Header list of 2b3i.pdb file
Complete list - r 9 2 Bytes
HEADER ELECTRON TRANSPORT 11-DEC-98 2B3I
TITLE NMR SOLUTION STRUCTURE OF PLASTOCYANIN FROM THE PHOTOSYNTHETIC
TITLE 2 PROKARYOTE, PROCHLOROTHRIX HOLLANDICA (19 STRUCTURES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (PLASTOCYANIN);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PETE PROTEIN;
COMPND 5 EC: 1.10.99.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: T2S MUTATION INTRODUCED TO CLONE IN EXPRESSION VECTOR
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PROCHLOROTHRIX HOLLANDICA;
SOURCE 3 ORGANISM_TAXID: 1223;
SOURCE 4 CELLULAR_LOCATION: THYLAKOID LUMEN;
SOURCE 5 GENE: PETE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM - INCLUSION BODIES;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PSCREEN;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PVAPC10;
SOURCE 13 EXPRESSION_SYSTEM_GENE: PETE;
SOURCE 14 OTHER_DETAILS: INCLUSION BODIES WERE REFOLDED IN-VITRO
KEYWDS ELECTRON TRANSPORT, TYPE I COPPER PROTEIN, PHOTOSYNTHESIS
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR C.R.BABU,B.F.VOLKMAN,G.S.BULLERJAHN
REVDAT 4 09-MAR-22 2B3I 1 REMARK LINK
REVDAT 3 24-FEB-09 2B3I 1 VERSN
REVDAT 2 19-MAY-00 2B3I 1 COMPND REMARK HET HETNAM
REVDAT 2 2 1 LINK CISPEP
REVDAT 1 27-APR-99 2B3I 0
JRNL AUTH C.R.BABU,B.F.VOLKMAN,G.S.BULLERJAHN
JRNL TITL NMR SOLUTION STRUCTURE OF PLASTOCYANIN FROM THE
JRNL TITL 2 PHOTOSYNTHETIC PROKARYOTE, PROCHLOROTHRIX HOLLANDICA.
JRNL REF BIOCHEMISTRY V. 38 4988 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10213601
JRNL DOI 10.1021/BI983024F
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : P.GUNTERT, C.MUMENTHALER, K.WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS, RESTRAINTS, AND
REMARK 3 CHEMICAL SHIFTS ARE IN THE SUBMITTED FILES AND IN THE JRNL
REMARK 3 CITATION ABOVE.
REMARK 4
REMARK 4 2B3I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-99.
REMARK 100 THE DEPOSITION ID IS D_1000000258.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 20MM POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, FELIX
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TWO-DIMENCIONAL NMR
REMARK 210 SPECTROSCOPY. WATER SUPPRESSION WAS ACHIEVED WITH A WATERGATE
REMARK 210 SEQ. WITH A 3-9-19 SELECTIVE INVERSION.
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 ILE A 23 H GLU A 97 1.57
REMARK 500 O TYR A 78 H ILE A 94 1.57
REMARK 500 H TYR A 78 O ILE A 94 1.59
REMARK 500 HA SER A 24 OXT GLU A 97 1.60
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 2 93.07 62.49
REMARK 500 1 LYS A 11 37.27 -90.78
REMARK 500 1 TYR A 12 29.15 38.98
REMARK 500 1 LYS A 19 -39.73 -39.59
REMARK 500 1 ASN A 40 -173.20 -175.41
REMARK 500 1 LYS A 45 146.05 167.24
REMARK 500 1 ALA A 48 134.85 -39.91
REMARK 500 1 ALA A 54 -48.60 -159.09
REMARK 500 1 ASN A 57 108.10 -160.57
REMARK 500 1 PHE A 67 -76.35 -37.51
REMARK 500 1 HIS A 85 67.96 -107.45
REMARK 500 1 MET A 90 77.87 -115.95
REMARK 500 2 LYS A 11 40.07 -90.41
REMARK 500 2 TYR A 12 28.29 40.24
REMARK 500 2 LYS A 35 -167.19 -171.19
REMARK 500 2 PRO A 38 -169.02 -75.03
REMARK 500 2 ASN A 40 167.40 171.84
REMARK 500 2 PHE A 43 157.81 -37.95
REMARK 500 2 LYS A 45 149.33 167.51
REMARK 500 2 ALA A 48 134.86 -39.26
REMARK 500 2 ALA A 54 -45.10 -159.43
REMARK 500 2 SER A 56 94.51 -56.47
REMARK 500 2 THR A 58 35.65 -90.28
REMARK 500 2 LEU A 60 103.74 -49.64
REMARK 500 2 SER A 66 89.92 55.21
REMARK 500 2 PHE A 67 -83.32 -37.49
REMARK 500 3 SER A 2 90.20 49.04
REMARK 500 3 LYS A 11 39.79 -90.74
REMARK 500 3 TYR A 12 29.96 38.11
REMARK 500 3 LYS A 35 -166.81 -169.03
REMARK 500 3 ASN A 40 169.70 169.61
REMARK 500 3 PHE A 43 159.58 -39.10
REMARK 500 3 LYS A 45 149.69 167.58
REMARK 500 3 ALA A 48 134.48 -38.91
REMARK 500 3 ALA A 54 -45.64 -155.41
REMARK 500 3 THR A 58 30.66 -91.08
REMARK 500 3 PHE A 67 -73.16 -37.14
REMARK 500 3 TYR A 68 173.50 173.42
REMARK 500 4 SER A 2 111.08 58.55
REMARK 500 4 LYS A 11 40.65 -90.18
REMARK 500 4 TYR A 12 29.67 38.35
REMARK 500 4 ALA A 25 106.01 -59.61
REMARK 500 4 PRO A 38 -169.19 -75.00
REMARK 500 4 ASN A 40 163.12 179.37
REMARK 500 4 LYS A 45 147.15 167.83
REMARK 500 4 ALA A 48 132.43 -39.83
REMARK 500 4 ALA A 54 -45.57 -157.90
REMARK 500 4 LYS A 59 95.18 -47.06
REMARK 500 4 LEU A 60 96.48 -67.53
REMARK 500 4 ALA A 63 100.05 -39.66
REMARK 500
REMARK 500 THIS ENTRY HAS 268 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 CU1 A 110 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 ND1
REMARK 620 2 CYS A 82 SG 112.5
REMARK 620 3 HIS A 85 ND1 115.6 111.0
REMARK 620 4 MET A 90 SD 106.6 104.5 105.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CU
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: COPPER BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 110
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 T2S - INTRODUCED TO CLONE, R61A - MISTAKE IN GB ENTRY
DBREF 2B3I A 1 97 UNP P50057 PLAS_PROHO 35 131
SEQADV 2B3I SER A 2 UNP P50057 THR 36 SEE REMARK 999
SEQADV 2B3I ALA A 61 UNP P50057 ARG 95 SEE REMARK 999
SEQRES 1 A 97 ALA SER VAL GLN ILE LYS MET GLY THR ASP LYS TYR ALA
SEQRES 2 A 97 PRO LEU TYR GLU PRO LYS ALA LEU SER ILE SER ALA GLY
SEQRES 3 A 97 ASP THR VAL GLU PHE VAL MET ASN LYS VAL GLY PRO HIS
SEQRES 4 A 97 ASN VAL ILE PHE ASP LYS VAL PRO ALA GLY GLU SER ALA
SEQRES 5 A 97 PRO ALA LEU SER ASN THR LYS LEU ALA ILE ALA PRO GLY
SEQRES 6 A 97 SER PHE TYR SER VAL THR LEU GLY THR PRO GLY THR TYR
SEQRES 7 A 97 SER PHE TYR CYS THR PRO HIS ARG GLY ALA GLY MET VAL
SEQRES 8 A 97 GLY THR ILE THR VAL GLU
HET CU1 A 110 1
HETNAM CU1 COPPER (I) ION
FORMUL 2 CU1 CU 1+
HELIX 1 1 ALA A 52 LEU A 55 1 4
SHEET 1 A 3 VAL A 3 MET A 7 0
SHEET 2 A 3 THR A 28 MET A 33 1 N GLU A 30 O VAL A 3
SHEET 3 A 3 TYR A 68 THR A 71 -1 N VAL A 70 O VAL A 29
SHEET 1 B 4 ALA A 20 ILE A 23 0
SHEET 2 B 4 VAL A 91 VAL A 96 1 N THR A 93 O LEU A 21
SHEET 3 B 4 GLY A 76 TYR A 81 -1 N PHE A 80 O GLY A 92
SHEET 4 B 4 ILE A 42 LYS A 45 -1 N LYS A 45 O SER A 79
LINK ND1 HIS A 39 CU CU1 A 110 1555 1555 1.99
LINK SG CYS A 82 CU CU1 A 110 1555 1555 2.36
LINK ND1 HIS A 85 CU CU1 A 110 1555 1555 2.03
LINK SD MET A 90 CU CU1 A 110 1555 1555 2.95
CISPEP 1 GLU A 17 PRO A 18 1 0.02
CISPEP 2 GLY A 37 PRO A 38 1 -0.08
CISPEP 3 GLU A 17 PRO A 18 2 -0.02
CISPEP 4 GLY A 37 PRO A 38 2 0.00
CISPEP 5 GLU A 17 PRO A 18 3 0.03
CISPEP 6 GLY A 37 PRO A 38 3 -0.03
CISPEP 7 GLU A 17 PRO A 18 4 -0.09
CISPEP 8 GLY A 37 PRO A 38 4 -0.01
CISPEP 9 GLU A 17 PRO A 18 5 -0.03
CISPEP 10 GLY A 37 PRO A 38 5 0.12
CISPEP 11 GLU A 17 PRO A 18 6 0.03
CISPEP 12 GLY A 37 PRO A 38 6 0.06
CISPEP 13 GLU A 17 PRO A 18 7 0.06
CISPEP 14 GLY A 37 PRO A 38 7 0.04
CISPEP 15 GLU A 17 PRO A 18 8 -0.04
CISPEP 16 GLY A 37 PRO A 38 8 -0.11
CISPEP 17 GLU A 17 PRO A 18 9 -0.14
CISPEP 18 GLY A 37 PRO A 38 9 0.11
CISPEP 19 GLU A 17 PRO A 18 10 -0.10
CISPEP 20 GLY A 37 PRO A 38 10 -0.13
CISPEP 21 GLU A 17 PRO A 18 11 -0.09
CISPEP 22 GLY A 37 PRO A 38 11 -0.05
CISPEP 23 GLU A 17 PRO A 18 12 -0.02
CISPEP 24 GLY A 37 PRO A 38 12 -0.04
CISPEP 25 GLU A 17 PRO A 18 13 0.05
CISPEP 26 GLY A 37 PRO A 38 13 0.02
CISPEP 27 GLU A 17 PRO A 18 14 -0.01
CISPEP 28 GLY A 37 PRO A 38 14 -0.11
CISPEP 29 GLU A 17 PRO A 18 15 -0.01
CISPEP 30 GLY A 37 PRO A 38 15 0.00
CISPEP 31 GLU A 17 PRO A 18 16 0.01
CISPEP 32 GLY A 37 PRO A 38 16 0.03
CISPEP 33 GLU A 17 PRO A 18 17 0.04
CISPEP 34 GLY A 37 PRO A 38 17 0.00
CISPEP 35 GLU A 17 PRO A 18 18 0.06
CISPEP 36 GLY A 37 PRO A 38 18 -0.07
CISPEP 37 GLU A 17 PRO A 18 19 0.02
CISPEP 38 GLY A 37 PRO A 38 19 0.00
SITE 1 CU 4 HIS A 39 CYS A 82 HIS A 85 MET A 90
SITE 1 AC1 4 HIS A 39 CYS A 82 HIS A 85 MET A 90
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 9 2 Bytes