Header list of 1dwl.pdb file
Complete list - 25 20 Bytes
HEADER ELECTRON TRANSFER 08-DEC-99 1DWL
TITLE THE FERREDOXIN-CYTOCHROME COMPLEX USING HETERONUCLEAR NMR
TITLE 2 AND DOCKING SIMULATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERREDOXIN I;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: CONTAINS A FE4S4 CLUSTER COVALENTLY LINKED
COMPND 6 BY FOUR CYSTEINS;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CYTOCHROME C553;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: LOW POTENTIAL CYTOCHROME C;
COMPND 11 OTHER_DETAILS: CONTAINS A HEME GROUP COVALENTLY LINKED BY
COMPND 12 2 CYSTEINES AND THE IRON ATOM IS COORDINATED BY A
COMPND 13 HISTIDINE AND A METHIONINE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOMICROBIUM NORVEGICUM;
SOURCE 3 ORGANISM_TAXID: 52561;
SOURCE 4 CELLULAR_LOCATION: PERIPLASM;
SOURCE 5 PLASMID: PETFDI;
SOURCE 6 GENE: FDXI;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS;
SOURCE 12 ORGANISM_TAXID: 882;
SOURCE 13 STRAIN: HILDENBOROUGH;
SOURCE 14 CELLULAR_LOCATION: CYTOPLASM
KEYWDS ELECTRON TRANSFER, FERREDOXIN-CYTOCHROME COMPLEX, MODEL,
KEYWDS 2 HETERONUCLEAR NMR, DOCKING
EXPDTA SOLUTION NMR; THEORETICAL MODEL
NUMMDL 3
AUTHOR X.MORELLI,F.GUERLESQUIN,M.CZJZEK,P.N.PALMA
REVDAT 5 24-FEB-09 1DWL 1 VERSN
REVDAT 4 01-SEP-00 1DWL 1 DBREF
REVDAT 3 08-JUL-00 1DWL 1 REMARK
REVDAT 2 10-APR-00 1DWL 1 JRNL
REVDAT 1 10-DEC-99 1DWL 0
JRNL AUTH X.MORELLI,A.DOLLA,M.CZJZEK,P.N.PALMA,F.BLASCO,
JRNL AUTH 2 L.KRIPPAHL,J.J.G.MOURA,F.GUERLESQUIN
JRNL TITL HETERONUCLEAR NMR AND SOFT DOCKING: AN
JRNL TITL 2 EXPERIMENTAL APPROACH FOR A STRUCTURAL MODEL OF
JRNL TITL 3 THE CYTOCHROME C553-FERREDOXIN COMPLEX
JRNL REF BIOCHEMISTRY V. 39 2530 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10704202
JRNL DOI 10.1021/BI992306S
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.N.PALMA,L.KRIPPAHL,J.E.WAMPLER,J.J.G.MOURA
REMARK 1 TITL BIGGER: A NEW (SOFT) DOCKING ALGORITHM FOR
REMARK 1 TITL 2 PREDICTING PROTEIN INTERACTIONS
REMARK 1 REF PROTEINS: STRUCT.,FUNCT., V. 39 372 2000
REMARK 1 REF 2 GENET.
REMARK 1 REFN ISSN 0887-3585
REMARK 1 PMID 10813819
REMARK 1 DOI 10.1002/(SICI)1097-0134(20000601)39:4<372::AI
REMARK 1 DOI 2 D-PROT100>3.3.CO;2-H
REMARK 1 REFERENCE 2
REMARK 1 AUTH X.MORELLI,F.GUERLESQUIN
REMARK 1 TITL MAPPING THE CYTOCHROME C553 INTERACTING SITE USING
REMARK 1 TITL 2 1H AND 15N NMR
REMARK 1 REF FEBS LETT. V. 460 77 1999
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 10571064
REMARK 1 DOI 10.1016/S0014-5793(99)01299-5
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MOLECULAR DYNAMICS CALCULATION USING
REMARK 3 AMBER FORCE FIELD THESE ARE 3 MODEL STRUCTURES FOR THE COMPLEX
REMARK 3 OF CYTOCHROME C553 WITH FERREDOXIN I
REMARK 4
REMARK 4 1DWL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-DEC-99.
REMARK 100 THE PDBE ID CODE IS EBI-4450.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 5.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 10% D2O/90% WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : MAPPING OF THE CHEMICAL
REMARK 210 SHIFT VARIATIONS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 3
REMARK 210 CONFORMERS, SELECTION CRITERIA : COMBINATION OF NMR SHIFT
REMARK 210 VARIATION AND A SOFT
REMARK 210 DOCKING ALGORITHM
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
REMARK 210
REMARK 210 REMARK: HETERONUCLEAR EXPERIMENTS ON 15N-LABELED FERREDOXIN
REMARK 210 AND CYTOCHROME, CHEMICAL SHIFT VARIATION ANALYSIS
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 220
REMARK 220 EXPERIMENTAL DETAILS
REMARK 220 EXPERIMENT TYPE : THEORETICAL MODELLING
REMARK 220 MODELLING PROGRAM : BIGGER
REMARK 220 PROGRAM AUTHORS : P.N. PALMA
REMARK 220
REMARK 220 REMARK: MODELLING EXPERIMENT: THE COMPLEX STRUCTURE WAS OBTAINED
REMARK 220 BY SOFT DOCKING ALGORITHM IMPLEMENTED WITH AN NMR FILTER.
REMARK 220 THE STARTING MODELS OF THE CYTOCHROME AND THE FERREDOXIN
REMARK 220 WERE BASED ON THE PDB ENTRIES 1DVH AND 1FXD
REMARK 225
REMARK 225 THEORETICAL MODEL
REMARK 225 THE COORDINATES IN THIS ENTRY REPRESENT A MODEL STRUCTURE.
REMARK 225 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1 AND
REMARK 225 SCALE RECORDS BE INCLUDED, BUT THE VALUES ON THESE
REMARK 225 RECORDS ARE MEANINGLESS.
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 HD1 HIS B 14 - O LYS B 20 1.59
REMARK 500 CG MET B 23 - CG ARG B 53 2.16
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 1 GLY A 11 C CYS A 12 N -0.198
REMARK 500 1 SER A 14 C CYS A 15 N -0.341
REMARK 500 1 GLU B 67 N GLU B 67 CA 0.130
REMARK 500 1 TYR B 75 C MET B 76 N 0.194
REMARK 500 2 ALA B 21 C ALA B 22 N 0.197
REMARK 500 2 GLY B 24 C SER B 25 N 0.211
REMARK 500 2 SER B 65 C SER B 65 O 0.127
REMARK 500 2 SER B 65 C ASP B 66 N 0.194
REMARK 500 2 LYS B 78 C LEU B 79 N 0.257
REMARK 500 3 SER A 14 N SER A 14 CA 0.120
REMARK 500 3 GLY B 24 C SER B 25 N 0.244
REMARK 500 3 TYR B 64 C SER B 65 N -0.298
REMARK 500 3 ASP B 66 C GLU B 67 N 0.164
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 1 GLY A 11 CA - C - N ANGL. DEV. = 25.3 DEGREES
REMARK 500 1 GLY A 11 O - C - N ANGL. DEV. = -26.7 DEGREES
REMARK 500 1 CYS A 12 C - N - CA ANGL. DEV. = 29.9 DEGREES
REMARK 500 1 SER A 14 CA - C - N ANGL. DEV. = 25.7 DEGREES
REMARK 500 1 SER A 14 O - C - N ANGL. DEV. = -28.3 DEGREES
REMARK 500 1 CYS A 15 C - N - CA ANGL. DEV. = 28.1 DEGREES
REMARK 500 1 GLU A 29 C - N - CA ANGL. DEV. = 15.8 DEGREES
REMARK 500 1 GLU A 59 N - CA - C ANGL. DEV. = -19.2 DEGREES
REMARK 500 1 CYS B 13 CA - CB - SG ANGL. DEV. = -6.8 DEGREES
REMARK 500 1 GLY B 24 N - CA - C ANGL. DEV. = -18.4 DEGREES
REMARK 500 1 MET B 23 CA - C - N ANGL. DEV. = -15.7 DEGREES
REMARK 500 1 MET B 23 O - C - N ANGL. DEV. = 19.4 DEGREES
REMARK 500 1 GLY B 24 C - N - CA ANGL. DEV. = 14.4 DEGREES
REMARK 500 1 ASP B 66 CB - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 1 TYR B 75 CA - C - N ANGL. DEV. = -14.5 DEGREES
REMARK 500 1 TYR B 75 O - C - N ANGL. DEV. = 20.6 DEGREES
REMARK 500 1 LEU B 79 N - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500 2 CYS A 9 CA - CB - SG ANGL. DEV. = -11.1 DEGREES
REMARK 500 2 CYS A 9 CA - CB - SG ANGL. DEV. = -10.9 DEGREES
REMARK 500 2 GLU A 29 O - C - N ANGL. DEV. = -13.5 DEGREES
REMARK 500 2 CYS A 51 CA - CB - SG ANGL. DEV. = -11.8 DEGREES
REMARK 500 2 CYS A 51 CA - CB - SG ANGL. DEV. = -11.6 DEGREES
REMARK 500 2 GLU A 59 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 2 GLY B 15 C - N - CA ANGL. DEV. = -13.4 DEGREES
REMARK 500 2 ALA B 21 CA - C - N ANGL. DEV. = -16.0 DEGREES
REMARK 500 2 ALA B 21 O - C - N ANGL. DEV. = 16.1 DEGREES
REMARK 500 2 ALA B 22 C - N - CA ANGL. DEV. = -28.8 DEGREES
REMARK 500 2 ALA B 22 O - C - N ANGL. DEV. = 11.4 DEGREES
REMARK 500 2 GLY B 24 CA - C - N ANGL. DEV. = -17.8 DEGREES
REMARK 500 2 GLY B 24 O - C - N ANGL. DEV. = -20.6 DEGREES
REMARK 500 2 SER B 25 C - N - CA ANGL. DEV. = 28.7 DEGREES
REMARK 500 2 SER B 65 CA - C - N ANGL. DEV. = -21.3 DEGREES
REMARK 500 2 SER B 65 O - C - N ANGL. DEV. = 26.5 DEGREES
REMARK 500 2 ASP B 66 C - N - CA ANGL. DEV. = 16.3 DEGREES
REMARK 500 2 TYR B 75 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 2 LEU B 79 N - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500 2 LYS B 78 CA - C - N ANGL. DEV. = -14.9 DEGREES
REMARK 500 2 LYS B 78 O - C - N ANGL. DEV. = 12.9 DEGREES
REMARK 500 3 CYS A 19 CA - CB - SG ANGL. DEV. = -8.1 DEGREES
REMARK 500 3 SER A 39 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 3 CYS A 51 CA - CB - SG ANGL. DEV. = -7.8 DEGREES
REMARK 500 3 GLU A 59 N - CA - C ANGL. DEV. = -18.6 DEGREES
REMARK 500 3 ALA B 4 O - C - N ANGL. DEV. = -13.2 DEGREES
REMARK 500 3 CYS B 13 CA - CB - SG ANGL. DEV. = -8.4 DEGREES
REMARK 500 3 GLU B 67 O - C - N ANGL. DEV. = 14.1 DEGREES
REMARK 500 3 LEU B 79 N - CA - C ANGL. DEV. = -18.8 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 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 GLU A 13 -4.27 70.69
REMARK 500 1 SER A 14 -78.99 -51.78
REMARK 500 1 GLU A 29 5.14 47.03
REMARK 500 1 GLU A 30 -15.64 -147.09
REMARK 500 1 SER A 39 98.57 -69.62
REMARK 500 1 THR A 40 66.63 -65.55
REMARK 500 1 ALA A 50 20.78 -151.75
REMARK 500 1 LYS B 54 3.39 31.70
REMARK 500 1 TYR B 64 67.33 -106.51
REMARK 500 1 SER B 65 77.44 -57.16
REMARK 500 1 ASP B 74 86.75 -69.66
REMARK 500 1 TYR B 75 -53.29 -161.83
REMARK 500 1 MET B 76 79.90 -67.31
REMARK 500 1 SER B 77 40.63 -146.39
REMARK 500 2 GLU A 8 36.59 -163.99
REMARK 500 2 CYS A 9 66.77 -101.88
REMARK 500 2 GLU A 13 -17.50 36.65
REMARK 500 2 SER A 14 -82.32 -45.49
REMARK 500 2 VAL A 22 -53.09 -136.28
REMARK 500 2 GLU A 29 -3.30 54.39
REMARK 500 2 ASP A 38 -53.36 -129.88
REMARK 500 2 ALA B 16 -2.87 33.59
REMARK 500 2 SER B 19 42.97 -94.87
REMARK 500 2 SER B 25 61.29 37.37
REMARK 500 2 ARG B 53 44.09 -97.29
REMARK 500 2 SER B 65 93.22 -40.87
REMARK 500 2 ASP B 66 7.53 41.43
REMARK 500 2 ALA B 71 -53.74 -138.42
REMARK 500 2 ASP B 74 -54.53 -155.72
REMARK 500 2 LYS B 78 -56.37 -138.01
REMARK 500 3 GLU A 13 -61.64 17.82
REMARK 500 3 SER A 14 -84.29 18.19
REMARK 500 3 VAL A 22 -58.69 -135.94
REMARK 500 3 GLU A 29 15.28 54.14
REMARK 500 3 GLU A 30 -3.93 -167.63
REMARK 500 3 SER A 39 82.31 -65.39
REMARK 500 3 THR A 40 77.19 -66.01
REMARK 500 3 ALA B 4 -92.27 11.63
REMARK 500 3 LEU B 6 44.44 -85.98
REMARK 500 3 LYS B 8 -83.62 12.15
REMARK 500 3 ALA B 22 41.12 -90.05
REMARK 500 3 SER B 25 -165.08 67.02
REMARK 500 3 ALA B 26 -178.81 166.88
REMARK 500 3 PRO B 28 108.56 -58.80
REMARK 500 3 ALA B 34 -27.19 34.59
REMARK 500 3 ARG B 53 54.65 -91.61
REMARK 500 3 TYR B 64 67.41 -113.98
REMARK 500 3 ASP B 66 -22.13 38.73
REMARK 500 3 GLU B 67 71.65 -169.45
REMARK 500 3 GLU B 68 -35.70 -147.85
REMARK 500 3 ALA B 71 51.28 -113.99
REMARK 500 3 TYR B 75 -50.43 -171.99
REMARK 500 3 LYS B 78 -39.36 -161.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE A 4 ASP A 5 1 -148.20
REMARK 500 ASP A 5 HIS A 6 1 142.91
REMARK 500 GLY A 11 CYS A 12 1 51.64
REMARK 500 CYS A 19 PRO A 20 1 -141.95
REMARK 500 GLU A 54 ALA A 55 1 -149.22
REMARK 500 LYS B 20 ALA B 21 1 142.08
REMARK 500 TYR B 64 SER B 65 1 -146.69
REMARK 500 SER B 65 ASP B 66 1 124.87
REMARK 500 LYS B 78 LEU B 79 1 141.35
REMARK 500 GLY A 11 CYS A 12 2 -78.59
REMARK 500 CYS A 19 PRO A 20 2 -147.36
REMARK 500 CYS A 51 PRO A 52 2 -143.11
REMARK 500 CYS B 10 ILE B 11 2 -149.70
REMARK 500 MET B 76 SER B 77 2 137.59
REMARK 500 GLY A 11 CYS A 12 3 -129.02
REMARK 500 CYS A 51 PRO A 52 3 -147.18
REMARK 500 ALA B 21 ALA B 22 3 -144.85
REMARK 500 GLY B 24 SER B 25 3 -149.34
REMARK 500 GLN B 32 GLY B 33 3 145.34
REMARK 500 TYR B 64 SER B 65 3 -134.78
REMARK 500 LYS B 78 LEU B 79 3 140.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 TYR B 64 0.13 SIDE CHAIN
REMARK 500 2 TYR B 49 0.09 SIDE CHAIN
REMARK 500 2 TYR B 75 0.30 SIDE CHAIN
REMARK 500 3 TYR B 7 0.08 SIDE CHAIN
REMARK 500 3 TYR B 44 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 MET B 76 11.62
REMARK 500 2 ASP B 17 -10.17
REMARK 500 2 GLY B 24 -30.30
REMARK 500 3 GLY B 24 20.42
REMARK 500 3 TYR B 64 -10.79
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 SF4 A 60 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 9 SG
REMARK 620 2 SF4 A 60 FE3 142.7
REMARK 620 3 SF4 A 60 S2 106.0 56.7
REMARK 620 4 SF4 A 60 FE4 141.0 62.0 57.3
REMARK 620 5 SF4 A 60 FE2 148.1 61.1 105.9 60.5
REMARK 620 6 SF4 A 60 S3 109.9 107.2 110.5 57.1 56.5
REMARK 620 7 SF4 A 60 S4 112.6 56.8 109.6 106.4 56.6 108.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 60 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SF4 A 60 FE3
REMARK 620 2 SF4 A 60 S2 55.5
REMARK 620 3 SF4 A 60 FE1 59.2 56.7
REMARK 620 4 SF4 A 60 FE2 60.2 105.4 60.5
REMARK 620 5 SF4 A 60 S3 104.5 109.5 56.7 56.4
REMARK 620 6 SF4 A 60 S1 55.4 106.2 104.0 56.3 109.3
REMARK 620 7 CYS A 12 SG 150.0 109.7 139.1 144.4 105.1 116.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 60 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 15 SG
REMARK 620 2 SF4 A 60 S2 108.7
REMARK 620 3 SF4 A 60 FE1 143.7 56.8
REMARK 620 4 SF4 A 60 FE4 145.5 56.1 58.9
REMARK 620 5 SF4 A 60 FE2 146.2 105.1 60.0 59.1
REMARK 620 6 SF4 A 60 S4 110.7 109.6 56.7 103.8 56.2
REMARK 620 7 SF4 A 60 S1 112.0 107.4 104.3 56.1 56.1 108.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 60 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SF4 A 60 FE3
REMARK 620 2 CYS A 51 SG 145.6
REMARK 620 3 SF4 A 60 FE1 58.9 144.0
REMARK 620 4 SF4 A 60 FE4 60.7 145.3 59.0
REMARK 620 5 SF4 A 60 S3 105.1 109.2 56.2 56.5
REMARK 620 6 SF4 A 60 S4 55.8 109.8 56.1 104.8 107.5
REMARK 620 7 SF4 A 60 S1 55.7 112.9 103.1 56.6 109.7 107.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 80 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEC B 80 NC
REMARK 620 2 HEC B 80 NB 89.3
REMARK 620 3 HEC B 80 ND 89.7 178.9
REMARK 620 4 MET B 57 SD 89.9 87.6 92.1
REMARK 620 5 HIS B 14 NE2 91.7 92.5 87.8 178.4
REMARK 620 6 HEC B 80 NA 178.4 90.6 90.5 91.6 86.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 80
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DVH RELATED DB: PDB
REMARK 900 CYTOCHROME C553 (REDUCED) (NMR, 36 STRUCTURES)
REMARK 900 RELATED ID: 2DVH RELATED DB: PDB
REMARK 900 THE Y64A MUTANT OF CYTOCHROME C553 FROM DESULFOVIBRIO
REMARK 900 VULGARIS HILDENBOROUGH, NMR, 39 STRUCTURES
REMARK 900 RELATED ID: 1FXD RELATED DB: PDB
REMARK 900 FERREDOXIN II OF DESULFOVIBRIO GIGAS (CRYSTAL STRUCTURE)
DBREF 1DWL A 1 59 UNP P07485 FER1_DESDN 1 59
DBREF 1DWL B 1 79 UNP P04032 C553_DESVH 25 103
SEQRES 1 A 59 THR ILE VAL ILE ASP HIS GLU GLU CYS ILE GLY CYS GLU
SEQRES 2 A 59 SER CYS VAL GLU LEU CYS PRO GLU VAL PHE ALA MET ILE
SEQRES 3 A 59 ASP GLY GLU GLU LYS ALA MET VAL THR ALA PRO ASP SER
SEQRES 4 A 59 THR ALA GLU CYS ALA GLN ASP ALA ILE ASP ALA CYS PRO
SEQRES 5 A 59 VAL GLU ALA ILE SER LYS GLU
SEQRES 1 B 79 ALA ASP GLY ALA ALA LEU TYR LYS SER CYS ILE GLY CYS
SEQRES 2 B 79 HIS GLY ALA ASP GLY SER LYS ALA ALA MET GLY SER ALA
SEQRES 3 B 79 LYS PRO VAL LYS GLY GLN GLY ALA GLU GLU LEU TYR LYS
SEQRES 4 B 79 LYS MET LYS GLY TYR ALA ASP GLY SER TYR GLY GLY GLU
SEQRES 5 B 79 ARG LYS ALA MET MET THR ASN ALA VAL LYS LYS TYR SER
SEQRES 6 B 79 ASP GLU GLU LEU LYS ALA LEU ALA ASP TYR MET SER LYS
SEQRES 7 B 79 LEU
HET SF4 A 60 8
HET HEC B 80 47
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM HEC HEME C
FORMUL 3 SF4 FE4 S4 2+
FORMUL 4 HEC C34 H34 FE N4 O4
HELIX 1 1 GLU A 13 LEU A 18 5 6
HELIX 2 2 ALA A 41 ASP A 46 5 6
HELIX 3 3 ASP A 46 CYS A 51 5 6
HELIX 4 4 ASP B 2 TYR B 7 5 6
HELIX 5 5 CYS B 10 GLY B 15 1 6
HELIX 6 6 GLY B 33 ASP B 46 1 14
HELIX 7 7 LYS B 54 TYR B 64 1 11
HELIX 8 8 GLU B 67 ALA B 73 1 7
SHEET 1 A 2 ILE A 2 ILE A 4 0
SHEET 2 A 2 ILE A 56 LYS A 58 -1 O SER A 57 N VAL A 3
SHEET 1 B 2 PHE A 23 ASP A 27 0
SHEET 2 B 2 ALA A 32 VAL A 34 -1 O MET A 33 N ALA A 24
LINK FE1 SF4 A 60 SG CYS A 9 1555 1555 2.32
LINK FE4 SF4 A 60 SG CYS A 12 1555 1555 2.28
LINK FE3 SF4 A 60 SG CYS A 15 1555 1555 2.34
LINK FE2 SF4 A 60 SG CYS A 51 1555 1555 2.34
LINK SG CYS B 10 CAB HEC B 80 1555 1555 1.83
LINK SG CYS B 13 CAC HEC B 80 1555 1555 1.83
LINK FE HEC B 80 NE2 HIS B 14 1555 1555 2.17
LINK FE HEC B 80 SD MET B 57 1555 1555 2.33
SITE 1 AC1 12 ILE A 4 CYS A 9 GLY A 11 CYS A 12
SITE 2 AC1 12 GLU A 13 SER A 14 CYS A 15 ASP A 27
SITE 3 AC1 12 ALA A 47 ALA A 50 CYS A 51 PRO A 52
SITE 1 AC2 24 CYS A 12 SER A 14 TYR B 7 CYS B 10
SITE 2 AC2 24 CYS B 13 HIS B 14 MET B 23 ALA B 26
SITE 3 AC2 24 LYS B 27 VAL B 29 LEU B 37 LYS B 40
SITE 4 AC2 24 MET B 41 TYR B 44 TYR B 49 GLY B 51
SITE 5 AC2 24 GLU B 52 ARG B 53 LYS B 54 MET B 56
SITE 6 AC2 24 MET B 57 TYR B 64 LEU B 72 MET B 76
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 - 25 20 Bytes