Header list of 1e08.pdb file
Complete list - 27 20 Bytes
HEADER HYDROGENASE 13-MAR-00 1E08
TITLE STRUCTURAL MODEL OF THE [FE]-HYDROGENASE/CYTOCHROME C553 COMPLEX
TITLE 2 COMBINING NMR AND SOFT-DOCKING
CAVEAT 1E08 MET A 54 HAS WRONG CHIRALITY AT ATOM CA ILE A 60 HAS WRONG
CAVEAT 2 1E08 CHIRALITY AT ATOM CB CYS A 142 HAS WRONG CHIRALITY AT ATOM
CAVEAT 3 1E08 CA THR A 148 HAS WRONG CHIRALITY AT ATOM CB PRO A 195 HAS
CAVEAT 4 1E08 WRONG CHIRALITY AT ATOM CA MET A 206 HAS WRONG CHIRALITY AT
CAVEAT 5 1E08 ATOM CA PRO A 319 HAS WRONG CHIRALITY AT ATOM CA LEU D 71
CAVEAT 6 1E08 HAS WRONG CHIRALITY AT ATOM CA HIS D 91 HAS WRONG CHIRALITY
CAVEAT 7 1E08 AT ATOM CA SER E 9 HAS WRONG CHIRALITY AT ATOM CA THERE ARE
CAVEAT 8 1E08 CHIRALITY ERRORS IN C-ALPHA CENTERS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: [FE]-HYDROGENASE (LARGE SUBUNIT);
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: [FE]-HYDROGENASE (SMALL SUBUNIT);
COMPND 6 CHAIN: D;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: CYTOCHROME C553;
COMPND 9 CHAIN: E
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO DESULFURICANS;
SOURCE 3 ORGANISM_TAXID: 876;
SOURCE 4 ATCC: 7757;
SOURCE 5 CELLULAR_LOCATION: PERIPLASM;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: DESULFOVIBRIO DESULFURICANS;
SOURCE 8 ORGANISM_TAXID: 876;
SOURCE 9 ATCC: 7757;
SOURCE 10 CELLULAR_LOCATION: PERIPLASM;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS;
SOURCE 13 ORGANISM_TAXID: 882;
SOURCE 14 STRAIN: HILDENBOROUGH;
SOURCE 15 CELLULAR_LOCATION: PERIPLASM
KEYWDS HYDROGENASE, CYTOCHROME C553, ELECTRON TRANSFER COMPLEX
EXPDTA SOLUTION NMR; THEORETICAL MODEL
MDLTYP MINIMIZED AVERAGE
AUTHOR X.MORELLI,M.CZJZEK,C.E.HATCHIKIAN,O.BORNET,J.C.FONTECILLA-CAMPS,
AUTHOR 2 N.P.PALMA,J.J.G.MOURA,F.GUERLESQUIN
REVDAT 7 27-NOV-19 1E08 1 REMARK LINK
REVDAT 6 25-SEP-19 1E08 1 CAVEAT COMPND HET HETNAM
REVDAT 6 2 1 HETSYN FORMUL LINK ATOM
REVDAT 5 21-AUG-19 1E08 1 REMARK LINK
REVDAT 4 24-FEB-09 1E08 1 VERSN
REVDAT 3 01-AUG-03 1E08 1 DBREF SEQRES LINK
REVDAT 2 31-AUG-00 1E08 1 FORMUL
REVDAT 1 25-AUG-00 1E08 0
JRNL AUTH X.MORELLI,M.CZJZEK,C.E.HATCHIKIAN,O.BORNET,
JRNL AUTH 2 J.C.FONTECILLA-CAMPS,N.P.PALMA,J.J.MOURA,F.GUERLESQUIN
JRNL TITL STRUCTURAL MODEL OF THE FE-HYDROGENASE/CYTOCHROME C553
JRNL TITL 2 COMPLEX COMBINING TRANSVERSE RELAXATION-OPTIMIZED
JRNL TITL 3 SPECTROSCOPY EXPERIMENTS AND SOFT DOCKING CALCULATIONS.
JRNL REF J.BIOL.CHEM. V. 275 23204 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10748163
JRNL DOI 10.1074/JBC.M909835199
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH X.MORELLI,A.DOLLA,M.CZJZEK,P.N.PALMA,F.BLASCO,L.KRIPPAHL,
REMARK 1 AUTH 2 J.J.G.MOURA
REMARK 1 TITL HETERONUCLEAR NMR AND SOFT DOCKING: AN EXPERIMENTAL APPROACH
REMARK 1 TITL 2 FOR A STRUCTURAL MODEL OF THE CYTOCHROME C553-FERREDOXIN
REMARK 1 TITL 3 COMPLEX
REMARK 1 REF BIOCHEMISTRY V. 39 2530 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 10704202
REMARK 1 DOI 10.1021/BI992306S
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE DEPOSITED STRUCTURE IS THE RESULT
REMARK 3 OF A HETERONUCLEAR NMR EXPERIMENT AND DOCKING SIMULATIONS. THE
REMARK 3 FINAL RESULT WAS MINIMIZED BY MOLECULAR DYNAMIC MINIMIZATION.
REMARK 4
REMARK 4 1E08 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1290004651.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.6
REMARK 210 IONIC STRENGTH : 10MM TRIS/HCL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10% D2O/90% WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TROSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : UXNMR UXNMR
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST SHIFT VARIATION VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: COMBINED DOCKING AND NMR FILTERING SOLUTION. THE TROSY
REMARK 210 EXPERIMENT WAS PERFORMED ON THE 15N-LABELED CYTOCHROME WITH
REMARK 210 SUBSEQUENTLY ADDING OF THE HYDROGENASE. THE RESIDUES HAVING THE
REMARK 210 STRONGEST SHIFTS WERE USED TO FILTER THE DOCKING SOLUTIONS.THE
REMARK 210 AMINO-ACIDS ALA E5, CYS E10, HIS E14, GLY E15, ALA E16, ALA E22,
REMARK 210 GLY E24, VAL E29, GLN E32, LYS E54, ASN E59, ALA E60 OF THE
REMARK 210 CYTOCHROME C553 SHOW STRONGEST SHIFTS IN THE TROSY EXPERIMENTS.
REMARK 210 EACH TIME ONE OF THE AMINO ACIDS IS IN CONTACT (LESS THAN 5A IN
REMARK 210 THE COMPLEX) WITH ITS PARTNER ONE POINT IS ATTRIBUTED TO THE
REMARK 210 STRUCTURE. THEN THE ONE THOUSAND BEST STRUCTURES ARE RANKED
REMARK 210 ACCORDING TO THIS CRITERIUM AND THE 10 BEST SOLUTIONS ARE
REMARK 210 MINIMISED. A COMPARISON OF THESE SOLUTIONS GENERATES STRUCTURE
REMARK 210 WITH 5 IDENTICAL SOLUTIONS
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
REMARK 220 REMARK: THIS THEORETICAL MODEL ENTRY WAS NOT ANNOTATED AND NOT
REMARK 220 VALIDATED BY THE WWPDB STAFF AND THEREFORE MAY NOT CONFORM
REMARK 220 TO THE PDB FORMAT.
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 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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E
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 FE FE2 A 5 FE FE2 A 6 0.81
REMARK 500 O LYS D 73 CG GLU D 77 1.18
REMARK 500 FE FE2 A 5 O HOH A 11 1.27
REMARK 500 FE FE2 A 6 O HOH A 11 1.31
REMARK 500 FE FE2 A 6 C CYN A 7 1.41
REMARK 500 FE FE2 A 5 C CMO A 10 1.42
REMARK 500 FE FE2 A 6 C CMO A 9 1.43
REMARK 500 O GLU D 123 HG SER E 19 1.47
REMARK 500 O ALA A 397 H2 ASP E 2 1.48
REMARK 500 C ILE A 63 H GLU A 64 1.48
REMARK 500 H ALA A 109 S1 PDT A 4 1.49
REMARK 500 O THR A 145 H2 HOH A 11 1.49
REMARK 500 O ALA A 293 H1 HOH A 11 1.49
REMARK 500 FE FE2 A 5 C CYN A 8 1.52
REMARK 500 C GLN A 71 H CYS A 72 1.54
REMARK 500 O ASP A 31 H ALA A 33 1.55
REMARK 500 O PRO A 173 HD1 HIS A 196 1.56
REMARK 500 CA GLN A 29 H ILE A 30 1.57
REMARK 500 OXT ALA A 397 H ALA E 4 1.59
REMARK 500 O HIS D 85 ZN ZN D 12 1.61
REMARK 500 CA GLN A 29 N ILE A 30 1.61
REMARK 500 O PHE A 27 N VAL A 28 1.63
REMARK 500 O HIS D 82 ZN ZN D 12 1.64
REMARK 500 NE2 HIS D 82 ZN ZN D 12 1.64
REMARK 500 O LYS D 73 CD GLU D 77 1.75
REMARK 500 O GLN A 29 N ILE A 30 1.76
REMARK 500 OE1 GLN A 71 O CYS A 384 1.89
REMARK 500 OG1 THR A 40 CA GLY E 12 2.05
REMARK 500 FE FE2 A 5 C CYN A 7 2.06
REMARK 500 S2 PDT A 4 C CYN A 8 2.12
REMARK 500 OG1 THR A 40 N GLY E 12 2.13
REMARK 500 FE FE2 A 6 C CMO A 10 2.14
REMARK 500 FE FE2 A 5 C CMO A 9 2.14
REMARK 500 NZ LYS E 42 OD1 ASP E 66 2.18
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 PHE A 27 C VAL A 28 N -0.324
REMARK 500 GLN A 29 C ILE A 30 N 0.205
REMARK 500 GLU A 64 C ALA A 65 N 0.207
REMARK 500 ALA A 65 N ALA A 65 CA 0.201
REMARK 500 ALA A 65 C CYS A 66 N -0.330
REMARK 500 GLN A 71 C CYS A 72 N -0.184
REMARK 500 SER A 202 C PRO A 203 N -0.161
REMARK 500 PRO A 203 CD PRO A 203 N -0.147
REMARK 500 VAL A 347 N VAL A 347 CA -0.131
REMARK 500 GLU D 77 C LYS D 78 N -0.391
REMARK 500 VAL D 99 N VAL D 99 CA -0.145
REMARK 500 PRO D 109 CD PRO D 109 N -0.143
REMARK 500 PRO D 109 C PRO D 109 O 0.131
REMARK 500 TYR E 64 C SER E 65 N -0.142
REMARK 500 GLU E 67 N GLU E 67 CA 0.126
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 PHE A 27 CA - C - N ANGL. DEV. = 24.3 DEGREES
REMARK 500 PHE A 27 O - C - N ANGL. DEV. = -25.6 DEGREES
REMARK 500 VAL A 28 C - N - CA ANGL. DEV. = 26.5 DEGREES
REMARK 500 VAL A 28 CA - C - N ANGL. DEV. = -22.8 DEGREES
REMARK 500 VAL A 28 O - C - N ANGL. DEV. = 23.1 DEGREES
REMARK 500 GLN A 29 C - N - CA ANGL. DEV. = 18.9 DEGREES
REMARK 500 GLN A 29 CA - C - N ANGL. DEV. = -53.3 DEGREES
REMARK 500 GLN A 29 O - C - N ANGL. DEV. = -45.1 DEGREES
REMARK 500 ILE A 63 CA - C - N ANGL. DEV. = -22.6 DEGREES
REMARK 500 ILE A 63 O - C - N ANGL. DEV. = 26.7 DEGREES
REMARK 500 GLU A 64 C - N - CA ANGL. DEV. = 19.6 DEGREES
REMARK 500 GLU A 64 N - CA - CB ANGL. DEV. = 12.2 DEGREES
REMARK 500 GLU A 64 CA - C - N ANGL. DEV. = -15.2 DEGREES
REMARK 500 GLU A 64 O - C - N ANGL. DEV. = 24.1 DEGREES
REMARK 500 ALA A 65 C - N - CA ANGL. DEV. = 17.7 DEGREES
REMARK 500 ALA A 65 O - C - N ANGL. DEV. = 13.3 DEGREES
REMARK 500 GLN A 71 O - C - N ANGL. DEV. = -21.6 DEGREES
REMARK 500 TRP A 87 CA - CB - CG ANGL. DEV. = 12.1 DEGREES
REMARK 500 PRO A 108 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 SER A 202 O - C - N ANGL. DEV. = -17.7 DEGREES
REMARK 500 PRO A 203 CA - C - N ANGL. DEV. = 16.2 DEGREES
REMARK 500 ASP A 255 CA - C - N ANGL. DEV. = 14.0 DEGREES
REMARK 500 ASP A 255 O - C - N ANGL. DEV. = -13.3 DEGREES
REMARK 500 ILE A 295 CB - CA - C ANGL. DEV. = -29.5 DEGREES
REMARK 500 LYS A 346 CA - C - N ANGL. DEV. = -20.3 DEGREES
REMARK 500 LYS A 346 O - C - N ANGL. DEV. = 23.1 DEGREES
REMARK 500 ALA A 397 N - CA - C ANGL. DEV. = -18.9 DEGREES
REMARK 500 ILE D 39 N - CA - CB ANGL. DEV. = 17.2 DEGREES
REMARK 500 ILE D 39 CA - CB - CG1 ANGL. DEV. = 20.8 DEGREES
REMARK 500 GLY D 81 O - C - N ANGL. DEV. = -12.3 DEGREES
REMARK 500 GLY D 98 CA - C - N ANGL. DEV. = -13.7 DEGREES
REMARK 500 GLY D 98 O - C - N ANGL. DEV. = 15.1 DEGREES
REMARK 500 VAL D 99 CA - CB - CG1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 LYS D 107 CA - C - N ANGL. DEV. = -13.8 DEGREES
REMARK 500 LYS D 107 O - C - N ANGL. DEV. = 13.9 DEGREES
REMARK 500 LEU D 108 C - N - CA ANGL. DEV. = 19.9 DEGREES
REMARK 500 LEU D 108 CA - CB - CG ANGL. DEV. = -16.1 DEGREES
REMARK 500 LEU D 108 N - CA - C ANGL. DEV. = 24.6 DEGREES
REMARK 500 LEU D 108 CA - C - N ANGL. DEV. = 24.7 DEGREES
REMARK 500 LEU D 108 O - C - N ANGL. DEV. = -22.4 DEGREES
REMARK 500 PRO D 109 CA - C - N ANGL. DEV. = -16.2 DEGREES
REMARK 500 PRO D 109 O - C - N ANGL. DEV. = 13.2 DEGREES
REMARK 500 GLY D 118 C - N - CA ANGL. DEV. = -15.9 DEGREES
REMARK 500 PRO D 119 O - C - N ANGL. DEV. = 19.3 DEGREES
REMARK 500 TYR D 120 CA - C - N ANGL. DEV. = -25.3 DEGREES
REMARK 500 TYR D 120 O - C - N ANGL. DEV. = 23.3 DEGREES
REMARK 500 GLU D 123 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 LEU E 79 N - CA - C ANGL. DEV. = -17.3 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 GLN A 29 171.03 -39.45
REMARK 500 ALA A 33 -24.43 -146.47
REMARK 500 LYS A 34 64.25 -111.04
REMARK 500 ILE A 36 37.29 -92.57
REMARK 500 CYS A 38 -53.89 86.41
REMARK 500 ASP A 39 -163.45 63.24
REMARK 500 MET A 54 94.58 -48.62
REMARK 500 GLU A 56 -159.43 -128.20
REMARK 500 GLU A 64 -67.83 163.23
REMARK 500 ALA A 65 -24.07 -33.49
REMARK 500 GLN A 71 -30.17 51.66
REMARK 500 ALA A 84 -106.92 48.47
REMARK 500 TRP A 87 37.97 -83.99
REMARK 500 CYS A 142 -156.57 117.75
REMARK 500 THR A 145 32.00 -70.52
REMARK 500 ASP A 169 52.60 -94.69
REMARK 500 PRO A 195 -83.10 33.83
REMARK 500 SER A 198 109.34 -48.08
REMARK 500 CYS A 200 94.51 -67.90
REMARK 500 SER A 202 137.98 -23.72
REMARK 500 PRO A 203 -30.06 -26.57
REMARK 500 LEU A 210 -67.17 -95.04
REMARK 500 THR A 228 100.53 -54.55
REMARK 500 ILE A 254 -70.35 -10.11
REMARK 500 ASP A 255 -95.46 61.39
REMARK 500 ASP A 279 159.86 176.82
REMARK 500 ASP A 283 76.81 -107.08
REMARK 500 SER A 284 35.97 -68.29
REMARK 500 ALA A 293 15.78 -166.55
REMARK 500 ILE A 295 -15.07 -164.03
REMARK 500 GLU A 312 51.04 -106.51
REMARK 500 ALA A 313 -56.02 -157.78
REMARK 500 VAL A 314 -62.61 -100.82
REMARK 500 THR A 315 47.52 -84.64
REMARK 500 LYS A 317 51.13 -92.62
REMARK 500 LYS A 318 98.82 -59.57
REMARK 500 PHE A 324 41.72 -90.93
REMARK 500 ARG A 328 59.64 -118.44
REMARK 500 VAL A 340 59.68 -119.02
REMARK 500 PRO A 369 33.29 -86.55
REMARK 500 PRO A 379 89.39 -56.74
REMARK 500 LEU A 395 -67.60 -122.06
REMARK 500 SER D 74 36.62 -93.36
REMARK 500 TYR D 75 -59.96 -162.70
REMARK 500 GLU D 77 6.39 56.17
REMARK 500 LEU D 80 5.72 56.68
REMARK 500 LYS D 83 -75.47 -57.33
REMARK 500 HIS D 85 82.32 -65.22
REMARK 500 ASP D 86 -48.85 -155.96
REMARK 500 LEU D 88 -62.06 -168.64
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
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 PHE A 27 VAL A 28 -46.39
REMARK 500 CYS A 76 PRO A 77 -123.66
REMARK 500 ALA A 80 ILE A 81 141.69
REMARK 500 ALA A 84 GLN A 85 149.92
REMARK 500 GLY A 123 SER A 124 142.42
REMARK 500 TRP A 143 ASP A 144 -149.91
REMARK 500 LEU A 194 PRO A 195 121.92
REMARK 500 SER A 198 THR A 199 -142.64
REMARK 500 PRO A 233 CYS A 234 -148.99
REMARK 500 GLY A 300 GLY A 301 144.51
REMARK 500 VAL A 314 THR A 315 -143.89
REMARK 500 VAL A 394 LEU A 395 147.10
REMARK 500 VAL D 36 LYS D 37 144.29
REMARK 500 GLU D 77 LYS D 78 144.34
REMARK 500 GLY D 81 HIS D 82 -131.43
REMARK 500 HIS D 89 THR D 90 148.61
REMARK 500 THR D 90 HIS D 91 -132.91
REMARK 500 LEU D 108 PRO D 109 115.56
REMARK 500 ALA E 22 MET E 23 -140.15
REMARK 500 LYS E 78 LEU E 79 -79.80
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 TYR A 112 0.12 SIDE CHAIN
REMARK 500 TYR A 189 0.12 SIDE CHAIN
REMARK 500 TYR A 214 0.07 SIDE CHAIN
REMARK 500 TYR A 311 0.12 SIDE CHAIN
REMARK 500 PHE A 356 0.09 SIDE CHAIN
REMARK 500 TYR A 375 0.11 SIDE CHAIN
REMARK 500 TYR D 51 0.10 SIDE CHAIN
REMARK 500 HIS D 82 0.24 SIDE CHAIN
REMARK 500 TYR E 7 0.19 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 ANGLE, 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 PHE A 27 -15.17
REMARK 500 GLN A 29 -31.36
REMARK 500 CYS A 41 -20.89
REMARK 500 ASP A 255 13.32
REMARK 500 ALA A 348 17.08
REMARK 500 GLY D 81 16.60
REMARK 500 LEU D 108 21.81
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 1 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 35 SG
REMARK 620 2 SF4 A 1 S1 105.1
REMARK 620 3 SF4 A 1 S2 108.0 108.7
REMARK 620 4 SF4 A 1 S4 114.4 109.9 110.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 1 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 38 SG
REMARK 620 2 SF4 A 1 S1 112.2
REMARK 620 3 SF4 A 1 S3 106.4 108.9
REMARK 620 4 SF4 A 1 S4 111.1 109.1 109.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 1 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 41 SG
REMARK 620 2 SF4 A 1 S1 104.5
REMARK 620 3 SF4 A 1 S2 116.6 108.6
REMARK 620 4 SF4 A 1 S3 110.3 109.5 107.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 2 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 45 SG
REMARK 620 2 SF4 A 2 S1 110.5
REMARK 620 3 SF4 A 2 S2 112.0 109.8
REMARK 620 4 SF4 A 2 S3 108.9 109.5 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 2 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 66 SG
REMARK 620 2 SF4 A 2 S1 107.3
REMARK 620 3 SF4 A 2 S3 112.4 110.6
REMARK 620 4 SF4 A 2 S4 106.7 107.9 111.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 2 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 69 SG
REMARK 620 2 SF4 A 2 S1 112.2
REMARK 620 3 SF4 A 2 S2 110.9 109.8
REMARK 620 4 SF4 A 2 S4 109.3 106.7 107.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 2 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 72 SG
REMARK 620 2 SF4 A 2 S2 101.4
REMARK 620 3 SF4 A 2 S3 113.7 106.1
REMARK 620 4 SF4 A 2 S4 116.4 107.8 110.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 1 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 76 SG
REMARK 620 2 SF4 A 1 S2 114.9
REMARK 620 3 SF4 A 1 S3 106.7 106.5
REMARK 620 4 SF4 A 1 S4 109.7 110.0 108.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 3 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 179 SG
REMARK 620 2 SF4 A 3 S1 115.9
REMARK 620 3 SF4 A 3 S3 113.9 111.3
REMARK 620 4 SF4 A 3 S4 101.6 106.1 106.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 3 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 234 SG
REMARK 620 2 SF4 A 3 S2 110.7
REMARK 620 3 SF4 A 3 S3 110.5 106.1
REMARK 620 4 SF4 A 3 S4 109.6 113.9 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 3 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 378 SG
REMARK 620 2 SF4 A 3 S1 105.9
REMARK 620 3 SF4 A 3 S2 112.7 105.2
REMARK 620 4 SF4 A 3 S4 113.4 105.0 113.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 3 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 382 SG
REMARK 620 2 SF4 A 3 S1 107.7
REMARK 620 3 SF4 A 3 S2 110.9 106.4
REMARK 620 4 SF4 A 3 S3 113.4 111.4 107.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC E 80 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 14 NE2
REMARK 620 2 HEC E 80 NA 89.0
REMARK 620 3 HEC E 80 NB 86.9 90.8
REMARK 620 4 HEC E 80 NC 93.2 177.8 89.8
REMARK 620 5 HEC E 80 ND 95.5 90.3 177.3 89.0
REMARK 620 6 MET E 57 SD 170.7 89.9 83.8 88.0 93.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 6 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PDT A 4 S1
REMARK 620 2 PDT A 4 S2 29.1
REMARK 620 3 CYN A 7 N 106.3 87.7
REMARK 620 4 CMO A 9 O 84.5 97.3 66.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 5 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PDT A 4 S1
REMARK 620 2 PDT A 4 S2 31.4
REMARK 620 3 CYN A 8 N 57.0 72.0
REMARK 620 4 CMO A 10 O 101.6 80.1 74.8
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 FE2 A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN A 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDT A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 80
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HFE RELATED DB: PDB
REMARK 900 HYDROGENASE 1.6 A RESOLUTION STRUCTURE OF THE FE-ONLY HYDROGENASE
REMARK 900 FROM DESULFOVIBRIO DESULFURICANS
REMARK 900 RELATED ID: 1DVH RELATED DB: PDB
REMARK 900 CYTOCHROME C553 (REDUCED) (NMR, 36 STRUCTURES)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINAL END C-TERMINAL RESIDUES WERE NOT DEPOSITED IN
REMARK 999 THE INITIAL PDB ENTRY 1HFE
REMARK 999 TER
REMARK 999 ALA: THE C-TERMINAL RESIDUES 398-421 ARE NOT PRESENT IN THE
REMARK 999 PDB FILE OF HYDROGENASE 1HFE
DBREF 1E08 A 27 397 PDB 1E08 1E08 27 397
DBREF 1E08 D 36 123 PDB 1E08 1E08 36 123
DBREF 1E08 E 2 79 PDB 1E08 1E08 2 79
SEQRES 1 A 371 PHE VAL GLN ILE ASP GLU ALA LYS CYS ILE GLY CYS ASP
SEQRES 2 A 371 THR CYS SER GLN TYR CYS PRO THR ALA ALA ILE PHE GLY
SEQRES 3 A 371 GLU MET GLY GLU PRO HIS SER ILE PRO HIS ILE GLU ALA
SEQRES 4 A 371 CYS ILE ASN CYS GLY GLN CYS LEU THR HIS CYS PRO GLU
SEQRES 5 A 371 ASN ALA ILE TYR GLU ALA GLN SER TRP VAL PRO GLU VAL
SEQRES 6 A 371 GLU LYS LYS LEU LYS ASP GLY LYS VAL LYS CYS ILE ALA
SEQRES 7 A 371 MET PRO ALA PRO ALA VAL ARG TYR ALA LEU GLY ASP ALA
SEQRES 8 A 371 PHE GLY MET PRO VAL GLY SER VAL THR THR GLY LYS MET
SEQRES 9 A 371 LEU ALA ALA LEU GLN LYS LEU GLY PHE ALA HIS CYS TRP
SEQRES 10 A 371 ASP THR GLU PHE THR ALA ASP VAL THR ILE TRP GLU GLU
SEQRES 11 A 371 GLY SER GLU PHE VAL GLU ARG LEU THR LYS LYS SER ASP
SEQRES 12 A 371 MET PRO LEU PRO GLN PHE THR SER CYS CYS PRO GLY TRP
SEQRES 13 A 371 GLN LYS TYR ALA GLU THR TYR TYR PRO GLU LEU LEU PRO
SEQRES 14 A 371 HIS PHE SER THR CYS LYS SER PRO ILE GLY MET ASN GLY
SEQRES 15 A 371 ALA LEU ALA LYS THR TYR GLY ALA GLU ARG MET LYS TYR
SEQRES 16 A 371 ASP PRO LYS GLN VAL TYR THR VAL SER ILE MET PRO CYS
SEQRES 17 A 371 ILE ALA LYS LYS TYR GLU GLY LEU ARG PRO GLU LEU LYS
SEQRES 18 A 371 SER SER GLY MET ARG ASP ILE ASP ALA THR LEU THR THR
SEQRES 19 A 371 ARG GLU LEU ALA TYR MET ILE LYS LYS ALA GLY ILE ASP
SEQRES 20 A 371 PHE ALA LYS LEU PRO ASP GLY LYS ARG ASP SER LEU MET
SEQRES 21 A 371 GLY GLU SER THR GLY GLY ALA THR ILE PHE GLY VAL THR
SEQRES 22 A 371 GLY GLY VAL MET GLU ALA ALA LEU ARG PHE ALA TYR GLU
SEQRES 23 A 371 ALA VAL THR GLY LYS LYS PRO ASP SER TRP ASP PHE LYS
SEQRES 24 A 371 ALA VAL ARG GLY LEU ASP GLY ILE LYS GLU ALA THR VAL
SEQRES 25 A 371 ASN VAL GLY GLY THR ASP VAL LYS VAL ALA VAL VAL HIS
SEQRES 26 A 371 GLY ALA LYS ARG PHE LYS GLN VAL CYS ASP ASP VAL LYS
SEQRES 27 A 371 ALA GLY LYS SER PRO TYR HIS PHE ILE GLU TYR MET ALA
SEQRES 28 A 371 CYS PRO GLY GLY CYS VAL CYS GLY GLY GLY GLN PRO VAL
SEQRES 29 A 371 MET PRO GLY VAL LEU GLU ALA
SEQRES 1 D 88 VAL LYS GLN ILE LYS ASP TYR MET LEU ASP ARG ILE ASN
SEQRES 2 D 88 GLY VAL TYR GLY ALA ASP ALA LYS PHE PRO VAL ARG ALA
SEQRES 3 D 88 SER GLN ASP ASN THR GLN VAL LYS ALA LEU TYR LYS SER
SEQRES 4 D 88 TYR LEU GLU LYS PRO LEU GLY HIS LYS SER HIS ASP LEU
SEQRES 5 D 88 LEU HIS THR HIS TRP PHE ASP LYS SER LYS GLY VAL LYS
SEQRES 6 D 88 GLU LEU THR THR ALA GLY LYS LEU PRO ASN PRO ARG ALA
SEQRES 7 D 88 SER GLU PHE GLU GLY PRO TYR PRO TYR GLU
SEQRES 1 E 78 ASP GLY ALA ALA LEU TYR LYS SER CYS ILE GLY CYS HIS
SEQRES 2 E 78 GLY ALA ASP GLY SER LYS ALA ALA MET GLY SER ALA LYS
SEQRES 3 E 78 PRO VAL LYS GLY GLN GLY ALA GLU GLU LEU TYR LYS LYS
SEQRES 4 E 78 MET LYS GLY TYR ALA ASP GLY SER TYR GLY GLY GLU ARG
SEQRES 5 E 78 LYS ALA MET MET THR ASN ALA VAL LYS LYS TYR SER ASP
SEQRES 6 E 78 GLU GLU LEU LYS ALA LEU ALA ASP TYR MET SER LYS LEU
HET SF4 A 1 8
HET SF4 A 2 8
HET SF4 A 3 8
HET PDT A 4 5
HET FE2 A 5 1
HET FE2 A 6 1
HET CYN A 7 2
HET CYN A 8 2
HET CMO A 9 2
HET CMO A 10 2
HET ZN D 12 1
HET HEC E 80 43
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM PDT 1,3-PROPANEDITHIOL
HETNAM FE2 FE (II) ION
HETNAM CYN CYANIDE ION
HETNAM CMO CARBON MONOXIDE
HETNAM ZN ZINC ION
HETNAM HEC HEME C
FORMUL 4 SF4 3(FE4 S4)
FORMUL 7 PDT C3 H8 S2
FORMUL 8 FE2 2(FE 2+)
FORMUL 10 CYN 2(C N 1-)
FORMUL 12 CMO 2(C O)
FORMUL 14 ZN ZN 2+
FORMUL 15 HEC C34 H34 FE N4 O4
FORMUL 16 HOH *(H2 O)
HELIX 1 1 GLN A 71 CYS A 76 1 6
HELIX 2 2 TRP A 87 ASP A 97 1 11
HELIX 3 3 ALA A 107 ALA A 113 1 7
HELIX 4 4 LEU A 114 GLY A 119 5 6
HELIX 5 5 VAL A 125 GLY A 128 5 4
HELIX 6 6 LYS A 129 LEU A 134 1 6
HELIX 7 7 GLN A 135 GLY A 138 5 4
HELIX 8 8 GLU A 146 THR A 165 1 20
HELIX 9 9 CYS A 179 TYR A 190 1 12
HELIX 10 10 LEU A 193 PHE A 197 5 5
HELIX 11 11 SER A 202 LEU A 210 1 9
HELIX 12 12 LEU A 210 MET A 219 1 10
HELIX 13 13 ASP A 222 LYS A 224 5 3
HELIX 14 14 CYS A 234 GLU A 240 1 7
HELIX 15 15 GLY A 241 LYS A 247 5 7
HELIX 16 16 THR A 259 ALA A 270 1 12
HELIX 17 17 ASP A 273 LEU A 277 5 5
HELIX 18 18 THR A 290 THR A 294 5 5
HELIX 19 19 GLY A 301 TYR A 311 1 11
HELIX 20 20 PHE A 324 ARG A 328 5 5
HELIX 21 21 ALA A 353 ALA A 365 1 13
HELIX 22 22 GLY A 381 GLY A 386 1 6
HELIX 23 23 GLN D 38 ALA D 55 1 18
HELIX 24 24 ALA D 61 ASP D 64 5 4
HELIX 25 25 ASN D 65 SER D 74 1 10
HELIX 26 26 SER D 96 LEU D 102 1 7
HELIX 27 27 THR D 103 GLY D 106 5 4
HELIX 28 28 ARG D 112 PHE D 116 5 5
HELIX 29 29 GLY E 3 LYS E 8 1 6
HELIX 30 30 SER E 9 HIS E 14 5 6
HELIX 31 31 GLY E 33 ALA E 45 1 13
HELIX 32 32 ALA E 55 TYR E 64 1 10
HELIX 33 33 GLU E 67 MET E 76 1 10
SHEET 1 A 2 ILE A 50 GLY A 52 0
SHEET 2 A 2 HIS A 58 ILE A 60 -1 N SER A 59 O PHE A 51
SHEET 1 B 3 LYS A 101 PRO A 106 0
SHEET 2 B 3 VAL A 226 ILE A 231 1 N TYR A 227 O LYS A 101
SHEET 3 B 3 ALA A 256 LEU A 258 1 N ALA A 256 O SER A 230
SHEET 1 C 3 ILE A 333 GLU A 335 0
SHEET 2 C 3 ALA A 348 HIS A 351 -1 N VAL A 349 O LYS A 334
SHEET 3 C 3 GLU A 374 MET A 376 1 N GLU A 374 O VAL A 350
SHEET 1 D 2 VAL A 338 VAL A 340 0
SHEET 2 D 2 THR A 343 VAL A 345 -1 N VAL A 345 O VAL A 338
LINK SG CYS A 35 FE3 SF4 A 1 1555 1555 2.27
LINK SG CYS A 38 FE2 SF4 A 1 1555 1555 2.18
LINK SG CYS A 41 FE4 SF4 A 1 1555 1555 2.26
LINK SG CYS A 45 FE4 SF4 A 2 1555 1555 2.26
LINK SG CYS A 66 FE2 SF4 A 2 1555 1555 2.17
LINK SG CYS A 69 FE3 SF4 A 2 1555 1555 2.26
LINK SG CYS A 72 FE1 SF4 A 2 1555 1555 2.24
LINK SG CYS A 76 FE1 SF4 A 1 1555 1555 2.21
LINK SG CYS A 179 FE2 SF4 A 3 1555 1555 2.31
LINK SG CYS A 234 FE1 SF4 A 3 1555 1555 2.28
LINK SG CYS A 378 FE3 SF4 A 3 1555 1555 2.20
LINK SG CYS A 382 FE4 SF4 A 3 1555 1555 2.29
LINK SG CYS E 10 CAB HEC E 80 1555 1555 1.84
LINK SG CYS E 13 CAC HEC E 80 1555 1555 1.84
LINK NE2 HIS E 14 FE HEC E 80 1555 1555 2.25
LINK SD MET E 57 FE HEC E 80 1555 1555 2.30
LINK S1 PDT A 4 FE FE2 A 6 1555 1555 2.54
LINK S1 PDT A 4 FE FE2 A 5 1555 1555 2.37
LINK S1 PDT A 4 C CYN A 8 1555 1555 1.83
LINK S2 PDT A 4 FE FE2 A 6 1555 1555 2.52
LINK S2 PDT A 4 FE FE2 A 5 1555 1555 2.32
LINK FE FE2 A 5 N CYN A 8 1555 1555 2.73
LINK FE FE2 A 5 O CMO A 10 1555 1555 2.48
LINK FE FE2 A 6 N CYN A 7 1555 1555 2.60
LINK FE FE2 A 6 O CMO A 9 1555 1555 2.63
LINK C CYN A 7 C CMO A 9 1555 1555 1.57
LINK C CYN A 8 C CMO A 10 1555 1555 1.43
CISPEP 1 LEU A 131 ALA A 132 0 11.87
CISPEP 2 HIS A 141 CYS A 142 0 -0.23
CISPEP 3 CYS A 142 TRP A 143 0 -16.13
CISPEP 4 MET A 170 PRO A 171 0 -5.55
CISPEP 5 LEU A 172 PRO A 173 0 -9.58
CISPEP 6 MET A 391 PRO A 392 0 6.66
CISPEP 7 HIS D 91 TRP D 92 0 -29.33
SITE 1 AC1 8 PDT A 4 FE2 A 6 CYN A 7 CYN A 8
SITE 2 AC1 8 CMO A 9 CMO A 10 HOH A 11 ALA A 293
SITE 1 AC2 10 PDT A 4 FE2 A 5 CYN A 7 CYN A 8
SITE 2 AC2 10 CMO A 9 CMO A 10 HOH A 11 PRO A 108
SITE 3 AC2 10 THR A 145 ALA A 149
SITE 1 AC3 4 HIS D 82 LYS D 83 HIS D 85 ASP D 86
SITE 1 AC4 10 PDT A 4 FE2 A 5 FE2 A 6 CYN A 8
SITE 2 AC4 10 CMO A 9 CMO A 10 HOH A 11 ALA A 149
SITE 3 AC4 10 PRO A 203 PHE A 296
SITE 1 AC5 13 PDT A 4 FE2 A 5 FE2 A 6 CYN A 7
SITE 2 AC5 13 CMO A 9 CMO A 10 HOH A 11 PRO A 108
SITE 3 AC5 13 ALA A 109 ALA A 293 THR A 294 ILE A 295
SITE 4 AC5 13 PHE A 296
SITE 1 AC6 13 ILE A 30 LYS A 34 CYS A 35 ILE A 36
SITE 2 AC6 13 GLY A 37 CYS A 38 ASP A 39 CYS A 41
SITE 3 AC6 13 SER A 42 HIS A 58 HIS A 75 CYS A 76
SITE 4 AC6 13 ILE A 81
SITE 1 AC7 8 VAL A 28 TYR A 44 CYS A 45 CYS A 66
SITE 2 AC7 8 ASN A 68 CYS A 69 GLY A 70 CYS A 72
SITE 1 AC8 10 CYS A 69 CYS A 179 PRO A 180 CYS A 234
SITE 2 AC8 10 LYS A 237 MET A 376 ALA A 377 CYS A 378
SITE 3 AC8 10 CYS A 382 GLY A 385
SITE 1 AC9 14 FE2 A 5 FE2 A 6 CYN A 7 CYN A 8
SITE 2 AC9 14 CMO A 9 CMO A 10 ALA A 107 PRO A 108
SITE 3 AC9 14 ALA A 109 VAL A 110 LYS A 237 ILE A 295
SITE 4 AC9 14 PHE A 296 GLY A 297
SITE 1 BC1 11 PDT A 4 FE2 A 5 FE2 A 6 CYN A 7
SITE 2 BC1 11 CYN A 8 CMO A 10 HOH A 11 ALA A 107
SITE 3 BC1 11 PRO A 108 THR A 145 PRO A 203
SITE 1 BC2 11 PDT A 4 FE2 A 5 FE2 A 6 CYN A 7
SITE 2 BC2 11 CYN A 8 CMO A 9 HOH A 11 ALA A 293
SITE 3 BC2 11 THR A 294 ILE A 295 PHE A 296
SITE 1 BC3 20 CYS A 38 GLY A 55 CYS E 10 CYS E 13
SITE 2 BC3 20 HIS E 14 MET E 23 GLY E 24 ALA E 26
SITE 3 BC3 20 LYS E 27 GLN E 32 LEU E 37 MET E 41
SITE 4 BC3 20 TYR E 44 TYR E 49 GLY E 51 GLU E 52
SITE 5 BC3 20 ARG E 53 MET E 56 MET E 57 TYR E 64
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
Complete list - 27 20 Bytes