 N 2 TYR B 359 MET B 360 0
SHEET 2 N 2 ILE B 419 VAL B 420 1 O VAL B 420 N TYR B 359
LINK SG CYS A 96 ZN ZN A 900 1555 1555 2.30
LINK SG CYS A 101 ZN ZN A 900 1555 1555 2.32
LINK SG CYS A 186 FE HEM A 500 1555 1555 2.39
LINK ZN ZN A 900 SG CYS B 96 1555 1555 2.36
LINK ZN ZN A 900 SG CYS B 101 1555 1555 2.34
LINK SG CYS B 186 FE HEM B 500 1555 1555 2.45
CISPEP 1 SER A 472 PRO A 473 0 2.58
CISPEP 2 SER B 472 PRO B 473 0 2.83
SITE 1 AC1 14 TRP A 180 CYS A 186 SER A 228 PHE A 355
SITE 2 AC1 14 SER A 356 TRP A 358 TRP A 449 PHE A 475
SITE 3 AC1 14 H4B A 600 JRR A 800 HOH A1089 HOH A1100
SITE 4 AC1 14 HOH A1193 HOH A1298
SITE 1 AC2 15 SER A 104 ARG A 367 ALA A 448 TRP A 449
SITE 2 AC2 15 HEM A 500 JRR A 800 GOL A 880 HOH A1048
SITE 3 AC2 15 HOH A1113 TRP B 447 PHE B 462 HIS B 463
SITE 4 AC2 15 GLN B 464 GLU B 465 HOH B1269
SITE 1 AC3 4 TRP A 358 SER A 428 HOH A1166 HOH A1178
SITE 1 AC4 7 ARG A 367 HIS A 373 H4B A 600 JRR A 800
SITE 2 AC4 7 HOH A1151 HOH A1239 HOH B1269
SITE 1 AC5 17 VAL A 106 ARG A 185 GLN A 249 PRO A 336
SITE 2 AC5 17 PHE A 355 SER A 356 GLY A 357 TRP A 358
SITE 3 AC5 17 GLU A 363 TRP A 449 TYR A 477 HEM A 500
SITE 4 AC5 17 H4B A 600 GOL A 880 HOH A1036 HOH A1151
SITE 5 AC5 17 HOH A1193
SITE 1 AC6 3 CYS A 384 GLN A 437 ARG A 440
SITE 1 AC7 4 CYS A 96 CYS A 101 CYS B 96 CYS B 101
SITE 1 AC8 14 TRP B 180 ARG B 185 CYS B 186 SER B 228
SITE 2 AC8 14 PHE B 355 SER B 356 TRP B 358 GLU B 363
SITE 3 AC8 14 PHE B 475 H4B B 600 JRR B 800 HOH B1062
SITE 4 AC8 14 HOH B1268 HOH B1276
SITE 1 AC9 13 TRP A 447 PHE A 462 HIS A 463 SER B 104
SITE 2 AC9 13 ARG B 367 ALA B 448 TRP B 449 HEM B 500
SITE 3 AC9 13 JRR B 800 GOL B 880 HOH B1044 HOH B1108
SITE 4 AC9 13 HOH B1151
SITE 1 BC1 6 TRP B 358 VAL B 420 SER B 428 HOH B1226
SITE 2 BC1 6 HOH B1271 HOH B1277
SITE 1 BC2 6 VAL B 106 ARG B 367 HIS B 373 H4B B 600
SITE 2 BC2 6 HOH B1108 HOH B1273
SITE 1 BC3 17 TRP A 76 VAL B 106 LEU B 107 ARG B 185
SITE 2 BC3 17 GLN B 249 PRO B 336 PHE B 355 SER B 356
SITE 3 BC3 17 GLY B 357 TRP B 358 GLU B 363 TRP B 449
SITE 4 BC3 17 TYR B 477 HEM B 500 H4B B 600 HOH B1181
SITE 5 BC3 17 HOH B1268
SITE 1 BC4 3 TYR B 83 TRP B 324 CYS B 384
CRYST1 57.959 106.797 156.628 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 0.017254 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009364 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006385 0.00000
(ATOM LINES ARE NOT SHOWN.)
END