Header list of 1sjg.pdb file
Complete list - r 25 2 Bytes
HEADER ELECTRON TRANSPORT 03-MAR-04 1SJG
TITLE SOLUTION STRUCTURE OF T4MOC, THE RIESKE FERREDOXIN COMPONENT OF THE
TITLE 2 TOLUENE 4-MONOOXYGENASE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOLUENE-4-MONOOXYGENASE SYSTEM PROTEIN C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: T4MOC;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS MENDOCINA;
SOURCE 3 ORGANISM_TAXID: 300;
SOURCE 4 STRAIN: KR1;
SOURCE 5 GENE: TMOC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PJP01
KEYWDS RIESKE [2FE-2S] DOMAIN, FERREDOXIN, PFAM PF00355, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.SKJELDAL,F.C.PETERSON,J.F.DORELEIJERS,L.A.MOE,J.D.PIKUS,
AUTHOR 2 B.F.VOLKMAN,W.M.WESTLER,J.L.MARKLEY,B.G.FOX
REVDAT 4 09-MAR-11 1SJG 1 REMARK
REVDAT 3 24-FEB-09 1SJG 1 VERSN
REVDAT 2 28-DEC-04 1SJG 1 JRNL
REVDAT 1 07-SEP-04 1SJG 0
JRNL AUTH L.SKJELDAL,F.C.PETERSON,J.F.DORELEIJERS,L.A.MOE,J.D.PIKUS,
JRNL AUTH 2 W.M.WESTLER,J.L.MARKLEY,B.F.VOLKMAN,B.G.FOX
JRNL TITL SOLUTION STRUCTURE OF T4MOC, THE RIESKE FERREDOXIN COMPONENT
JRNL TITL 2 OF THE TOLUENE 4-MONOOXYGENASE COMPLEX
JRNL REF J.BIOL.INORG.CHEM. V. 9 945 2004
JRNL REFN ISSN 0949-8257
JRNL PMID 15452777
JRNL DOI 10.1007/S00775-004-0594-4
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.D.PIKUS,J.M.STUDTS,C.ACHIM,K.E.KAUFFMANN,E.MUNCK,
REMARK 1 AUTH 2 R.J.STEFFAN,K.MCCLAY,B.G.FOX
REMARK 1 TITL RECOMBINANT TOLUENE-4-MONOOXYGENASE: CATALYTIC AND MOSSBAUER
REMARK 1 TITL 2 STUDIES OF THE PURIFIED DIIRON AND RIESKE COMPONENTS OF A
REMARK 1 TITL 3 FOUR-PROTEIN COMPLEX
REMARK 1 REF BIOCHEMISTRY V. 35 9106 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 8703915
REMARK 1 DOI 10.1021/BI960456M
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.XIA,J.D.PIKUS,W.XIA,K.MCCLAY,R.J.STEFFAN,Y.K.CHAE,
REMARK 1 AUTH 2 W.M.WESTLER,J.L.MARKLEY,B.G.FOX
REMARK 1 TITL DETECTION AND CLASSIFICATION OF HYPERFINE-SHIFTED 1H, 2H,
REMARK 1 TITL 2 AND 15N RESONANCES OF THE RIESKE FERREDOXIN COMPONENT FROM
REMARK 1 TITL 3 TOLUENE 4-MONOOXYGENASE
REMARK 1 REF BIOCHEMISTRY V. 38 727 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 9888813
REMARK 1 DOI 10.1021/BI981851A
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.M.STUDTS,B.G.FOX
REMARK 1 TITL APPLICATION OF FED-BATCH FERMENTATION TO THE PREPARATION OF
REMARK 1 TITL 2 ISOTOPICALLY LABELED OR SELENOMETHIONYL-LABELED PROTEINS
REMARK 1 REF PROTEIN EXPR.PURIF. V. 16 109 1999
REMARK 1 REFN ISSN 1046-5928
REMARK 1 PMID 10336868
REMARK 1 DOI 10.1006/PREP.1999.1067
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1, TALOS 1
REMARK 3 AUTHORS : GNTERT (CYANA), CORNILESCU (TALOS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SJG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-04.
REMARK 100 THE RCSB ID CODE IS RCSB021761.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : 20 MM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20 MM PHOSPHATE, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; HNCA-J; 3D_
REMARK 210 13C-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 95, CANDID 1, XPLOR-NIH 1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 O LEU A 68 H THR A 70 1.58
REMARK 500 H3 MET A 1 OE1 GLU A 4 1.58
REMARK 500 H GLY A 60 H VAL A 61 1.60
REMARK 500 HZ1 LYS A 39 OD2 ASP A 73 1.63
REMARK 500 HG SER A 8 OD2 ASP A 11 1.64
REMARK 500 HZ3 LYS A 5 OD2 ASP A 97 1.64
REMARK 500 HD1 HIS A 36 OD2 ASP A 73 1.65
REMARK 500 H GLU A 92 O TYR A 99 1.68
REMARK 500 H THR A 22 O THR A 26 1.71
REMARK 500 H GLY A 15 O ASN A 32 1.72
REMARK 500 O GLU A 58 H VAL A 61 1.73
REMARK 500 HG1 THR A 19 O VAL A 28 1.74
REMARK 500 OE2 GLU A 92 HZ1 LYS A 94 1.74
REMARK 500 H GLU A 58 O VAL A 61 1.75
REMARK 500 H ILE A 62 O PHE A 71 1.76
REMARK 500 H GLU A 27 OG SER A 112 1.76
REMARK 500 O VAL A 31 H LYS A 39 1.77
REMARK 500 O ALA A 40 H TYR A 89 1.78
REMARK 500 H SER A 33 O GLY A 37 1.78
REMARK 500 H TRP A 13 OE1 GLU A 16 1.78
REMARK 500 H LEU A 29 O TYR A 41 1.81
REMARK 500 H VAL A 31 O LYS A 39 1.82
REMARK 500 O GLU A 18 H ILE A 30 1.82
REMARK 500 H GLY A 78 O CYS A 84 1.83
REMARK 500 O PHE A 20 H VAL A 28 1.83
REMARK 500 H GLU A 4 O VAL A 100 1.83
REMARK 500 HG SER A 33 O GLY A 37 1.84
REMARK 500 HH TYR A 57 O GLY A 59 1.84
REMARK 500 O PRO A 90 H SER A 101 1.84
REMARK 500 H CYS A 85 O LYS A 109 1.84
REMARK 500 O GLY A 60 H ASP A 73 1.85
REMARK 500 O HIS A 67 H TRP A 69 1.86
REMARK 500 O GLU A 4 H VAL A 100 1.86
REMARK 500 HD21 ASN A 72 OG1 THR A 75 1.87
REMARK 500 OG SER A 2 HG SER A 101 1.88
REMARK 500 H PHE A 20 O VAL A 28 1.90
REMARK 500 O GLU A 58 H GLY A 60 1.90
REMARK 500 HE2 HIS A 77 O ASP A 82 1.93
REMARK 500 O LYS A 94 H ASP A 97 1.94
REMARK 500 O GLU A 16 H ASN A 32 1.96
REMARK 500 H ALA A 66 S1 FES A 113 1.98
REMARK 500 O SER A 8 H ASP A 11 1.98
REMARK 500 H HIS A 47 S1 FES A 113 1.98
REMARK 500 O TRP A 13 H GLU A 16 1.99
REMARK 500 H GLU A 18 O ILE A 30 1.99
REMARK 500 HB3 SER A 56 OG1 THR A 63 2.00
REMARK 500 O LEU A 52 H GLY A 55 2.01
REMARK 500 O GLY A 76 H LEU A 86 2.01
REMARK 500 O CYS A 7 H ILE A 98 2.03
REMARK 500 O VAL A 31 HA VAL A 38 2.03
REMARK 500
REMARK 500 THIS ENTRY HAS 1413 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 14 CYS A 45 CB CYS A 45 SG 0.122
REMARK 500 14 CYS A 64 CA CYS A 64 CB 0.239
REMARK 500 14 CYS A 64 CB CYS A 64 SG 0.164
REMARK 500 14 CYS A 64 CA CYS A 64 C 0.264
REMARK 500 14 ARG A 65 N ARG A 65 CA 0.193
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 14 CYS A 45 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 14 CYS A 64 CB - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 14 CYS A 64 CA - CB - SG ANGL. DEV. = 9.8 DEGREES
REMARK 500 14 ARG A 65 C - N - CA ANGL. DEV. = 15.8 DEGREES
REMARK 500 14 HIS A 67 CA - CB - CG ANGL. DEV. = 12.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 PRO A 46 105.44 -50.06
REMARK 500 1 TRP A 69 -31.91 35.94
REMARK 500 1 ASN A 80 113.96 -160.68
REMARK 500 1 ALA A 110 -63.78 178.24
REMARK 500 1 HIS A 111 -164.95 56.23
REMARK 500 2 PHE A 3 97.97 58.28
REMARK 500 2 PRO A 46 42.25 -78.47
REMARK 500 2 HIS A 47 -67.00 -96.26
REMARK 500 2 GLN A 48 -35.62 -161.70
REMARK 500 2 LEU A 51 41.85 -89.26
REMARK 500 2 CYS A 64 -72.11 -63.85
REMARK 500 2 ARG A 65 104.85 161.05
REMARK 500 2 LEU A 68 82.74 58.15
REMARK 500 2 THR A 75 -47.98 -148.78
REMARK 500 2 ASP A 96 -6.40 72.23
REMARK 500 2 LYS A 109 -53.32 64.10
REMARK 500 2 ALA A 110 -156.80 -86.59
REMARK 500 3 PHE A 3 103.41 68.70
REMARK 500 3 PRO A 46 42.50 -1.44
REMARK 500 3 GLN A 48 123.70 68.31
REMARK 500 3 SER A 56 -73.29 -130.76
REMARK 500 3 LEU A 68 -95.25 -157.56
REMARK 500 3 TRP A 69 -16.46 172.96
REMARK 500 3 LYS A 109 -87.46 49.66
REMARK 500 3 ALA A 110 -156.95 44.99
REMARK 500 3 HIS A 111 116.33 69.22
REMARK 500 4 SER A 2 -145.93 -148.70
REMARK 500 4 CYS A 7 -173.79 -171.98
REMARK 500 4 CYS A 45 85.57 -159.25
REMARK 500 4 GLU A 49 100.05 -52.16
REMARK 500 4 ILE A 50 -79.84 63.75
REMARK 500 4 ARG A 65 80.95 46.39
REMARK 500 4 ALA A 66 -45.40 174.02
REMARK 500 4 TRP A 69 -69.45 -96.71
REMARK 500 4 ASP A 96 -19.53 78.92
REMARK 500 4 HIS A 111 97.98 -64.31
REMARK 500 5 SER A 2 -87.95 60.63
REMARK 500 5 GLN A 48 -63.89 -140.95
REMARK 500 5 ILE A 50 -161.57 -108.42
REMARK 500 5 ARG A 65 107.00 -49.82
REMARK 500 5 LEU A 68 -170.34 64.95
REMARK 500 5 THR A 75 -38.62 -151.40
REMARK 500 5 ASN A 80 105.49 159.34
REMARK 500 5 LYS A 109 -169.16 57.00
REMARK 500 5 ALA A 110 -167.53 65.40
REMARK 500 5 HIS A 111 116.09 74.12
REMARK 500 6 SER A 2 -60.49 -159.13
REMARK 500 6 PRO A 46 21.78 -76.15
REMARK 500 6 GLN A 48 -172.11 60.11
REMARK 500 6 GLU A 49 -48.88 -161.66
REMARK 500
REMARK 500 THIS ENTRY HAS 203 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 1 TRP A 69 23.0 L L OUTSIDE RANGE
REMARK 500 4 ARG A 65 23.9 L L OUTSIDE RANGE
REMARK 500 14 ALA A 66 25.0 L L OUTSIDE RANGE
REMARK 500 16 MET A 44 24.5 L L OUTSIDE RANGE
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 1 FES A 113 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 47 ND1
REMARK 620 2 FES A 113 S1 110.9
REMARK 620 3 FES A 113 S2 110.6 106.2
REMARK 620 4 HIS A 67 ND1 112.8 107.6 108.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 FES A 113 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 45 SG
REMARK 620 2 FES A 113 S1 111.4
REMARK 620 3 FES A 113 S2 111.1 108.8
REMARK 620 4 CYS A 64 SG 114.5 104.5 106.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 113
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FQT RELATED DB: PDB
REMARK 900 BPHF, RIESKE FERREDOXIN OF BIPHENYL DIOXYGENASE
DBREF 1SJG A 1 112 UNP Q00458 TMOC_PSEME 0 111
SEQRES 1 A 112 MET SER PHE GLU LYS ILE CYS SER LEU ASP ASP ILE TRP
SEQRES 2 A 112 VAL GLY GLU MET GLU THR PHE GLU THR SER ASP GLY THR
SEQRES 3 A 112 GLU VAL LEU ILE VAL ASN SER GLU GLU HIS GLY VAL LYS
SEQRES 4 A 112 ALA TYR GLN ALA MET CYS PRO HIS GLN GLU ILE LEU LEU
SEQRES 5 A 112 SER GLU GLY SER TYR GLU GLY GLY VAL ILE THR CYS ARG
SEQRES 6 A 112 ALA HIS LEU TRP THR PHE ASN ASP GLY THR GLY HIS GLY
SEQRES 7 A 112 ILE ASN PRO ASP ASP CYS CYS LEU ALA GLU TYR PRO VAL
SEQRES 8 A 112 GLU VAL LYS GLY ASP ASP ILE TYR VAL SER THR LYS GLY
SEQRES 9 A 112 ILE LEU PRO ASN LYS ALA HIS SER
HET FES A 113 4
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
FORMUL 2 FES FE2 S2
HELIX 1 1 LEU A 51 GLY A 55 5 5
SHEET 1 A 3 PHE A 3 SER A 8 0
SHEET 2 A 3 ASP A 97 SER A 101 -1 O VAL A 100 N GLU A 4
SHEET 3 A 3 VAL A 91 LYS A 94 -1 N GLU A 92 O TYR A 99
SHEET 1 B 4 GLU A 16 GLU A 21 0
SHEET 2 B 4 GLU A 27 ASN A 32 -1 O VAL A 28 N PHE A 20
SHEET 3 B 4 VAL A 38 GLN A 42 -1 O TYR A 41 N LEU A 29
SHEET 4 B 4 GLU A 88 TYR A 89 -1 O TYR A 89 N ALA A 40
SHEET 1 C 4 TYR A 57 GLU A 58 0
SHEET 2 C 4 VAL A 61 THR A 63 -1 O VAL A 61 N GLU A 58
SHEET 3 C 4 THR A 70 ASN A 72 -1 O PHE A 71 N ILE A 62
SHEET 4 C 4 HIS A 77 GLY A 78 -1 O HIS A 77 N ASN A 72
LINK ND1 HIS A 47 FE2 FES A 113 1555 1555 2.13
LINK ND1 HIS A 67 FE2 FES A 113 1555 1555 2.12
LINK SG CYS A 45 FE1 FES A 113 1555 1555 2.32
LINK SG CYS A 64 FE1 FES A 113 1555 1555 2.24
CISPEP 1 ASN A 80 PRO A 81 1 4.35
CISPEP 2 ASN A 80 PRO A 81 2 -1.02
CISPEP 3 ASN A 80 PRO A 81 3 3.31
CISPEP 4 ASN A 80 PRO A 81 4 -0.52
CISPEP 5 ASN A 80 PRO A 81 5 1.04
CISPEP 6 ASN A 80 PRO A 81 6 0.38
CISPEP 7 ASN A 80 PRO A 81 7 -0.14
CISPEP 8 ASN A 80 PRO A 81 8 -4.36
CISPEP 9 ASN A 80 PRO A 81 9 1.06
CISPEP 10 ASN A 80 PRO A 81 10 -3.05
CISPEP 11 ASN A 80 PRO A 81 11 -4.47
CISPEP 12 ASN A 80 PRO A 81 12 -1.09
CISPEP 13 ASN A 80 PRO A 81 13 -3.91
CISPEP 14 ASN A 80 PRO A 81 14 0.22
CISPEP 15 ASN A 80 PRO A 81 15 -3.99
CISPEP 16 ASN A 80 PRO A 81 16 -0.87
CISPEP 17 ASN A 80 PRO A 81 17 -2.32
CISPEP 18 ASN A 80 PRO A 81 18 -1.32
CISPEP 19 ASN A 80 PRO A 81 19 -2.39
CISPEP 20 ASN A 80 PRO A 81 20 0.11
SITE 1 AC1 8 CYS A 45 PRO A 46 HIS A 47 CYS A 64
SITE 2 AC1 8 ARG A 65 ALA A 66 HIS A 67 CYS A 84
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 25 2 Bytes