Header list of 1k9r.pdb file
Complete list - v 10 2 Bytes
HEADER STRUCTURAL PROTEIN 30-OCT-01 1K9R
TITLE YAP65 WW DOMAIN COMPLEXED TO ACETYL-PLPPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 65 KDA YES-ASSOCIATED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: WILD TYPE WW DOMAIN;
COMPND 5 SYNONYM: YAP65;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: WW DOMAIN BINDING PROTEIN-1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES 149-153;
COMPND 11 SYNONYM: WBP-1;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE WAS SYNTHETICALLY OBTAINED, BY
SOURCE 4 SEMIAUTOMATED SPOT SYNTHESIS IN A CELLULOSE SUPPORT.;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 OTHER_DETAILS: THIS SEQUENCE WAS SYNTHETICALLY OBTAINED BY SPOT
SOURCE 10 SYNTHESIS IN A CELLULOSE SUPPORT.
KEYWDS WW DOMAIN, YAP65, BETA-SHEET PROTEINS, LIGANDS, PROLINE-RICH
KEYWDS 2 PEPTIDES, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.R.PIRES,F.TAHA-NEJAD,F.TOEPERT,T.AST,U.HOFFMULLER,J.SCHNEIDER-
AUTHOR 2 MERGENER,R.KUHNE,M.J.MACIAS,H.OSCHKINAT
REVDAT 5 10-NOV-21 1K9R 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1K9R 1 VERSN
REVDAT 3 30-SEP-03 1K9R 1 DBREF
REVDAT 2 04-DEC-02 1K9R 1 REMARK
REVDAT 1 28-DEC-01 1K9R 0
JRNL AUTH J.R.PIRES,F.TAHA-NEJAD,F.TOEPERT,T.AST,U.HOFFMULLER,
JRNL AUTH 2 J.SCHNEIDER-MERGENER,R.KUHNE,M.J.MACIAS,H.OSCHKINAT
JRNL TITL SOLUTION STRUCTURES OF THE YAP65 WW DOMAIN AND THE VARIANT
JRNL TITL 2 L30 K IN COMPLEX WITH THE PEPTIDES GTPPPPYTVG,
JRNL TITL 3 N-(N-OCTYL)-GPPPY AND PLPPY AND THE APPLICATION OF PEPTIDE
JRNL TITL 4 LIBRARIES REVEAL A MINIMAL BINDING EPITOPE.
JRNL REF J.MOL.BIOL. V. 314 1147 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11743730
JRNL DOI 10.1006/JMBI.2000.5199
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 2000K, 200 RUNS, FORCE CONSTANTS FOR
REMARK 3 NOES 50KCAL MOL-1 RAD-2, 330 RESTRAINTS
REMARK 4
REMARK 4 1K9R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014737.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288; 288
REMARK 210 PH : 6; 6
REMARK 210 IONIC STRENGTH : 100MM NACL; 100MM NACL
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : PHOSPHATE BUFFER 10MM, NACL
REMARK 210 100MM, DTT 0.1MM, EDTA 0.1MM, PH
REMARK 210 6, WW DOMAIN 1.2MM, LIGAND 2.4MM;
REMARK 210 PHOSPHATE BUFFER 10MM, NACL
REMARK 210 100MM, DTT 0.1MM, EDTA 0.1MM, PH
REMARK 210 6, WW DOMAIN 1.2MM, LIGAND 2.4MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3
REMARK 210 METHOD USED : SIMULATED ANNELING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 OD1 ASN A 31 H ASP A 34 1.58
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 GLU A 6 -176.14 53.30
REMARK 500 1 ASP A 10 -82.87 -127.68
REMARK 500 1 PRO A 14 -163.11 -72.02
REMARK 500 1 THR A 22 -158.97 -134.48
REMARK 500 1 SER A 23 -91.74 47.40
REMARK 500 1 SER A 24 -42.20 -150.35
REMARK 500 1 GLN A 35 88.36 54.52
REMARK 500 1 LEU B 47 139.15 61.39
REMARK 500 2 ILE A 7 97.06 53.60
REMARK 500 2 ASP A 10 -81.69 -92.92
REMARK 500 2 PRO A 14 -165.70 -72.30
REMARK 500 2 ALA A 20 -151.25 -150.96
REMARK 500 2 SER A 23 -91.85 47.33
REMARK 500 2 SER A 24 -42.07 -153.02
REMARK 500 2 GLN A 35 74.77 50.48
REMARK 500 2 LEU B 47 113.27 -174.50
REMARK 500 3 GLU A 6 50.19 -110.04
REMARK 500 3 PRO A 8 -167.27 -72.29
REMARK 500 3 ASP A 9 66.38 -119.93
REMARK 500 3 ASP A 10 -75.80 -53.33
REMARK 500 3 PRO A 12 -86.50 -73.35
REMARK 500 3 PRO A 14 -164.93 -72.24
REMARK 500 3 ALA A 20 -152.24 -153.50
REMARK 500 3 SER A 23 89.26 -68.45
REMARK 500 3 SER A 24 -32.24 175.64
REMARK 500 3 GLN A 35 76.86 49.90
REMARK 500 3 GLN A 40 -157.76 -73.33
REMARK 500 3 LEU B 47 109.80 -175.68
REMARK 500 3 PRO B 49 -164.65 -72.71
REMARK 500 4 GLU A 6 -178.20 53.23
REMARK 500 4 ASP A 9 52.86 -115.33
REMARK 500 4 PRO A 12 -159.00 -76.88
REMARK 500 4 PRO A 14 -164.83 -72.34
REMARK 500 4 ALA A 20 -151.61 -153.22
REMARK 500 4 SER A 24 -33.57 177.70
REMARK 500 4 GLN A 35 76.21 50.51
REMARK 500 4 GLN A 40 -155.66 -79.89
REMARK 500 4 ARG A 43 79.41 53.23
REMARK 500 4 LEU B 47 129.92 -174.95
REMARK 500 4 PRO B 49 -162.97 -72.63
REMARK 500 5 GLU A 6 -166.79 53.30
REMARK 500 5 PRO A 8 -87.53 -71.62
REMARK 500 5 PRO A 12 -158.85 -71.35
REMARK 500 5 PRO A 14 -162.78 -72.94
REMARK 500 5 SER A 23 -149.62 45.75
REMARK 500 5 GLN A 26 135.82 -173.18
REMARK 500 5 GLN A 35 76.63 35.28
REMARK 500 6 GLU A 6 87.30 -175.00
REMARK 500 6 ASP A 9 26.02 47.21
REMARK 500 6 PRO A 14 -163.04 -72.75
REMARK 500
REMARK 500 THIS ENTRY HAS 200 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JMQ RELATED DB: PDB
REMARK 900 1JMQ CONTAINS YAP65 (L30K MUTANT) WW DOMAIN IN COMPLEXED WITH
REMARK 900 GTPPPPYTVG PEPTIDE
REMARK 900 RELATED ID: 1K9Q RELATED DB: PDB
REMARK 900 1K9Q CONTAINS YAP65 WW DOMAIN COMPLEXED WITH N-(N-OCTYL)-GPPPY-NH2
REMARK 900 RELATED ID: 1E0M RELATED DB: PDB
REMARK 900 1E0M CONTAINS PROTOTYPE WW DOMAIN
REMARK 900 RELATED ID: 1EG3 RELATED DB: PDB
REMARK 900 1EG3 CONTAINS DYSTROPHIN WW DOMAIN FRAGMENT
REMARK 900 RELATED ID: 1EG4 RELATED DB: PDB
REMARK 900 1EG4 CONTAINS DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEXED WITH BETA-
REMARK 900 DYSTROGLYCAN PEPTIDE
REMARK 900 RELATED ID: 1I5H RELATED DB: PDB
REMARK 900 1I5H CONTAINS RNEDD4 WWIII DOMAIN-RENAC BP2 PEPTIDE COMPLEX
DBREF 1K9R A 5 44 UNP P46937 YAP1_HUMAN 165 204
DBREF 1K9R B 46 50 GB 4205084 AAD10950 149 153
SEQADV 1K9R LEU B 47 GB 4205084 PRO 150 ENGINEERED MUTATION
SEQRES 1 A 40 PHE GLU ILE PRO ASP ASP VAL PRO LEU PRO ALA GLY TRP
SEQRES 2 A 40 GLU MET ALA LYS THR SER SER GLY GLN ARG TYR PHE LEU
SEQRES 3 A 40 ASN HIS ILE ASP GLN THR THR THR TRP GLN ASP PRO ARG
SEQRES 4 A 40 LYS
SEQRES 1 B 6 ACE PRO LEU PRO PRO TYR
HET ACE B 45 6
HETNAM ACE ACETYL GROUP
FORMUL 2 ACE C2 H4 O
SHEET 1 A 3 TRP A 17 THR A 22 0
SHEET 2 A 3 GLN A 26 ASN A 31 -1 O LEU A 30 N GLU A 18
SHEET 3 A 3 THR A 36 THR A 38 -1 O THR A 36 N ASN A 31
LINK C ACE B 45 N PRO B 46 1555 1555 1.31
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 - v 10 2 Bytes