HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 31-JAN-17 5UO3
TITLE STRUCTURE OF HUMAN NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN
TITLE 2 COMPLEX WITH 3-[(2-AMINO-4-METHYLQUINOLIN-7-YL)METHOXY]-5-
TITLE 3 ((METHYLAMINO)METHYL)BENZONITRILE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 302-722;
COMPND 5 SYNONYM: CONSTITUTIVE NOS, NC-NOS, NOS TYPE I, NEURONAL NOS, NNOS,
COMPND 6 PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1, BNOS;
COMPND 7 EC: 1.14.13.39;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 GENE: NOS1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS NITRIC, OXIDE, SYNTHASE, INHIBITOR, COMPLEX, HEME, ENZYME,
KEYWDS 2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,T.L.POULOS
REVDAT 5 04-OCT-23 5UO3 1 REMARK
REVDAT 4 25-DEC-19 5UO3 1 REMARK
REVDAT 3 13-SEP-17 5UO3 1 REMARK
REVDAT 2 24-MAY-17 5UO3 1 JRNL
REVDAT 1 03-MAY-17 5UO3 0
JRNL AUTH M.A.CINELLI,H.LI,G.CHREIFI,T.L.POULOS,R.B.SILVERMAN
JRNL TITL NITRILE IN THE HOLE: DISCOVERY OF A SMALL AUXILIARY POCKET
JRNL TITL 2 IN NEURONAL NITRIC OXIDE SYNTHASE LEADING TO THE DEVELOPMENT
JRNL TITL 3 OF POTENT AND SELECTIVE 2-AMINOQUINOLINE INHIBITORS.
JRNL REF J. MED. CHEM. V. 60 3958 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28422508
JRNL DOI 10.1021/ACS.JMEDCHEM.7B00259
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 55068
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 2692
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 57.7672 - 6.8323 1.00 3337 136 0.1590 0.1851
REMARK 3 2 6.8323 - 5.4243 1.00 3316 169 0.1539 0.1759
REMARK 3 3 5.4243 - 4.7390 1.00 3316 162 0.1292 0.1827
REMARK 3 4 4.7390 - 4.3058 1.00 3328 172 0.1180 0.1411
REMARK 3 5 4.3058 - 3.9973 1.00 3288 168 0.1251 0.1764
REMARK 3 6 3.9973 - 3.7617 1.00 3303 184 0.1292 0.1721
REMARK 3 7 3.7617 - 3.5733 1.00 3326 189 0.1335 0.1901
REMARK 3 8 3.5733 - 3.4178 1.00 3286 171 0.1496 0.2080
REMARK 3 9 3.4178 - 3.2862 1.00 3289 178 0.1558 0.2291
REMARK 3 10 3.2862 - 3.1728 1.00 3335 162 0.1828 0.2350
REMARK 3 11 3.1728 - 3.0736 1.00 3299 158 0.1856 0.2430
REMARK 3 12 3.0736 - 2.9858 1.00 3360 167 0.1898 0.2458
REMARK 3 13 2.9858 - 2.9072 1.00 3252 173 0.1916 0.2504
REMARK 3 14 2.9072 - 2.8363 1.00 3377 160 0.1918 0.2117
REMARK 3 15 2.8363 - 2.7718 1.00 3316 150 0.2036 0.2592
REMARK 3 16 2.7718 - 2.7128 1.00 3370 134 0.2193 0.2898
REMARK 3 17 2.7128 - 2.6585 1.00 3300 190 0.2323 0.2719
REMARK 3 18 2.6585 - 2.6084 1.00 3265 190 0.2312 0.2728
REMARK 3 19 2.6084 - 2.5618 1.00 3314 166 0.2338 0.2983
REMARK 3 20 2.5618 - 2.5183 1.00 3345 163 0.2437 0.3173
REMARK 3 21 2.5183 - 2.4777 1.00 3274 199 0.2631 0.2928
REMARK 3 22 2.4777 - 2.4396 1.00 3329 179 0.2812 0.3642
REMARK 3 23 2.4396 - 2.4037 1.00 3275 190 0.2922 0.3876
REMARK 3 24 2.4037 - 2.3699 1.00 3299 181 0.2809 0.3074
REMARK 3 25 2.3699 - 2.3378 1.00 3309 205 0.2893 0.3969
REMARK 3 26 2.3378 - 2.3075 1.00 3313 143 0.3044 0.3034
REMARK 3 27 2.3075 - 2.2786 1.00 3222 178 0.3167 0.3544
REMARK 3 28 2.2786 - 2.2512 1.00 3418 153 0.3258 0.3818
REMARK 3 29 2.2512 - 2.2250 0.99 3305 176 0.3556 0.4019
REMARK 3 30 2.2250 - 2.2000 1.00 3303 147 0.3333 0.3798
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.420
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 : 0.008 7129
REMARK 3 ANGLE : 1.124 9707
REMARK 3 CHIRALITY : 0.070 997
REMARK 3 PLANARITY : 0.005 1222
REMARK 3 DIHEDRAL : 15.389 2586
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 302:721)
REMARK 3 ORIGIN FOR THE GROUP (A): 117.5982 251.5820 359.7454
REMARK 3 T TENSOR
REMARK 3 T11: 0.1844 T22: 0.2642
REMARK 3 T33: 0.2485 T12: -0.0208
REMARK 3 T13: 0.0346 T23: 0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 0.4619 L22: 1.0666
REMARK 3 L33: 1.3164 L12: -0.1409
REMARK 3 L13: 0.1784 L23: 0.1460
REMARK 3 S TENSOR
REMARK 3 S11: 0.0185 S12: 0.0353 S13: 0.0461
REMARK 3 S21: -0.0567 S22: -0.0622 S23: -0.0412
REMARK 3 S31: 0.0678 S32: 0.1188 S33: 0.0397
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 304:721)
REMARK 3 ORIGIN FOR THE GROUP (A): 115.9584 250.5403 322.5020
REMARK 3 T TENSOR
REMARK 3 T11: 0.2216 T22: 0.2717
REMARK 3 T33: 0.2569 T12: -0.0055
REMARK 3 T13: 0.0290 T23: -0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 0.5019 L22: 0.7914
REMARK 3 L33: 2.3486 L12: -0.1506
REMARK 3 L13: 0.0718 L23: 0.0950
REMARK 3 S TENSOR
REMARK 3 S11: 0.0185 S12: 0.0042 S13: 0.0142
REMARK 3 S21: 0.0379 S22: -0.0641 S23: 0.0912
REMARK 3 S31: -0.0061 S32: -0.0656 S33: 0.0380
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 5UO3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1000223039.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
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 : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.1.0
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55149
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.14800
REMARK 200 R SYM (I) : 0.14800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 1.84600
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5.8.0049
REMARK 200 STARTING MODEL: PDB ENTRY 4UH5
REMARK 200
REMARK 200 REMARK: PLATE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG3350, 35 MM CITRIC ACID, 65 MM
REMARK 280 BIS-TRIS PROPANE, 10% GLYCEROL, 5 MM TCEP, PH 7.2, VAPOR
REMARK 280 DIFFUSION, SITTING DROP
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 26.17500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.31500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.66550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.31500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.17500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.66550
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: 9250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 344
REMARK 465 GLN A 345
REMARK 465 HIS A 346
REMARK 465 ALA A 347
REMARK 465 ARG A 348
REMARK 465 ARG A 349
REMARK 465 PRO A 350
REMARK 465 GLU A 351
REMARK 465 CYS B 302
REMARK 465 PRO B 303
REMARK 465 GLN B 345
REMARK 465 HIS B 346
REMARK 465 ALA B 347
REMARK 465 ARG B 348
REMARK 465 ARG B 349
REMARK 465 PRO B 350
REMARK 465 GLU B 351
REMARK 465 ASP B 352
REMARK 465 VAL B 353
REMARK 465 LYS B 722
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 314 -2.94 63.68
REMARK 500 THR A 326 -64.74 -100.88
REMARK 500 THR A 471 -90.79 -108.96
REMARK 500 CYS A 587 59.90 -150.82
REMARK 500 ARG A 608 -139.02 -123.10
REMARK 500 ARG B 376 25.54 -141.88
REMARK 500 THR B 471 -75.16 -108.60
REMARK 500 ASP B 494 22.18 -78.30
REMARK 500 SER B 496 -162.29 -73.13
REMARK 500 CYS B 587 54.38 -155.04
REMARK 500 ARG B 608 -140.90 -120.96
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 B1109 DISTANCE = 5.82 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 B 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 331 SG
REMARK 620 2 CYS A 336 SG 109.9
REMARK 620 3 CYS B 331 SG 122.7 104.5
REMARK 620 4 CYS B 336 SG 102.3 98.1 116.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 420 SG
REMARK 620 2 HEM A 801 NA 99.9
REMARK 620 3 HEM A 801 NB 99.1 88.7
REMARK 620 4 HEM A 801 NC 97.8 162.2 87.2
REMARK 620 5 HEM A 801 ND 101.6 88.7 159.3 89.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 802 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 420 SG
REMARK 620 2 HEM B 802 NA 100.8
REMARK 620 3 HEM B 802 NB 97.9 86.8
REMARK 620 4 HEM B 802 NC 93.2 165.9 89.9
REMARK 620 5 HEM B 802 ND 100.1 92.6 161.7 86.3
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 HEM A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8EY A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8EY A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8EY B 804
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UNR RELATED DB: PDB
REMARK 900 RELATED ID: 5UNU RELATED DB: PDB
REMARK 900 RELATED ID: 5UNX RELATED DB: PDB
REMARK 900 RELATED ID: 5UNW RELATED DB: PDB
REMARK 900 RELATED ID: 5UO1 RELATED DB: PDB
REMARK 900 RELATED ID: 5UNY RELATED DB: PDB
REMARK 900 RELATED ID: 5UO5 RELATED DB: PDB
REMARK 900 RELATED ID: 5UO4 RELATED DB: PDB
REMARK 900 RELATED ID: 5UO6 RELATED DB: PDB
REMARK 900 RELATED ID: 5UO7 RELATED DB: PDB
REMARK 900 RELATED ID: 5UO8 RELATED DB: PDB
REMARK 900 RELATED ID: 5UO2 RELATED DB: PDB
REMARK 900 RELATED ID: 5UNS RELATED DB: PDB
REMARK 900 RELATED ID: 5UNZ RELATED DB: PDB
REMARK 900 RELATED ID: 5UO0 RELATED DB: PDB
REMARK 900 RELATED ID: 5UNT RELATED DB: PDB
REMARK 900 RELATED ID: 5UNV RELATED DB: PDB
REMARK 900 RELATED ID: 5UOD RELATED DB: PDB
REMARK 900 RELATED ID: 5UO9 RELATED DB: PDB
REMARK 900 RELATED ID: 5UOA RELATED DB: PDB
REMARK 900 RELATED ID: 5UOB RELATED DB: PDB
REMARK 900 RELATED ID: 5UOC RELATED DB: PDB
DBREF 5UO3 A 302 722 UNP P29475 NOS1_HUMAN 302 722
DBREF 5UO3 B 302 722 UNP P29475 NOS1_HUMAN 302 722
SEQADV 5UO3 ALA A 354 UNP P29475 ARG 354 ENGINEERED MUTATION
SEQADV 5UO3 ASP A 357 UNP P29475 GLY 357 ENGINEERED MUTATION
SEQADV 5UO3 ALA B 354 UNP P29475 ARG 354 ENGINEERED MUTATION
SEQADV 5UO3 ASP B 357 UNP P29475 GLY 357 ENGINEERED MUTATION
SEQRES 1 A 421 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR GLU
SEQRES 2 A 421 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 A 421 GLU THR GLY CYS THR GLU TYR ILE CYS MET GLY SER ILE
SEQRES 4 A 421 MET HIS PRO SER GLN HIS ALA ARG ARG PRO GLU ASP VAL
SEQRES 5 A 421 ALA THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 A 421 ILE ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 A 421 LYS ALA HIS MET GLU ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 A 421 ILE ASP THR THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 A 421 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 A 421 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 A 421 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 A 421 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 A 421 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 A 421 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 A 421 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 A 421 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 A 421 CYS ILE GLN GLN GLY TRP LYS PRO PRO ARG GLY ARG PHE
SEQRES 18 A 421 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 A 421 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 A 421 VAL PRO ILE ARG HIS PRO LYS PHE GLU TRP PHE LYS ASP
SEQRES 21 A 421 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 A 421 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 A 421 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 A 421 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 A 421 GLU VAL ALA LYS LYS MET ASN LEU ASP MET ARG LYS THR
SEQRES 26 A 421 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 A 421 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 A 421 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 A 421 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 A 421 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 A 421 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 A 421 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 A 421 THR HIS VAL TRP LYS
SEQRES 1 B 421 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR GLU
SEQRES 2 B 421 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 B 421 GLU THR GLY CYS THR GLU TYR ILE CYS MET GLY SER ILE
SEQRES 4 B 421 MET HIS PRO SER GLN HIS ALA ARG ARG PRO GLU ASP VAL
SEQRES 5 B 421 ALA THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 B 421 ILE ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 B 421 LYS ALA HIS MET GLU ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 B 421 ILE ASP THR THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 B 421 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 B 421 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 B 421 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 B 421 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 B 421 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 B 421 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 B 421 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 B 421 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 B 421 CYS ILE GLN GLN GLY TRP LYS PRO PRO ARG GLY ARG PHE
SEQRES 18 B 421 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 B 421 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 B 421 VAL PRO ILE ARG HIS PRO LYS PHE GLU TRP PHE LYS ASP
SEQRES 21 B 421 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 B 421 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 B 421 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 B 421 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 B 421 GLU VAL ALA LYS LYS MET ASN LEU ASP MET ARG LYS THR
SEQRES 26 B 421 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 B 421 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 B 421 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 B 421 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 B 421 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 B 421 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 B 421 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 B 421 THR HIS VAL TRP LYS
HET HEM A 801 43
HET H4B A 802 17
HET 8EY A 803 25
HET 8EY A 804 25
HET ZN B 801 1
HET HEM B 802 43
HET H4B B 803 17
HET 8EY B 804 25
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM 8EY 3-[(2-AMINO-4-METHYLQUINOLIN-7-YL)METHOXY]-5-
HETNAM 2 8EY [(METHYLAMINO)METHYL]BENZONITRILE
HETNAM ZN ZINC ION
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 H4B 2(C9 H15 N5 O3)
FORMUL 5 8EY 3(C20 H20 N4 O)
FORMUL 7 ZN ZN 2+
FORMUL 11 HOH *487(H2 O)
HELIX 1 AA1 THR A 320 SER A 325 5 6
HELIX 2 AA2 THR A 355 ILE A 374 1 20
HELIX 3 AA3 SER A 379 SER A 397 1 19
HELIX 4 AA4 LYS A 402 ASN A 416 1 15
HELIX 5 AA5 GLY A 422 TRP A 426 5 5
HELIX 6 AA6 THR A 439 ASN A 456 1 18
HELIX 7 AA7 LYS A 457 ASN A 459 5 3
HELIX 8 AA8 ASN A 503 GLN A 513 1 11
HELIX 9 AA9 PRO A 542 VAL A 546 5 5
HELIX 10 AB1 PHE A 556 GLY A 563 5 8
HELIX 11 AB2 GLY A 595 VAL A 600 1 6
HELIX 12 AB3 VAL A 600 ASP A 605 1 6
HELIX 13 AB4 ILE A 611 MET A 619 1 9
HELIX 14 AB5 LYS A 625 SER A 628 5 4
HELIX 15 AB6 LEU A 629 ASP A 649 1 21
HELIX 16 AB7 ASP A 655 GLY A 675 1 21
HELIX 17 AB8 ASP A 680 VAL A 685 1 6
HELIX 18 AB9 SER A 689 THR A 693 5 5
HELIX 19 AC1 ASP A 714 HIS A 719 1 6
HELIX 20 AC2 THR B 320 SER B 325 5 6
HELIX 21 AC3 THR B 355 ILE B 374 1 20
HELIX 22 AC4 SER B 379 SER B 397 1 19
HELIX 23 AC5 LYS B 402 ASN B 416 1 15
HELIX 24 AC6 GLY B 422 TRP B 426 5 5
HELIX 25 AC7 THR B 439 ASN B 456 1 18
HELIX 26 AC8 LYS B 457 ASN B 459 5 3
HELIX 27 AC9 ASN B 503 GLN B 513 1 11
HELIX 28 AD1 PRO B 542 VAL B 546 5 5
HELIX 29 AD2 PHE B 556 GLY B 563 5 8
HELIX 30 AD3 GLY B 595 VAL B 600 1 6
HELIX 31 AD4 VAL B 600 ASP B 605 1 6
HELIX 32 AD5 ILE B 611 MET B 619 1 9
HELIX 33 AD6 LYS B 625 SER B 628 5 4
HELIX 34 AD7 LEU B 629 ASP B 649 1 21
HELIX 35 AD8 ASP B 655 GLY B 675 1 21
HELIX 36 AD9 ASP B 680 VAL B 685 1 6
HELIX 37 AE1 SER B 689 THR B 693 5 5
HELIX 38 AE2 ASP B 714 THR B 718 5 5
SHEET 1 AA1 2 LEU A 306 LYS A 309 0
SHEET 2 AA1 2 VAL A 316 ASP A 319 -1 O ASP A 319 N LEU A 306
SHEET 1 AA2 4 GLN A 430 ASP A 433 0
SHEET 2 AA2 4 ALA A 463 ILE A 466 1 O ILE A 464 N PHE A 432
SHEET 3 AA2 4 PHE A 589 SER A 590 -1 O SER A 590 N ALA A 463
SHEET 4 AA2 4 ALA A 571 VAL A 572 -1 N VAL A 572 O PHE A 589
SHEET 1 AA3 3 ARG A 478 VAL A 479 0
SHEET 2 AA3 3 LEU A 527 GLN A 530 -1 O GLN A 530 N ARG A 478
SHEET 3 AA3 3 GLU A 537 PHE A 539 -1 O PHE A 539 N LEU A 527
SHEET 1 AA4 2 GLY A 489 LYS A 491 0
SHEET 2 AA4 2 THR A 497 GLY A 499 -1 O LEU A 498 N TYR A 490
SHEET 1 AA5 2 GLU A 548 PRO A 550 0
SHEET 2 AA5 2 LYS A 565 TYR A 567 -1 O TRP A 566 N VAL A 549
SHEET 1 AA6 3 LEU A 582 PHE A 584 0
SHEET 2 AA6 3 LEU A 576 ILE A 579 -1 N LEU A 577 O PHE A 584
SHEET 3 AA6 3 SER A 708 GLU A 710 -1 O GLU A 710 N LEU A 576
SHEET 1 AA7 2 TYR A 593 MET A 594 0
SHEET 2 AA7 2 ILE A 653 VAL A 654 1 O VAL A 654 N TYR A 593
SHEET 1 AA8 2 LEU B 306 LYS B 309 0
SHEET 2 AA8 2 VAL B 316 ASP B 319 -1 O ASP B 319 N LEU B 306
SHEET 1 AA9 4 GLN B 430 ASP B 433 0
SHEET 2 AA9 4 ALA B 463 ILE B 466 1 O ILE B 464 N PHE B 432
SHEET 3 AA9 4 PHE B 589 SER B 590 -1 O SER B 590 N ALA B 463
SHEET 4 AA9 4 ALA B 571 VAL B 572 -1 N VAL B 572 O PHE B 589
SHEET 1 AB1 3 ARG B 478 VAL B 479 0
SHEET 2 AB1 3 LEU B 527 GLN B 530 -1 O GLN B 530 N ARG B 478
SHEET 3 AB1 3 GLU B 537 PHE B 539 -1 O GLU B 537 N LEU B 529
SHEET 1 AB2 2 GLY B 489 LYS B 491 0
SHEET 2 AB2 2 THR B 497 GLY B 499 -1 O LEU B 498 N TYR B 490
SHEET 1 AB3 2 GLU B 548 PRO B 550 0
SHEET 2 AB3 2 LYS B 565 TYR B 567 -1 O TRP B 566 N VAL B 549
SHEET 1 AB4 3 LEU B 582 PHE B 584 0
SHEET 2 AB4 3 LEU B 576 ILE B 579 -1 N LEU B 577 O PHE B 584
SHEET 3 AB4 3 SER B 708 GLU B 710 -1 O SER B 708 N GLU B 578
SHEET 1 AB5 2 TYR B 593 MET B 594 0
SHEET 2 AB5 2 ILE B 653 VAL B 654 1 O VAL B 654 N TYR B 593
LINK SG CYS A 331 ZN ZN B 801 1555 1555 2.30
LINK SG CYS A 336 ZN ZN B 801 1555 1555 2.36
LINK SG CYS A 420 FE HEM A 801 1555 1555 2.40
LINK SG CYS B 331 ZN ZN B 801 1555 1555 2.31
LINK SG CYS B 336 ZN ZN B 801 1555 1555 2.30
LINK SG CYS B 420 FE HEM B 802 1555 1555 2.37
CISPEP 1 THR A 706 PRO A 707 0 0.81
CISPEP 2 THR B 706 PRO B 707 0 0.25
SITE 1 AC1 13 TRP A 414 ARG A 419 CYS A 420 PHE A 589
SITE 2 AC1 13 SER A 590 TRP A 592 GLU A 597 TRP A 683
SITE 3 AC1 13 PHE A 709 TYR A 711 8EY A 803 HOH A1016
SITE 4 AC1 13 HOH A1030
SITE 1 AC2 15 SER A 339 MET A 341 ARG A 601 VAL A 682
SITE 2 AC2 15 TRP A 683 HEM A 801 HOH A 908 HOH A 992
SITE 3 AC2 15 HOH A 997 HOH A1016 TRP B 681 PHE B 696
SITE 4 AC2 15 HIS B 697 GLN B 698 GLU B 699
SITE 1 AC3 11 VAL A 572 ASN A 574 MET A 575 GLY A 591
SITE 2 AC3 11 TRP A 592 TYR A 593 GLU A 597 TRP A 683
SITE 3 AC3 11 TYR A 711 HEM A 801 HOH A1026
SITE 1 AC4 2 CYS A 302 ARG A 304
SITE 1 AC5 4 CYS A 331 CYS A 336 CYS B 331 CYS B 336
SITE 1 AC6 15 TRP B 414 ARG B 419 CYS B 420 SER B 462
SITE 2 AC6 15 PHE B 589 SER B 590 GLY B 591 TRP B 592
SITE 3 AC6 15 MET B 594 GLU B 597 TRP B 683 TYR B 711
SITE 4 AC6 15 8EY B 804 HOH B 901 HOH B 916
SITE 1 AC7 15 TRP A 681 PHE A 696 HIS A 697 GLN A 698
SITE 2 AC7 15 GLU A 699 SER B 339 ARG B 601 VAL B 682
SITE 3 AC7 15 TRP B 683 HEM B 802 HOH B 901 HOH B 920
SITE 4 AC7 15 HOH B 983 HOH B 987 HOH B1038
SITE 1 AC8 10 VAL B 572 ASN B 574 MET B 575 GLY B 591
SITE 2 AC8 10 TRP B 592 GLU B 597 TYR B 711 HEM B 802
SITE 3 AC8 10 HOH B 901 HOH B1010
CRYST1 52.350 123.331 164.630 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 0.019102 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008108 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006074 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
