HEADER OXIDOREDUCTASE 10-JAN-99 1NSI
TITLE HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-BOUND, L-ARG COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (NITRIC OXIDE SYNTHASE);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: HEME DOMAIN;
COMPND 5 SYNONYM: INOS;
COMPND 6 EC: 1.14.13.39;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL: ADENOCARCINOMA DLD-1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NITRIC OXIDE SYNTHASE, HEME PROTEIN, TETRAHYDROBIOPTERIN,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,C.S.RAMAN,C.B.GLASER,E.BLASKO,T.A.YOUNG,J.F.PARKINSON,M.WHITLOW,
AUTHOR 2 T.L.POULOS
REVDAT 3 13-JUL-11 1NSI 1 VERSN
REVDAT 2 24-FEB-09 1NSI 1 VERSN
REVDAT 1 07-JAN-00 1NSI 0
JRNL AUTH H.LI,C.S.RAMAN,C.B.GLASER,E.BLASKO,T.A.YOUNG,J.F.PARKINSON,
JRNL AUTH 2 M.WHITLOW,T.L.POULOS
JRNL TITL CRYSTAL STRUCTURES OF ZINC-FREE AND -BOUND HEME DOMAIN OF
JRNL TITL 2 HUMAN INDUCIBLE NITRIC-OXIDE SYNTHASE. IMPLICATIONS FOR
JRNL TITL 3 DIMER STABILITY AND COMPARISON WITH ENDOTHELIAL NITRIC-OXIDE
JRNL TITL 4 SYNTHASE.
JRNL REF J.BIOL.CHEM. V. 274 21276 1999
JRNL REFN ISSN 0021-9258
JRNL PMID 10409685
JRNL DOI 10.1074/JBC.274.30.21276
REMARK 1
REMARK 1 REFERENCE 1
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 2
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 1 REFERENCE 3
REMARK 1 AUTH C.S.RAMAN,H.LI,P.MARTASEK,V.KRAL,B.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 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 80.5
REMARK 3 NUMBER OF REFLECTIONS : 111401
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) : 0.209
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5651
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 46.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7561
REMARK 3 BIN R VALUE (WORKING SET) : 0.3130
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 415
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13676
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 359
REMARK 3 SOLVENT ATOMS : 295
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.32
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.49
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.20
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 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 1NSI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-99.
REMARK 100 THE RCSB ID CODE IS RCSB007219.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : YES
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 125717
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 (%) : 95.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
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 (%) : 71.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: ENOS HEME DOMAIN
REMARK 200
REMARK 200 REMARK: ONE DIMER AS THE SEARCH MODEL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 78.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.74500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 93.67500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 93.67500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 170.61750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 93.67500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 93.67500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 56.87250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 93.67500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 93.67500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 170.61750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 93.67500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 93.67500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.87250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 113.74500
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 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 LEU A 74
REMARK 465 ASP A 75
REMARK 465 ALA A 76
REMARK 465 THR A 77
REMARK 465 PRO A 78
REMARK 465 LEU A 79
REMARK 465 SER A 80
REMARK 465 SER A 81
REMARK 465 PRO A 82
REMARK 465 ASP A 503
REMARK 465 GLU A 504
REMARK 465 LEU B 74
REMARK 465 ASP B 75
REMARK 465 ALA B 76
REMARK 465 THR B 77
REMARK 465 PRO B 78
REMARK 465 LEU B 79
REMARK 465 SER B 80
REMARK 465 SER B 81
REMARK 465 PRO B 82
REMARK 465 ASP B 503
REMARK 465 GLU B 504
REMARK 465 LEU C 74
REMARK 465 ASP C 75
REMARK 465 ALA C 76
REMARK 465 THR C 77
REMARK 465 PRO C 78
REMARK 465 LEU C 79
REMARK 465 SER C 80
REMARK 465 SER C 81
REMARK 465 PRO C 82
REMARK 465 ASP C 503
REMARK 465 GLU C 504
REMARK 465 LEU D 74
REMARK 465 ASP D 75
REMARK 465 ALA D 76
REMARK 465 THR D 77
REMARK 465 PRO D 78
REMARK 465 LEU D 79
REMARK 465 SER D 80
REMARK 465 SER D 81
REMARK 465 PRO D 82
REMARK 465 ASP D 503
REMARK 465 GLU D 504
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 110 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 CYS A 200 CA - CB - SG ANGL. DEV. = -15.8 DEGREES
REMARK 500 CYS D 110 CA - CB - SG ANGL. DEV. = 11.0 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 GLU A 156 -154.37 -79.88
REMARK 500 ILE A 159 -50.59 -6.82
REMARK 500 ASN A 208 79.57 -107.41
REMARK 500 SER A 218 -15.98 -147.93
REMARK 500 SER A 251 -83.95 -102.16
REMARK 500 ASN A 312 74.58 25.32
REMARK 500 LYS A 335 -48.50 -130.46
REMARK 500 CYS A 367 66.24 -154.08
REMARK 500 ARG A 381 -72.33 -73.14
REMARK 500 ARG A 388 -140.52 -128.10
REMARK 500 THR A 403 1.61 -68.00
REMARK 500 SER A 453 -69.09 -92.10
REMARK 500 LEU A 485 -163.15 -121.21
REMARK 500 ALA A 495 -60.39 -26.56
REMARK 500 GLU B 156 -138.43 -78.46
REMARK 500 ILE B 159 -59.17 -21.27
REMARK 500 SER B 207 32.36 -82.85
REMARK 500 CYS B 217 153.07 -44.51
REMARK 500 SER B 218 -26.66 -142.31
REMARK 500 SER B 251 -87.33 -120.12
REMARK 500 TYR B 299 41.39 28.26
REMARK 500 PHE B 302 56.06 -103.93
REMARK 500 ARG B 314 -166.23 -70.62
REMARK 500 ASN B 354 8.85 -67.24
REMARK 500 CYS B 367 59.71 -170.53
REMARK 500 ARG B 381 -71.58 -80.16
REMARK 500 ARG B 388 -139.51 -123.55
REMARK 500 SER B 453 -88.80 -72.92
REMARK 500 CYS B 457 98.97 -162.54
REMARK 500 LEU B 485 -158.54 -106.73
REMARK 500 HIS B 499 137.45 -39.06
REMARK 500 LEU C 116 51.22 -113.57
REMARK 500 PRO C 133 158.90 -45.17
REMARK 500 ILE C 159 -59.51 -19.55
REMARK 500 THR C 178 -170.87 -174.91
REMARK 500 SER C 218 -12.36 -141.81
REMARK 500 ASN C 236 48.38 39.25
REMARK 500 PRO C 248 134.72 -39.67
REMARK 500 SER C 251 -82.61 -109.12
REMARK 500 HIS C 255 63.36 -117.85
REMARK 500 ASN C 312 73.98 15.57
REMARK 500 LYS C 335 -58.38 -123.62
REMARK 500 CYS C 367 62.60 -163.65
REMARK 500 ARG C 381 -75.80 -70.50
REMARK 500 ARG C 388 -144.19 -118.68
REMARK 500 ASN C 390 67.39 36.41
REMARK 500 THR C 403 2.57 -63.13
REMARK 500 CYS C 457 100.32 -164.27
REMARK 500 LEU C 485 -157.41 -118.36
REMARK 500 ARG D 130 -166.69 -118.64
REMARK 500
REMARK 500 THIS ENTRY HAS 65 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASN A 312 24.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 991 DISTANCE = 5.42 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 115 SG
REMARK 620 2 CYS A 110 SG 100.5
REMARK 620 3 CYS B 115 SG 110.8 103.8
REMARK 620 4 CYS B 110 SG 101.0 125.3 114.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 902 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 115 SG
REMARK 620 2 CYS C 110 SG 106.4
REMARK 620 3 CYS D 115 SG 113.8 104.0
REMARK 620 4 CYS D 110 SG 105.0 122.7 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 550 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 200 SG
REMARK 620 2 HEM A 550 NA 87.7
REMARK 620 3 HEM A 550 NB 94.4 90.5
REMARK 620 4 HEM A 550 NC 104.9 167.0 91.4
REMARK 620 5 HEM A 550 ND 91.4 87.7 173.9 89.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 550 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 200 SG
REMARK 620 2 HEM B 550 NA 102.5
REMARK 620 3 HEM B 550 NB 89.2 85.8
REMARK 620 4 HEM B 550 NC 99.6 157.6 90.5
REMARK 620 5 HEM B 550 ND 104.8 89.5 165.9 88.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 550 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 200 SG
REMARK 620 2 HEM C 550 NA 92.9
REMARK 620 3 HEM C 550 NB 92.9 89.6
REMARK 620 4 HEM C 550 NC 101.9 165.2 89.5
REMARK 620 5 HEM C 550 ND 97.1 90.2 170.0 88.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 550 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 200 SG
REMARK 620 2 HEM D 550 NA 95.4
REMARK 620 3 HEM D 550 NB 88.5 91.0
REMARK 620 4 HEM D 550 NC 95.1 169.5 89.3
REMARK 620 5 HEM D 550 ND 93.3 89.0 178.2 90.3
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 SO4 A 910
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 920
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 930
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 911
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 921
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 912
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 922
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 913
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 923
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B D 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 880
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 881
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 882
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 883
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NSI RELATED DB: PDB
DBREF 1NSI A 74 504 UNP P35228 NOS2A_HUMAN 74 504
DBREF 1NSI B 74 504 UNP P35228 NOS2A_HUMAN 74 504
DBREF 1NSI C 74 504 UNP P35228 NOS2A_HUMAN 74 504
DBREF 1NSI D 74 504 UNP P35228 NOS2A_HUMAN 74 504
SEQRES 1 A 431 LEU ASP ALA THR PRO LEU SER SER PRO ARG HIS VAL ARG
SEQRES 2 A 431 ILE LYS ASN TRP GLY SER GLY MET THR PHE GLN ASP THR
SEQRES 3 A 431 LEU HIS HIS LYS ALA LYS GLY ILE LEU THR CYS ARG SER
SEQRES 4 A 431 LYS SER CYS LEU GLY SER ILE MET THR PRO LYS SER LEU
SEQRES 5 A 431 THR ARG GLY PRO ARG ASP LYS PRO THR PRO PRO ASP GLU
SEQRES 6 A 431 LEU LEU PRO GLN ALA ILE GLU PHE VAL ASN GLN TYR TYR
SEQRES 7 A 431 GLY SER PHE LYS GLU ALA LYS ILE GLU GLU HIS LEU ALA
SEQRES 8 A 431 ARG VAL GLU ALA VAL THR LYS GLU ILE GLU THR THR GLY
SEQRES 9 A 431 THR TYR GLN LEU THR GLY ASP GLU LEU ILE PHE ALA THR
SEQRES 10 A 431 LYS GLN ALA TRP ARG ASN ALA PRO ARG CYS ILE GLY ARG
SEQRES 11 A 431 ILE GLN TRP SER ASN LEU GLN VAL PHE ASP ALA ARG SER
SEQRES 12 A 431 CYS SER THR ALA ARG GLU MET PHE GLU HIS ILE CYS ARG
SEQRES 13 A 431 HIS VAL ARG TYR SER THR ASN ASN GLY ASN ILE ARG SER
SEQRES 14 A 431 ALA ILE THR VAL PHE PRO GLN ARG SER ASP GLY LYS HIS
SEQRES 15 A 431 ASP PHE ARG VAL TRP ASN ALA GLN LEU ILE ARG TYR ALA
SEQRES 16 A 431 GLY TYR GLN MET PRO ASP GLY SER ILE ARG GLY ASP PRO
SEQRES 17 A 431 ALA ASN VAL GLU PHE THR GLN LEU CYS ILE ASP LEU GLY
SEQRES 18 A 431 TRP LYS PRO LYS TYR GLY ARG PHE ASP VAL VAL PRO LEU
SEQRES 19 A 431 VAL LEU GLN ALA ASN GLY ARG ASP PRO GLU LEU PHE GLU
SEQRES 20 A 431 ILE PRO PRO ASP LEU VAL LEU GLU VAL ALA MET GLU HIS
SEQRES 21 A 431 PRO LYS TYR GLU TRP PHE ARG GLU LEU GLU LEU LYS TRP
SEQRES 22 A 431 TYR ALA LEU PRO ALA VAL ALA ASN MET LEU LEU GLU VAL
SEQRES 23 A 431 GLY GLY LEU GLU PHE PRO GLY CYS PRO PHE ASN GLY TRP
SEQRES 24 A 431 TYR MET GLY THR GLU ILE GLY VAL ARG ASP PHE CYS ASP
SEQRES 25 A 431 VAL GLN ARG TYR ASN ILE LEU GLU GLU VAL GLY ARG ARG
SEQRES 26 A 431 MET GLY LEU GLU THR HIS LYS LEU ALA SER LEU TRP LYS
SEQRES 27 A 431 ASP GLN ALA VAL VAL GLU ILE ASN ILE ALA VAL LEU HIS
SEQRES 28 A 431 SER PHE GLN LYS GLN ASN VAL THR ILE MET ASP HIS HIS
SEQRES 29 A 431 SER ALA ALA GLU SER PHE MET LYS TYR MET GLN ASN GLU
SEQRES 30 A 431 TYR ARG SER ARG GLY GLY CYS PRO ALA ASP TRP ILE TRP
SEQRES 31 A 431 LEU VAL PRO PRO MET SER GLY SER ILE THR PRO VAL PHE
SEQRES 32 A 431 HIS GLN GLU MET LEU ASN TYR VAL LEU SER PRO PHE TYR
SEQRES 33 A 431 TYR TYR GLN VAL GLU ALA TRP LYS THR HIS VAL TRP GLN
SEQRES 34 A 431 ASP GLU
SEQRES 1 B 431 LEU ASP ALA THR PRO LEU SER SER PRO ARG HIS VAL ARG
SEQRES 2 B 431 ILE LYS ASN TRP GLY SER GLY MET THR PHE GLN ASP THR
SEQRES 3 B 431 LEU HIS HIS LYS ALA LYS GLY ILE LEU THR CYS ARG SER
SEQRES 4 B 431 LYS SER CYS LEU GLY SER ILE MET THR PRO LYS SER LEU
SEQRES 5 B 431 THR ARG GLY PRO ARG ASP LYS PRO THR PRO PRO ASP GLU
SEQRES 6 B 431 LEU LEU PRO GLN ALA ILE GLU PHE VAL ASN GLN TYR TYR
SEQRES 7 B 431 GLY SER PHE LYS GLU ALA LYS ILE GLU GLU HIS LEU ALA
SEQRES 8 B 431 ARG VAL GLU ALA VAL THR LYS GLU ILE GLU THR THR GLY
SEQRES 9 B 431 THR TYR GLN LEU THR GLY ASP GLU LEU ILE PHE ALA THR
SEQRES 10 B 431 LYS GLN ALA TRP ARG ASN ALA PRO ARG CYS ILE GLY ARG
SEQRES 11 B 431 ILE GLN TRP SER ASN LEU GLN VAL PHE ASP ALA ARG SER
SEQRES 12 B 431 CYS SER THR ALA ARG GLU MET PHE GLU HIS ILE CYS ARG
SEQRES 13 B 431 HIS VAL ARG TYR SER THR ASN ASN GLY ASN ILE ARG SER
SEQRES 14 B 431 ALA ILE THR VAL PHE PRO GLN ARG SER ASP GLY LYS HIS
SEQRES 15 B 431 ASP PHE ARG VAL TRP ASN ALA GLN LEU ILE ARG TYR ALA
SEQRES 16 B 431 GLY TYR GLN MET PRO ASP GLY SER ILE ARG GLY ASP PRO
SEQRES 17 B 431 ALA ASN VAL GLU PHE THR GLN LEU CYS ILE ASP LEU GLY
SEQRES 18 B 431 TRP LYS PRO LYS TYR GLY ARG PHE ASP VAL VAL PRO LEU
SEQRES 19 B 431 VAL LEU GLN ALA ASN GLY ARG ASP PRO GLU LEU PHE GLU
SEQRES 20 B 431 ILE PRO PRO ASP LEU VAL LEU GLU VAL ALA MET GLU HIS
SEQRES 21 B 431 PRO LYS TYR GLU TRP PHE ARG GLU LEU GLU LEU LYS TRP
SEQRES 22 B 431 TYR ALA LEU PRO ALA VAL ALA ASN MET LEU LEU GLU VAL
SEQRES 23 B 431 GLY GLY LEU GLU PHE PRO GLY CYS PRO PHE ASN GLY TRP
SEQRES 24 B 431 TYR MET GLY THR GLU ILE GLY VAL ARG ASP PHE CYS ASP
SEQRES 25 B 431 VAL GLN ARG TYR ASN ILE LEU GLU GLU VAL GLY ARG ARG
SEQRES 26 B 431 MET GLY LEU GLU THR HIS LYS LEU ALA SER LEU TRP LYS
SEQRES 27 B 431 ASP GLN ALA VAL VAL GLU ILE ASN ILE ALA VAL LEU HIS
SEQRES 28 B 431 SER PHE GLN LYS GLN ASN VAL THR ILE MET ASP HIS HIS
SEQRES 29 B 431 SER ALA ALA GLU SER PHE MET LYS TYR MET GLN ASN GLU
SEQRES 30 B 431 TYR ARG SER ARG GLY GLY CYS PRO ALA ASP TRP ILE TRP
SEQRES 31 B 431 LEU VAL PRO PRO MET SER GLY SER ILE THR PRO VAL PHE
SEQRES 32 B 431 HIS GLN GLU MET LEU ASN TYR VAL LEU SER PRO PHE TYR
SEQRES 33 B 431 TYR TYR GLN VAL GLU ALA TRP LYS THR HIS VAL TRP GLN
SEQRES 34 B 431 ASP GLU
SEQRES 1 C 431 LEU ASP ALA THR PRO LEU SER SER PRO ARG HIS VAL ARG
SEQRES 2 C 431 ILE LYS ASN TRP GLY SER GLY MET THR PHE GLN ASP THR
SEQRES 3 C 431 LEU HIS HIS LYS ALA LYS GLY ILE LEU THR CYS ARG SER
SEQRES 4 C 431 LYS SER CYS LEU GLY SER ILE MET THR PRO LYS SER LEU
SEQRES 5 C 431 THR ARG GLY PRO ARG ASP LYS PRO THR PRO PRO ASP GLU
SEQRES 6 C 431 LEU LEU PRO GLN ALA ILE GLU PHE VAL ASN GLN TYR TYR
SEQRES 7 C 431 GLY SER PHE LYS GLU ALA LYS ILE GLU GLU HIS LEU ALA
SEQRES 8 C 431 ARG VAL GLU ALA VAL THR LYS GLU ILE GLU THR THR GLY
SEQRES 9 C 431 THR TYR GLN LEU THR GLY ASP GLU LEU ILE PHE ALA THR
SEQRES 10 C 431 LYS GLN ALA TRP ARG ASN ALA PRO ARG CYS ILE GLY ARG
SEQRES 11 C 431 ILE GLN TRP SER ASN LEU GLN VAL PHE ASP ALA ARG SER
SEQRES 12 C 431 CYS SER THR ALA ARG GLU MET PHE GLU HIS ILE CYS ARG
SEQRES 13 C 431 HIS VAL ARG TYR SER THR ASN ASN GLY ASN ILE ARG SER
SEQRES 14 C 431 ALA ILE THR VAL PHE PRO GLN ARG SER ASP GLY LYS HIS
SEQRES 15 C 431 ASP PHE ARG VAL TRP ASN ALA GLN LEU ILE ARG TYR ALA
SEQRES 16 C 431 GLY TYR GLN MET PRO ASP GLY SER ILE ARG GLY ASP PRO
SEQRES 17 C 431 ALA ASN VAL GLU PHE THR GLN LEU CYS ILE ASP LEU GLY
SEQRES 18 C 431 TRP LYS PRO LYS TYR GLY ARG PHE ASP VAL VAL PRO LEU
SEQRES 19 C 431 VAL LEU GLN ALA ASN GLY ARG ASP PRO GLU LEU PHE GLU
SEQRES 20 C 431 ILE PRO PRO ASP LEU VAL LEU GLU VAL ALA MET GLU HIS
SEQRES 21 C 431 PRO LYS TYR GLU TRP PHE ARG GLU LEU GLU LEU LYS TRP
SEQRES 22 C 431 TYR ALA LEU PRO ALA VAL ALA ASN MET LEU LEU GLU VAL
SEQRES 23 C 431 GLY GLY LEU GLU PHE PRO GLY CYS PRO PHE ASN GLY TRP
SEQRES 24 C 431 TYR MET GLY THR GLU ILE GLY VAL ARG ASP PHE CYS ASP
SEQRES 25 C 431 VAL GLN ARG TYR ASN ILE LEU GLU GLU VAL GLY ARG ARG
SEQRES 26 C 431 MET GLY LEU GLU THR HIS LYS LEU ALA SER LEU TRP LYS
SEQRES 27 C 431 ASP GLN ALA VAL VAL GLU ILE ASN ILE ALA VAL LEU HIS
SEQRES 28 C 431 SER PHE GLN LYS GLN ASN VAL THR ILE MET ASP HIS HIS
SEQRES 29 C 431 SER ALA ALA GLU SER PHE MET LYS TYR MET GLN ASN GLU
SEQRES 30 C 431 TYR ARG SER ARG GLY GLY CYS PRO ALA ASP TRP ILE TRP
SEQRES 31 C 431 LEU VAL PRO PRO MET SER GLY SER ILE THR PRO VAL PHE
SEQRES 32 C 431 HIS GLN GLU MET LEU ASN TYR VAL LEU SER PRO PHE TYR
SEQRES 33 C 431 TYR TYR GLN VAL GLU ALA TRP LYS THR HIS VAL TRP GLN
SEQRES 34 C 431 ASP GLU
SEQRES 1 D 431 LEU ASP ALA THR PRO LEU SER SER PRO ARG HIS VAL ARG
SEQRES 2 D 431 ILE LYS ASN TRP GLY SER GLY MET THR PHE GLN ASP THR
SEQRES 3 D 431 LEU HIS HIS LYS ALA LYS GLY ILE LEU THR CYS ARG SER
SEQRES 4 D 431 LYS SER CYS LEU GLY SER ILE MET THR PRO LYS SER LEU
SEQRES 5 D 431 THR ARG GLY PRO ARG ASP LYS PRO THR PRO PRO ASP GLU
SEQRES 6 D 431 LEU LEU PRO GLN ALA ILE GLU PHE VAL ASN GLN TYR TYR
SEQRES 7 D 431 GLY SER PHE LYS GLU ALA LYS ILE GLU GLU HIS LEU ALA
SEQRES 8 D 431 ARG VAL GLU ALA VAL THR LYS GLU ILE GLU THR THR GLY
SEQRES 9 D 431 THR TYR GLN LEU THR GLY ASP GLU LEU ILE PHE ALA THR
SEQRES 10 D 431 LYS GLN ALA TRP ARG ASN ALA PRO ARG CYS ILE GLY ARG
SEQRES 11 D 431 ILE GLN TRP SER ASN LEU GLN VAL PHE ASP ALA ARG SER
SEQRES 12 D 431 CYS SER THR ALA ARG GLU MET PHE GLU HIS ILE CYS ARG
SEQRES 13 D 431 HIS VAL ARG TYR SER THR ASN ASN GLY ASN ILE ARG SER
SEQRES 14 D 431 ALA ILE THR VAL PHE PRO GLN ARG SER ASP GLY LYS HIS
SEQRES 15 D 431 ASP PHE ARG VAL TRP ASN ALA GLN LEU ILE ARG TYR ALA
SEQRES 16 D 431 GLY TYR GLN MET PRO ASP GLY SER ILE ARG GLY ASP PRO
SEQRES 17 D 431 ALA ASN VAL GLU PHE THR GLN LEU CYS ILE ASP LEU GLY
SEQRES 18 D 431 TRP LYS PRO LYS TYR GLY ARG PHE ASP VAL VAL PRO LEU
SEQRES 19 D 431 VAL LEU GLN ALA ASN GLY ARG ASP PRO GLU LEU PHE GLU
SEQRES 20 D 431 ILE PRO PRO ASP LEU VAL LEU GLU VAL ALA MET GLU HIS
SEQRES 21 D 431 PRO LYS TYR GLU TRP PHE ARG GLU LEU GLU LEU LYS TRP
SEQRES 22 D 431 TYR ALA LEU PRO ALA VAL ALA ASN MET LEU LEU GLU VAL
SEQRES 23 D 431 GLY GLY LEU GLU PHE PRO GLY CYS PRO PHE ASN GLY TRP
SEQRES 24 D 431 TYR MET GLY THR GLU ILE GLY VAL ARG ASP PHE CYS ASP
SEQRES 25 D 431 VAL GLN ARG TYR ASN ILE LEU GLU GLU VAL GLY ARG ARG
SEQRES 26 D 431 MET GLY LEU GLU THR HIS LYS LEU ALA SER LEU TRP LYS
SEQRES 27 D 431 ASP GLN ALA VAL VAL GLU ILE ASN ILE ALA VAL LEU HIS
SEQRES 28 D 431 SER PHE GLN LYS GLN ASN VAL THR ILE MET ASP HIS HIS
SEQRES 29 D 431 SER ALA ALA GLU SER PHE MET LYS TYR MET GLN ASN GLU
SEQRES 30 D 431 TYR ARG SER ARG GLY GLY CYS PRO ALA ASP TRP ILE TRP
SEQRES 31 D 431 LEU VAL PRO PRO MET SER GLY SER ILE THR PRO VAL PHE
SEQRES 32 D 431 HIS GLN GLU MET LEU ASN TYR VAL LEU SER PRO PHE TYR
SEQRES 33 D 431 TYR TYR GLN VAL GLU ALA TRP LYS THR HIS VAL TRP GLN
SEQRES 34 D 431 ASP GLU
HET SO4 A 910 5
HET SO4 A 920 5
HET SO4 A 930 5
HET SO4 B 911 5
HET SO4 B 921 5
HET SO4 C 912 5
HET SO4 C 922 5
HET SO4 D 913 5
HET SO4 D 923 5
HET ZN A 901 1
HET ZN C 902 1
HET HEM A 550 43
HET H4B A 600 17
HET ARG A 700 12
HET HEM B 550 43
HET H4B B 601 17
HET ARG B 701 12
HET HEM C 550 43
HET H4B C 602 17
HET ARG C 702 12
HET HEM D 550 43
HET H4B D 603 17
HET ARG D 703 12
HET GOL A 880 6
HET GOL B 881 6
HET GOL C 882 6
HET GOL D 883 6
HETNAM SO4 SULFATE ION
HETNAM ZN ZINC ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM ARG ARGININE
HETNAM GOL GLYCEROL
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 SO4 9(O4 S 2-)
FORMUL 14 ZN 2(ZN 2+)
FORMUL 16 HEM 4(C34 H32 FE N4 O4)
FORMUL 17 H4B 4(C9 H15 N5 O3)
FORMUL 18 ARG 4(C6 H15 N4 O2 1+)
FORMUL 28 GOL 4(C3 H8 O3)
FORMUL 32 HOH *295(H2 O)
HELIX 1 1 LEU A 100 HIS A 102 5 3
HELIX 2 2 LYS A 123 LEU A 125 5 3
HELIX 3 3 PRO A 136 SER A 153 1 18
HELIX 4 4 ILE A 159 THR A 176 1 18
HELIX 5 5 GLY A 183 ARG A 195 1 13
HELIX 6 6 ARG A 203 GLN A 205 5 3
HELIX 7 7 ALA A 220 GLY A 238 1 19
HELIX 8 8 PRO A 281 ASP A 292 5 12
HELIX 9 9 PRO A 323 LEU A 325 5 3
HELIX 10 10 GLU A 337 LEU A 342 5 6
HELIX 11 11 GLY A 375 GLY A 379 1 5
HELIX 12 12 ARG A 381 CYS A 384 1 4
HELIX 13 13 LEU A 392 ARG A 398 1 7
HELIX 14 14 LEU A 406 SER A 408 5 3
HELIX 15 15 TRP A 410 LYS A 428 1 19
HELIX 16 16 HIS A 436 SER A 453 1 18
HELIX 17 17 TRP A 461 LEU A 464 1 4
HELIX 18 18 GLY A 470 ILE A 472 5 3
HELIX 19 19 ALA A 495 THR A 498 1 4
HELIX 20 20 LEU B 100 LYS B 103 5 4
HELIX 21 21 LYS B 123 LEU B 125 5 3
HELIX 22 22 PRO B 136 SER B 153 1 18
HELIX 23 23 ILE B 159 THR B 176 1 18
HELIX 24 24 GLY B 183 ARG B 195 1 13
HELIX 25 25 ARG B 203 GLN B 205 5 3
HELIX 26 26 ALA B 220 GLY B 238 1 19
HELIX 27 27 PRO B 281 ASP B 292 5 12
HELIX 28 28 PRO B 323 LEU B 325 5 3
HELIX 29 29 GLU B 337 LEU B 342 5 6
HELIX 30 30 GLY B 375 GLY B 379 1 5
HELIX 31 31 ARG B 381 CYS B 384 1 4
HELIX 32 32 LEU B 392 MET B 399 1 8
HELIX 33 33 LEU B 406 SER B 408 5 3
HELIX 34 34 TRP B 410 LYS B 428 1 19
HELIX 35 35 HIS B 436 SER B 453 1 18
HELIX 36 36 TRP B 461 LEU B 464 1 4
HELIX 37 37 GLY B 470 ILE B 472 5 3
HELIX 38 38 PRO B 474 HIS B 477 5 4
HELIX 39 39 ALA B 495 LYS B 497 5 3
HELIX 40 40 LEU C 100 LYS C 103 5 4
HELIX 41 41 LYS C 123 LEU C 125 5 3
HELIX 42 42 PRO C 136 SER C 153 1 18
HELIX 43 43 ILE C 159 THR C 176 1 18
HELIX 44 44 GLY C 183 ARG C 195 1 13
HELIX 45 45 ARG C 203 GLN C 205 5 3
HELIX 46 46 ALA C 220 GLY C 238 1 19
HELIX 47 47 PRO C 281 ASP C 292 5 12
HELIX 48 48 PRO C 323 LEU C 325 5 3
HELIX 49 49 GLU C 337 LEU C 342 5 6
HELIX 50 50 GLY C 375 GLY C 379 1 5
HELIX 51 51 ARG C 381 CYS C 384 1 4
HELIX 52 52 LEU C 392 ARG C 398 1 7
HELIX 53 53 LEU C 406 SER C 408 5 3
HELIX 54 54 TRP C 410 LYS C 428 1 19
HELIX 55 55 HIS C 436 SER C 453 1 18
HELIX 56 56 TRP C 461 LEU C 464 1 4
HELIX 57 57 GLY C 470 ILE C 472 5 3
HELIX 58 58 ALA C 495 LYS C 497 5 3
HELIX 59 59 LEU D 100 LYS D 103 5 4
HELIX 60 60 LYS D 123 LEU D 125 5 3
HELIX 61 61 PRO D 136 GLY D 152 1 17
HELIX 62 62 ILE D 159 THR D 175 1 17
HELIX 63 63 GLY D 183 ARG D 195 1 13
HELIX 64 64 ARG D 203 GLN D 205 5 3
HELIX 65 65 ALA D 220 GLY D 238 1 19
HELIX 66 66 PRO D 281 ASP D 292 5 12
HELIX 67 67 GLU D 337 LEU D 342 5 6
HELIX 68 68 GLY D 375 GLY D 379 1 5
HELIX 69 69 ARG D 381 CYS D 384 1 4
HELIX 70 70 LEU D 392 ARG D 398 1 7
HELIX 71 71 LEU D 406 SER D 408 5 3
HELIX 72 72 TRP D 410 LYS D 428 1 19
HELIX 73 73 HIS D 436 SER D 453 1 18
HELIX 74 74 TRP D 461 LEU D 464 1 4
HELIX 75 75 GLY D 470 ILE D 472 5 3
HELIX 76 76 PRO D 474 HIS D 477 1 4
HELIX 77 77 ALA D 495 LYS D 497 5 3
SHEET 1 A 2 VAL A 85 LYS A 88 0
SHEET 2 A 2 THR A 95 ASP A 98 -1 N ASP A 98 O VAL A 85
SHEET 1 B 2 GLN A 210 ALA A 214 0
SHEET 2 B 2 ALA A 243 PHE A 247 1 N ILE A 244 O GLN A 210
SHEET 1 C 2 GLY A 269 GLN A 271 0
SHEET 2 C 2 ILE A 277 GLY A 279 -1 N ARG A 278 O TYR A 270
SHEET 1 D 2 LEU A 307 LEU A 309 0
SHEET 2 D 2 GLU A 317 PHE A 319 -1 N PHE A 319 O LEU A 307
SHEET 1 E 2 GLU A 328 ALA A 330 0
SHEET 2 E 2 LYS A 345 TYR A 347 -1 N TRP A 346 O VAL A 329
SHEET 1 F 3 PHE A 488 TYR A 490 0
SHEET 2 F 3 LEU A 356 VAL A 359 -1 N GLU A 358 O PHE A 488
SHEET 3 F 3 LEU A 362 PHE A 364 -1 N PHE A 364 O LEU A 357
SHEET 1 G 2 VAL B 85 LYS B 88 0
SHEET 2 G 2 THR B 95 ASP B 98 -1 N ASP B 98 O VAL B 85
SHEET 1 H 2 GLN B 210 ALA B 214 0
SHEET 2 H 2 ALA B 243 PHE B 247 1 N ILE B 244 O GLN B 210
SHEET 1 I 2 GLY B 269 GLN B 271 0
SHEET 2 I 2 ILE B 277 GLY B 279 -1 N ARG B 278 O TYR B 270
SHEET 1 J 2 LEU B 307 LEU B 309 0
SHEET 2 J 2 GLU B 317 PHE B 319 -1 N PHE B 319 O LEU B 307
SHEET 1 K 2 GLU B 328 ALA B 330 0
SHEET 2 K 2 LYS B 345 TYR B 347 -1 N TRP B 346 O VAL B 329
SHEET 1 L 3 PHE B 488 TYR B 490 0
SHEET 2 L 3 LEU B 356 VAL B 359 -1 N GLU B 358 O PHE B 488
SHEET 3 L 3 LEU B 362 PHE B 364 -1 N PHE B 364 O LEU B 357
SHEET 1 M 2 VAL C 85 LYS C 88 0
SHEET 2 M 2 THR C 95 ASP C 98 -1 N ASP C 98 O VAL C 85
SHEET 1 N 2 GLN C 210 ALA C 214 0
SHEET 2 N 2 ALA C 243 PHE C 247 1 N ILE C 244 O GLN C 210
SHEET 1 O 2 GLY C 269 GLN C 271 0
SHEET 2 O 2 ILE C 277 GLY C 279 -1 N ARG C 278 O TYR C 270
SHEET 1 P 2 LEU C 307 LEU C 309 0
SHEET 2 P 2 GLU C 317 PHE C 319 -1 N PHE C 319 O LEU C 307
SHEET 1 Q 2 GLU C 328 ALA C 330 0
SHEET 2 Q 2 LYS C 345 TYR C 347 -1 N TRP C 346 O VAL C 329
SHEET 1 R 2 PRO C 350 VAL C 352 0
SHEET 2 R 2 PHE C 369 GLY C 371 -1 N GLY C 371 O PRO C 350
SHEET 1 S 3 PHE C 488 TYR C 490 0
SHEET 2 S 3 LEU C 356 VAL C 359 -1 N GLU C 358 O PHE C 488
SHEET 3 S 3 LEU C 362 PHE C 364 -1 N PHE C 364 O LEU C 357
SHEET 1 T 2 VAL D 85 LYS D 88 0
SHEET 2 T 2 THR D 95 ASP D 98 -1 N ASP D 98 O VAL D 85
SHEET 1 U 4 GLN D 210 ALA D 214 0
SHEET 2 U 4 ALA D 243 PHE D 247 1 N ILE D 244 O GLN D 210
SHEET 3 U 4 CYS D 367 TRP D 372 -1 N ASN D 370 O ALA D 243
SHEET 4 U 4 LEU D 349 VAL D 352 -1 N VAL D 352 O PHE D 369
SHEET 1 V 2 GLY D 269 GLN D 271 0
SHEET 2 V 2 ILE D 277 GLY D 279 -1 N ARG D 278 O TYR D 270
SHEET 1 W 2 LEU D 307 LEU D 309 0
SHEET 2 W 2 GLU D 317 PHE D 319 -1 N PHE D 319 O LEU D 307
SHEET 1 X 2 GLU D 328 ALA D 330 0
SHEET 2 X 2 LYS D 345 TYR D 347 -1 N TRP D 346 O VAL D 329
SHEET 1 Y 2 LEU D 356 GLU D 358 0
SHEET 2 Y 2 PHE D 488 TYR D 490 -1 N TYR D 490 O LEU D 356
LINK SG CYS A 115 ZN ZN A 901 1555 1555 2.29
LINK SG CYS A 110 ZN ZN A 901 1555 1555 2.32
LINK SG CYS B 115 ZN ZN A 901 1555 1555 2.32
LINK SG CYS B 110 ZN ZN A 901 1555 1555 2.28
LINK SG CYS C 115 ZN ZN C 902 1555 1555 2.32
LINK SG CYS C 110 ZN ZN C 902 1555 1555 2.33
LINK SG CYS D 115 ZN ZN C 902 1555 1555 2.32
LINK SG CYS D 110 ZN ZN C 902 1555 1555 2.36
LINK FE HEM A 550 SG CYS A 200 1555 1555 2.21
LINK FE HEM B 550 SG CYS B 200 1555 1555 2.20
LINK FE HEM C 550 SG CYS C 200 1555 1555 2.22
LINK FE HEM D 550 SG CYS D 200 1555 1555 2.24
CISPEP 1 SER A 486 PRO A 487 0 1.13
CISPEP 2 SER B 486 PRO B 487 0 -0.43
CISPEP 3 SER C 486 PRO C 487 0 0.68
CISPEP 4 SER D 486 PRO D 487 0 -0.17
SITE 1 AC1 4 ARG A 301 HOH A1015 HOH A1016 HOH A1017
SITE 1 AC2 5 LYS A 335 TYR A 336 GLU A 337 TRP A 338
SITE 2 AC2 5 ARG D 340
SITE 1 AC3 4 ASN A 236 ASN A 239 ASN C 236 ASN C 239
SITE 1 AC4 3 GLY B 300 ARG B 301 HOH B 973
SITE 1 AC5 5 LYS B 335 GLU B 337 TRP B 338 TYR D 336
SITE 2 AC5 5 HOH D 960
SITE 1 AC6 1 ARG C 301
SITE 1 AC7 6 ARG B 340 LYS C 335 TYR C 336 GLU C 337
SITE 2 AC7 6 TRP C 338 HOH C 977
SITE 1 AC8 2 ARG D 301 HOH D 961
SITE 1 AC9 5 LYS D 335 TYR D 336 GLU D 337 TRP D 338
SITE 2 AC9 5 HOH D 925
SITE 1 BC1 4 CYS A 110 CYS A 115 CYS B 110 CYS B 115
SITE 1 BC2 4 CYS C 110 CYS C 115 CYS D 110 CYS D 115
SITE 1 BC3 15 TRP A 194 ALA A 197 ARG A 199 CYS A 200
SITE 2 BC3 15 SER A 242 PHE A 369 ASN A 370 GLY A 371
SITE 3 BC3 15 TRP A 372 TRP A 463 TYR A 491 H4B A 600
SITE 4 BC3 15 ARG A 700 HOH A 943 HOH A 953
SITE 1 BC4 12 SER A 118 ARG A 381 ILE A 462 TRP A 463
SITE 2 BC4 12 HEM A 550 HOH A 964 HOH A 999 TRP B 461
SITE 3 BC4 12 PHE B 476 HIS B 477 GLN B 478 GLU B 479
SITE 1 BC5 8 GLN A 263 TYR A 347 PRO A 350 TRP A 372
SITE 2 BC5 8 TYR A 373 GLU A 377 ASP A 382 HEM A 550
SITE 1 BC6 14 TRP B 194 ARG B 199 CYS B 200 PHE B 369
SITE 2 BC6 14 ASN B 370 TRP B 372 GLU B 377 TRP B 463
SITE 3 BC6 14 TYR B 489 TYR B 491 H4B B 601 ARG B 701
SITE 4 BC6 14 HOH B 932 HOH B 995
SITE 1 BC7 14 TRP A 461 PHE A 476 HIS A 477 GLN A 478
SITE 2 BC7 14 SER B 118 ARG B 381 ILE B 462 TRP B 463
SITE 3 BC7 14 HEM B 550 HOH B 928 HOH B 932 HOH B 986
SITE 4 BC7 14 HOH B 987 HOH B 997
SITE 1 BC8 8 GLN B 263 TYR B 347 PRO B 350 TRP B 372
SITE 2 BC8 8 TYR B 373 GLU B 377 ASP B 382 HEM B 550
SITE 1 BC9 14 TRP C 194 ARG C 199 CYS C 200 SER C 242
SITE 2 BC9 14 PHE C 369 ASN C 370 GLY C 371 TRP C 372
SITE 3 BC9 14 GLU C 377 TRP C 463 TYR C 491 H4B C 602
SITE 4 BC9 14 ARG C 702 HOH C 934
SITE 1 CC1 13 SER C 118 ARG C 381 ILE C 462 TRP C 463
SITE 2 CC1 13 HEM C 550 HOH C 931 HOH C 934 HOH C 960
SITE 3 CC1 13 TRP D 461 PHE D 476 HIS D 477 GLN D 478
SITE 4 CC1 13 GLU D 479
SITE 1 CC2 7 GLN C 263 TYR C 347 TRP C 372 TYR C 373
SITE 2 CC2 7 GLU C 377 ASP C 382 HEM C 550
SITE 1 CC3 11 TRP D 194 ALA D 197 CYS D 200 PHE D 369
SITE 2 CC3 11 ASN D 370 TRP D 372 GLU D 377 TRP D 463
SITE 3 CC3 11 TYR D 491 H4B D 603 ARG D 703
SITE 1 CC4 12 TRP C 461 PHE C 476 HIS C 477 GLN C 478
SITE 2 CC4 12 GLU C 479 SER D 118 ARG D 381 ILE D 462
SITE 3 CC4 12 TRP D 463 HEM D 550 HOH D 936 HOH D 959
SITE 1 CC5 9 GLN D 263 TYR D 347 PRO D 350 TRP D 372
SITE 2 CC5 9 TYR D 373 GLU D 377 ASP D 382 HEM D 550
SITE 3 CC5 9 HOH D 944
SITE 1 CC6 5 ASP A 256 ARG A 258 GLN A 310 THR A 498
SITE 2 CC6 5 HIS A 499
SITE 1 CC7 5 ASP B 256 ARG B 258 GLN B 310 THR B 498
SITE 2 CC7 5 HIS B 499
SITE 1 CC8 6 ASP C 256 ARG C 258 GLN C 310 ALA C 495
SITE 2 CC8 6 THR C 498 HIS C 499
SITE 1 CC9 5 ASP D 256 ARG D 258 GLN D 310 THR D 498
SITE 2 CC9 5 HIS D 499
CRYST1 187.350 187.350 227.490 90.00 90.00 90.00 P 43 21 2 32
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 0.005338 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005338 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004396 0.00000
MTRIX1 1 -0.462454 -0.877798 0.124929 74.55360 1
MTRIX2 1 -0.880955 0.438969 -0.176704 55.41630 1
MTRIX3 1 0.100271 -0.191774 -0.976304 76.43760 1
MTRIX1 2 -0.873852 0.486131 -0.007712 47.98690 1
MTRIX2 2 -0.486179 -0.873599 0.021323 81.36220 1
MTRIX3 2 0.003629 0.022383 0.999743 40.33540 1
MTRIX1 3 -0.011838 0.983449 -0.180800 8.67220 1
MTRIX2 3 0.995748 0.028115 0.087728 -1.27190 1
MTRIX3 3 0.091359 -0.178993 -0.979599 117.70460 1
(ATOM LINES ARE NOT SHOWN.)
END
