HEADER OXIDOREDUCTASE 09-AUG-17 5Y5I
TITLE TIME-RESOLVED SFX STRUCTURE OF CYTOCHROME P450NOR: 20 MS AFTER PHOTO-
TITLE 2 IRRADIATION OF CAGED NO IN THE PRESENCE OF NADH (NO-BOUND STATE),
TITLE 3 LIGHT DATA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NADP NITROUS OXIDE-FORMING NITRIC OXIDE REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: NITRIC-OXIDE REDUCTASE CYTOCHROME P450;
COMPND 5 SYNONYM: NOR,CYPLVA1,CYTOCHROME P450 55A1,CYTOCHROME P450 DNIR,
COMPND 6 CYTOCHROME P450NOR,FUNGAL NITRIC OXIDE REDUCTASE;
COMPND 7 EC: 1.7.1.14;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM OXYSPORUM;
SOURCE 3 ORGANISM_COMMON: FUSARIUM VASCULAR WILT;
SOURCE 4 ORGANISM_TAXID: 5507;
SOURCE 5 GENE: CYP55A1, CYP55;
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: PRSET-C
KEYWDS METAL-BINDING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.TOSHA,T.NOMURA,T.NISHIDA,N.SAEKI,K.OKUBAYASHI,R.YAMAGIWA,
AUTHOR 2 M.SUGAHARA,T.NAKANE,K.YAMASHITA,K.HIRATA,G.UENO,T.KIMURA,T.HISANO,
AUTHOR 3 K.MURAMOTO,H.SAWAI,H.TAKEDA,E.MIZOHATA,A.YAMASHITA,Y.KANEMATSU,
AUTHOR 4 Y.TAKANO,E.NANGO,R.TANAKA,O.NUREKI,Y.IKEMOTO,H.MURAKAMI,S.OWADA,
AUTHOR 5 K.TONO,M.YABASHI,M.YAMAMOTO,H.AGO,S.IWATA,H.SUGIMOTO,Y.SHIRO,M.KUBO
REVDAT 4 22-NOV-23 5Y5I 1 REMARK
REVDAT 3 06-SEP-23 5Y5I 1 LINK
REVDAT 2 19-SEP-18 5Y5I 1 REMARK LINK
REVDAT 1 06-DEC-17 5Y5I 0
JRNL AUTH T.TOSHA,T.NOMURA,T.NISHIDA,N.SAEKI,K.OKUBAYASHI,R.YAMAGIWA,
JRNL AUTH 2 M.SUGAHARA,T.NAKANE,K.YAMASHITA,K.HIRATA,G.UENO,T.KIMURA,
JRNL AUTH 3 T.HISANO,K.MURAMOTO,H.SAWAI,H.TAKEDA,E.MIZOHATA,A.YAMASHITA,
JRNL AUTH 4 Y.KANEMATSU,Y.TAKANO,E.NANGO,R.TANAKA,O.NUREKI,O.SHOJI,
JRNL AUTH 5 Y.IKEMOTO,H.MURAKAMI,S.OWADA,K.TONO,M.YABASHI,M.YAMAMOTO,
JRNL AUTH 6 H.AGO,S.IWATA,H.SUGIMOTO,Y.SHIRO,M.KUBO
JRNL TITL CAPTURING AN INITIAL INTERMEDIATE DURING THE P450NOR
JRNL TITL 2 ENZYMATIC REACTION USING TIME-RESOLVED XFEL CRYSTALLOGRAPHY
JRNL TITL 3 AND CAGED-SUBSTRATE.
JRNL REF NAT COMMUN V. 8 1585 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 29147002
JRNL DOI 10.1038/S41467-017-01702-1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.05
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 47179
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 2345
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 41.0529 - 5.3958 1.00 2711 131 0.1496 0.1814
REMARK 3 2 5.3958 - 4.2843 1.00 2673 121 0.1233 0.1385
REMARK 3 3 4.2843 - 3.7432 1.00 2644 148 0.1177 0.1656
REMARK 3 4 3.7432 - 3.4011 1.00 2638 132 0.1328 0.1720
REMARK 3 5 3.4011 - 3.1574 1.00 2655 143 0.1464 0.2015
REMARK 3 6 3.1574 - 2.9713 1.00 2638 143 0.1530 0.2332
REMARK 3 7 2.9713 - 2.8226 1.00 2617 149 0.1571 0.2195
REMARK 3 8 2.8226 - 2.6997 1.00 2660 125 0.1625 0.2392
REMARK 3 9 2.6997 - 2.5958 1.00 2616 137 0.1616 0.2133
REMARK 3 10 2.5958 - 2.5062 1.00 2646 138 0.1631 0.1993
REMARK 3 11 2.5062 - 2.4279 1.00 2605 138 0.1548 0.2117
REMARK 3 12 2.4279 - 2.3585 1.00 2624 147 0.1651 0.2049
REMARK 3 13 2.3585 - 2.2964 1.00 2613 151 0.1668 0.2533
REMARK 3 14 2.2964 - 2.2404 1.00 2636 144 0.1754 0.2256
REMARK 3 15 2.2404 - 2.1895 1.00 2609 129 0.1866 0.2452
REMARK 3 16 2.1895 - 2.1429 1.00 2656 135 0.2076 0.2498
REMARK 3 17 2.1429 - 2.1000 1.00 2593 134 0.2345 0.2993
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.430
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.06
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 6656
REMARK 3 ANGLE : 0.884 9078
REMARK 3 CHIRALITY : 0.048 1014
REMARK 3 PLANARITY : 0.006 1192
REMARK 3 DIHEDRAL : 12.420 4073
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 5Y5I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1300004714.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER
REMARK 200 BEAMLINE : BL3
REMARK 200 X-RAY GENERATOR MODEL : SACLA BEAMLINE BL3
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MPCCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL
REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54628
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 43.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 119.4
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 82.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1CL6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 34-38% PEG 10000, 0.1 M BIS-TRIS
REMARK 280 PROPANE 0.15 M AMMONIUM ACETATE, PH 8.5, BATCH MODE, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 51.15000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLY A 4
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLY B 4
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 OG1 THR B 175 O HOH B 601 2.11
REMARK 500 O GLY B 177 NH1 ARG B 392 2.19
REMARK 500 OE1 GLU A 126 NZ LYS A 372 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 796 O HOH B 656 1556 2.15
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 ASN A 29 74.47 -155.01
REMARK 500 PHE A 144 -54.39 -143.84
REMARK 500 LYS A 207 -156.88 -112.61
REMARK 500 ASP A 208 78.72 -109.34
REMARK 500 GLN A 218 -45.91 -134.16
REMARK 500 ASN B 29 68.75 -159.50
REMARK 500 PHE B 144 -52.51 -143.98
REMARK 500 ARG B 174 -78.69 -95.26
REMARK 500 ASN B 176 93.05 -44.80
REMARK 500 SER B 178 57.60 -61.69
REMARK 500 LYS B 207 -155.40 -126.37
REMARK 500 ASP B 208 77.77 -108.66
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 HEM A 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 352 SG
REMARK 620 2 HEM A 501 NA 99.0
REMARK 620 3 HEM A 501 NB 94.3 90.6
REMARK 620 4 HEM A 501 NC 88.8 172.1 87.5
REMARK 620 5 HEM A 501 ND 94.0 89.6 171.6 91.1
REMARK 620 6 NO A 502 N 173.3 74.5 84.4 97.7 87.6
REMARK 620 7 HOH A 710 O 171.5 88.5 89.6 83.8 82.0 15.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 352 SG
REMARK 620 2 HEM B 501 NA 100.4
REMARK 620 3 HEM B 501 NB 93.0 91.3
REMARK 620 4 HEM B 501 NC 88.8 170.5 85.7
REMARK 620 5 HEM B 501 ND 96.5 90.7 169.7 90.7
REMARK 620 6 NO B 502 N 176.2 76.8 84.6 94.0 86.1
REMARK 620 7 HOH B 677 O 169.3 88.4 92.8 82.8 77.1 14.5
REMARK 620 N 1 2 3 4 5 6
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 504
DBREF 5Y5I A 1 403 UNP P23295 NOR_FUSOX 1 403
DBREF 5Y5I B 1 403 UNP P23295 NOR_FUSOX 1 403
SEQRES 1 A 403 MET ALA SER GLY ALA PRO SER PHE PRO PHE SER ARG ALA
SEQRES 2 A 403 SER GLY PRO GLU PRO PRO ALA GLU PHE ALA LYS LEU ARG
SEQRES 3 A 403 ALA THR ASN PRO VAL SER GLN VAL LYS LEU PHE ASP GLY
SEQRES 4 A 403 SER LEU ALA TRP LEU VAL THR LYS HIS LYS ASP VAL CYS
SEQRES 5 A 403 PHE VAL ALA THR SER GLU LYS LEU SER LYS VAL ARG THR
SEQRES 6 A 403 ARG GLN GLY PHE PRO GLU LEU SER ALA SER GLY LYS GLN
SEQRES 7 A 403 ALA ALA LYS ALA LYS PRO THR PHE VAL ASP MET ASP PRO
SEQRES 8 A 403 PRO GLU HIS MET HIS GLN ARG SER MET VAL GLU PRO THR
SEQRES 9 A 403 PHE THR PRO GLU ALA VAL LYS ASN LEU GLN PRO TYR ILE
SEQRES 10 A 403 GLN ARG THR VAL ASP ASP LEU LEU GLU GLN MET LYS GLN
SEQRES 11 A 403 LYS GLY CYS ALA ASN GLY PRO VAL ASP LEU VAL LYS GLU
SEQRES 12 A 403 PHE ALA LEU PRO VAL PRO SER TYR ILE ILE TYR THR LEU
SEQRES 13 A 403 LEU GLY VAL PRO PHE ASN ASP LEU GLU TYR LEU THR GLN
SEQRES 14 A 403 GLN ASN ALA ILE ARG THR ASN GLY SER SER THR ALA ARG
SEQRES 15 A 403 GLU ALA SER ALA ALA ASN GLN GLU LEU LEU ASP TYR LEU
SEQRES 16 A 403 ALA ILE LEU VAL GLU GLN ARG LEU VAL GLU PRO LYS ASP
SEQRES 17 A 403 ASP ILE ILE SER LYS LEU CYS THR GLU GLN VAL LYS PRO
SEQRES 18 A 403 GLY ASN ILE ASP LYS SER ASP ALA VAL GLN ILE ALA PHE
SEQRES 19 A 403 LEU LEU LEU VAL ALA GLY ASN ALA THR MET VAL ASN MET
SEQRES 20 A 403 ILE ALA LEU GLY VAL ALA THR LEU ALA GLN HIS PRO ASP
SEQRES 21 A 403 GLN LEU ALA GLN LEU LYS ALA ASN PRO SER LEU ALA PRO
SEQRES 22 A 403 GLN PHE VAL GLU GLU LEU CYS ARG TYR HIS THR ALA SER
SEQRES 23 A 403 ALA LEU ALA ILE LYS ARG THR ALA LYS GLU ASP VAL MET
SEQRES 24 A 403 ILE GLY ASP LYS LEU VAL ARG ALA ASN GLU GLY ILE ILE
SEQRES 25 A 403 ALA SER ASN GLN SER ALA ASN ARG ASP GLU GLU VAL PHE
SEQRES 26 A 403 GLU ASN PRO ASP GLU PHE ASN MET ASN ARG LYS TRP PRO
SEQRES 27 A 403 PRO GLN ASP PRO LEU GLY PHE GLY PHE GLY ASP HIS ARG
SEQRES 28 A 403 CYS ILE ALA GLU HIS LEU ALA LYS ALA GLU LEU THR THR
SEQRES 29 A 403 VAL PHE SER THR LEU TYR GLN LYS PHE PRO ASP LEU LYS
SEQRES 30 A 403 VAL ALA VAL PRO LEU GLY LYS ILE ASN TYR THR PRO LEU
SEQRES 31 A 403 ASN ARG ASP VAL GLY ILE VAL ASP LEU PRO VAL ILE PHE
SEQRES 1 B 403 MET ALA SER GLY ALA PRO SER PHE PRO PHE SER ARG ALA
SEQRES 2 B 403 SER GLY PRO GLU PRO PRO ALA GLU PHE ALA LYS LEU ARG
SEQRES 3 B 403 ALA THR ASN PRO VAL SER GLN VAL LYS LEU PHE ASP GLY
SEQRES 4 B 403 SER LEU ALA TRP LEU VAL THR LYS HIS LYS ASP VAL CYS
SEQRES 5 B 403 PHE VAL ALA THR SER GLU LYS LEU SER LYS VAL ARG THR
SEQRES 6 B 403 ARG GLN GLY PHE PRO GLU LEU SER ALA SER GLY LYS GLN
SEQRES 7 B 403 ALA ALA LYS ALA LYS PRO THR PHE VAL ASP MET ASP PRO
SEQRES 8 B 403 PRO GLU HIS MET HIS GLN ARG SER MET VAL GLU PRO THR
SEQRES 9 B 403 PHE THR PRO GLU ALA VAL LYS ASN LEU GLN PRO TYR ILE
SEQRES 10 B 403 GLN ARG THR VAL ASP ASP LEU LEU GLU GLN MET LYS GLN
SEQRES 11 B 403 LYS GLY CYS ALA ASN GLY PRO VAL ASP LEU VAL LYS GLU
SEQRES 12 B 403 PHE ALA LEU PRO VAL PRO SER TYR ILE ILE TYR THR LEU
SEQRES 13 B 403 LEU GLY VAL PRO PHE ASN ASP LEU GLU TYR LEU THR GLN
SEQRES 14 B 403 GLN ASN ALA ILE ARG THR ASN GLY SER SER THR ALA ARG
SEQRES 15 B 403 GLU ALA SER ALA ALA ASN GLN GLU LEU LEU ASP TYR LEU
SEQRES 16 B 403 ALA ILE LEU VAL GLU GLN ARG LEU VAL GLU PRO LYS ASP
SEQRES 17 B 403 ASP ILE ILE SER LYS LEU CYS THR GLU GLN VAL LYS PRO
SEQRES 18 B 403 GLY ASN ILE ASP LYS SER ASP ALA VAL GLN ILE ALA PHE
SEQRES 19 B 403 LEU LEU LEU VAL ALA GLY ASN ALA THR MET VAL ASN MET
SEQRES 20 B 403 ILE ALA LEU GLY VAL ALA THR LEU ALA GLN HIS PRO ASP
SEQRES 21 B 403 GLN LEU ALA GLN LEU LYS ALA ASN PRO SER LEU ALA PRO
SEQRES 22 B 403 GLN PHE VAL GLU GLU LEU CYS ARG TYR HIS THR ALA SER
SEQRES 23 B 403 ALA LEU ALA ILE LYS ARG THR ALA LYS GLU ASP VAL MET
SEQRES 24 B 403 ILE GLY ASP LYS LEU VAL ARG ALA ASN GLU GLY ILE ILE
SEQRES 25 B 403 ALA SER ASN GLN SER ALA ASN ARG ASP GLU GLU VAL PHE
SEQRES 26 B 403 GLU ASN PRO ASP GLU PHE ASN MET ASN ARG LYS TRP PRO
SEQRES 27 B 403 PRO GLN ASP PRO LEU GLY PHE GLY PHE GLY ASP HIS ARG
SEQRES 28 B 403 CYS ILE ALA GLU HIS LEU ALA LYS ALA GLU LEU THR THR
SEQRES 29 B 403 VAL PHE SER THR LEU TYR GLN LYS PHE PRO ASP LEU LYS
SEQRES 30 B 403 VAL ALA VAL PRO LEU GLY LYS ILE ASN TYR THR PRO LEU
SEQRES 31 B 403 ASN ARG ASP VAL GLY ILE VAL ASP LEU PRO VAL ILE PHE
HET HEM A 501 43
HET NO A 502 2
HET GOL A 503 6
HET HEM B 501 43
HET NO B 502 2
HET GOL B 503 6
HET GOL B 504 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM NO NITRIC OXIDE
HETNAM GOL GLYCEROL
HETSYN HEM HEME
HETSYN NO NITROGEN MONOXIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 NO 2(N O)
FORMUL 5 GOL 3(C3 H8 O3)
FORMUL 10 HOH *400(H2 O)
HELIX 1 AA1 ALA A 20 ASN A 29 1 10
HELIX 2 AA2 LYS A 47 SER A 57 1 11
HELIX 3 AA3 SER A 73 ALA A 80 1 8
HELIX 4 AA4 THR A 85 MET A 89 5 5
HELIX 5 AA5 PRO A 92 GLU A 102 1 11
HELIX 6 AA6 PRO A 103 PHE A 105 5 3
HELIX 7 AA7 THR A 106 GLY A 132 1 27
HELIX 8 AA8 LEU A 140 PHE A 144 1 5
HELIX 9 AA9 LEU A 146 GLY A 158 1 13
HELIX 10 AB1 PRO A 160 ASN A 162 5 3
HELIX 11 AB2 ASP A 163 ASN A 176 1 14
HELIX 12 AB3 THR A 180 GLU A 205 1 26
HELIX 13 AB4 ASP A 209 GLN A 218 1 10
HELIX 14 AB5 ASP A 225 ALA A 239 1 15
HELIX 15 AB6 GLY A 240 HIS A 258 1 19
HELIX 16 AB7 HIS A 258 ASN A 268 1 11
HELIX 17 AB8 LEU A 271 HIS A 283 1 13
HELIX 18 AB9 SER A 314 ASN A 319 1 6
HELIX 19 AC1 ALA A 354 PHE A 373 1 20
HELIX 20 AC2 PRO A 381 ILE A 385 5 5
HELIX 21 AC3 ALA B 20 ASN B 29 1 10
HELIX 22 AC4 LYS B 47 SER B 57 1 11
HELIX 23 AC5 SER B 73 ALA B 80 1 8
HELIX 24 AC6 THR B 85 MET B 89 5 5
HELIX 25 AC7 PRO B 92 SER B 99 1 8
HELIX 26 AC8 MET B 100 PHE B 105 5 6
HELIX 27 AC9 THR B 106 GLY B 132 1 27
HELIX 28 AD1 LEU B 140 PHE B 144 1 5
HELIX 29 AD2 LEU B 146 GLY B 158 1 13
HELIX 30 AD3 PRO B 160 ASN B 162 5 3
HELIX 31 AD4 ASP B 163 ARG B 174 1 12
HELIX 32 AD5 THR B 180 GLU B 205 1 26
HELIX 33 AD6 ASP B 209 GLN B 218 1 10
HELIX 34 AD7 ASP B 225 ALA B 239 1 15
HELIX 35 AD8 GLY B 240 HIS B 258 1 19
HELIX 36 AD9 HIS B 258 ASN B 268 1 11
HELIX 37 AE1 LEU B 271 HIS B 283 1 13
HELIX 38 AE2 SER B 314 ASN B 319 1 6
HELIX 39 AE3 ALA B 354 PHE B 373 1 20
HELIX 40 AE4 PRO B 381 ILE B 385 5 5
SHEET 1 AA1 5 VAL A 31 LYS A 35 0
SHEET 2 AA1 5 LEU A 41 VAL A 45 -1 O LEU A 44 N SER A 32
SHEET 3 AA1 5 GLY A 310 ALA A 313 1 O GLY A 310 N TRP A 43
SHEET 4 AA1 5 LYS A 291 ALA A 294 -1 N ARG A 292 O ILE A 311
SHEET 5 AA1 5 LEU A 60 SER A 61 -1 N SER A 61 O THR A 293
SHEET 1 AA2 3 VAL A 138 ASP A 139 0
SHEET 2 AA2 3 PRO A 400 ILE A 402 -1 O VAL A 401 N VAL A 138
SHEET 3 AA2 3 LYS A 377 VAL A 378 -1 N LYS A 377 O ILE A 402
SHEET 1 AA3 2 VAL A 298 ILE A 300 0
SHEET 2 AA3 2 LYS A 303 VAL A 305 -1 O VAL A 305 N VAL A 298
SHEET 1 AA4 2 ASN A 386 TYR A 387 0
SHEET 2 AA4 2 ILE A 396 ASP A 398 -1 O VAL A 397 N ASN A 386
SHEET 1 AA5 5 VAL B 31 LYS B 35 0
SHEET 2 AA5 5 LEU B 41 VAL B 45 -1 O LEU B 44 N SER B 32
SHEET 3 AA5 5 GLY B 310 ALA B 313 1 O GLY B 310 N TRP B 43
SHEET 4 AA5 5 LYS B 291 ALA B 294 -1 N ARG B 292 O ILE B 311
SHEET 5 AA5 5 LEU B 60 SER B 61 -1 N SER B 61 O THR B 293
SHEET 1 AA6 3 VAL B 138 ASP B 139 0
SHEET 2 AA6 3 PRO B 400 ILE B 402 -1 O VAL B 401 N VAL B 138
SHEET 3 AA6 3 LYS B 377 VAL B 378 -1 N LYS B 377 O ILE B 402
SHEET 1 AA7 2 VAL B 298 ILE B 300 0
SHEET 2 AA7 2 LYS B 303 VAL B 305 -1 O VAL B 305 N VAL B 298
SHEET 1 AA8 2 ASN B 386 TYR B 387 0
SHEET 2 AA8 2 ILE B 396 ASP B 398 -1 O VAL B 397 N ASN B 386
LINK SG CYS A 352 FE HEM A 501 1555 1555 2.27
LINK FE HEM A 501 N A NO A 502 1555 1555 1.67
LINK FE HEM A 501 O BHOH A 710 1555 1555 2.40
LINK SG CYS B 352 FE HEM B 501 1555 1555 2.26
LINK FE HEM B 501 N A NO B 502 1555 1555 1.68
LINK FE HEM B 501 O BHOH B 677 1555 1555 2.40
CISPEP 1 PHE A 8 PRO A 9 0 1.29
CISPEP 2 PRO A 91 PRO A 92 0 -3.96
CISPEP 3 PHE B 8 PRO B 9 0 6.83
CISPEP 4 PRO B 91 PRO B 92 0 -0.69
SITE 1 AC1 23 PHE A 86 VAL A 87 HIS A 94 ARG A 98
SITE 2 AC1 23 ILE A 153 LEU A 236 ALA A 239 GLY A 240
SITE 3 AC1 23 MET A 244 MET A 247 GLY A 344 PHE A 345
SITE 4 AC1 23 GLY A 346 PHE A 347 HIS A 350 CYS A 352
SITE 5 AC1 23 ILE A 353 ALA A 354 NO A 502 HOH A 609
SITE 6 AC1 23 HOH A 648 HOH A 692 HOH A 710
SITE 1 AC2 4 ALA A 239 HEM A 501 GOL A 503 HOH A 710
SITE 1 AC3 4 ALA A 239 SER A 286 NO A 502 HOH A 601
SITE 1 AC4 23 PHE B 86 VAL B 87 HIS B 94 ARG B 98
SITE 2 AC4 23 ILE B 153 LEU B 236 GLY B 240 MET B 244
SITE 3 AC4 23 MET B 247 GLY B 344 PHE B 345 GLY B 346
SITE 4 AC4 23 PHE B 347 HIS B 350 CYS B 352 ILE B 353
SITE 5 AC4 23 ALA B 354 NO B 502 GOL B 503 HOH B 602
SITE 6 AC4 23 HOH B 607 HOH B 619 HOH B 677
SITE 1 AC5 4 ALA B 239 HEM B 501 GOL B 503 HOH B 677
SITE 1 AC6 7 VAL B 87 ALA B 239 SER B 286 ALA B 289
SITE 2 AC6 7 HEM B 501 NO B 502 HOH B 619
SITE 1 AC7 10 ALA B 55 LEU B 60 LYS B 62 MET B 89
SITE 2 AC7 10 ASP B 90 PRO B 91 ARG B 292 ASP B 349
SITE 3 AC7 10 HIS B 350 HOH B 691
CRYST1 54.600 102.300 73.700 90.00 92.60 90.00 P 1 21 1 4
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 0.018315 0.000000 0.000832 0.00000
SCALE2 0.000000 0.009775 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013583 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
