Header list of 1b3i.pdb file
Complete list - 16 20 Bytes
HEADER ELECTRON TRANSPORT 11-DEC-98 1B3I TITLE NMR SOLUTION STRUCTURE OF PLASTOCYANIN FROM THE PHOTOSYNTHETIC TITLE 2 PROKARYOTE, PROCHLOROTHRIX HOLLANDICA (MINIMIZED AVERAGE STRUCTURE) 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 AUTHOR C.R.BABU,B.F.VOLKMAN,G.S.BULLERJAHN REVDAT 4 16-FEB-22 1B3I 1 REMARK LINK REVDAT 3 24-FEB-09 1B3I 1 VERSN REVDAT 2 18-MAY-00 1B3I 1 COMPND REMARK HET HETNAM REVDAT 2 2 1 LINK CISPEP REVDAT 1 27-APR-99 1B3I 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 ARE IN THE SUBMITTED REMARK 3 FILE AND IN THE JRNL CITATION ABOVE. THE RESTRAINTS ARE IN THE REMARK 3 FILES WITH THE 19 CONFORMERS. REMARK 4 REMARK 4 1B3I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-98. REMARK 100 THE DEPOSITION ID IS D_1000000246. 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 : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: MINIMIZED AVERAGE STRUCTURE. THE STRUCTURE WAS DETERMINED REMARK 210 USING TWO- DIMENCIONAL NMR SPECTROSCOPY. WATER SUPPRESSION WAS REMARK 210 ACHIEVED WITH A WATERGATE 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 H TYR A 78 O ILE A 94 1.50 REMARK 500 H LYS A 6 O GLU A 17 1.57 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 LYS A 11 39.68 -90.62 REMARK 500 TYR A 12 29.67 38.26 REMARK 500 ALA A 25 105.43 -58.14 REMARK 500 LYS A 35 -167.52 -168.89 REMARK 500 PRO A 38 -168.90 -74.97 REMARK 500 ASN A 40 166.99 173.98 REMARK 500 PHE A 43 160.64 -47.67 REMARK 500 LYS A 45 143.56 167.31 REMARK 500 ALA A 54 -45.67 -157.32 REMARK 500 LEU A 60 102.47 -40.42 REMARK 500 SER A 66 97.36 -178.70 REMARK 500 PHE A 67 -86.71 -38.19 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 117.6 107.9 REMARK 620 4 MET A 90 SD 106.8 104.6 106.5 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 1B3I A 1 97 UNP P50057 PLAS_PROHO 35 131 SEQADV 1B3I SER A 2 UNP P50057 THR 36 SEE REMARK 999 SEQADV 1B3I 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 THR A 77 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 1.98 LINK SG CYS A 82 CU CU1 A 110 1555 1555 2.35 LINK ND1 HIS A 85 CU CU1 A 110 1555 1555 2.00 LINK SD MET A 90 CU CU1 A 110 1555 1555 2.95 CISPEP 1 GLU A 17 PRO A 18 0 0.09 CISPEP 2 GLY A 37 PRO A 38 0 -0.06 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
Complete list - 16 20 Bytes