HEADER OXIDOREDUCTASE 28-SEP-01 1K2S
TITLE STRUCTURE OF RAT BRAIN NNOS HEME DOMAIN COMPLEXED WITH NG-ALLYL-L-
TITLE 2 ARGININE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC-OXIDE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HEME-CONTAINING OXYGENASE DOMAIN;
COMPND 5 EC: 1.14.13.39;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NITRIC OXIDE SYNTHASE, HEME-THIOLATE PROTEIN, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,P.MARTASEK,B.S.S.MASTERS,T.L.POULOS,C.S.RAMAN
REVDAT 3 07-FEB-24 1K2S 1 REMARK LINK
REVDAT 2 24-FEB-09 1K2S 1 VERSN
REVDAT 1 04-MAR-03 1K2S 0
JRNL AUTH H.LI,P.MARTASEK,B.S.S.MASTERS,T.L.POULOS,C.S.RAMAN
JRNL TITL STRUCTURE OF RAT BRAIN NNOS HEME DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
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 SYNTHASE: A PARADIGM FOR PTERIN FUNCTION INVOLVING A NOVEL
REMARK 1 TITL 3 METAL CENTER
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 95 939 1998
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/S0092-8674(00)81718-3
REMARK 2
REMARK 2 RESOLUTION. 2.55 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2060704.670
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 31666
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 : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1622
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.64
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2919
REMARK 3 BIN R VALUE (WORKING SET) : 0.4090
REMARK 3 BIN FREE R VALUE : 0.4060
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 144
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6654
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 159
REMARK 3 SOLVENT ATOMS : 195
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 31.71000
REMARK 3 B22 (A**2) : -4.69000
REMARK 3 B33 (A**2) : -27.01000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.65
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) : 0.46
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.71
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) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.030
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 : 0.35
REMARK 3 BSOL : 37.93
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : HETERO.PAR
REMARK 3 PARAMETER FILE 4 : ALR.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : HETERO.TOP
REMARK 3 TOPOLOGY FILE 4 : ALR.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K2S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014488.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
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) : 1.08
REMARK 200 MONOCHROMATOR : YES
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31687
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
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 (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : 0.11300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.60900
REMARK 200 R SYM FOR SHELL (I) : 0.60900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 (%): 49.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MES, AMMONIUM ACETATE, PH
REMARK 280 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 280K
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 25.86500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.52500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.51500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.52500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.86500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.51500
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: 9400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 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 339
REMARK 465 GLN A 340
REMARK 465 HIS A 341
REMARK 465 THR A 342
REMARK 465 ARG A 343
REMARK 465 LYS A 344
REMARK 465 PRO A 345
REMARK 465 GLU A 346
REMARK 465 ASP A 347
REMARK 465 VAL A 348
REMARK 465 ARG A 349
REMARK 465 LYS A 717
REMARK 465 SER B 339
REMARK 465 GLN B 340
REMARK 465 HIS B 341
REMARK 465 THR B 342
REMARK 465 ARG B 343
REMARK 465 LYS B 344
REMARK 465 PRO B 345
REMARK 465 GLU B 346
REMARK 465 ASP B 347
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 CYS A 326 CA - CB - SG ANGL. DEV. = 12.4 DEGREES
REMARK 500 CYS B 326 CA - CB - SG ANGL. DEV. = 12.1 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 ASP A 309 -3.08 62.02
REMARK 500 THR A 321 -71.57 -112.03
REMARK 500 LEU A 337 102.77 -160.86
REMARK 500 ARG A 371 32.34 -141.83
REMARK 500 SER A 374 168.70 -38.05
REMARK 500 THR A 393 -173.35 178.70
REMARK 500 ALA A 412 88.17 -63.53
REMARK 500 THR A 433 -8.77 -145.10
REMARK 500 THR A 466 -64.36 -125.27
REMARK 500 SER A 491 -168.40 -67.71
REMARK 500 ARG A 514 55.19 36.89
REMARK 500 LEU A 520 162.20 -48.47
REMARK 500 ASN A 527 25.67 46.22
REMARK 500 PRO A 538 -36.97 -39.97
REMARK 500 LYS A 550 -12.93 -147.09
REMARK 500 LYS A 555 -19.65 -48.61
REMARK 500 CYS A 582 56.85 -148.97
REMARK 500 ARG A 603 -127.82 -123.79
REMARK 500 ASN A 605 67.72 28.65
REMARK 500 LYS A 613 -9.98 -58.66
REMARK 500 ASP A 615 72.14 59.85
REMARK 500 ASP A 617 94.17 -67.51
REMARK 500 SER A 622 2.26 -66.25
REMARK 500 ILE A 648 141.23 -172.03
REMARK 500 CYS A 672 98.46 -160.49
REMARK 500 THR A 713 -13.40 -146.48
REMARK 500 THR B 321 -75.21 -107.77
REMARK 500 LEU B 322 171.02 -59.47
REMARK 500 LEU B 337 89.76 -155.77
REMARK 500 LYS B 370 60.72 64.00
REMARK 500 ARG B 371 29.73 -151.77
REMARK 500 SER B 374 173.78 -57.35
REMARK 500 THR B 393 -166.79 -164.46
REMARK 500 TYR B 394 139.27 -174.83
REMARK 500 ALA B 412 91.01 -65.08
REMARK 500 ARG B 418 -7.24 -57.38
REMARK 500 THR B 433 -11.55 -143.28
REMARK 500 PRO B 463 128.21 -35.43
REMARK 500 THR B 466 -82.25 -125.87
REMARK 500 ASN B 527 24.28 48.00
REMARK 500 LYS B 550 -18.75 -145.63
REMARK 500 CYS B 582 51.25 -151.61
REMARK 500 ARG B 603 -134.18 -121.58
REMARK 500 ASN B 605 72.02 28.52
REMARK 500 ASP B 615 73.32 50.02
REMARK 500 SER B 622 -0.08 -58.58
REMARK 500 CYS B 672 90.43 -161.00
REMARK 500 SER B 684 24.22 47.70
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 326 SG
REMARK 620 2 CYS A 331 SG 100.1
REMARK 620 3 CYS B 326 SG 123.3 108.1
REMARK 620 4 CYS B 331 SG 104.9 109.8 109.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 750 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 415 SG
REMARK 620 2 HEM A 750 NA 102.6
REMARK 620 3 HEM A 750 NB 96.2 88.3
REMARK 620 4 HEM A 750 NC 98.0 159.4 90.8
REMARK 620 5 HEM A 750 ND 99.0 89.0 164.8 86.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 750 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 415 SG
REMARK 620 2 HEM B 750 NA 98.1
REMARK 620 3 HEM B 750 NB 97.3 89.7
REMARK 620 4 HEM B 750 NC 97.3 164.6 89.6
REMARK 620 5 HEM B 750 ND 90.3 90.1 172.3 88.6
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 ACT A 1860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 2860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 1760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARV A 1780
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 2760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARV B 2780
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NSE RELATED DB: PDB
REMARK 900 BOVINE ENOS HEME DOMAIN COMPLEXED WITH L-ARGININE
DBREF 1K2S A 299 717 UNP P29476 NOS1_RAT 299 717
DBREF 1K2S B 299 717 UNP P29476 NOS1_RAT 299 717
SEQRES 1 A 419 ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP VAL VAL
SEQRES 2 A 419 LEU THR ASP THR LEU HIS LEU LYS SER THR LEU GLU THR
SEQRES 3 A 419 GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE MET LEU
SEQRES 4 A 419 PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL ARG THR
SEQRES 5 A 419 LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE LEU ASP
SEQRES 6 A 419 GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER LYS ALA
SEQRES 7 A 419 HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU ILE GLU
SEQRES 8 A 419 SER THR SER THR TYR GLN LEU LYS ASP THR GLU LEU ILE
SEQRES 9 A 419 TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER ARG CYS
SEQRES 10 A 419 VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL PHE ASP
SEQRES 11 A 419 ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE ASN TYR
SEQRES 12 A 419 ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS GLY ASN
SEQRES 13 A 419 LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG THR ASP
SEQRES 14 A 419 GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN LEU ILE
SEQRES 15 A 419 ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER THR LEU
SEQRES 16 A 419 GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE CYS ILE
SEQRES 17 A 419 GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE ASP VAL
SEQRES 18 A 419 LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP PRO GLU
SEQRES 19 A 419 LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU VAL PRO
SEQRES 20 A 419 ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP LEU GLY
SEQRES 21 A 419 LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN MET LEU
SEQRES 22 A 419 LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS PRO PHE
SEQRES 23 A 419 SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL ARG ASP
SEQRES 24 A 419 TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU GLU VAL
SEQRES 25 A 419 ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR SER SER
SEQRES 26 A 419 LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN ILE ALA
SEQRES 27 A 419 VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR ILE VAL
SEQRES 28 A 419 ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS HIS MET
SEQRES 29 A 419 GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO ALA ASP
SEQRES 30 A 419 TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER ILE THR
SEQRES 31 A 419 PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG LEU THR
SEQRES 32 A 419 PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN THR HIS
SEQRES 33 A 419 VAL TRP LYS
SEQRES 1 B 419 ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP VAL VAL
SEQRES 2 B 419 LEU THR ASP THR LEU HIS LEU LYS SER THR LEU GLU THR
SEQRES 3 B 419 GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE MET LEU
SEQRES 4 B 419 PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL ARG THR
SEQRES 5 B 419 LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE LEU ASP
SEQRES 6 B 419 GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER LYS ALA
SEQRES 7 B 419 HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU ILE GLU
SEQRES 8 B 419 SER THR SER THR TYR GLN LEU LYS ASP THR GLU LEU ILE
SEQRES 9 B 419 TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER ARG CYS
SEQRES 10 B 419 VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL PHE ASP
SEQRES 11 B 419 ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE ASN TYR
SEQRES 12 B 419 ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS GLY ASN
SEQRES 13 B 419 LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG THR ASP
SEQRES 14 B 419 GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN LEU ILE
SEQRES 15 B 419 ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER THR LEU
SEQRES 16 B 419 GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE CYS ILE
SEQRES 17 B 419 GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE ASP VAL
SEQRES 18 B 419 LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP PRO GLU
SEQRES 19 B 419 LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU VAL PRO
SEQRES 20 B 419 ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP LEU GLY
SEQRES 21 B 419 LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN MET LEU
SEQRES 22 B 419 LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS PRO PHE
SEQRES 23 B 419 SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL ARG ASP
SEQRES 24 B 419 TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU GLU VAL
SEQRES 25 B 419 ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR SER SER
SEQRES 26 B 419 LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN ILE ALA
SEQRES 27 B 419 VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR ILE VAL
SEQRES 28 B 419 ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS HIS MET
SEQRES 29 B 419 GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO ALA ASP
SEQRES 30 B 419 TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER ILE THR
SEQRES 31 B 419 PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG LEU THR
SEQRES 32 B 419 PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN THR HIS
SEQRES 33 B 419 VAL TRP LYS
HET ACT A1860 4
HET ZN A 900 1
HET HEM A 750 43
HET H4B A1760 17
HET ARV A1780 15
HET ACT B2860 4
HET HEM B 750 43
HET H4B B2760 17
HET ARV B2780 15
HETNAM ACT ACETATE ION
HETNAM ZN ZINC ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM ARV 5-N-ALLYL-ARGININE
HETSYN HEM HEME
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 4 ZN ZN 2+
FORMUL 5 HEM 2(C34 H32 FE N4 O4)
FORMUL 6 H4B 2(C9 H15 N5 O3)
FORMUL 7 ARV 2(C9 H19 N4 O2 1+)
FORMUL 12 HOH *195(H2 O)
HELIX 1 1 THR A 315 SER A 320 5 6
HELIX 2 2 THR A 350 LYS A 370 1 21
HELIX 3 3 SER A 374 SER A 392 1 19
HELIX 4 4 LYS A 397 ASN A 411 1 15
HELIX 5 5 GLY A 417 TRP A 421 5 5
HELIX 6 6 THR A 434 ASN A 451 1 18
HELIX 7 7 LYS A 452 ASN A 454 5 3
HELIX 8 8 ASN A 498 GLN A 508 1 11
HELIX 9 9 PRO A 537 VAL A 541 5 5
HELIX 10 10 TRP A 553 GLY A 558 5 6
HELIX 11 11 MET A 589 VAL A 595 1 7
HELIX 12 12 VAL A 595 ASP A 600 1 6
HELIX 13 13 ILE A 606 LYS A 613 1 8
HELIX 14 14 LYS A 620 SER A 623 5 4
HELIX 15 15 LEU A 624 ASP A 644 1 21
HELIX 16 16 ASP A 650 GLY A 670 1 21
HELIX 17 17 ASP A 675 VAL A 680 1 6
HELIX 18 18 SER A 684 GLN A 693 5 10
HELIX 19 19 ASP A 709 THR A 713 5 5
HELIX 20 20 THR B 315 SER B 320 5 6
HELIX 21 21 THR B 350 ILE B 369 1 20
HELIX 22 22 SER B 374 SER B 392 1 19
HELIX 23 23 LYS B 397 ASN B 411 1 15
HELIX 24 24 GLY B 417 TRP B 421 5 5
HELIX 25 25 THR B 434 ASN B 451 1 18
HELIX 26 26 LYS B 452 ASN B 454 5 3
HELIX 27 27 ASN B 498 GLN B 507 1 10
HELIX 28 28 PRO B 537 VAL B 541 5 5
HELIX 29 29 PHE B 554 GLY B 558 5 5
HELIX 30 30 MET B 589 VAL B 595 1 7
HELIX 31 31 ILE B 606 ASP B 615 1 10
HELIX 32 32 LYS B 620 SER B 623 5 4
HELIX 33 33 LEU B 624 ASP B 644 1 21
HELIX 34 34 ASP B 650 GLY B 670 1 21
HELIX 35 35 ASP B 675 VAL B 680 1 6
HELIX 36 36 SER B 684 GLN B 693 5 10
HELIX 37 37 ASP B 709 THR B 713 5 5
SHEET 1 A 2 LEU A 301 LYS A 304 0
SHEET 2 A 2 VAL A 311 ASP A 314 -1 O ASP A 314 N LEU A 301
SHEET 1 B 4 GLN A 425 ASP A 428 0
SHEET 2 B 4 ALA A 458 ILE A 461 1 O ILE A 459 N PHE A 427
SHEET 3 B 4 PHE A 584 SER A 585 -1 O SER A 585 N ALA A 458
SHEET 4 B 4 ALA A 566 VAL A 567 -1 N VAL A 567 O PHE A 584
SHEET 1 C 3 ARG A 473 VAL A 474 0
SHEET 2 C 3 LEU A 522 GLN A 525 -1 O GLN A 525 N ARG A 473
SHEET 3 C 3 GLU A 532 PHE A 534 -1 O GLU A 532 N LEU A 524
SHEET 1 D 2 GLY A 484 LYS A 486 0
SHEET 2 D 2 THR A 492 GLY A 494 -1 O LEU A 493 N TYR A 485
SHEET 1 E 2 GLU A 543 PRO A 545 0
SHEET 2 E 2 LYS A 560 TYR A 562 -1 O TRP A 561 N VAL A 544
SHEET 1 F 3 LEU A 577 PHE A 579 0
SHEET 2 F 3 LEU A 571 ILE A 574 -1 N ILE A 574 O LEU A 577
SHEET 3 F 3 SER A 703 GLU A 705 -1 O GLU A 705 N LEU A 571
SHEET 1 G 2 LEU B 301 LYS B 304 0
SHEET 2 G 2 VAL B 311 ASP B 314 -1 O ASP B 314 N LEU B 301
SHEET 1 H 4 GLN B 425 ASP B 428 0
SHEET 2 H 4 ALA B 458 ILE B 461 1 O ILE B 459 N PHE B 427
SHEET 3 H 4 PHE B 584 SER B 585 -1 O SER B 585 N ALA B 458
SHEET 4 H 4 ALA B 566 VAL B 567 -1 N VAL B 567 O PHE B 584
SHEET 1 I 3 ARG B 473 VAL B 474 0
SHEET 2 I 3 LEU B 522 GLN B 525 -1 O GLN B 525 N ARG B 473
SHEET 3 I 3 GLU B 532 PHE B 534 -1 O PHE B 534 N LEU B 522
SHEET 1 J 2 GLY B 484 LYS B 486 0
SHEET 2 J 2 THR B 492 GLY B 494 -1 O LEU B 493 N TYR B 485
SHEET 1 K 2 GLU B 543 PRO B 545 0
SHEET 2 K 2 LYS B 560 TYR B 562 -1 O TRP B 561 N VAL B 544
SHEET 1 L 3 LEU B 577 PHE B 579 0
SHEET 2 L 3 LEU B 571 ILE B 574 -1 N ILE B 574 O LEU B 577
SHEET 3 L 3 SER B 703 GLU B 705 -1 O SER B 703 N GLU B 573
LINK SG CYS A 326 ZN ZN A 900 1555 1555 2.30
LINK SG CYS A 331 ZN ZN A 900 1555 1555 2.30
LINK SG CYS A 415 FE HEM A 750 1555 1555 2.20
LINK ZN ZN A 900 SG CYS B 326 1555 1555 2.29
LINK ZN ZN A 900 SG CYS B 331 1555 1555 2.28
LINK SG CYS B 415 FE HEM B 750 1555 1555 2.23
CISPEP 1 THR A 701 PRO A 702 0 0.09
CISPEP 2 THR B 701 PRO B 702 0 0.44
SITE 1 AC1 4 ILE A 419 TRP A 587 VAL A 649 HEM A 750
SITE 1 AC2 3 HOH B 109 GLY B 417 TRP B 587
SITE 1 AC3 4 CYS A 326 CYS A 331 CYS B 326 CYS B 331
SITE 1 AC4 16 HOH A 25 HOH A 47 HOH A 133 TRP A 409
SITE 2 AC4 16 CYS A 415 MET A 570 PHE A 584 SER A 585
SITE 3 AC4 16 TRP A 587 GLU A 592 TRP A 678 PHE A 704
SITE 4 AC4 16 TYR A 706 H4B A1760 ARV A1780 ACT A1860
SITE 1 AC5 10 HOH A 25 HOH A 167 SER A 334 ARG A 596
SITE 2 AC5 10 VAL A 677 TRP A 678 HEM A 750 PHE B 691
SITE 3 AC5 10 HIS B 692 GLN B 693
SITE 1 AC6 13 HOH A 4 GLN A 478 TYR A 562 PRO A 565
SITE 2 AC6 13 VAL A 567 PHE A 584 SER A 585 GLY A 586
SITE 3 AC6 13 TRP A 587 TYR A 588 GLU A 592 ASP A 597
SITE 4 AC6 13 HEM A 750
SITE 1 AC7 13 HOH B 32 HOH B 76 HOH B 176 HOH B 187
SITE 2 AC7 13 TRP B 409 CYS B 415 PHE B 584 TRP B 587
SITE 3 AC7 13 GLU B 592 TRP B 678 TYR B 706 H4B B2760
SITE 4 AC7 13 ARV B2780
SITE 1 AC8 11 TRP A 676 PHE A 691 HIS A 692 HOH B 32
SITE 2 AC8 11 HOH B 64 HOH B 173 SER B 334 ARG B 596
SITE 3 AC8 11 VAL B 677 TRP B 678 HEM B 750
SITE 1 AC9 14 HOH B 76 GLN B 478 TYR B 562 PRO B 565
SITE 2 AC9 14 ALA B 566 VAL B 567 PHE B 584 SER B 585
SITE 3 AC9 14 GLY B 586 TRP B 587 TYR B 588 GLU B 592
SITE 4 AC9 14 ASP B 597 HEM B 750
CRYST1 51.730 111.030 165.050 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 0.019331 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009007 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006059 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
