Header list of 1k0t.pdb file
Complete list - r 25 2 Bytes
HEADER ELECTRON TRANSPORT 20-SEP-01 1K0T
TITLE NMR SOLUTION STRUCTURE OF UNBOUND, OXIDIZED PHOTOSYSTEM I SUBUNIT
TITLE 2 PSAC, CONTAINING [4FE-4S] CLUSTERS FA AND FB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PSAC SUBUNIT OF PHOTOSYSTEM I;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 32049;
SOURCE 4 STRAIN: PCC 7002;
SOURCE 5 GENE: PSAC;
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: PET-3D
KEYWDS IRON-SULFUR PROTEIN, SOLUTION STRUCTURE, PARAMAGNETIC, CONFORMATIONAL
KEYWDS 2 CHANGE, ELECTRON TRANSPORT, PHOTOSYSTEM I, PSAC
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR M.L.ANTONKINE,G.LIU,D.BENTROP,D.A.BRYANT,I.BERTINI,C.LUCHINAT,
AUTHOR 2 J.H.GOLBECK,D.STEHLIK
REVDAT 4 13-JUL-11 1K0T 1 VERSN
REVDAT 3 24-MAR-09 1K0T 1 ATOM CONECT
REVDAT 2 24-FEB-09 1K0T 1 VERSN
REVDAT 1 05-JUN-02 1K0T 0
JRNL AUTH M.L.ANTONKINE,G.LIU,D.BENTROP,D.A.BRYANT,I.BERTINI,
JRNL AUTH 2 C.LUCHINAT,J.H.GOLBECK,D.STEHLIK
JRNL TITL SOLUTION STRUCTURE OF THE UNBOUND, OXIDIZED PHOTOSYSTEM I
JRNL TITL 2 SUBUNIT PSAC, CONTAINING [4FE-4S] CLUSTERS F(A) AND F(B): A
JRNL TITL 3 CONFORMATIONAL CHANGE OCCURS UPON BINDING TO PHOTOSYSTEM I.
JRNL REF J.BIOL.INORG.CHEM. V. 7 461 2002
JRNL REFN ISSN 0949-8257
JRNL PMID 11941504
JRNL DOI 10.1007/S00775-001-0321-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUENTERT P, MUMENTHALER C., WUETHRICH K.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-01.
REMARK 100 THE RCSB ID CODE IS RCSB014417.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 285.00; 285.00; 298.00; 298.00
REMARK 210 PH : 7.60; 8.0; 7.6; 8.0
REMARK 210 IONIC STRENGTH : 25 MM; 25 MM; 25 MM; 25 MM
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 2.5MM PSAC U-15N; 25MM PHOSPHATE
REMARK 210 BUFFER PH=7.6; 90% H2O, 10% D2O;
REMARK 210 2.5MM PSAC U-15N; 25MM PHOSPHATE
REMARK 210 BUFFER PH=8.0; 90% H2O, 10% D2O;
REMARK 210 2.5MM PSAC; 25MM PHOSPHATE BUFFER
REMARK 210 PH=8.0; 99% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D DQF-COSY; 2D TOCSY;
REMARK 210 1D-NOE; 3D HSQC-NOESY; 3D-HSQC-
REMARK 210 TOCSY; 1H-15N HSQC; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE 800; AVANCE 600; DRX 500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS COMBINED
REMARK 210 WITH A SIMULATED ANNEALING
REMARK 210 ALGORITHM
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 1H AND 15N NMR
REMARK 210 SPECTROSCOPY. EXPERIMENTAL DETAILS CAN BE FOUND IN THE JRNL
REMARK 210 CITATION ABOVE.
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: 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 SER A 3 164.30 57.29
REMARK 500 1 VAL A 4 35.12 -169.54
REMARK 500 1 LYS A 5 -174.74 -55.09
REMARK 500 1 ASP A 8 42.34 -88.49
REMARK 500 1 ILE A 11 -45.74 -131.70
REMARK 500 1 THR A 14 -31.85 87.47
REMARK 500 1 CYS A 16 -42.31 89.31
REMARK 500 1 ARG A 18 -51.36 -133.15
REMARK 500 1 CYS A 20 93.63 -178.91
REMARK 500 1 ASP A 23 74.55 72.56
REMARK 500 1 VAL A 24 -64.29 -102.11
REMARK 500 1 LEU A 25 92.24 -62.56
REMARK 500 1 CYS A 47 112.00 166.02
REMARK 500 1 VAL A 48 44.28 -104.50
REMARK 500 1 ARG A 52 -63.81 -141.03
REMARK 500 1 CYS A 53 -87.47 -42.42
REMARK 500 1 GLU A 54 41.74 35.97
REMARK 500 1 THR A 55 27.10 -161.82
REMARK 500 1 ALA A 56 90.45 -61.74
REMARK 500 1 CYS A 57 176.53 53.00
REMARK 500 1 THR A 59 -8.29 83.17
REMARK 500 1 PHE A 61 -98.60 -120.22
REMARK 500 1 LEU A 62 89.06 38.18
REMARK 500 1 SER A 63 135.56 -39.54
REMARK 500 1 ILE A 64 91.93 -64.08
REMARK 500 1 ARG A 65 -42.26 -131.43
REMARK 500 1 VAL A 66 136.88 65.61
REMARK 500 1 TYR A 67 -63.64 -159.34
REMARK 500 1 ALA A 70 -64.24 -122.75
REMARK 500 1 THR A 72 48.81 38.40
REMARK 500 2 LYS A 5 160.07 -40.77
REMARK 500 2 ILE A 6 74.48 -68.16
REMARK 500 2 ASP A 8 41.55 -90.03
REMARK 500 2 THR A 14 66.01 -114.23
REMARK 500 2 CYS A 16 -38.97 89.92
REMARK 500 2 ALA A 19 92.79 -69.73
REMARK 500 2 CYS A 20 102.03 179.32
REMARK 500 2 ASP A 23 73.26 64.37
REMARK 500 2 ARG A 43 11.37 -140.12
REMARK 500 2 THR A 44 22.39 44.28
REMARK 500 2 ASP A 46 -166.54 -109.02
REMARK 500 2 CYS A 47 127.19 77.20
REMARK 500 2 ARG A 52 64.08 -159.95
REMARK 500 2 CYS A 53 49.46 177.24
REMARK 500 2 THR A 55 34.27 -167.43
REMARK 500 2 PRO A 58 -74.92 -74.98
REMARK 500 2 THR A 59 -153.57 -140.62
REMARK 500 2 ASP A 60 -46.53 83.67
REMARK 500 2 PHE A 61 -51.83 -120.07
REMARK 500 2 LEU A 62 96.04 -42.90
REMARK 500
REMARK 500 THIS ENTRY HAS 821 RAMACHANDRAN OUTLIERS.
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 SF4 A 81 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 10 SG
REMARK 620 2 SF4 A 81 S2 97.8
REMARK 620 3 SF4 A 81 S3 114.4 104.8
REMARK 620 4 SF4 A 81 S4 131.6 101.2 103.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 SF4 A 81 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 13 SG
REMARK 620 2 SF4 A 81 S1 86.3
REMARK 620 3 SF4 A 81 S3 125.1 107.7
REMARK 620 4 SF4 A 81 S4 114.4 108.8 110.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 SF4 A 81 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 16 SG
REMARK 620 2 SF4 A 81 S1 110.3
REMARK 620 3 SF4 A 81 S2 114.4 107.8
REMARK 620 4 SF4 A 81 S4 116.8 99.4 106.8
REMARK 620 5 GLN A 15 O 71.9 71.5 173.0 66.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 SF4 A 81 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 57 SG
REMARK 620 2 SF4 A 81 S1 120.4
REMARK 620 3 SF4 A 81 S2 124.2 113.1
REMARK 620 4 SF4 A 81 S3 95.9 101.0 88.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 SF4 A 82 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 47 SG
REMARK 620 2 SF4 A 82 S2 121.1
REMARK 620 3 SF4 A 82 S3 114.4 106.5
REMARK 620 4 SF4 A 82 S4 108.2 97.3 107.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 SF4 A 82 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 50 SG
REMARK 620 2 SF4 A 82 S1 103.3
REMARK 620 3 SF4 A 82 S3 122.3 100.7
REMARK 620 4 SF4 A 82 S4 114.4 109.1 105.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 SF4 A 82 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 53 SG
REMARK 620 2 SF4 A 82 S1 104.2
REMARK 620 3 SF4 A 82 S2 114.4 101.8
REMARK 620 4 SF4 A 82 S4 123.0 108.1 103.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 SF4 A 82 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 20 SG
REMARK 620 2 SF4 A 82 S1 114.3
REMARK 620 3 SF4 A 82 S2 136.7 99.7
REMARK 620 4 SF4 A 82 S3 95.2 104.4 101.7
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 SF4 A 81
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 82
DBREF 1K0T A 1 80 UNP P31087 PSAC_SYNP2 1 80
SEQRES 1 A 80 SER HIS SER VAL LYS ILE TYR ASP THR CYS ILE GLY CYS
SEQRES 2 A 80 THR GLN CYS VAL ARG ALA CYS PRO LEU ASP VAL LEU GLU
SEQRES 3 A 80 MET VAL PRO TRP ASP GLY CYS LYS ALA GLY GLN ILE ALA
SEQRES 4 A 80 SER SER PRO ARG THR GLU ASP CYS VAL GLY CYS LYS ARG
SEQRES 5 A 80 CYS GLU THR ALA CYS PRO THR ASP PHE LEU SER ILE ARG
SEQRES 6 A 80 VAL TYR LEU GLY ALA GLU THR THR ARG SER MET GLY LEU
SEQRES 7 A 80 ALA TYR
HET SF4 A 81 8
HET SF4 A 82 8
HETNAM SF4 IRON/SULFUR CLUSTER
FORMUL 2 SF4 2(FE4 S4)
SHEET 1 A 2 GLU A 26 PRO A 29 0
SHEET 2 A 2 GLN A 37 SER A 40 -1 O SER A 40 N GLU A 26
LINK FE1 SF4 A 81 SG CYS A 10 1555 1555 2.18
LINK FE2 SF4 A 81 SG CYS A 13 1555 1555 2.18
LINK FE3 SF4 A 81 SG CYS A 16 1555 1555 2.18
LINK FE4 SF4 A 81 SG CYS A 57 1555 1555 2.15
LINK FE1 SF4 A 82 SG CYS A 47 1555 1555 2.18
LINK FE2 SF4 A 82 SG CYS A 50 1555 1555 2.18
LINK FE3 SF4 A 82 SG CYS A 53 1555 1555 2.18
LINK FE4 SF4 A 82 SG CYS A 20 1555 1555 2.18
LINK O GLN A 15 FE3 SF4 A 81 1555 1555 2.53
SITE 1 AC1 11 THR A 9 CYS A 10 ILE A 11 GLY A 12
SITE 2 AC1 11 CYS A 13 THR A 14 GLN A 15 CYS A 16
SITE 3 AC1 11 VAL A 17 THR A 55 CYS A 57
SITE 1 AC2 9 ALA A 19 CYS A 20 LEU A 22 VAL A 24
SITE 2 AC2 9 CYS A 47 GLY A 49 CYS A 50 ARG A 52
SITE 3 AC2 9 CYS A 53
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