Header list of 1pla.pdb file
Complete list - v 29 2 Bytes
HEADER ELECTRON TRANSPORT PROTEIN 20-MAY-94 1PLA
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
NUMMDL 30
AUTHOR S.BAGBY,P.C.DRISCOLL,T.S.HARVEY,H.A.O.HILL
REVDAT 4 29-NOV-17 1PLA 1 REMARK HELIX
REVDAT 3 24-FEB-09 1PLA 1 VERSN
REVDAT 2 01-APR-03 1PLA 1 JRNL
REVDAT 1 31-AUG-94 1PLA 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 1PLA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175718.
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 : 30
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: 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
REMARK 500 REMARK: NULL
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 1 HIS A 37 NE2 HIS A 37 CD2 -0.129
REMARK 500 1 HIS A 85 NE2 HIS A 85 CD2 -0.122
REMARK 500 2 HIS A 37 NE2 HIS A 37 CD2 -0.130
REMARK 500 2 HIS A 85 NE2 HIS A 85 CD2 -0.122
REMARK 500 3 HIS A 37 NE2 HIS A 37 CD2 -0.129
REMARK 500 3 HIS A 85 NE2 HIS A 85 CD2 -0.121
REMARK 500 4 HIS A 37 NE2 HIS A 37 CD2 -0.130
REMARK 500 4 HIS A 85 NE2 HIS A 85 CD2 -0.122
REMARK 500 5 HIS A 37 NE2 HIS A 37 CD2 -0.131
REMARK 500 5 HIS A 85 NE2 HIS A 85 CD2 -0.122
REMARK 500 6 HIS A 37 NE2 HIS A 37 CD2 -0.128
REMARK 500 6 HIS A 85 NE2 HIS A 85 CD2 -0.123
REMARK 500 7 HIS A 37 NE2 HIS A 37 CD2 -0.129
REMARK 500 7 HIS A 85 NE2 HIS A 85 CD2 -0.123
REMARK 500 8 HIS A 37 NE2 HIS A 37 CD2 -0.132
REMARK 500 8 HIS A 85 NE2 HIS A 85 CD2 -0.123
REMARK 500 9 HIS A 37 NE2 HIS A 37 CD2 -0.128
REMARK 500 9 HIS A 85 NE2 HIS A 85 CD2 -0.123
REMARK 500 10 HIS A 37 NE2 HIS A 37 CD2 -0.130
REMARK 500 10 HIS A 85 NE2 HIS A 85 CD2 -0.121
REMARK 500 11 HIS A 37 NE2 HIS A 37 CD2 -0.128
REMARK 500 11 HIS A 85 NE2 HIS A 85 CD2 -0.121
REMARK 500 12 HIS A 37 NE2 HIS A 37 CD2 -0.131
REMARK 500 12 HIS A 85 NE2 HIS A 85 CD2 -0.122
REMARK 500 13 HIS A 37 NE2 HIS A 37 CD2 -0.128
REMARK 500 13 HIS A 85 NE2 HIS A 85 CD2 -0.121
REMARK 500 14 HIS A 37 NE2 HIS A 37 CD2 -0.133
REMARK 500 14 HIS A 85 NE2 HIS A 85 CD2 -0.122
REMARK 500 15 HIS A 37 NE2 HIS A 37 CD2 -0.129
REMARK 500 15 HIS A 85 NE2 HIS A 85 CD2 -0.121
REMARK 500 16 HIS A 37 NE2 HIS A 37 CD2 -0.128
REMARK 500 16 HIS A 85 NE2 HIS A 85 CD2 -0.121
REMARK 500 17 HIS A 37 NE2 HIS A 37 CD2 -0.128
REMARK 500 17 HIS A 85 NE2 HIS A 85 CD2 -0.121
REMARK 500 18 HIS A 37 NE2 HIS A 37 CD2 -0.129
REMARK 500 18 HIS A 85 NE2 HIS A 85 CD2 -0.121
REMARK 500 19 HIS A 37 NE2 HIS A 37 CD2 -0.128
REMARK 500 19 HIS A 85 NE2 HIS A 85 CD2 -0.121
REMARK 500 20 HIS A 37 NE2 HIS A 37 CD2 -0.133
REMARK 500 20 HIS A 85 NE2 HIS A 85 CD2 -0.122
REMARK 500 21 HIS A 37 NE2 HIS A 37 CD2 -0.128
REMARK 500 21 HIS A 85 NE2 HIS A 85 CD2 -0.122
REMARK 500 22 HIS A 37 NE2 HIS A 37 CD2 -0.132
REMARK 500 22 HIS A 85 NE2 HIS A 85 CD2 -0.124
REMARK 500 23 HIS A 37 NE2 HIS A 37 CD2 -0.130
REMARK 500 23 HIS A 85 NE2 HIS A 85 CD2 -0.122
REMARK 500 24 HIS A 37 NE2 HIS A 37 CD2 -0.128
REMARK 500 24 HIS A 85 NE2 HIS A 85 CD2 -0.124
REMARK 500 25 HIS A 37 NE2 HIS A 37 CD2 -0.130
REMARK 500 25 HIS A 85 NE2 HIS A 85 CD2 -0.122
REMARK 500
REMARK 500 THIS ENTRY HAS 60 BOND DEVIATIONS.
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 ASP A 9 -9.70 -170.28
REMARK 500 1 ALA A 23 88.90 -60.40
REMARK 500 1 ALA A 33 11.94 178.11
REMARK 500 1 ASP A 42 99.33 -55.40
REMARK 500 1 GLU A 43 5.26 -64.01
REMARK 500 1 GLU A 59 95.67 -59.21
REMARK 500 1 TYR A 60 163.11 -42.71
REMARK 500 1 THR A 73 46.07 -149.94
REMARK 500 1 LYS A 75 112.48 -39.45
REMARK 500 1 TYR A 81 -179.76 -171.25
REMARK 500 2 SER A 7 -81.29 -87.44
REMARK 500 2 ASP A 8 -25.31 -161.12
REMARK 500 2 ASP A 9 78.40 178.50
REMARK 500 2 SER A 17 -60.43 -94.94
REMARK 500 2 ALA A 23 73.03 -67.27
REMARK 500 2 ALA A 33 133.57 175.44
REMARK 500 2 GLU A 45 52.56 -146.18
REMARK 500 2 SER A 56 -178.63 -58.95
REMARK 500 2 TYR A 60 164.49 -47.54
REMARK 500 2 THR A 73 42.61 -150.57
REMARK 500 2 TYR A 81 -172.74 -170.46
REMARK 500 3 SER A 7 -179.16 -66.29
REMARK 500 3 SER A 17 -64.51 -90.23
REMARK 500 3 ALA A 33 118.08 164.69
REMARK 500 3 PHE A 35 164.66 -47.69
REMARK 500 3 GLU A 45 19.30 -140.60
REMARK 500 3 GLU A 59 103.67 -52.96
REMARK 500 3 TYR A 60 161.56 -42.63
REMARK 500 3 ASN A 62 -12.56 -148.20
REMARK 500 3 THR A 73 47.32 -150.92
REMARK 500 3 TYR A 81 -175.33 -171.83
REMARK 500 3 ALA A 86 0.27 -65.52
REMARK 500 4 ASP A 9 68.74 -164.04
REMARK 500 4 SER A 17 -68.64 -96.03
REMARK 500 4 ALA A 23 71.10 -68.38
REMARK 500 4 ALA A 33 128.19 170.52
REMARK 500 4 GLU A 43 35.22 -71.40
REMARK 500 4 GLU A 45 -5.39 -145.81
REMARK 500 4 ASN A 51 162.33 -44.61
REMARK 500 4 GLN A 57 78.55 -159.96
REMARK 500 4 PRO A 58 0.99 -60.56
REMARK 500 4 TYR A 60 164.79 -41.92
REMARK 500 4 THR A 73 34.45 -150.95
REMARK 500 5 SER A 7 159.17 -47.41
REMARK 500 5 SER A 17 -64.96 -95.71
REMARK 500 5 ALA A 23 73.02 -67.99
REMARK 500 5 ALA A 33 90.74 177.70
REMARK 500 5 GLU A 43 15.10 -68.35
REMARK 500 5 GLU A 45 14.64 -143.10
REMARK 500 5 ALA A 48 44.08 -81.53
REMARK 500
REMARK 500 THIS ENTRY HAS 307 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 100 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 82 SG
REMARK 620 2 HIS A 85 ND1 115.7
REMARK 620 3 HIS A 37 ND1 139.8 92.3
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: 1PLB RELATED DB: PDB
DBREF 1PLA 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 2.01
LINK CU CU A 100 ND1 HIS A 85 1555 1555 2.18
LINK CU CU A 100 ND1 HIS A 37 1555 1555 2.30
CISPEP 1 SER A 15 PRO A 16 1 -0.56
CISPEP 2 PHE A 35 PRO A 36 1 -1.27
CISPEP 3 SER A 15 PRO A 16 2 -0.82
CISPEP 4 PHE A 35 PRO A 36 2 -0.69
CISPEP 5 SER A 15 PRO A 16 3 -0.54
CISPEP 6 PHE A 35 PRO A 36 3 -0.48
CISPEP 7 SER A 15 PRO A 16 4 -0.47
CISPEP 8 PHE A 35 PRO A 36 4 -0.95
CISPEP 9 SER A 15 PRO A 16 5 -0.21
CISPEP 10 PHE A 35 PRO A 36 5 -0.66
CISPEP 11 SER A 15 PRO A 16 6 -0.66
CISPEP 12 PHE A 35 PRO A 36 6 -0.54
CISPEP 13 SER A 15 PRO A 16 7 -0.74
CISPEP 14 PHE A 35 PRO A 36 7 -0.48
CISPEP 15 SER A 15 PRO A 16 8 -1.48
CISPEP 16 PHE A 35 PRO A 36 8 -0.84
CISPEP 17 SER A 15 PRO A 16 9 -0.19
CISPEP 18 PHE A 35 PRO A 36 9 -0.71
CISPEP 19 SER A 15 PRO A 16 10 -0.16
CISPEP 20 PHE A 35 PRO A 36 10 0.01
CISPEP 21 SER A 15 PRO A 16 11 -0.20
CISPEP 22 PHE A 35 PRO A 36 11 -0.43
CISPEP 23 SER A 15 PRO A 16 12 -0.90
CISPEP 24 PHE A 35 PRO A 36 12 -0.59
CISPEP 25 SER A 15 PRO A 16 13 -0.25
CISPEP 26 PHE A 35 PRO A 36 13 -0.73
CISPEP 27 SER A 15 PRO A 16 14 -0.21
CISPEP 28 PHE A 35 PRO A 36 14 -0.55
CISPEP 29 SER A 15 PRO A 16 15 0.12
CISPEP 30 PHE A 35 PRO A 36 15 -1.08
CISPEP 31 SER A 15 PRO A 16 16 0.96
CISPEP 32 PHE A 35 PRO A 36 16 -0.95
CISPEP 33 SER A 15 PRO A 16 17 -0.34
CISPEP 34 PHE A 35 PRO A 36 17 -0.50
CISPEP 35 SER A 15 PRO A 16 18 -0.76
CISPEP 36 PHE A 35 PRO A 36 18 -1.17
CISPEP 37 SER A 15 PRO A 16 19 -1.08
CISPEP 38 PHE A 35 PRO A 36 19 -0.04
CISPEP 39 SER A 15 PRO A 16 20 -1.05
CISPEP 40 PHE A 35 PRO A 36 20 -0.32
CISPEP 41 SER A 15 PRO A 16 21 -0.13
CISPEP 42 PHE A 35 PRO A 36 21 -0.36
CISPEP 43 SER A 15 PRO A 16 22 -0.83
CISPEP 44 PHE A 35 PRO A 36 22 -1.12
CISPEP 45 SER A 15 PRO A 16 23 -0.38
CISPEP 46 PHE A 35 PRO A 36 23 -0.76
CISPEP 47 SER A 15 PRO A 16 24 -0.40
CISPEP 48 PHE A 35 PRO A 36 24 -0.21
CISPEP 49 SER A 15 PRO A 16 25 -0.44
CISPEP 50 PHE A 35 PRO A 36 25 -0.81
CISPEP 51 SER A 15 PRO A 16 26 -0.69
CISPEP 52 PHE A 35 PRO A 36 26 -0.48
CISPEP 53 SER A 15 PRO A 16 27 -0.41
CISPEP 54 PHE A 35 PRO A 36 27 -0.64
CISPEP 55 SER A 15 PRO A 16 28 0.10
CISPEP 56 PHE A 35 PRO A 36 28 -0.76
CISPEP 57 SER A 15 PRO A 16 29 -0.94
CISPEP 58 PHE A 35 PRO A 36 29 -0.38
CISPEP 59 SER A 15 PRO A 16 30 -0.49
CISPEP 60 PHE A 35 PRO A 36 30 -1.02
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
MODEL 1
Complete list - v 29 2 Bytes