HEADER OXIDOREDUCTASE 02-MAY-14 4D1O
TITLE STRUCTURE OF HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN WITH
TITLE 2 L-ARG BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, ENDOTHELIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 41-480;
COMPND 5 SYNONYM: CONSTITUTIVE NOS, CNOS, EC-NOS, ENDOTHELIAL NOS, ENOS, NOS
COMPND 6 TYPE III, NOSIII, CONSTITUTIVE NOS, NC-NOS, NOS TYPE I, NEURONAL NOS,
COMPND 7 N-NOS, NNOS, PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1, BNOS, NEURONAL
COMPND 8 NITRIC OXIDE SYNTHASE, NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 9 EC: 1.14.13.39;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PCWORI
KEYWDS OXIDOREDUCTASE, NITRIC OXIDE SYNTHASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,T.L.POULOS
REVDAT 3 20-DEC-23 4D1O 1 REMARK LINK
REVDAT 2 22-OCT-14 4D1O 1 JRNL
REVDAT 1 15-OCT-14 4D1O 0
JRNL AUTH H.LI,J.JAMAL,C.PLAZA,S.H.PINEDA,G.CHREIFI,Q.JING,
JRNL AUTH 2 M.A.CINELLI,R.B.SILVERMAN,T.L.POULOS
JRNL TITL STRUCTURES OF HUMAN CONSTITUTIVE NITRIC OXIDE SYNTHASES
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 2667 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 25286850
JRNL DOI 10.1107/S1399004714017064
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 95245
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4706
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 48.4094 - 5.6478 1.00 3292 149 0.1831 0.1766
REMARK 3 2 5.6478 - 4.4838 1.00 3103 168 0.1261 0.1350
REMARK 3 3 4.4838 - 3.9173 1.00 3086 167 0.1199 0.1563
REMARK 3 4 3.9173 - 3.5593 1.00 3080 150 0.1243 0.1854
REMARK 3 5 3.5593 - 3.3042 1.00 3063 161 0.1451 0.1752
REMARK 3 6 3.3042 - 3.1095 1.00 3037 162 0.1517 0.1858
REMARK 3 7 3.1095 - 2.9538 1.00 3049 137 0.1546 0.1899
REMARK 3 8 2.9538 - 2.8252 1.00 3029 161 0.1520 0.1942
REMARK 3 9 2.8252 - 2.7165 1.00 3054 148 0.1540 0.2079
REMARK 3 10 2.7165 - 2.6227 1.00 2991 186 0.1469 0.2028
REMARK 3 11 2.6227 - 2.5407 1.00 3063 152 0.1465 0.1771
REMARK 3 12 2.5407 - 2.4681 1.00 3018 143 0.1475 0.2073
REMARK 3 13 2.4681 - 2.4031 1.00 3009 148 0.1548 0.2097
REMARK 3 14 2.4031 - 2.3445 1.00 3036 152 0.1502 0.2246
REMARK 3 15 2.3445 - 2.2912 1.00 2976 158 0.1529 0.1950
REMARK 3 16 2.2912 - 2.2424 1.00 3025 155 0.1468 0.1960
REMARK 3 17 2.2424 - 2.1976 1.00 3016 153 0.1519 0.2136
REMARK 3 18 2.1976 - 2.1561 1.00 2976 156 0.1487 0.1865
REMARK 3 19 2.1561 - 2.1176 1.00 3026 173 0.1685 0.2157
REMARK 3 20 2.1176 - 2.0817 1.00 2972 154 0.1704 0.2062
REMARK 3 21 2.0817 - 2.0481 1.00 3004 157 0.1737 0.2331
REMARK 3 22 2.0481 - 2.0166 1.00 2974 168 0.1707 0.2095
REMARK 3 23 2.0166 - 1.9870 1.00 3006 151 0.1798 0.2201
REMARK 3 24 1.9870 - 1.9590 1.00 2985 154 0.1875 0.2401
REMARK 3 25 1.9590 - 1.9325 0.99 2957 184 0.2009 0.2540
REMARK 3 26 1.9325 - 1.9074 1.00 2977 167 0.2150 0.2915
REMARK 3 27 1.9074 - 1.8836 0.99 2969 156 0.2343 0.2492
REMARK 3 28 1.8836 - 1.8609 0.99 2953 169 0.2436 0.2747
REMARK 3 29 1.8609 - 1.8392 1.00 2959 140 0.2728 0.3314
REMARK 3 30 1.8392 - 1.8186 0.93 2854 127 0.3161 0.3740
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.007 6923
REMARK 3 ANGLE : 1.183 9512
REMARK 3 CHIRALITY : 0.072 982
REMARK 3 PLANARITY : 0.005 1219
REMARK 3 DIHEDRAL : 15.149 2527
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 68:480)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2053 242.5309 32.0844
REMARK 3 T TENSOR
REMARK 3 T11: 0.1394 T22: 0.1322
REMARK 3 T33: 0.1226 T12: 0.0016
REMARK 3 T13: 0.0034 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.0915 L22: 0.5595
REMARK 3 L33: 0.6711 L12: 0.0311
REMARK 3 L13: -0.0538 L23: -0.1205
REMARK 3 S TENSOR
REMARK 3 S11: 0.0290 S12: 0.0025 S13: 0.0574
REMARK 3 S21: 0.1421 S22: -0.0118 S23: 0.0129
REMARK 3 S31: -0.0718 S32: -0.0354 S33: -0.0033
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 67:480)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2571 215.2089 9.8123
REMARK 3 T TENSOR
REMARK 3 T11: 0.0906 T22: 0.1164
REMARK 3 T33: 0.1085 T12: -0.0092
REMARK 3 T13: 0.0087 T23: 0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 0.1463 L22: 0.8096
REMARK 3 L33: 0.4047 L12: 0.1728
REMARK 3 L13: -0.1047 L23: -0.1498
REMARK 3 S TENSOR
REMARK 3 S11: 0.0050 S12: -0.0113 S13: 0.0029
REMARK 3 S21: -0.0922 S22: -0.0584 S23: -0.0559
REMARK 3 S31: 0.0796 S32: 0.0058 S33: -0.0708
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 110-118 IN CHAIN A AND 107-118
REMARK 3 IN CHAIN B ARE DISORDERED
REMARK 4
REMARK 4 4D1O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1290060519.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95342
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 1.00000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1NSE
REMARK 200
REMARK 200 REMARK: RPIM 0.594 CC ONE HALF 0.533
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-12% PEG3350, 0.1M BIS TRIS, PH7.5,
REMARK 280 0.3M MG ACETATE, 0.1M GDCL3, 5 MM TCEP
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 31.19750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.66100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.04550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.66100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.19750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.04550
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: 12150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.2 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 ALA A 41
REMARK 465 PRO A 42
REMARK 465 ALA A 43
REMARK 465 SER A 44
REMARK 465 LEU A 45
REMARK 465 LEU A 46
REMARK 465 PRO A 47
REMARK 465 PRO A 48
REMARK 465 ALA A 49
REMARK 465 PRO A 50
REMARK 465 GLU A 51
REMARK 465 HIS A 52
REMARK 465 SER A 53
REMARK 465 PRO A 54
REMARK 465 PRO A 55
REMARK 465 SER A 56
REMARK 465 SER A 57
REMARK 465 PRO A 58
REMARK 465 LEU A 59
REMARK 465 THR A 60
REMARK 465 GLN A 61
REMARK 465 PRO A 62
REMARK 465 PRO A 63
REMARK 465 GLU A 64
REMARK 465 GLY A 65
REMARK 465 PRO A 66
REMARK 465 LYS A 67
REMARK 465 ARG A 107
REMARK 465 LYS A 108
REMARK 465 LEU A 109
REMARK 465 GLN A 110
REMARK 465 GLY A 111
REMARK 465 ARG A 112
REMARK 465 PRO A 113
REMARK 465 SER A 114
REMARK 465 PRO A 115
REMARK 465 GLY A 116
REMARK 465 PRO A 117
REMARK 465 PRO A 118
REMARK 465 ALA B 41
REMARK 465 PRO B 42
REMARK 465 ALA B 43
REMARK 465 SER B 44
REMARK 465 LEU B 45
REMARK 465 LEU B 46
REMARK 465 PRO B 47
REMARK 465 PRO B 48
REMARK 465 ALA B 49
REMARK 465 PRO B 50
REMARK 465 GLU B 51
REMARK 465 HIS B 52
REMARK 465 SER B 53
REMARK 465 PRO B 54
REMARK 465 PRO B 55
REMARK 465 SER B 56
REMARK 465 SER B 57
REMARK 465 PRO B 58
REMARK 465 LEU B 59
REMARK 465 THR B 60
REMARK 465 GLN B 61
REMARK 465 PRO B 62
REMARK 465 PRO B 63
REMARK 465 GLU B 64
REMARK 465 GLY B 65
REMARK 465 PRO B 66
REMARK 465 ARG B 107
REMARK 465 LYS B 108
REMARK 465 LEU B 109
REMARK 465 GLN B 110
REMARK 465 GLY B 111
REMARK 465 ARG B 112
REMARK 465 PRO B 113
REMARK 465 SER B 114
REMARK 465 PRO B 115
REMARK 465 GLY B 116
REMARK 465 PRO B 117
REMARK 465 PRO B 118
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O3 BTB A 870 O HOH A 2297 2.16
REMARK 500 O HOH B 2023 O HOH B 2024 2.17
REMARK 500 C3 BTB A 870 O HOH A 2298 2.18
REMARK 500 OD1 ASP A 91 O HOH A 2024 2.19
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 GLN A 89 -80.98 -62.96
REMARK 500 ASN A 283 29.04 -147.66
REMARK 500 ALA A 351 70.44 -155.33
REMARK 500 ARG A 372 -135.53 -118.35
REMARK 500 CYS A 441 118.02 -164.46
REMARK 500 PRO A 479 0.57 -69.03
REMARK 500 ASN B 283 26.13 -141.29
REMARK 500 ALA B 351 66.57 -158.39
REMARK 500 ARG B 372 -131.97 -117.57
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 B2387 DISTANCE = 6.06 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 900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 94 SG
REMARK 620 2 CYS A 99 SG 107.1
REMARK 620 3 CYS B 94 SG 121.6 106.4
REMARK 620 4 CYS B 99 SG 105.4 105.3 110.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 184 SG
REMARK 620 2 HEM A 500 NA 98.9
REMARK 620 3 HEM A 500 NB 99.7 85.7
REMARK 620 4 HEM A 500 NC 100.5 160.5 89.3
REMARK 620 5 HEM A 500 ND 101.3 92.0 158.9 86.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 GD A1482 GD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 BTB A 870 O6
REMARK 620 2 BTB A 870 O8 65.4
REMARK 620 3 BTB A 870 O3 135.9 103.9
REMARK 620 4 BTB A 870 N 59.5 52.7 79.7
REMARK 620 5 BTB A 870 O1 67.6 114.7 81.2 65.2
REMARK 620 6 HOH A2298 O 119.1 54.2 60.4 77.0 130.2
REMARK 620 7 HOH A2372 O 125.1 168.4 72.0 134.7 75.8 115.7
REMARK 620 8 HOH A2373 O 65.8 126.4 126.6 115.0 63.5 166.1 61.7
REMARK 620 9 HOH A2374 O 78.7 68.7 140.0 117.2 138.4 87.0 107.1 81.2
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 184 SG
REMARK 620 2 HEM B 500 NA 100.2
REMARK 620 3 HEM B 500 NB 100.4 87.0
REMARK 620 4 HEM B 500 NC 99.3 160.4 87.8
REMARK 620 5 HEM B 500 ND 100.1 88.8 159.5 89.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 GD B1482 GD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 319 O
REMARK 620 2 GLU B 321 OE1 67.2
REMARK 620 3 BTB B 870 O8 143.3 133.2
REMARK 620 4 BTB B 870 O6 136.7 69.8 69.9
REMARK 620 5 BTB B 870 N 139.4 113.3 68.2 64.7
REMARK 620 6 BTB B 870 O1 78.8 71.9 132.4 92.6 64.4
REMARK 620 7 BTB B 870 O3 87.3 135.5 88.9 128.6 63.9 67.6
REMARK 620 8 HOH B2284 O 71.9 126.0 72.1 134.7 120.7 131.7 73.4
REMARK 620 9 HOH B2285 O 83.7 69.1 79.4 76.8 136.0 140.9 146.3 73.0
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB A 870
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB A 871
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 880
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 881
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB B 870
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB B 871
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 880
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GD A 1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GD B 1482
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4D1N RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN NNOS HEME DOMAIN WITH L-ARG BOUND
REMARK 900 RELATED ID: 4D1P RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN
REMARK 900 COMPLEX WITH 6-((((3S, 5R)-5-(((6- AMINO-4-METHYLPYRIDIN-2-YL)
REMARK 900 METHOXY)METHYL)PYRROLIDIN-3 -YL)OXY) METHYL)-4-METHYLPYRIDIN-2-AMINE
DBREF 4D1O A 41 480 UNP P29474 NOS3_HUMAN 41 480
DBREF 4D1O B 41 480 UNP P29474 NOS3_HUMAN 41 480
SEQRES 1 A 440 ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER
SEQRES 2 A 440 PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO
SEQRES 3 A 440 LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE
SEQRES 4 A 440 THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY
SEQRES 5 A 440 PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE
SEQRES 6 A 440 PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO
SEQRES 7 A 440 ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE
SEQRES 8 A 440 ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN
SEQRES 9 A 440 ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL
SEQRES 10 A 440 ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU
SEQRES 11 A 440 VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG
SEQRES 12 A 440 CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE
SEQRES 13 A 440 ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR
SEQRES 14 A 440 TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY
SEQRES 15 A 440 ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS
SEQRES 16 A 440 PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU
SEQRES 17 A 440 VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL
SEQRES 18 A 440 ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS
SEQRES 19 A 440 ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP
SEQRES 20 A 440 VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO
SEQRES 21 A 440 GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL
SEQRES 22 A 440 PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU
SEQRES 23 A 440 GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET
SEQRES 24 A 440 LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO
SEQRES 25 A 440 PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG
SEQRES 26 A 440 ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP
SEQRES 27 A 440 VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER
SEQRES 28 A 440 SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL
SEQRES 29 A 440 ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE
SEQRES 30 A 440 VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS
SEQRES 31 A 440 LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA
SEQRES 32 A 440 ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU
SEQRES 33 A 440 THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU
SEQRES 34 A 440 SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP
SEQRES 1 B 440 ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER
SEQRES 2 B 440 PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO
SEQRES 3 B 440 LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE
SEQRES 4 B 440 THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY
SEQRES 5 B 440 PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE
SEQRES 6 B 440 PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO
SEQRES 7 B 440 ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE
SEQRES 8 B 440 ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN
SEQRES 9 B 440 ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL
SEQRES 10 B 440 ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU
SEQRES 11 B 440 VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG
SEQRES 12 B 440 CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE
SEQRES 13 B 440 ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR
SEQRES 14 B 440 TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY
SEQRES 15 B 440 ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS
SEQRES 16 B 440 PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU
SEQRES 17 B 440 VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL
SEQRES 18 B 440 ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS
SEQRES 19 B 440 ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP
SEQRES 20 B 440 VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO
SEQRES 21 B 440 GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL
SEQRES 22 B 440 PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU
SEQRES 23 B 440 GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET
SEQRES 24 B 440 LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO
SEQRES 25 B 440 PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG
SEQRES 26 B 440 ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP
SEQRES 27 B 440 VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER
SEQRES 28 B 440 SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL
SEQRES 29 B 440 ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE
SEQRES 30 B 440 VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS
SEQRES 31 B 440 LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA
SEQRES 32 B 440 ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU
SEQRES 33 B 440 THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU
SEQRES 34 B 440 SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP
HET ARG A 700 12
HET HEM A 500 43
HET ACT A 860 4
HET BTB A 870 14
HET BTB A 871 14
HET GOL A 880 6
HET GOL A 881 6
HET ZN A 900 1
HET H4B A1481 17
HET GD A1482 1
HET ARG B 700 12
HET HEM B 500 43
HET ACT B 860 4
HET BTB B 870 14
HET BTB B 871 14
HET GOL B 880 6
HET H4B B1481 17
HET GD B1482 1
HETNAM ARG ARGININE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM ACT ACETATE ION
HETNAM BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-
HETNAM 2 BTB PROPANE-1,3-DIOL
HETNAM GOL GLYCEROL
HETNAM ZN ZINC ION
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM GD GADOLINIUM ATOM
HETSYN HEM HEME
HETSYN BTB BIS-TRIS BUFFER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ARG 2(C6 H15 N4 O2 1+)
FORMUL 4 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 ACT 2(C2 H3 O2 1-)
FORMUL 6 BTB 4(C8 H19 N O5)
FORMUL 8 GOL 3(C3 H8 O3)
FORMUL 10 ZN ZN 2+
FORMUL 11 H4B 2(C9 H15 N5 O3)
FORMUL 12 GD 2(GD)
FORMUL 21 HOH *766(H2 O)
HELIX 1 1 THR A 83 ALA A 88 5 6
HELIX 2 2 ALA A 119 ILE A 138 1 20
HELIX 3 3 SER A 143 GLY A 161 1 19
HELIX 4 4 ARG A 166 ASN A 180 1 15
HELIX 5 5 GLY A 186 TRP A 190 5 5
HELIX 6 6 SER A 203 ASN A 220 1 18
HELIX 7 7 ARG A 221 ASN A 223 5 3
HELIX 8 8 ASN A 267 HIS A 277 1 11
HELIX 9 9 PRO A 306 VAL A 310 5 5
HELIX 10 10 TRP A 322 GLY A 327 5 6
HELIX 11 11 SER A 359 THR A 364 1 6
HELIX 12 12 THR A 364 ASP A 369 1 6
HELIX 13 13 ILE A 375 MET A 383 1 9
HELIX 14 14 THR A 389 SER A 392 5 4
HELIX 15 15 LEU A 393 ALA A 413 1 21
HELIX 16 16 ASP A 419 GLY A 439 1 21
HELIX 17 17 ASP A 444 VAL A 449 1 6
HELIX 18 18 SER A 453 THR A 457 5 5
HELIX 19 19 THR A 457 HIS A 461 5 5
HELIX 20 20 THR B 83 ALA B 88 5 6
HELIX 21 21 ALA B 119 ILE B 138 1 20
HELIX 22 22 SER B 143 GLY B 161 1 19
HELIX 23 23 ARG B 166 ASN B 180 1 15
HELIX 24 24 GLY B 186 TRP B 190 5 5
HELIX 25 25 SER B 203 ASN B 220 1 18
HELIX 26 26 ARG B 221 ASN B 223 5 3
HELIX 27 27 ASN B 267 HIS B 277 1 11
HELIX 28 28 PRO B 306 VAL B 310 5 5
HELIX 29 29 LEU B 320 GLY B 327 5 8
HELIX 30 30 SER B 359 THR B 364 1 6
HELIX 31 31 THR B 364 ASP B 369 1 6
HELIX 32 32 ILE B 375 MET B 383 1 9
HELIX 33 33 THR B 389 SER B 392 5 4
HELIX 34 34 LEU B 393 ALA B 413 1 21
HELIX 35 35 ASP B 419 GLY B 439 1 21
HELIX 36 36 ASP B 444 VAL B 449 1 6
HELIX 37 37 SER B 453 THR B 457 5 5
HELIX 38 38 THR B 457 HIS B 461 5 5
SHEET 1 AA 2 ARG A 70 LYS A 72 0
SHEET 2 AA 2 ILE A 79 TYR A 81 -1 O THR A 80 N VAL A 71
SHEET 1 AB 4 GLN A 194 ASP A 197 0
SHEET 2 AB 4 ALA A 227 VAL A 230 1 O ILE A 228 N PHE A 196
SHEET 3 AB 4 PHE A 353 SER A 354 -1 O SER A 354 N ALA A 227
SHEET 4 AB 4 ALA A 335 VAL A 336 -1 O VAL A 336 N PHE A 353
SHEET 1 AC 3 ARG A 242 ILE A 243 0
SHEET 2 AC 3 LEU A 291 GLN A 294 -1 O GLN A 294 N ARG A 242
SHEET 3 AC 3 GLU A 301 PHE A 303 -1 O GLU A 301 N LEU A 293
SHEET 1 AD 2 GLY A 253 ARG A 255 0
SHEET 2 AD 2 VAL A 261 GLY A 263 -1 O ARG A 262 N TYR A 254
SHEET 1 AE 2 GLU A 312 PRO A 314 0
SHEET 2 AE 2 ARG A 329 TYR A 331 -1 O TRP A 330 N VAL A 313
SHEET 1 AF 3 LEU A 346 PHE A 348 0
SHEET 2 AF 3 LEU A 340 ILE A 343 -1 O LEU A 341 N PHE A 348
SHEET 3 AF 3 ALA A 472 ARG A 474 -1 O ALA A 472 N GLU A 342
SHEET 1 AG 2 TYR A 357 MET A 358 0
SHEET 2 AG 2 ILE A 417 VAL A 418 1 N VAL A 418 O TYR A 357
SHEET 1 BA 2 ARG B 70 LYS B 72 0
SHEET 2 BA 2 ILE B 79 TYR B 81 -1 O THR B 80 N VAL B 71
SHEET 1 BB 4 GLN B 194 ASP B 197 0
SHEET 2 BB 4 ALA B 227 VAL B 230 1 O ILE B 228 N PHE B 196
SHEET 3 BB 4 PHE B 353 SER B 354 -1 O SER B 354 N ALA B 227
SHEET 4 BB 4 ALA B 335 VAL B 336 -1 O VAL B 336 N PHE B 353
SHEET 1 BC 3 ARG B 242 ILE B 243 0
SHEET 2 BC 3 LEU B 291 GLN B 294 -1 O GLN B 294 N ARG B 242
SHEET 3 BC 3 GLU B 301 PHE B 303 -1 O GLU B 301 N LEU B 293
SHEET 1 BD 2 GLY B 253 ARG B 255 0
SHEET 2 BD 2 VAL B 261 GLY B 263 -1 O ARG B 262 N TYR B 254
SHEET 1 BE 2 GLU B 312 PRO B 314 0
SHEET 2 BE 2 ARG B 329 TYR B 331 -1 O TRP B 330 N VAL B 313
SHEET 1 BF 3 LEU B 346 PHE B 348 0
SHEET 2 BF 3 LEU B 340 ILE B 343 -1 O LEU B 341 N PHE B 348
SHEET 3 BF 3 ALA B 472 ARG B 474 -1 O ALA B 472 N GLU B 342
SHEET 1 BG 2 TYR B 357 MET B 358 0
SHEET 2 BG 2 ILE B 417 VAL B 418 1 N VAL B 418 O TYR B 357
LINK SG CYS A 94 ZN ZN A 900 1555 1555 2.39
LINK SG CYS A 99 ZN ZN A 900 1555 1555 2.34
LINK SG CYS A 184 FE HEM A 500 1555 1555 2.36
LINK O6 BTB A 870 GD GD A1482 1555 1555 2.47
LINK O8 BTB A 870 GD GD A1482 1555 1555 2.75
LINK O3 BTB A 870 GD GD A1482 1555 1555 2.45
LINK N BTB A 870 GD GD A1482 1555 1555 2.86
LINK O1 BTB A 870 GD GD A1482 1555 1555 2.26
LINK ZN ZN A 900 SG CYS B 94 1555 1555 2.32
LINK ZN ZN A 900 SG CYS B 99 1555 1555 2.31
LINK GD GD A1482 O HOH A2298 1555 1555 2.14
LINK GD GD A1482 O HOH A2372 1555 1555 2.76
LINK GD GD A1482 O HOH A2373 1555 1555 2.53
LINK GD GD A1482 O HOH A2374 1555 1555 2.52
LINK GD GD A1482 O HOH A2379 1555 1555 2.88
LINK SG CYS B 184 FE HEM B 500 1555 1555 2.35
LINK O THR B 319 GD GD B1482 1555 1555 2.21
LINK OE1 GLU B 321 GD GD B1482 1555 1555 2.47
LINK O8 BTB B 870 GD GD B1482 1555 1555 2.29
LINK O6 BTB B 870 GD GD B1482 1555 1555 2.35
LINK N BTB B 870 GD GD B1482 1555 1555 2.72
LINK O1 BTB B 870 GD GD B1482 1555 1555 2.25
LINK O3 BTB B 870 GD GD B1482 1555 1555 2.44
LINK GD GD B1482 O HOH B2284 1555 1555 2.40
LINK GD GD B1482 O HOH B2285 1555 1555 2.44
CISPEP 1 SER A 470 PRO A 471 0 -3.46
CISPEP 2 SER B 470 PRO B 471 0 2.46
SITE 1 AC1 20 TRP A 178 ARG A 183 CYS A 184 SER A 226
SITE 2 AC1 20 PHE A 353 SER A 354 TRP A 356 MET A 358
SITE 3 AC1 20 GLU A 361 TRP A 447 PHE A 473 TYR A 475
SITE 4 AC1 20 ARG A 700 ACT A 860 H4B A1481 HOH A2365
SITE 5 AC1 20 HOH A2366 HOH A2368 HOH A2369 HOH A2370
SITE 1 AC2 8 GLN A 247 TYR A 331 TRP A 356 TYR A 357
SITE 2 AC2 8 GLU A 361 ASN A 366 HEM A 500 HOH A2278
SITE 1 AC3 6 GLY A 186 TRP A 356 VAL A 418 SER A 426
SITE 2 AC3 6 HEM A 500 HOH A2128
SITE 1 AC4 9 VAL A 381 CYS A 382 ASP A 384 GD A1482
SITE 2 AC4 9 HOH A2297 HOH A2298 HOH A2372 HOH A2373
SITE 3 AC4 9 HOH A2374
SITE 1 AC5 2 GLU A 377 HOH A2375
SITE 1 AC6 6 ARG A 365 HIS A 371 H4B A1481 HOH A2281
SITE 2 AC6 6 HOH A2282 HOH A2376
SITE 1 AC7 3 GLU A 167 HOH A2377 HOH A2378
SITE 1 AC8 4 CYS A 94 CYS A 99 CYS B 94 CYS B 99
SITE 1 AC9 14 SER A 102 ARG A 365 ALA A 446 TRP A 447
SITE 2 AC9 14 HEM A 500 GOL A 880 HOH A2056 HOH A2281
SITE 3 AC9 14 HOH A2339 HOH A2370 TRP B 445 PHE B 460
SITE 4 AC9 14 HIS B 461 GLU B 463
SITE 1 BC1 19 TRP B 178 ARG B 183 CYS B 184 SER B 226
SITE 2 BC1 19 PHE B 353 SER B 354 TRP B 356 MET B 358
SITE 3 BC1 19 GLU B 361 TRP B 447 PHE B 473 TYR B 475
SITE 4 BC1 19 ARG B 700 H4B B1481 HOH B2373 HOH B2374
SITE 5 BC1 19 HOH B2380 HOH B2381 HOH B2382
SITE 1 BC2 10 GLN B 247 ARG B 250 TYR B 331 TRP B 356
SITE 2 BC2 10 TYR B 357 GLU B 361 ASN B 366 HEM B 500
SITE 3 BC2 10 HOH B2233 HOH B2304
SITE 1 BC3 4 TRP B 356 SER B 426 HOH B2140 HOH B2383
SITE 1 BC4 8 THR B 319 GLU B 321 GD B1482 HOH B2284
SITE 2 BC4 8 HOH B2285 HOH B2384 HOH B2385 HOH B2386
SITE 1 BC5 1 GLU B 298
SITE 1 BC6 7 TRP A 74 HOH A2350 VAL B 104 ARG B 365
SITE 2 BC6 7 HIS B 371 H4B B1481 HOH B2205
SITE 1 BC7 13 TRP A 445 PHE A 460 HIS A 461 HOH A2350
SITE 2 BC7 13 SER B 102 ARG B 365 ALA B 446 TRP B 447
SITE 3 BC7 13 HEM B 500 GOL B 880 HOH B2047 HOH B2361
SITE 4 BC7 13 HOH B2382
SITE 1 BC8 7 BTB A 870 HOH A2298 HOH A2299 HOH A2372
SITE 2 BC8 7 HOH A2373 HOH A2374 HOH A2379
SITE 1 BC9 5 THR B 319 GLU B 321 BTB B 870 HOH B2284
SITE 2 BC9 5 HOH B2285
CRYST1 62.395 110.091 153.322 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 0.016027 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006522 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
