Header list of 1jxf.pdb file
Complete list - t 27 2 Bytes
HEADER PROTON TRANSPORT 07-SEP-01 1JXF
TITLE SOLUTION STRUCTURE OF REDUCED CU(I) PLASTOCYANIN FROM SYNECHOCYSTIS
TITLE 2 PCC6803
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASTOCYANIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;
SOURCE 3 ORGANISM_TAXID: 1148;
SOURCE 4 STRAIN: PCC6803;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BLR(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS COPPER PROTEIN BETA BARREL ELECTRON TRANSFER, PROTON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 35
AUTHOR I.BERTINI,D.A.BRYANT,S.CIURLI,A.DIKIY,C.O.FERNANDEZ,C.LUCHINAT,
AUTHOR 2 N.SAFAROV,A.J.VILA,J.ZHAO
REVDAT 4 27-OCT-21 1JXF 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1JXF 1 VERSN
REVDAT 2 20-MAR-02 1JXF 1 JRNL
REVDAT 1 26-SEP-01 1JXF 0
JRNL AUTH I.BERTINI,D.A.BRYANT,S.CIURLI,A.DIKIY,C.O.FERNANDEZ,
JRNL AUTH 2 C.LUCHINAT,N.SAFAROV,A.J.VILA,J.ZHAO
JRNL TITL BACKBONE DYNAMICS OF PLASTOCYANIN IN BOTH OXIDATION STATES.
JRNL TITL 2 SOLUTION STRUCTURE OF THE REDUCED FORM AND COMPARISON WITH
JRNL TITL 3 THE OXIDIZED STATE.
JRNL REF J.BIOL.CHEM. V. 276 47217 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11509552
JRNL DOI 10.1074/JBC.M100304200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.BERTINI,S.CIURLI,A.DIKIY,C.O.FERNANDEZ,C.LUCHINAT,
REMARK 1 AUTH 2 N.SAFAROV,S.SHUMILIN,A.J.VILA
REMARK 1 TITL THE FIRST SOLUTION STRUCTURE OF A PARAMAGNETIC COPPER(II)
REMARK 1 TITL 2 PROTEIN: THE CASE OF OXIDIZED PLASTOCYANIN FROM THE
REMARK 1 TITL 3 CYANOBACTERIUM SYNECHOCYSTIS PCC6803
REMARK 1 REF J.AM.CHEM.SOC. V. 123 2405 2001
REMARK 1 REFN ISSN 0002-7863
REMARK 1 DOI 10.1021/JA0033685
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : GUENTERT (DYANA), GUENTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JXF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014297.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 5.2
REMARK 210 IONIC STRENGTH : 50 MM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3 MM PLASTOCYANIN U-15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 700 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35
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 ALA A 54 HG SER A 57 1.44
REMARK 500 HE1 HIS A 39 CU CU A 132 1.45
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 SER A 11 -68.62 -168.63
REMARK 500 1 ALA A 45 95.64 -46.40
REMARK 500 1 LYS A 59 49.36 -86.23
REMARK 500 1 PHE A 63 -43.12 -133.32
REMARK 500 1 PHE A 73 43.75 -103.20
REMARK 500 1 ALA A 89 -50.34 -137.53
REMARK 500 2 MET A 7 37.10 -94.96
REMARK 500 2 SER A 11 -72.50 -150.14
REMARK 500 2 ASN A 34 -167.19 -103.24
REMARK 500 2 LEU A 36 69.82 77.90
REMARK 500 2 ALA A 45 97.98 -50.23
REMARK 500 2 ASP A 46 62.60 -110.05
REMARK 500 2 LYS A 59 43.03 -97.29
REMARK 500 2 PHE A 63 -47.46 -140.63
REMARK 500 2 PHE A 73 64.68 -104.03
REMARK 500 2 HIS A 86 42.17 167.78
REMARK 500 2 ALA A 89 -47.01 -135.63
REMARK 500 3 SER A 11 -64.93 -173.31
REMARK 500 3 ASN A 34 -80.33 -145.42
REMARK 500 3 ALA A 45 96.27 -44.00
REMARK 500 3 LYS A 59 50.87 -105.75
REMARK 500 3 LEU A 61 159.95 -40.31
REMARK 500 3 ALA A 89 -50.50 -128.68
REMARK 500 4 SER A 11 -70.79 -149.05
REMARK 500 4 ASN A 34 -86.68 -126.30
REMARK 500 4 ALA A 45 95.64 -44.95
REMARK 500 4 LYS A 59 44.75 -98.84
REMARK 500 4 PHE A 63 -50.84 162.05
REMARK 500 4 THR A 74 -71.08 -60.71
REMARK 500 4 HIS A 86 47.07 -92.94
REMARK 500 5 SER A 11 -69.59 -157.56
REMARK 500 5 ALA A 45 97.00 -40.31
REMARK 500 5 LYS A 59 -44.72 -161.87
REMARK 500 5 LEU A 61 154.52 -46.70
REMARK 500 5 PHE A 73 47.00 -105.89
REMARK 500 5 HIS A 86 59.04 -96.53
REMARK 500 6 SER A 11 -58.45 -160.43
REMARK 500 6 ASN A 34 -70.72 -123.77
REMARK 500 6 ALA A 45 98.07 -53.39
REMARK 500 6 ASP A 46 60.91 -118.51
REMARK 500 6 ALA A 65 42.65 -89.04
REMARK 500 6 HIS A 86 48.82 -85.84
REMARK 500 6 ALA A 89 -47.03 -137.18
REMARK 500 7 MET A 7 -165.48 -72.64
REMARK 500 7 SER A 11 -71.62 -146.45
REMARK 500 7 ASN A 34 -87.06 -126.95
REMARK 500 7 LEU A 36 69.91 75.29
REMARK 500 7 ALA A 45 96.21 -45.86
REMARK 500 7 ALA A 54 -70.06 -67.49
REMARK 500 7 LYS A 59 -82.29 -70.06
REMARK 500
REMARK 500 THIS ENTRY HAS 292 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 CU A 132 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 ND1
REMARK 620 2 CYS A 83 SG 89.4
REMARK 620 3 HIS A 86 ND1 135.7 88.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 132
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JXD RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE OF THE REDUCED PLASTOCYANIN FROM
REMARK 900 SYNECHOCYSTIS PCC6803
REMARK 900 RELATED ID: 1I0Y RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE OF THE OXIDIZED PLASTOCYANIN FROM
REMARK 900 SYNECHOCYSTIS PCC6803
REMARK 900 RELATED ID: 1I0W RELATED DB: PDB
REMARK 900 STRUCTURE ENSEMBLE FOR THE OXIDIZED PLASTOCYANIN FROM SYNECHOCYSTIS
REMARK 900 PCC6803
DBREF 1JXF A 1 98 UNP P21697 PLAS_SYNY3 29 126
SEQADV 1JXF ASP A 98 UNP P21697 GLU 126 ENGINEERED MUTATION
SEQRES 1 A 98 ALA ASN ALA THR VAL LYS MET GLY SER ASP SER GLY ALA
SEQRES 2 A 98 LEU VAL PHE GLU PRO SER THR VAL THR ILE LYS ALA GLY
SEQRES 3 A 98 GLU GLU VAL LYS TRP VAL ASN ASN LYS LEU SER PRO HIS
SEQRES 4 A 98 ASN ILE VAL PHE ALA ALA ASP GLY VAL ASP ALA ASP THR
SEQRES 5 A 98 ALA ALA LYS LEU SER HIS LYS GLY LEU ALA PHE ALA ALA
SEQRES 6 A 98 GLY GLU SER PHE THR SER THR PHE THR GLU PRO GLY THR
SEQRES 7 A 98 TYR THR TYR TYR CYS GLU PRO HIS ARG GLY ALA GLY MET
SEQRES 8 A 98 VAL GLY LYS VAL VAL VAL ASP
HET CU A 132 1
HETNAM CU COPPER (II) ION
FORMUL 2 CU CU 2+
HELIX 1 1 ASP A 49 SER A 57 1 9
SHEET 1 A 3 ALA A 3 LYS A 6 0
SHEET 2 A 3 GLU A 28 VAL A 32 1 O LYS A 30 N ALA A 3
SHEET 3 A 3 THR A 70 THR A 72 -1 O SER A 71 N VAL A 29
SHEET 1 B 4 THR A 20 ILE A 23 0
SHEET 2 B 4 VAL A 92 VAL A 97 1 O VAL A 96 N VAL A 21
SHEET 3 B 4 THR A 80 TYR A 82 -1 N TYR A 81 O GLY A 93
SHEET 4 B 4 VAL A 42 ALA A 44 -1 N VAL A 42 O TYR A 82
LINK ND1 HIS A 39 CU CU A 132 1555 1555 2.02
LINK SG CYS A 83 CU CU A 132 1555 1555 2.11
LINK ND1 HIS A 86 CU CU A 132 1555 1555 2.09
CISPEP 1 GLU A 17 PRO A 18 1 0.04
CISPEP 2 SER A 37 PRO A 38 1 -0.03
CISPEP 3 GLU A 17 PRO A 18 2 0.06
CISPEP 4 SER A 37 PRO A 38 2 0.02
CISPEP 5 GLU A 17 PRO A 18 3 0.03
CISPEP 6 SER A 37 PRO A 38 3 -0.03
CISPEP 7 GLU A 17 PRO A 18 4 -0.05
CISPEP 8 SER A 37 PRO A 38 4 -0.04
CISPEP 9 GLU A 17 PRO A 18 5 0.08
CISPEP 10 SER A 37 PRO A 38 5 0.00
CISPEP 11 GLU A 17 PRO A 18 6 -0.01
CISPEP 12 SER A 37 PRO A 38 6 0.10
CISPEP 13 GLU A 17 PRO A 18 7 -0.15
CISPEP 14 SER A 37 PRO A 38 7 -0.02
CISPEP 15 GLU A 17 PRO A 18 8 -0.06
CISPEP 16 SER A 37 PRO A 38 8 0.00
CISPEP 17 GLU A 17 PRO A 18 9 0.08
CISPEP 18 SER A 37 PRO A 38 9 -0.01
CISPEP 19 GLU A 17 PRO A 18 10 -0.05
CISPEP 20 SER A 37 PRO A 38 10 -0.01
CISPEP 21 GLU A 17 PRO A 18 11 0.00
CISPEP 22 SER A 37 PRO A 38 11 0.01
CISPEP 23 GLU A 17 PRO A 18 12 0.00
CISPEP 24 SER A 37 PRO A 38 12 0.05
CISPEP 25 GLU A 17 PRO A 18 13 -0.11
CISPEP 26 SER A 37 PRO A 38 13 0.09
CISPEP 27 GLU A 17 PRO A 18 14 0.00
CISPEP 28 SER A 37 PRO A 38 14 0.07
CISPEP 29 GLU A 17 PRO A 18 15 -0.02
CISPEP 30 SER A 37 PRO A 38 15 0.09
CISPEP 31 GLU A 17 PRO A 18 16 0.09
CISPEP 32 SER A 37 PRO A 38 16 -0.10
CISPEP 33 GLU A 17 PRO A 18 17 -0.03
CISPEP 34 SER A 37 PRO A 38 17 -0.02
CISPEP 35 GLU A 17 PRO A 18 18 -0.07
CISPEP 36 SER A 37 PRO A 38 18 -0.04
CISPEP 37 GLU A 17 PRO A 18 19 0.04
CISPEP 38 SER A 37 PRO A 38 19 0.01
CISPEP 39 GLU A 17 PRO A 18 20 -0.06
CISPEP 40 SER A 37 PRO A 38 20 -0.03
CISPEP 41 GLU A 17 PRO A 18 21 0.07
CISPEP 42 SER A 37 PRO A 38 21 -0.11
CISPEP 43 GLU A 17 PRO A 18 22 0.00
CISPEP 44 SER A 37 PRO A 38 22 -0.01
CISPEP 45 GLU A 17 PRO A 18 23 -0.07
CISPEP 46 SER A 37 PRO A 38 23 -0.05
CISPEP 47 GLU A 17 PRO A 18 24 -0.03
CISPEP 48 SER A 37 PRO A 38 24 0.02
CISPEP 49 GLU A 17 PRO A 18 25 0.03
CISPEP 50 SER A 37 PRO A 38 25 -0.08
CISPEP 51 GLU A 17 PRO A 18 26 0.04
CISPEP 52 SER A 37 PRO A 38 26 -0.04
CISPEP 53 GLU A 17 PRO A 18 27 0.03
CISPEP 54 SER A 37 PRO A 38 27 -0.08
CISPEP 55 GLU A 17 PRO A 18 28 0.04
CISPEP 56 SER A 37 PRO A 38 28 -0.05
CISPEP 57 GLU A 17 PRO A 18 29 -0.07
CISPEP 58 SER A 37 PRO A 38 29 0.05
CISPEP 59 GLU A 17 PRO A 18 30 -0.10
CISPEP 60 SER A 37 PRO A 38 30 -0.06
CISPEP 61 GLU A 17 PRO A 18 31 -0.06
CISPEP 62 SER A 37 PRO A 38 31 -0.05
CISPEP 63 GLU A 17 PRO A 18 32 -0.03
CISPEP 64 SER A 37 PRO A 38 32 0.00
CISPEP 65 GLU A 17 PRO A 18 33 0.03
CISPEP 66 SER A 37 PRO A 38 33 -0.03
CISPEP 67 GLU A 17 PRO A 18 34 -0.02
CISPEP 68 SER A 37 PRO A 38 34 -0.04
CISPEP 69 GLU A 17 PRO A 18 35 -0.07
CISPEP 70 SER A 37 PRO A 38 35 0.00
SITE 1 AC1 4 HIS A 39 CYS A 83 HIS A 86 MET A 91
CRYST1 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 - t 27 2 Bytes