Header list of 1pyc.pdb file
Complete list - 2 20 Bytes
HEADER TRANSCRIPTION REGULATION 17-FEB-96 1PYC
TITLE CYP1 (HAP1) DNA-BINDING DOMAIN (RESIDUES 60-100), NMR, 15 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYP1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 56 - 126;
COMPND 5 SYNONYM: HAP1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS TRANSCRIPTION REGULATION, ACTIVATOR, DNA-BINDING, NUCLEAR PROTEIN,
KEYWDS 2 ZINC, METAL-BINDING, HEME
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR J.TIMMERMAN,A.-L.VUIDEPOT,F.BONTEMS,J.-Y.LALLEMAND,M.GERVAIS,
AUTHOR 2 E.SHECHTER,B.GUIARD
REVDAT 3 02-MAR-22 1PYC 1 REMARK LINK
REVDAT 2 24-FEB-09 1PYC 1 VERSN
REVDAT 1 01-AUG-96 1PYC 0
JRNL AUTH J.TIMMERMAN,A.L.VUIDEPOT,F.BONTEMS,J.Y.LALLEMAND,M.GERVAIS,
JRNL AUTH 2 E.SHECHTER,B.GUIARD
JRNL TITL 1H, 15N RESONANCE ASSIGNMENT AND THREE-DIMENSIONAL STRUCTURE
JRNL TITL 2 OF CYP1 (HAP1) DNA-BINDING DOMAIN.
JRNL REF J.MOL.BIOL. V. 259 792 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8683583
JRNL DOI 10.1006/JMBI.1996.0358
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.E.TIMMERMAN,B.GUIARD,E.SHECHTER,M.A.DELSUC,J.Y.LALLEMAND,
REMARK 1 AUTH 2 M.GERVAIS
REMARK 1 TITL THE DNA-BINDING DOMAIN OF THE YEAST SACCHAROMYCES CEREVISIAE
REMARK 1 TITL 2 CYP1(HAP1) TRANSCRIPTION FACTOR POSSESSES TWO ZINC IONS
REMARK 1 TITL 3 WHICH ARE COMPLEXED IN A ZINC CLUSTER
REMARK 1 REF EUR.J.BIOCHEM. V. 225 593 1994
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PYC 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_1000175876.
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 : 15
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 LYS A 56
REMARK 465 ARG A 57
REMARK 465 ASN A 58
REMARK 465 ARG A 59
REMARK 465 ALA A 101
REMARK 465 GLU A 102
REMARK 465 GLU A 103
REMARK 465 ALA A 104
REMARK 465 GLU A 105
REMARK 465 LYS A 106
REMARK 465 GLU A 107
REMARK 465 LEU A 108
REMARK 465 LEU A 109
REMARK 465 LYS A 110
REMARK 465 ASP A 111
REMARK 465 ASN A 112
REMARK 465 GLU A 113
REMARK 465 LEU A 114
REMARK 465 LYS A 115
REMARK 465 LYS A 116
REMARK 465 LEU A 117
REMARK 465 ARG A 118
REMARK 465 GLU A 119
REMARK 465 ARG A 120
REMARK 465 VAL A 121
REMARK 465 LYS A 122
REMARK 465 SER A 123
REMARK 465 LEU A 124
REMARK 465 GLU A 125
REMARK 465 LYS A 126
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 2 VAL A 89 CA - CB - CG2 ANGL. DEV. = 17.3 DEGREES
REMARK 500 2 TYR A 95 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 3 TYR A 95 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 5 VAL A 89 CA - CB - CG1 ANGL. DEV. = -14.6 DEGREES
REMARK 500 5 VAL A 89 CA - CB - CG2 ANGL. DEV. = 12.1 DEGREES
REMARK 500 5 TYR A 95 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 6 VAL A 89 CA - CB - CG2 ANGL. DEV. = 16.8 DEGREES
REMARK 500 7 VAL A 89 CA - CB - CG1 ANGL. DEV. = -11.3 DEGREES
REMARK 500 8 VAL A 89 CG1 - CB - CG2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 8 VAL A 89 CA - CB - CG1 ANGL. DEV. = -12.9 DEGREES
REMARK 500 8 VAL A 89 CA - CB - CG2 ANGL. DEV. = 17.1 DEGREES
REMARK 500 11 VAL A 89 CA - CB - CG2 ANGL. DEV. = 18.1 DEGREES
REMARK 500 11 TYR A 95 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 12 VAL A 89 CA - CB - CG2 ANGL. DEV. = 16.1 DEGREES
REMARK 500 13 VAL A 89 CG1 - CB - CG2 ANGL. DEV. = 13.0 DEGREES
REMARK 500 14 VAL A 89 CA - CB - CG1 ANGL. DEV. = -13.7 DEGREES
REMARK 500 14 VAL A 89 CA - CB - CG2 ANGL. DEV. = 13.0 DEGREES
REMARK 500 15 VAL A 89 CA - CB - CG1 ANGL. DEV. = -11.2 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 1 LYS A 71 64.17 73.87
REMARK 500 2 LYS A 71 72.60 72.46
REMARK 500 2 LYS A 76 43.23 70.40
REMARK 500 2 GLU A 97 -52.13 -128.55
REMARK 500 2 THR A 99 -21.18 -142.87
REMARK 500 3 LYS A 71 55.90 75.66
REMARK 500 3 LYS A 76 31.22 75.55
REMARK 500 3 VAL A 89 42.36 -102.37
REMARK 500 3 GLU A 97 114.01 74.32
REMARK 500 4 LYS A 71 60.73 73.41
REMARK 500 4 VAL A 89 40.50 -100.58
REMARK 500 5 LEU A 62 156.65 72.51
REMARK 500 5 LYS A 71 78.59 74.85
REMARK 500 5 LYS A 76 70.05 69.11
REMARK 500 5 ARG A 78 129.00 59.90
REMARK 500 5 VAL A 89 42.14 -96.76
REMARK 500 6 LYS A 71 74.98 71.92
REMARK 500 7 LYS A 71 58.60 71.74
REMARK 500 7 LYS A 76 52.87 75.61
REMARK 500 7 ARG A 78 115.69 75.75
REMARK 500 7 VAL A 89 41.08 -109.22
REMARK 500 7 GLU A 97 -107.76 67.21
REMARK 500 8 LYS A 71 80.48 75.45
REMARK 500 8 VAL A 89 54.57 -115.61
REMARK 500 8 GLU A 97 86.47 69.69
REMARK 500 9 LYS A 71 55.95 71.18
REMARK 500 9 ASP A 75 -110.01 -133.95
REMARK 500 9 LYS A 76 22.32 177.39
REMARK 500 9 VAL A 89 48.80 -107.45
REMARK 500 10 LYS A 71 76.49 67.52
REMARK 500 10 VAL A 89 41.77 -102.04
REMARK 500 11 LYS A 71 58.65 74.52
REMARK 500 11 LYS A 76 37.33 73.16
REMARK 500 12 LYS A 71 78.35 73.36
REMARK 500 12 ARG A 78 128.23 93.96
REMARK 500 12 VAL A 89 31.83 -147.80
REMARK 500 13 LYS A 71 58.76 79.45
REMARK 500 13 LYS A 76 39.00 72.86
REMARK 500 14 LYS A 71 80.19 74.36
REMARK 500 14 ASP A 75 -47.63 -135.69
REMARK 500 14 LYS A 76 73.51 47.06
REMARK 500 14 ARG A 78 136.06 72.57
REMARK 500 14 VAL A 89 49.01 -109.42
REMARK 500 14 GLU A 97 117.91 60.12
REMARK 500 15 LEU A 62 162.67 70.66
REMARK 500 15 LYS A 71 56.78 73.11
REMARK 500 15 ASP A 75 -83.19 -150.01
REMARK 500 15 LYS A 76 -17.99 167.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 CYS A 74 ASP A 75 5 -140.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 6 TYR A 95 0.08 SIDE CHAIN
REMARK 500 8 TYR A 95 0.09 SIDE CHAIN
REMARK 500 12 TYR A 95 0.07 SIDE CHAIN
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 ZN A 127 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 64 SG
REMARK 620 2 CYS A 67 SG 77.0
REMARK 620 3 CYS A 74 SG 104.2 119.6
REMARK 620 4 CYS A 81 SG 108.5 132.4 105.1
REMARK 620 5 ZN A 128 ZN 56.6 96.9 134.9 56.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 128 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 64 SG
REMARK 620 2 CYS A 81 SG 108.4
REMARK 620 3 CYS A 84 SG 109.6 120.1
REMARK 620 4 CYS A 93 SG 115.7 93.0 109.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 127
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 128
DBREF 1PYC A 56 126 UNP P12351 CYP1_YEAST 56 126
SEQRES 1 A 71 LYS ARG ASN ARG ILE PRO LEU SER CYS THR ILE CYS ARG
SEQRES 2 A 71 LYS ARG LYS VAL LYS CYS ASP LYS LEU ARG PRO HIS CYS
SEQRES 3 A 71 GLN GLN CYS THR LYS THR GLY VAL ALA HIS LEU CYS HIS
SEQRES 4 A 71 TYR MET GLU GLN THR TRP ALA GLU GLU ALA GLU LYS GLU
SEQRES 5 A 71 LEU LEU LYS ASP ASN GLU LEU LYS LYS LEU ARG GLU ARG
SEQRES 6 A 71 VAL LYS SER LEU GLU LYS
HET ZN A 127 1
HET ZN A 128 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 THR A 65 ARG A 70 1 6
HELIX 2 2 GLN A 82 THR A 87 1 6
LINK SG CYS A 64 ZN ZN A 127 1555 1555 2.50
LINK SG CYS A 64 ZN ZN A 128 1555 1555 2.50
LINK SG CYS A 67 ZN ZN A 127 1555 1555 2.50
LINK SG CYS A 74 ZN ZN A 127 1555 1555 2.50
LINK SG CYS A 81 ZN ZN A 127 1555 1555 2.50
LINK SG CYS A 81 ZN ZN A 128 1555 1555 2.50
LINK SG CYS A 84 ZN ZN A 128 1555 1555 2.50
LINK SG CYS A 93 ZN ZN A 128 1555 1555 2.50
LINK ZN ZN A 127 ZN ZN A 128 1555 1555 2.76
CISPEP 1 ARG A 78 PRO A 79 1 4.75
CISPEP 2 ARG A 78 PRO A 79 2 -11.56
CISPEP 3 ARG A 78 PRO A 79 3 -8.83
CISPEP 4 ARG A 78 PRO A 79 4 -9.99
CISPEP 5 ARG A 78 PRO A 79 5 11.67
CISPEP 6 ARG A 78 PRO A 79 6 -15.05
CISPEP 7 ARG A 78 PRO A 79 7 10.16
CISPEP 8 ARG A 78 PRO A 79 8 -4.94
CISPEP 9 ARG A 78 PRO A 79 9 -11.67
CISPEP 10 ARG A 78 PRO A 79 10 -8.01
CISPEP 11 ARG A 78 PRO A 79 11 -3.14
CISPEP 12 ARG A 78 PRO A 79 12 -4.40
CISPEP 13 ARG A 78 PRO A 79 13 -2.02
CISPEP 14 ARG A 78 PRO A 79 14 4.02
CISPEP 15 ARG A 78 PRO A 79 15 -13.56
SITE 1 AC1 5 CYS A 64 CYS A 67 CYS A 74 CYS A 81
SITE 2 AC1 5 ZN A 128
SITE 1 AC2 5 CYS A 64 CYS A 81 CYS A 84 CYS A 93
SITE 2 AC2 5 ZN A 127
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 - 2 20 Bytes