HEADER OXIDOREDUCTASE 22-MAR-13 4JS9
TITLE STRUCTURAL CHARACTERIZATION OF INDUCIBLE NITRIC OXIDE SYNTHASE
TITLE 2 SUBSTITUTED WITH MESOHEME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, INDUCIBLE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: OXYGENASE DOMAIN 66-496;
COMPND 5 SYNONYM: INDUCIBLE NO SYNTHASE, INDUCIBLE NOS, INOS, MACROPHAGE NOS,
COMPND 6 MAC-NOS, NOS TYPE II, PEPTIDYL-CYSTEINE S-NITROSYLASE NOS2;
COMPND 7 EC: 1.14.13.39;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: INOSL, NOS2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS OXIDOREDUCTASE, CALMODULIN-BINDING, FAD, FMN, IRON, METAL-BINDING,
KEYWDS 2 NADP, MESOHEME
EXPDTA X-RAY DIFFRACTION
AUTHOR L.HANNIBAL,R.C.PAGE,K.BOLISETTY,Z.YU,S.MISRA,D.J.STUEHR
REVDAT 2 20-SEP-23 4JS9 1 REMARK
REVDAT 1 23-APR-14 4JS9 0
JRNL AUTH L.HANNIBAL,R.C.PAGE,K.BOLISETTY,Z.YU,S.MISRA,D.J.STUEHR
JRNL TITL KINETIC AND STRUCTURAL CHARACTERIZATION OF INDUCIBLE NITRIC
JRNL TITL 2 OXIDE SYNTHASE SUBSTITUTED WITH MESOHEME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.410
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 39436
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1970
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.0994 - 6.7045 0.97 2849 153 0.2343 0.2615
REMARK 3 2 6.7045 - 5.3237 1.00 2760 145 0.2346 0.2740
REMARK 3 3 5.3237 - 4.6513 0.99 2711 143 0.2051 0.2418
REMARK 3 4 4.6513 - 4.2263 0.99 2703 141 0.2044 0.2444
REMARK 3 5 4.2263 - 3.9235 0.98 2621 137 0.2425 0.2823
REMARK 3 6 3.9235 - 3.6923 0.99 2678 142 0.2548 0.3300
REMARK 3 7 3.6923 - 3.5074 0.99 2638 138 0.2884 0.3390
REMARK 3 8 3.5074 - 3.3548 0.99 2659 138 0.2902 0.3171
REMARK 3 9 3.3548 - 3.2256 1.00 2652 138 0.2716 0.3233
REMARK 3 10 3.2256 - 3.1144 1.00 2663 140 0.2774 0.3096
REMARK 3 11 3.1144 - 3.0170 1.00 2651 140 0.2701 0.3071
REMARK 3 12 3.0170 - 2.9308 0.99 2639 141 0.3031 0.3105
REMARK 3 13 2.9308 - 2.8536 0.99 2638 139 0.3039 0.3690
REMARK 3 14 2.8536 - 2.7840 0.98 2604 135 0.3300 0.3646
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.44
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 6875
REMARK 3 ANGLE : 1.297 9382
REMARK 3 CHIRALITY : 0.080 982
REMARK 3 PLANARITY : 0.007 1193
REMARK 3 DIHEDRAL : 14.491 2470
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4JS9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078439.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 5.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : VARIMAX CONFOCAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39539
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.780
REMARK 200 RESOLUTION RANGE LOW (A) : 72.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.44
REMARK 200 R MERGE FOR SHELL (I) : 0.29500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.8.1_1168
REMARK 200 STARTING MODEL: PDB ENTRY 3DWJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5% OCTYL-GLUCOSIDE, 20% GLYCEROL,
REMARK 280 0.7M AMMONIUM SULFATE, 0.1M 2-(N-MORPHOLINO)ETHANESULFONIC ACID,
REMARK 280 PH 5.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.51567
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 77.03133
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.77350
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 96.28917
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 19.25783
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 38.51567
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 77.03133
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 96.28917
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 57.77350
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 19.25783
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 8050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350 BIOMT1 2 0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -19.25783
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 7720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -115.54700
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B1029 LIES ON A SPECIAL POSITION.
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 66
REMARK 465 ASP A 67
REMARK 465 LYS A 68
REMARK 465 LEU A 69
REMARK 465 HIS A 70
REMARK 465 VAL A 71
REMARK 465 THR A 72
REMARK 465 SER A 73
REMARK 465 THR A 74
REMARK 465 ARG A 75
REMARK 465 PRO A 76
REMARK 465 ASP A 101
REMARK 465 PHE A 102
REMARK 465 THR A 103
REMARK 465 CYS A 104
REMARK 465 LYS A 105
REMARK 465 SER A 106
REMARK 465 LYS A 107
REMARK 465 SER A 108
REMARK 465 CYS A 109
REMARK 465 LEU A 110
REMARK 465 GLY A 111
REMARK 465 ASP A 268
REMARK 465 GLY A 269
REMARK 465 TRP A 495
REMARK 465 GLN A 496
REMARK 465 LEU B 66
REMARK 465 ASP B 67
REMARK 465 LYS B 68
REMARK 465 LEU B 69
REMARK 465 HIS B 70
REMARK 465 VAL B 71
REMARK 465 THR B 72
REMARK 465 SER B 73
REMARK 465 THR B 74
REMARK 465 ARG B 75
REMARK 465 PRO B 76
REMARK 465 GLN B 77
REMARK 465 ASP B 101
REMARK 465 PHE B 102
REMARK 465 THR B 103
REMARK 465 CYS B 104
REMARK 465 LYS B 105
REMARK 465 SER B 106
REMARK 465 LYS B 107
REMARK 465 SER B 108
REMARK 465 CYS B 109
REMARK 465 LEU B 110
REMARK 465 PRO B 267
REMARK 465 ASP B 268
REMARK 465 GLY B 269
REMARK 465 HIS B 493
REMARK 465 ILE B 494
REMARK 465 TRP B 495
REMARK 465 GLN B 496
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 126 CG CD CE NZ
REMARK 470 LYS A 149 CG CD CE NZ
REMARK 470 GLU A 150 CG CD OE1 OE2
REMARK 470 LYS A 152 CG CD CE NZ
REMARK 470 ILE A 153 CG1 CG2 CD1
REMARK 470 GLU A 154 CG CD OE1 OE2
REMARK 470 GLU A 155 CG CD OE1 OE2
REMARK 470 LYS A 165 CG CD CE NZ
REMARK 470 GLU B 150 CG CD OE1 OE2
REMARK 470 ARG B 292 CG CD NE CZ NH1 NH2
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 TYR A 78 169.97 175.99
REMARK 500 THR A 99 -155.09 -118.73
REMARK 500 ASN A 115 65.29 -113.35
REMARK 500 THR A 172 -163.18 -168.20
REMARK 500 ARG A 197 1.22 -64.80
REMARK 500 ASN A 202 73.05 -117.14
REMARK 500 SER A 245 -80.16 -110.36
REMARK 500 LYS A 329 -34.48 -136.64
REMARK 500 CYS A 361 62.45 -150.63
REMARK 500 TYR A 383 -53.68 74.33
REMARK 500 ARG A 448 25.67 -145.68
REMARK 500 THR A 492 10.84 -141.84
REMARK 500 THR B 99 -155.94 -120.05
REMARK 500 ASN B 115 66.74 -116.93
REMARK 500 THR B 172 -176.58 -177.98
REMARK 500 ARG B 197 2.41 -66.87
REMARK 500 ASN B 202 72.61 -115.85
REMARK 500 SER B 245 -80.20 -109.81
REMARK 500 LYS B 329 -34.89 -133.82
REMARK 500 CYS B 361 68.48 -151.27
REMARK 500 TYR B 383 -59.29 75.24
REMARK 500 ARG B 448 22.68 -147.93
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 MH0 A 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 194 SG
REMARK 620 2 MH0 A 501 NB 92.0
REMARK 620 3 MH0 A 501 NC 82.8 89.2
REMARK 620 4 MH0 A 501 NA 103.3 88.9 173.7
REMARK 620 5 MH0 A 501 ND 98.0 169.9 90.8 90.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MH0 B 900 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 194 SG
REMARK 620 2 MH0 B 900 NB 89.0
REMARK 620 3 MH0 B 900 NC 89.5 88.5
REMARK 620 4 MH0 B 900 NA 94.6 89.2 175.3
REMARK 620 5 MH0 B 900 ND 99.3 171.7 91.6 90.1
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 MH0 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MH0 B 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NOD RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH HEME.
DBREF 4JS9 A 66 496 UNP P29477 NOS2_MOUSE 66 496
DBREF 4JS9 B 66 496 UNP P29477 NOS2_MOUSE 66 496
SEQRES 1 A 431 LEU ASP LYS LEU HIS VAL THR SER THR ARG PRO GLN TYR
SEQRES 2 A 431 VAL ARG ILE LYS ASN TRP GLY SER GLY GLU ILE LEU HIS
SEQRES 3 A 431 ASP THR LEU HIS HIS LYS ALA THR SER ASP PHE THR CYS
SEQRES 4 A 431 LYS SER LYS SER CYS LEU GLY SER ILE MET ASN PRO LYS
SEQRES 5 A 431 SER LEU THR ARG GLY PRO ARG ASP LYS PRO THR PRO LEU
SEQRES 6 A 431 GLU GLU LEU LEU PRO HIS ALA ILE GLU PHE ILE ASN GLN
SEQRES 7 A 431 TYR TYR GLY SER PHE LYS GLU ALA LYS ILE GLU GLU HIS
SEQRES 8 A 431 LEU ALA ARG LEU GLU ALA VAL THR LYS GLU ILE GLU THR
SEQRES 9 A 431 THR GLY THR TYR GLN LEU THR LEU ASP GLU LEU ILE PHE
SEQRES 10 A 431 ALA THR LYS MET ALA TRP ARG ASN ALA PRO ARG CYS ILE
SEQRES 11 A 431 GLY ARG ILE GLN TRP SER ASN LEU GLN VAL PHE ASP ALA
SEQRES 12 A 431 ARG ASN CYS SER THR ALA GLN GLU MET PHE GLN HIS ILE
SEQRES 13 A 431 CYS ARG HIS ILE LEU TYR ALA THR ASN ASN GLY ASN ILE
SEQRES 14 A 431 ARG SER ALA ILE THR VAL PHE PRO GLN ARG SER ASP GLY
SEQRES 15 A 431 LYS HIS ASP PHE ARG LEU TRP ASN SER GLN LEU ILE ARG
SEQRES 16 A 431 TYR ALA GLY TYR GLN MET PRO ASP GLY THR ILE ARG GLY
SEQRES 17 A 431 ASP ALA ALA THR LEU GLU PHE THR GLN LEU CYS ILE ASP
SEQRES 18 A 431 LEU GLY TRP LYS PRO ARG TYR GLY ARG PHE ASP VAL LEU
SEQRES 19 A 431 PRO LEU VAL LEU GLN ALA ASP GLY GLN ASP PRO GLU VAL
SEQRES 20 A 431 PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU VAL THR MET
SEQRES 21 A 431 GLU HIS PRO LYS TYR GLU TRP PHE GLN GLU LEU GLY LEU
SEQRES 22 A 431 LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN MET LEU LEU
SEQRES 23 A 431 GLU VAL GLY GLY LEU GLU PHE PRO ALA CYS PRO PHE ASN
SEQRES 24 A 431 GLY TRP TYR MET GLY THR GLU ILE GLY VAL ARG ASP PHE
SEQRES 25 A 431 CYS ASP THR GLN ARG TYR ASN ILE LEU GLU GLU VAL GLY
SEQRES 26 A 431 ARG ARG MET GLY LEU GLU THR HIS THR LEU ALA SER LEU
SEQRES 27 A 431 TRP LYS ASP ARG ALA VAL THR GLU ILE ASN VAL ALA VAL
SEQRES 28 A 431 LEU HIS SER PHE GLN LYS GLN ASN VAL THR ILE MET ASP
SEQRES 29 A 431 HIS HIS THR ALA SER GLU SER PHE MET LYS HIS MET GLN
SEQRES 30 A 431 ASN GLU TYR ARG ALA ARG GLY GLY CYS PRO ALA ASP TRP
SEQRES 31 A 431 ILE TRP LEU VAL PRO PRO VAL SER GLY SER ILE THR PRO
SEQRES 32 A 431 VAL PHE HIS GLN GLU MET LEU ASN TYR VAL LEU SER PRO
SEQRES 33 A 431 PHE TYR TYR TYR GLN ILE GLU PRO TRP LYS THR HIS ILE
SEQRES 34 A 431 TRP GLN
SEQRES 1 B 431 LEU ASP LYS LEU HIS VAL THR SER THR ARG PRO GLN TYR
SEQRES 2 B 431 VAL ARG ILE LYS ASN TRP GLY SER GLY GLU ILE LEU HIS
SEQRES 3 B 431 ASP THR LEU HIS HIS LYS ALA THR SER ASP PHE THR CYS
SEQRES 4 B 431 LYS SER LYS SER CYS LEU GLY SER ILE MET ASN PRO LYS
SEQRES 5 B 431 SER LEU THR ARG GLY PRO ARG ASP LYS PRO THR PRO LEU
SEQRES 6 B 431 GLU GLU LEU LEU PRO HIS ALA ILE GLU PHE ILE ASN GLN
SEQRES 7 B 431 TYR TYR GLY SER PHE LYS GLU ALA LYS ILE GLU GLU HIS
SEQRES 8 B 431 LEU ALA ARG LEU GLU ALA VAL THR LYS GLU ILE GLU THR
SEQRES 9 B 431 THR GLY THR TYR GLN LEU THR LEU ASP GLU LEU ILE PHE
SEQRES 10 B 431 ALA THR LYS MET ALA TRP ARG ASN ALA PRO ARG CYS ILE
SEQRES 11 B 431 GLY ARG ILE GLN TRP SER ASN LEU GLN VAL PHE ASP ALA
SEQRES 12 B 431 ARG ASN CYS SER THR ALA GLN GLU MET PHE GLN HIS ILE
SEQRES 13 B 431 CYS ARG HIS ILE LEU TYR ALA THR ASN ASN GLY ASN ILE
SEQRES 14 B 431 ARG SER ALA ILE THR VAL PHE PRO GLN ARG SER ASP GLY
SEQRES 15 B 431 LYS HIS ASP PHE ARG LEU TRP ASN SER GLN LEU ILE ARG
SEQRES 16 B 431 TYR ALA GLY TYR GLN MET PRO ASP GLY THR ILE ARG GLY
SEQRES 17 B 431 ASP ALA ALA THR LEU GLU PHE THR GLN LEU CYS ILE ASP
SEQRES 18 B 431 LEU GLY TRP LYS PRO ARG TYR GLY ARG PHE ASP VAL LEU
SEQRES 19 B 431 PRO LEU VAL LEU GLN ALA ASP GLY GLN ASP PRO GLU VAL
SEQRES 20 B 431 PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU VAL THR MET
SEQRES 21 B 431 GLU HIS PRO LYS TYR GLU TRP PHE GLN GLU LEU GLY LEU
SEQRES 22 B 431 LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN MET LEU LEU
SEQRES 23 B 431 GLU VAL GLY GLY LEU GLU PHE PRO ALA CYS PRO PHE ASN
SEQRES 24 B 431 GLY TRP TYR MET GLY THR GLU ILE GLY VAL ARG ASP PHE
SEQRES 25 B 431 CYS ASP THR GLN ARG TYR ASN ILE LEU GLU GLU VAL GLY
SEQRES 26 B 431 ARG ARG MET GLY LEU GLU THR HIS THR LEU ALA SER LEU
SEQRES 27 B 431 TRP LYS ASP ARG ALA VAL THR GLU ILE ASN VAL ALA VAL
SEQRES 28 B 431 LEU HIS SER PHE GLN LYS GLN ASN VAL THR ILE MET ASP
SEQRES 29 B 431 HIS HIS THR ALA SER GLU SER PHE MET LYS HIS MET GLN
SEQRES 30 B 431 ASN GLU TYR ARG ALA ARG GLY GLY CYS PRO ALA ASP TRP
SEQRES 31 B 431 ILE TRP LEU VAL PRO PRO VAL SER GLY SER ILE THR PRO
SEQRES 32 B 431 VAL PHE HIS GLN GLU MET LEU ASN TYR VAL LEU SER PRO
SEQRES 33 B 431 PHE TYR TYR TYR GLN ILE GLU PRO TRP LYS THR HIS ILE
SEQRES 34 B 431 TRP GLN
HET MH0 A 501 43
HET H4B A 502 17
HET SO4 A 503 5
HET MH0 B 900 43
HET H4B B 901 17
HETNAM MH0 MESOHEME
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM SO4 SULFATE ION
FORMUL 3 MH0 2(C34 H36 FE N4 O4)
FORMUL 4 H4B 2(C9 H15 N5 O3)
FORMUL 5 SO4 O4 S 2-
FORMUL 8 HOH *164(H2 O)
HELIX 1 1 THR A 93 ALA A 98 5 6
HELIX 2 2 PRO A 116 THR A 120 5 5
HELIX 3 3 PRO A 129 GLY A 146 1 18
HELIX 4 4 LYS A 152 GLY A 171 1 20
HELIX 5 5 THR A 176 ASN A 190 1 15
HELIX 6 6 GLY A 196 TRP A 200 5 5
HELIX 7 7 THR A 213 ASN A 230 1 18
HELIX 8 8 ASN A 231 ASN A 233 5 3
HELIX 9 9 THR A 277 LEU A 287 1 11
HELIX 10 10 TYR A 330 GLY A 337 5 8
HELIX 11 11 GLY A 369 VAL A 374 1 6
HELIX 12 12 VAL A 374 ASP A 379 1 6
HELIX 13 13 ILE A 385 MET A 393 1 9
HELIX 14 14 THR A 399 SER A 402 5 4
HELIX 15 15 LEU A 403 GLN A 423 1 21
HELIX 16 16 ASP A 429 GLY A 449 1 21
HELIX 17 17 ASP A 454 VAL A 459 1 6
HELIX 18 18 SER A 463 GLN A 472 5 10
HELIX 19 19 GLU A 488 THR A 492 5 5
HELIX 20 20 THR B 93 ALA B 98 5 6
HELIX 21 21 PRO B 116 THR B 120 5 5
HELIX 22 22 PRO B 129 GLY B 146 1 18
HELIX 23 23 LYS B 152 GLY B 171 1 20
HELIX 24 24 THR B 176 ASN B 190 1 15
HELIX 25 25 GLY B 196 TRP B 200 5 5
HELIX 26 26 THR B 213 ASN B 230 1 18
HELIX 27 27 ASN B 231 ASN B 233 5 3
HELIX 28 28 THR B 277 LEU B 287 1 11
HELIX 29 29 TYR B 330 GLY B 337 5 8
HELIX 30 30 GLY B 369 VAL B 374 1 6
HELIX 31 31 VAL B 374 ASP B 379 1 6
HELIX 32 32 ILE B 385 MET B 393 1 9
HELIX 33 33 THR B 399 SER B 402 5 4
HELIX 34 34 LEU B 403 GLN B 423 1 21
HELIX 35 35 ASP B 429 GLY B 449 1 21
HELIX 36 36 ASP B 454 VAL B 459 1 6
HELIX 37 37 SER B 463 GLN B 472 5 10
HELIX 38 38 GLU B 488 THR B 492 5 5
SHEET 1 A 2 VAL A 79 LYS A 82 0
SHEET 2 A 2 ILE A 89 ASP A 92 -1 O LEU A 90 N ILE A 81
SHEET 1 B 4 GLN A 204 ASP A 207 0
SHEET 2 B 4 ALA A 237 VAL A 240 1 O ILE A 238 N PHE A 206
SHEET 3 B 4 PHE A 363 ASN A 364 -1 O ASN A 364 N ALA A 237
SHEET 4 B 4 ALA A 345 VAL A 346 -1 N VAL A 346 O PHE A 363
SHEET 1 C 3 ARG A 252 LEU A 253 0
SHEET 2 C 3 LEU A 301 GLN A 304 -1 O GLN A 304 N ARG A 252
SHEET 3 C 3 GLU A 311 PHE A 313 -1 O PHE A 313 N LEU A 301
SHEET 1 D 2 GLY A 263 GLN A 265 0
SHEET 2 D 2 ILE A 271 GLY A 273 -1 O ARG A 272 N TYR A 264
SHEET 1 E 2 GLU A 322 THR A 324 0
SHEET 2 E 2 LYS A 339 TYR A 341 -1 O TRP A 340 N VAL A 323
SHEET 1 F 3 LEU A 356 PHE A 358 0
SHEET 2 F 3 LEU A 350 VAL A 353 -1 N VAL A 353 O LEU A 356
SHEET 3 F 3 PHE A 482 TYR A 484 -1 O PHE A 482 N GLU A 352
SHEET 1 G 2 TYR A 367 MET A 368 0
SHEET 2 G 2 ILE A 427 MET A 428 1 O MET A 428 N TYR A 367
SHEET 1 H 2 VAL B 79 LYS B 82 0
SHEET 2 H 2 ILE B 89 ASP B 92 -1 O LEU B 90 N ILE B 81
SHEET 1 I 4 GLN B 204 ASP B 207 0
SHEET 2 I 4 ALA B 237 VAL B 240 1 O ILE B 238 N PHE B 206
SHEET 3 I 4 PHE B 363 ASN B 364 -1 O ASN B 364 N ALA B 237
SHEET 4 I 4 ALA B 345 VAL B 346 -1 N VAL B 346 O PHE B 363
SHEET 1 J 3 ARG B 252 LEU B 253 0
SHEET 2 J 3 LEU B 301 GLN B 304 -1 O GLN B 304 N ARG B 252
SHEET 3 J 3 GLU B 311 PHE B 313 -1 O PHE B 313 N LEU B 301
SHEET 1 K 2 GLY B 263 TYR B 264 0
SHEET 2 K 2 ARG B 272 GLY B 273 -1 O ARG B 272 N TYR B 264
SHEET 1 L 2 GLU B 322 THR B 324 0
SHEET 2 L 2 LYS B 339 TYR B 341 -1 O TRP B 340 N VAL B 323
SHEET 1 M 3 LEU B 356 PHE B 358 0
SHEET 2 M 3 LEU B 350 VAL B 353 -1 N VAL B 353 O LEU B 356
SHEET 3 M 3 PHE B 482 TYR B 484 -1 O PHE B 482 N GLU B 352
SHEET 1 N 2 TYR B 367 MET B 368 0
SHEET 2 N 2 ILE B 427 MET B 428 1 O MET B 428 N TYR B 367
LINK SG CYS A 194 FE MH0 A 501 1555 1555 2.56
LINK SG CYS B 194 FE MH0 B 900 1555 1555 2.61
CISPEP 1 SER A 480 PRO A 481 0 2.70
CISPEP 2 SER B 480 PRO B 481 0 0.66
SITE 1 AC1 13 TRP A 188 ARG A 193 CYS A 194 PHE A 363
SITE 2 AC1 13 ASN A 364 GLY A 365 TRP A 366 GLU A 371
SITE 3 AC1 13 TRP A 457 TYR A 485 H4B A 502 HOH A 645
SITE 4 AC1 13 HOH A 668
SITE 1 AC2 13 SER A 112 MET A 114 ARG A 375 TRP A 455
SITE 2 AC2 13 ILE A 456 TRP A 457 PHE A 470 GLU A 473
SITE 3 AC2 13 MH0 A 501 HOH A 668 HOH A 669 HOH A 682
SITE 4 AC2 13 HOH A 686
SITE 1 AC3 3 LYS A 97 GLN A 143 ARG A 448
SITE 1 AC4 12 TRP B 188 CYS B 194 GLY B 196 PHE B 363
SITE 2 AC4 12 ASN B 364 GLY B 365 TRP B 366 GLU B 371
SITE 3 AC4 12 TRP B 457 TYR B 485 H4B B 901 HOH B1013
SITE 1 AC5 11 SER B 112 ARG B 375 TRP B 455 ILE B 456
SITE 2 AC5 11 TRP B 457 PHE B 470 HIS B 471 MH0 B 900
SITE 3 AC5 11 HOH B1012 HOH B1047 HOH B1074
CRYST1 215.039 215.039 115.547 90.00 90.00 120.00 P 61 2 2 24
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 0.004650 0.002685 0.000000 0.00000
SCALE2 0.000000 0.005370 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008654 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
