Header list of 1v5r.pdb file
Complete list - r 2 2 Bytes
HEADER APOPTOSIS 25-NOV-03 1V5R
TITLE SOLUTION STRUCTURE OF THE GAS2 DOMAIN OF THE GROWTH ARREST SPECIFIC 2
TITLE 2 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROWTH-ARREST-SPECIFIC PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GAS2 DOMAIN;
COMPND 5 SYNONYM: GROWTH ARREST SPECIFIC 2 PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RIKEN CDNA 4631403A13;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020417-07;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS GAS2 DOMAIN, ZINC BINDING DOMAIN, GROWTH ARREST, APOPTOSIS, CELL
KEYWDS 2 CYCLE, STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 3 INITIATIVE, RSGI
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.MIYAMOTO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1V5R 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1V5R 1 VERSN
REVDAT 1 18-JAN-05 1V5R 0
JRNL AUTH K.MIYAMOTO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE GAS2 DOMAIN OF THE GROWTH ARREST
JRNL TITL 2 SPECIFIC 2 PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V5R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000006240.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.03MM GAS2 DOMAIN U-13C, 15N;
REMARK 210 20MM D-TRIS-HCL(PH 7.5); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3;
REMARK 210 100UM ZNCL2; 90% H2O, 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.863, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 6 175.68 -55.16
REMARK 500 1 ASP A 20 104.99 -172.49
REMARK 500 1 CYS A 25 152.64 -36.84
REMARK 500 1 PRO A 26 1.04 -69.73
REMARK 500 1 GLN A 36 109.52 -34.72
REMARK 500 1 LYS A 54 -35.71 -130.12
REMARK 500 1 ILE A 82 108.14 -53.74
REMARK 500 1 ASP A 86 -60.73 -106.62
REMARK 500 1 SER A 92 152.47 -38.38
REMARK 500 2 SER A 5 42.31 -99.12
REMARK 500 2 ASN A 8 44.60 72.73
REMARK 500 2 ASP A 20 105.11 -174.55
REMARK 500 2 CYS A 25 152.63 -44.55
REMARK 500 2 LYS A 54 -37.90 -131.45
REMARK 500 2 MET A 79 -36.09 -39.74
REMARK 500 2 GLN A 81 175.21 -56.35
REMARK 500 3 SER A 2 41.96 37.76
REMARK 500 3 ASP A 20 105.00 -173.06
REMARK 500 3 CYS A 23 103.43 -48.75
REMARK 500 3 CYS A 25 153.01 -47.69
REMARK 500 3 PRO A 26 3.67 -69.69
REMARK 500 3 PHE A 29 153.25 -35.52
REMARK 500 3 GLN A 36 91.04 -55.12
REMARK 500 3 GLN A 81 30.98 -84.51
REMARK 500 3 PRO A 94 2.43 -69.75
REMARK 500 3 SER A 96 41.75 -85.22
REMARK 500 4 SER A 5 42.26 -83.15
REMARK 500 4 ASP A 20 104.98 -174.95
REMARK 500 4 CYS A 25 152.66 -37.80
REMARK 500 4 PRO A 26 2.33 -69.73
REMARK 500 4 SER A 83 128.44 -171.93
REMARK 500 4 LYS A 88 104.95 -51.90
REMARK 500 5 CYS A 25 153.30 -37.84
REMARK 500 5 PRO A 26 3.29 -69.75
REMARK 500 5 LYS A 54 -33.81 -131.66
REMARK 500 5 LEU A 80 -31.26 -38.60
REMARK 500 5 GLN A 81 30.93 -85.20
REMARK 500 5 ARG A 84 140.26 -33.31
REMARK 500 5 ASP A 86 149.38 -36.25
REMARK 500 5 PRO A 91 -175.16 -69.73
REMARK 500 5 SER A 92 -60.46 -91.30
REMARK 500 5 PRO A 94 -176.62 -69.75
REMARK 500 6 LEU A 9 -63.27 -90.09
REMARK 500 6 ALA A 13 -70.03 -67.39
REMARK 500 6 CYS A 25 147.60 -37.20
REMARK 500 6 PRO A 26 3.03 -69.82
REMARK 500 6 GLN A 36 98.71 -56.87
REMARK 500 6 VAL A 60 78.56 -111.47
REMARK 500 6 MET A 79 -25.48 -39.98
REMARK 500 6 LEU A 80 39.97 -81.79
REMARK 500
REMARK 500 THIS ENTRY HAS 167 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 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 23 SG
REMARK 620 2 CYS A 25 SG 110.1
REMARK 620 3 ASP A 75 OD1 114.7 116.5
REMARK 620 4 CYS A 77 SG 116.6 112.0 85.1
REMARK 620 N 1 2 3
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
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 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007016392 RELATED DB: TARGETDB
DBREF 1V5R A 8 91 UNP P11862 GAS2_MOUSE 201 284
SEQADV 1V5R GLY A 1 UNP P11862 CLONING ARTIFACT
SEQADV 1V5R SER A 2 UNP P11862 CLONING ARTIFACT
SEQADV 1V5R SER A 3 UNP P11862 CLONING ARTIFACT
SEQADV 1V5R GLY A 4 UNP P11862 CLONING ARTIFACT
SEQADV 1V5R SER A 5 UNP P11862 CLONING ARTIFACT
SEQADV 1V5R SER A 6 UNP P11862 CLONING ARTIFACT
SEQADV 1V5R GLY A 7 UNP P11862 CLONING ARTIFACT
SEQADV 1V5R SER A 92 UNP P11862 CLONING ARTIFACT
SEQADV 1V5R GLY A 93 UNP P11862 CLONING ARTIFACT
SEQADV 1V5R PRO A 94 UNP P11862 CLONING ARTIFACT
SEQADV 1V5R SER A 95 UNP P11862 CLONING ARTIFACT
SEQADV 1V5R SER A 96 UNP P11862 CLONING ARTIFACT
SEQADV 1V5R GLY A 97 UNP P11862 CLONING ARTIFACT
SEQRES 1 A 97 GLY SER SER GLY SER SER GLY ASN LEU LEU ASP ASP ALA
SEQRES 2 A 97 VAL LYS ARG ILE SER GLU ASP PRO PRO CYS LYS CYS PRO
SEQRES 3 A 97 THR LYS PHE CYS VAL GLU ARG LEU SER GLN GLY ARG TYR
SEQRES 4 A 97 ARG VAL GLY GLU LYS ILE LEU PHE ILE ARG MET LEU HIS
SEQRES 5 A 97 ASN LYS HIS VAL MET VAL ARG VAL GLY GLY GLY TRP GLU
SEQRES 6 A 97 THR PHE ALA GLY TYR LEU LEU LYS HIS ASP PRO CYS ARG
SEQRES 7 A 97 MET LEU GLN ILE SER ARG VAL ASP GLY LYS THR SER PRO
SEQRES 8 A 97 SER GLY PRO SER SER GLY
HET ZN A 201 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 LEU A 9 SER A 18 1 10
HELIX 2 2 PHE A 67 HIS A 74 1 8
HELIX 3 3 PRO A 76 MET A 79 1 4
SHEET 1 A 5 VAL A 31 SER A 35 0
SHEET 2 A 5 ARG A 38 VAL A 41 -1 O ARG A 40 N GLU A 32
SHEET 3 A 5 LYS A 44 LEU A 51 -1 O LYS A 44 N VAL A 41
SHEET 4 A 5 HIS A 55 VAL A 60 -1 O HIS A 55 N LEU A 51
SHEET 5 A 5 GLY A 63 THR A 66 -1 O GLY A 63 N VAL A 60
LINK SG CYS A 23 ZN ZN A 201 1555 1555 2.33
LINK SG CYS A 25 ZN ZN A 201 1555 1555 2.34
LINK OD1 ASP A 75 ZN ZN A 201 1555 1555 2.36
LINK SG CYS A 77 ZN ZN A 201 1555 1555 2.37
CISPEP 1 ASP A 20 PRO A 21 1 0.03
CISPEP 2 ASP A 20 PRO A 21 2 0.03
CISPEP 3 ASP A 20 PRO A 21 3 0.06
CISPEP 4 ASP A 20 PRO A 21 4 0.04
CISPEP 5 ASP A 20 PRO A 21 5 0.05
CISPEP 6 ASP A 20 PRO A 21 6 -0.01
CISPEP 7 ASP A 20 PRO A 21 7 0.07
CISPEP 8 ASP A 20 PRO A 21 8 0.00
CISPEP 9 ASP A 20 PRO A 21 9 0.06
CISPEP 10 ASP A 20 PRO A 21 10 -0.01
CISPEP 11 ASP A 20 PRO A 21 11 0.01
CISPEP 12 ASP A 20 PRO A 21 12 0.02
CISPEP 13 ASP A 20 PRO A 21 13 -0.01
CISPEP 14 ASP A 20 PRO A 21 14 0.03
CISPEP 15 ASP A 20 PRO A 21 15 -0.05
CISPEP 16 ASP A 20 PRO A 21 16 0.07
CISPEP 17 ASP A 20 PRO A 21 17 0.01
CISPEP 18 ASP A 20 PRO A 21 18 0.00
CISPEP 19 ASP A 20 PRO A 21 19 0.01
CISPEP 20 ASP A 20 PRO A 21 20 0.03
SITE 1 AC1 4 CYS A 23 CYS A 25 ASP A 75 CYS A 77
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 2 2 Bytes