Header list of 2cr8.pdb file
Complete list - r 9 2 Bytes
HEADER CELL CYCLE 20-MAY-05 2CR8
TITLE SOLUTION STRUCTURE OF THE ZF-RANBP DOMAIN OF P53-BINDING PROTEIN MDM4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MDM4 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZF-RANBP DOMAIN;
COMPND 5 SYNONYM: P53-BINDING PROTEIN MDM4, MDM2-LIKE P53-BINDING PROTEIN,
COMPND 6 MDMX PROTEIN, DOUBLE MINUTE 4 PROTEIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MDM4;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040809-07;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS ZF-RANBP DOMAIN; MDM4 PROTEIN; P53-BINDING PROTEIN MDM4; MDM2-LIKE
KEYWDS 2 P53-BINDING DE PROTEIN; MDMX PROTEIN; DOUBLE MINUTE 4 PROTEIN,
KEYWDS 3 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 4 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 5 INITIATIVE, RSGI, CELL CYCLE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.P.ZHANG,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CR8 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2CR8 1 VERSN
REVDAT 1 20-NOV-05 2CR8 0
JRNL AUTH H.P.ZHANG,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE ZF-RANBP DOMAIN OF P53-BINDING
JRNL TITL 2 PROTEIN MDM4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT,P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CR8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024535.
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 : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.42MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL (PH7.0); 200MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3;
REMARK 210 0.01MM ZNCL2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.04,
REMARK 210 KUJIRA 0.9296, 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 : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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 42.32 35.43
REMARK 500 1 GLU A 9 40.50 -109.06
REMARK 500 1 ASP A 10 40.74 -106.36
REMARK 500 1 CYS A 42 -50.68 -130.52
REMARK 500 1 PRO A 50 -174.27 -69.71
REMARK 500 2 TRP A 32 52.44 34.03
REMARK 500 2 ARG A 35 167.81 -44.25
REMARK 500 3 SER A 6 148.49 -36.10
REMARK 500 3 CYS A 28 116.82 -33.19
REMARK 500 3 PHE A 29 40.05 -82.17
REMARK 500 3 ARG A 30 -40.66 -134.60
REMARK 500 3 ARG A 35 -75.32 -54.13
REMARK 500 3 ASP A 37 42.03 -86.62
REMARK 500 3 LEU A 45 111.82 -38.58
REMARK 500 3 SER A 51 -50.29 -128.34
REMARK 500 3 SER A 52 41.80 39.88
REMARK 500 4 SER A 8 94.83 -65.65
REMARK 500 4 LYS A 18 28.38 38.94
REMARK 500 4 ARG A 26 -63.81 -121.04
REMARK 500 4 TRP A 32 54.62 34.00
REMARK 500 4 LYS A 44 41.24 -96.57
REMARK 500 4 SER A 52 -49.41 -133.74
REMARK 500 5 PRO A 23 2.72 -69.79
REMARK 500 5 TRP A 32 41.55 34.38
REMARK 500 5 SER A 43 137.54 -37.01
REMARK 500 5 SER A 48 149.07 -174.41
REMARK 500 5 SER A 52 41.95 37.17
REMARK 500 6 SER A 8 139.78 -170.22
REMARK 500 6 GLU A 9 153.58 -37.19
REMARK 500 6 LYS A 18 26.65 40.52
REMARK 500 6 PRO A 23 5.88 -69.72
REMARK 500 6 ARG A 30 -33.71 -133.41
REMARK 500 6 TRP A 32 48.38 37.16
REMARK 500 6 ASP A 37 121.54 -35.82
REMARK 500 7 SER A 6 43.29 70.74
REMARK 500 7 ASP A 10 43.77 -82.64
REMARK 500 7 LYS A 18 26.99 40.07
REMARK 500 7 ARG A 30 -35.34 -134.87
REMARK 500 7 TRP A 32 49.37 34.75
REMARK 500 7 LEU A 34 155.34 -43.47
REMARK 500 8 SER A 2 42.16 -98.38
REMARK 500 8 PRO A 23 2.81 -69.70
REMARK 500 8 TRP A 32 38.80 31.72
REMARK 500 8 ARG A 35 43.62 -81.63
REMARK 500 9 GLU A 16 -52.12 -128.81
REMARK 500 9 ARG A 30 -35.33 -134.66
REMARK 500 9 TRP A 32 48.74 33.69
REMARK 500 9 ARG A 35 102.05 -33.96
REMARK 500 9 PRO A 50 88.22 -69.78
REMARK 500 10 LYS A 18 37.37 33.90
REMARK 500
REMARK 500 THIS ENTRY HAS 132 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 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 14 SG
REMARK 620 2 CYS A 17 SG 111.9
REMARK 620 3 CYS A 28 SG 102.1 106.1
REMARK 620 4 CYS A 31 SG 105.0 117.2 113.6
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 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001003497.1 RELATED DB: TARGETDB
DBREF 2CR8 A 8 47 UNP O15151 MDM4_HUMAN 300 339
SEQADV 2CR8 GLY A 1 UNP O15151 CLONING ARTIFACT
SEQADV 2CR8 SER A 2 UNP O15151 CLONING ARTIFACT
SEQADV 2CR8 SER A 3 UNP O15151 CLONING ARTIFACT
SEQADV 2CR8 GLY A 4 UNP O15151 CLONING ARTIFACT
SEQADV 2CR8 SER A 5 UNP O15151 CLONING ARTIFACT
SEQADV 2CR8 SER A 6 UNP O15151 CLONING ARTIFACT
SEQADV 2CR8 GLY A 7 UNP O15151 CLONING ARTIFACT
SEQADV 2CR8 SER A 48 UNP O15151 CLONING ARTIFACT
SEQADV 2CR8 GLY A 49 UNP O15151 CLONING ARTIFACT
SEQADV 2CR8 PRO A 50 UNP O15151 CLONING ARTIFACT
SEQADV 2CR8 SER A 51 UNP O15151 CLONING ARTIFACT
SEQADV 2CR8 SER A 52 UNP O15151 CLONING ARTIFACT
SEQADV 2CR8 GLY A 53 UNP O15151 CLONING ARTIFACT
SEQRES 1 A 53 GLY SER SER GLY SER SER GLY SER GLU ASP GLU TRP GLN
SEQRES 2 A 53 CYS THR GLU CYS LYS LYS PHE ASN SER PRO SER LYS ARG
SEQRES 3 A 53 TYR CYS PHE ARG CYS TRP ALA LEU ARG LYS ASP TRP TYR
SEQRES 4 A 53 SER ASP CYS SER LYS LEU THR HIS SER GLY PRO SER SER
SEQRES 5 A 53 GLY
HET ZN A 401 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
LINK SG CYS A 14 ZN ZN A 401 1555 1555 2.35
LINK SG CYS A 17 ZN ZN A 401 1555 1555 2.25
LINK SG CYS A 28 ZN ZN A 401 1555 1555 2.34
LINK SG CYS A 31 ZN ZN A 401 1555 1555 2.25
SITE 1 AC1 4 CYS A 14 CYS A 17 CYS A 28 CYS A 31
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 9 2 Bytes