HEADER OXIDOREDUCTASE 14-JAN-99 8NSE
TITLE BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE, NNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (NITRIC OXIDE SYNTHASE);
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HEME DOMAIN;
COMPND 5 SYNONYM: NOS, ENOS;
COMPND 6 EC: 1.14.13.39;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 CELL: ENDOTHELIAL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS NITRIC OXIDE SYNTHASE, HEME PROTEIN, TETRAHYDROBIOPTERIN,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.S.RAMAN,H.LI,P.MARTASEK,B.S.S.MASTERS,T.L.POULOS
REVDAT 5 15-NOV-23 8NSE 1 REMARK LINK ATOM
REVDAT 4 13-JUL-11 8NSE 1 VERSN
REVDAT 3 24-FEB-09 8NSE 1 VERSN
REVDAT 2 01-APR-03 8NSE 1 JRNL
REVDAT 1 21-NOV-01 8NSE 0
JRNL AUTH C.S.RAMAN,H.LI,P.MARTASEK,G.SOUTHAN,B.S.MASTERS,T.L.POULOS
JRNL TITL CRYSTAL STRUCTURE OF NITRIC OXIDE SYNTHASE BOUND TO NITRO
JRNL TITL 2 INDAZOLE REVEALS A NOVEL INACTIVATION MECHANISM.
JRNL REF BIOCHEMISTRY V. 40 13448 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11695891
JRNL DOI 10.1021/BI010957U
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.S.RAMAN,H.LI,P.MARTASEK,V.KRAL,B.S.S.MASTERS,T.L.POULOS
REMARK 1 TITL CRYSTAL STRUCTURE OF CONSTITUTIVE ENDOTHELIAL NITRIC OXIDE:
REMARK 1 TITL 2 A PARADIGM FOR PTERIN FUNCTION INVOLVING A NOVEL METAL
REMARK 1 TITL 3 CENTER
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 95 939 1998
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.R.CRANE,A.S.ARVAI,D.K.GHOSH,C.WU,E.D.GETZOFF,D.J.STUEHR,
REMARK 1 AUTH 2 J.A.TAINER
REMARK 1 TITL STRUCTURE OF NITRIC OXIDE SYNTHASE OXYGENASE DIMER WITH
REMARK 1 TITL 2 PTERIN AND SUBSTRATE
REMARK 1 REF SCIENCE V. 279 2121 1998
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH B.R.CRANE,A.S.ARVAI,R.GACHHUI,C.WU,D.K.GHOSH,E.D.GETZOFF,
REMARK 1 AUTH 2 D.J.STUEHR,J.A.TAINER
REMARK 1 TITL THE STRUCTURE OF NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN AND
REMARK 1 TITL 2 INHIBITOR COMPLEX
REMARK 1 REF SCIENCE V. 278 425 1997
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2754114.140
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.4
REMARK 3 NUMBER OF REFLECTIONS : 39054
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 SET) : 0.227
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1920
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 36.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1618
REMARK 3 BIN R VALUE (WORKING SET) : 0.3340
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 73
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6593
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 169
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 29.23000
REMARK 3 B22 (A**2) : -12.31000
REMARK 3 B33 (A**2) : -16.91000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.45
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.50
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.060
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 42.56
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8NSE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000007231.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-98
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 : CHESS
REMARK 200 BEAMLINE : F2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : YES
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44385
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.21600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5
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 29.15500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.30500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.89000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.30500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.15500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.89000
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: 11630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.0 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 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 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 LYS A 69 38.17 -89.46
REMARK 500 ARG A 109 88.33 -63.90
REMARK 500 LYS A 110 -66.74 -136.60
REMARK 500 GLN A 112 130.92 -30.60
REMARK 500 THR A 113 79.15 -113.88
REMARK 500 PRO A 115 96.22 -38.49
REMARK 500 THR A 164 -149.98 -134.08
REMARK 500 TYR A 165 167.21 179.71
REMARK 500 ALA A 183 106.09 -58.85
REMARK 500 ALA A 200 30.30 -150.25
REMARK 500 CYS A 203 135.33 -37.90
REMARK 500 ASP A 260 9.60 -62.76
REMARK 500 SER A 262 -169.60 -68.24
REMARK 500 HIS A 279 42.46 -96.99
REMARK 500 ASN A 285 35.05 -156.17
REMARK 500 PHE A 288 58.86 -112.79
REMARK 500 PRO A 309 -30.49 -38.67
REMARK 500 ALA A 353 65.29 -158.82
REMARK 500 SER A 361 -55.53 -24.41
REMARK 500 ARG A 374 -134.76 -125.72
REMARK 500 THR A 391 112.59 -160.59
REMARK 500 SER A 393 -1.01 -59.91
REMARK 500 PRO A 473 166.32 -43.69
REMARK 500 PRO B 108 -102.79 -100.48
REMARK 500 ARG B 109 -10.49 127.42
REMARK 500 PRO B 115 -169.57 -56.84
REMARK 500 PRO B 121 118.39 -30.86
REMARK 500 ARG B 142 32.04 -89.61
REMARK 500 SER B 145 -170.10 -58.93
REMARK 500 ALA B 183 98.51 -57.55
REMARK 500 ASP B 202 59.85 -98.02
REMARK 500 GLN B 259 -62.09 3.30
REMARK 500 ASP B 260 -1.15 -50.41
REMARK 500 PRO B 283 174.66 -58.50
REMARK 500 PRO B 298 124.43 -38.46
REMARK 500 LEU B 328 -18.72 -45.23
REMARK 500 ARG B 374 -136.76 -119.10
REMARK 500 ASN B 376 59.83 26.35
REMARK 500 MET B 385 2.46 -67.92
REMARK 500 PRO B 473 154.83 -49.80
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 ZN A 900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 96 SG
REMARK 620 2 CYS A 101 SG 110.7
REMARK 620 3 CYS B 96 SG 119.3 103.9
REMARK 620 4 CYS B 101 SG 101.4 105.8 115.2
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 100.9
REMARK 620 3 HEM A 500 NB 90.7 89.4
REMARK 620 4 HEM A 500 NC 102.1 157.0 89.0
REMARK 620 5 HEM A 500 ND 99.0 90.7 170.0 87.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CAD A 950 AS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 384 SG
REMARK 620 2 CAD A 950 C1 96.2
REMARK 620 3 CAD A 950 C2 93.3 94.7
REMARK 620 N 1 2
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 100.4
REMARK 620 3 HEM B 500 NB 97.3 87.3
REMARK 620 4 HEM B 500 NC 103.9 155.6 87.0
REMARK 620 5 HEM B 500 ND 99.8 90.1 163.0 88.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CAD B 950 AS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 384 SG
REMARK 620 2 CAD B 950 C1 95.2
REMARK 620 3 CAD B 950 C2 95.3 94.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NRG A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAD A 950
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NRG B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAD B 950
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 881
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 880
DBREF 8NSE A 39 482 UNP P29473 NOS3_BOVIN 39 482
DBREF 8NSE B 39 482 UNP P29473 NOS3_BOVIN 39 482
SEQADV 8NSE ARG A 100 UNP P29473 CYS 100 SEE REMARK 999
SEQADV 8NSE ARG B 100 UNP P29473 CYS 100 SEE REMARK 999
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 ASN 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 ASN 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 ZN A 900 1
HET HEM A 500 43
HET H4B A 600 17
HET NRG A 705 15
HET CAD A 950 3
HET GOL A 880 6
HET HEM B 500 43
HET H4B B 601 17
HET NRG B 706 15
HET CAD B 950 3
HET GOL B 881 6
HETNAM ZN ZINC ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM NRG N-OMEGA-NITRO-L-ARGININE
HETNAM CAD CACODYLIC ACID
HETNAM GOL GLYCEROL
HETSYN HEM HEME
HETSYN NRG NNA
HETSYN CAD HYDROXYDIMETHYLARSINE OXIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ZN ZN 2+
FORMUL 4 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 H4B 2(C9 H15 N5 O3)
FORMUL 6 NRG 2(C6 H13 N5 O4)
FORMUL 7 CAD 2(C2 H7 AS O2)
FORMUL 8 GOL 2(C3 H8 O3)
FORMUL 14 HOH *194(H2 O)
HELIX 1 1 LEU A 86 GLN A 89 5 4
HELIX 2 2 ALA A 122 ILE A 140 1 19
HELIX 3 3 GLN A 146 SER A 161 1 16
HELIX 4 4 GLU A 169 ARG A 181 1 13
HELIX 5 5 ARG A 189 GLN A 191 5 3
HELIX 6 6 ALA A 206 GLY A 224 1 19
HELIX 7 7 PRO A 267 GLN A 278 5 12
HELIX 8 8 GLU A 323 LEU A 328 1 6
HELIX 9 9 SER A 361 GLY A 365 1 5
HELIX 10 10 ARG A 367 CYS A 370 1 4
HELIX 11 11 LEU A 378 MET A 385 1 8
HELIX 12 12 THR A 392 SER A 394 5 3
HELIX 13 13 TRP A 396 LEU A 414 1 19
HELIX 14 14 HIS A 422 ARG A 440 1 19
HELIX 15 15 TRP A 447 ILE A 450 1 4
HELIX 16 16 GLY A 456 LEU A 458 5 3
HELIX 17 17 PRO A 460 HIS A 463 5 4
HELIX 18 18 LEU B 86 GLN B 89 5 4
HELIX 19 19 ALA B 122 SER B 139 1 18
HELIX 20 20 GLN B 146 THR B 162 1 17
HELIX 21 21 GLU B 169 ARG B 181 1 13
HELIX 22 22 ARG B 189 GLY B 193 5 5
HELIX 23 23 ALA B 206 GLY B 224 1 19
HELIX 24 24 GLU B 271 HIS B 279 1 9
HELIX 25 25 GLU B 323 LEU B 328 5 6
HELIX 26 26 SER B 361 GLY B 365 1 5
HELIX 27 27 ARG B 367 CYS B 370 1 4
HELIX 28 28 LEU B 378 CYS B 384 1 7
HELIX 29 29 THR B 392 SER B 394 5 3
HELIX 30 30 TRP B 396 LEU B 414 1 19
HELIX 31 31 HIS B 422 ARG B 440 1 19
HELIX 32 32 TRP B 447 ILE B 450 1 4
HELIX 33 33 GLY B 456 LEU B 458 5 3
SHEET 1 A 2 PRO A 71 ASN A 75 0
SHEET 2 A 2 SER A 80 ASP A 84 -1 N ASP A 84 O PRO A 71
SHEET 1 B 2 GLN A 196 ALA A 200 0
SHEET 2 B 2 ALA A 229 PHE A 233 1 N ILE A 230 O GLN A 196
SHEET 1 C 2 GLY A 255 ARG A 257 0
SHEET 2 C 2 VAL A 263 GLY A 265 -1 N ARG A 264 O TYR A 256
SHEET 1 D 2 LEU A 293 LEU A 295 0
SHEET 2 D 2 GLU A 303 PHE A 305 -1 N PHE A 305 O LEU A 293
SHEET 1 E 2 GLU A 314 PRO A 316 0
SHEET 2 E 2 ARG A 331 TYR A 333 -1 N TRP A 332 O VAL A 315
SHEET 1 F 3 ALA A 474 ARG A 476 0
SHEET 2 F 3 LEU A 342 ILE A 345 -1 N GLU A 344 O ALA A 474
SHEET 3 F 3 LEU A 348 PHE A 350 -1 N PHE A 350 O LEU A 343
SHEET 1 G 2 PRO B 71 LYS B 74 0
SHEET 2 G 2 ILE B 81 ASP B 84 -1 N ASP B 84 O PRO B 71
SHEET 1 H 3 GLN B 196 ALA B 200 0
SHEET 2 H 3 ALA B 229 PHE B 233 1 N ILE B 230 O GLN B 196
SHEET 3 H 3 ALA B 353 SER B 356 -1 N SER B 356 O ALA B 229
SHEET 1 I 2 GLY B 255 ARG B 257 0
SHEET 2 I 2 VAL B 263 GLY B 265 -1 N ARG B 264 O TYR B 256
SHEET 1 J 2 LEU B 293 LEU B 295 0
SHEET 2 J 2 GLU B 303 PHE B 305 -1 N PHE B 305 O LEU B 293
SHEET 1 K 2 GLU B 314 PRO B 316 0
SHEET 2 K 2 ARG B 331 TYR B 333 -1 N TRP B 332 O VAL B 315
SHEET 1 L 3 ALA B 474 ARG B 476 0
SHEET 2 L 3 LEU B 342 ILE B 345 -1 N GLU B 344 O ALA B 474
SHEET 3 L 3 LEU B 348 PHE B 350 -1 N PHE B 350 O LEU B 343
LINK SG CYS A 96 ZN ZN A 900 1555 1555 2.36
LINK SG CYS A 101 ZN ZN A 900 1555 1555 2.32
LINK SG CYS A 186 FE HEM A 500 1555 1555 2.29
LINK SG CYS A 384 AS CAD A 950 1555 1555 2.28
LINK ZN ZN A 900 SG CYS B 96 1555 1555 2.31
LINK ZN ZN A 900 SG CYS B 101 1555 1555 2.30
LINK SG CYS B 186 FE HEM B 500 1555 1555 2.26
LINK SG CYS B 384 AS CAD B 950 1555 1555 2.26
CISPEP 1 SER A 472 PRO A 473 0 1.79
CISPEP 2 SER B 472 PRO B 473 0 -2.15
SITE 1 AC1 4 CYS A 96 CYS A 101 CYS B 96 CYS B 101
SITE 1 AC2 19 TRP A 180 ARG A 185 CYS A 186 SER A 228
SITE 2 AC2 19 MET A 341 PHE A 355 SER A 356 TRP A 358
SITE 3 AC2 19 MET A 360 GLU A 363 TRP A 449 PHE A 475
SITE 4 AC2 19 TYR A 477 H4B A 600 NRG A 705 HOH A1001
SITE 5 AC2 19 HOH A1026 HOH A1034 HOH A1044
SITE 1 AC3 12 SER A 104 ARG A 367 ALA A 448 TRP A 449
SITE 2 AC3 12 HEM A 500 GOL A 880 HOH A 956 HOH A 963
SITE 3 AC3 12 HOH A1001 TRP B 447 PHE B 462 GLN B 464
SITE 1 AC4 10 GLN A 249 TYR A 333 SER A 356 GLY A 357
SITE 2 AC4 10 TRP A 358 TYR A 359 GLU A 363 ASN A 368
SITE 3 AC4 10 HEM A 500 HOH A1047
SITE 1 AC5 2 CYS A 384 GLY A 441
SITE 1 AC6 17 TRP B 180 ARG B 185 CYS B 186 VAL B 187
SITE 2 AC6 17 MET B 341 PHE B 355 SER B 356 TRP B 358
SITE 3 AC6 17 GLU B 363 PHE B 475 TYR B 477 H4B B 601
SITE 4 AC6 17 NRG B 706 HOH B 955 HOH B 966 HOH B 967
SITE 5 AC6 17 HOH B 969
SITE 1 AC7 13 TRP A 447 PHE A 462 GLU A 465 SER B 104
SITE 2 AC7 13 ARG B 367 ALA B 448 TRP B 449 HEM B 500
SITE 3 AC7 13 GOL B 881 HOH B 962 HOH B 967 HOH B 970
SITE 4 AC7 13 HOH B 981
SITE 1 AC8 13 GLN B 249 TYR B 333 PRO B 336 VAL B 338
SITE 2 AC8 13 SER B 356 GLY B 357 TRP B 358 TYR B 359
SITE 3 AC8 13 GLU B 363 ASN B 368 HEM B 500 HOH B 975
SITE 4 AC8 13 HOH B 985
SITE 1 AC9 3 PHE B 70 TYR B 83 CYS B 384
SITE 1 BC1 6 TRP A 76 VAL B 106 ARG B 367 HIS B 373
SITE 2 BC1 6 H4B B 601 HOH B 962
SITE 1 BC2 5 VAL A 106 ARG A 367 HIS A 373 H4B A 600
SITE 2 BC2 5 TRP B 76
CRYST1 58.310 105.780 156.610 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 0.017150 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009453 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006385 0.00000
MTRIX1 1 0.324087 -0.930014 0.173325 3.52610 1
MTRIX2 1 -0.932487 -0.344928 -0.107206 22.55770 1
MTRIX3 1 0.159488 -0.126879 -0.979012 98.20610 1
(ATOM LINES ARE NOT SHOWN.)
END
