Header list of 1plb.pdb file
Complete list - 29 20 Bytes
HEADER ELECTRON TRANSPORT PROTEIN 20-MAY-94 1PLB TITLE HIGH-RESOLUTION SOLUTION STRUCTURE OF REDUCED PARSLEY PLASTOCYANIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PLASTOCYANIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PETROSELINUM CRISPUM; SOURCE 3 ORGANISM_COMMON: PARSLEY; SOURCE 4 ORGANISM_TAXID: 4043 KEYWDS ELECTRON TRANSPORT PROTEIN EXPDTA SOLUTION NMR AUTHOR S.BAGBY,P.C.DRISCOLL,T.S.HARVEY,H.A.O.HILL REVDAT 4 29-NOV-17 1PLB 1 REMARK HELIX REVDAT 3 24-FEB-09 1PLB 1 VERSN REVDAT 2 01-APR-03 1PLB 1 JRNL REVDAT 1 31-AUG-94 1PLB 0 JRNL AUTH S.BAGBY,P.C.DRISCOLL,T.S.HARVEY,H.A.HILL JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF REDUCED PARSLEY JRNL TITL 2 PLASTOCYANIN. JRNL REF BIOCHEMISTRY V. 33 6611 1994 JRNL REFN ISSN 0006-2960 JRNL PMID 8204598 JRNL DOI 10.1021/BI00187A031 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : NILGES,GRONENBORN,BRUNGER,CLORE,KUSZEWSKI (YASAP), REMARK 3 BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1PLB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000175719. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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: 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 HIS A 37 NE2 HIS A 37 CD2 -0.129 REMARK 500 HIS A 85 NE2 HIS A 85 CD2 -0.121 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 LYS A 30 CD - CE - NZ ANGL. DEV. = 19.8 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 ASP A 9 -16.06 -167.45 REMARK 500 ALA A 23 75.70 -64.43 REMARK 500 ALA A 33 112.83 164.94 REMARK 500 GLU A 43 25.20 -70.14 REMARK 500 TYR A 60 172.89 -54.53 REMARK 500 THR A 73 36.91 -150.79 REMARK 500 LYS A 75 109.22 -47.18 REMARK 500 TYR A 81 -178.34 -170.60 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 100 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 82 SG REMARK 620 2 HIS A 85 ND1 112.4 REMARK 620 3 HIS A 37 ND1 144.5 96.2 REMARK 620 N 1 2 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: CU REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 100 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1PLA RELATED DB: PDB DBREF 1PLB A 1 97 UNP P17341 PLAS_PETCR 1 97 SEQRES 1 A 97 ALA GLU VAL LYS LEU GLY SER ASP ASP GLY GLY LEU VAL SEQRES 2 A 97 PHE SER PRO SER SER PHE THR VAL ALA ALA GLY GLU LYS SEQRES 3 A 97 ILE THR PHE LYS ASN ASN ALA GLY PHE PRO HIS ASN ILE SEQRES 4 A 97 VAL PHE ASP GLU ASP GLU VAL PRO ALA GLY VAL ASN ALA SEQRES 5 A 97 GLU LYS ILE SER GLN PRO GLU TYR LEU ASN GLY ALA GLY SEQRES 6 A 97 GLU THR TYR GLU VAL THR LEU THR GLU LYS GLY THR TYR SEQRES 7 A 97 LYS PHE TYR CYS GLU PRO HIS ALA GLY ALA GLY MET LYS SEQRES 8 A 97 GLY GLU VAL THR VAL ASN HET CU A 100 1 HETNAM CU COPPER (II) ION FORMUL 2 CU CU 2+ HELIX 1 H1 ALA A 52 SER A 56 5 5 SHEET 1 I 4 GLY A 11 PHE A 14 0 SHEET 2 I 4 ALA A 1 SER A 7 -1 N GLY A 6 O VAL A 13 SHEET 3 I 4 GLU A 25 ASN A 32 1 O LYS A 26 N ALA A 1 SHEET 4 I 4 THR A 67 GLU A 74 -1 O TYR A 68 N ASN A 31 SHEET 1 II 4 SER A 17 VAL A 21 0 SHEET 2 II 4 GLY A 92 ASN A 97 1 N THR A 95 O SER A 17 SHEET 3 II 4 TYR A 78 HIS A 85 -1 N TYR A 78 O VAL A 96 SHEET 4 II 4 PRO A 36 PHE A 41 -1 N VAL A 40 O GLU A 83 LINK CU CU A 100 SG CYS A 82 1555 1555 2.02 LINK CU CU A 100 ND1 HIS A 85 1555 1555 2.22 LINK CU CU A 100 ND1 HIS A 37 1555 1555 2.09 CISPEP 1 SER A 15 PRO A 16 0 -0.16 CISPEP 2 PHE A 35 PRO A 36 0 -0.65 SITE 1 CU 4 HIS A 37 PRO A 84 GLY A 87 GLY A 92 SITE 1 AC1 4 HIS A 37 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 - 29 20 Bytes