HEADER TRANSCRIPTION 30-MAR-07 2EPQ
TITLE SOLUTION STRUCTURE OF THE THIRD ZINC FINGER DOMAIN OF ZINC FINGER
TITLE 2 PROTEIN 278
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POZ-, AT HOOK-, AND ZINC FINGER-CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC FINGER DOMAIN;
COMPND 5 SYNONYM: ZINC FINGER PROTEIN 278, ZINC FINGER SARCOMA GENE PROTEIN,
COMPND 6 BTB-POZ DOMAIN ZINC FINGER TRANSCRIPTION FACTOR, PROTEIN KINASE A RI-
COMPND 7 SUBUNIT ALPHA- ASSOCIATED PROTEIN, ZINC FINGER AND BTB DOMAIN-
COMPND 8 CONTAINING PROTEIN 19;
COMPND 9 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: PATZ1, PATZ, RIAZ, ZBTB19, ZNF278, ZSG;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P061204-01;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS C2H2, ZINC FINGER DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.TANABE,S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2EPQ 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2EPQ 1 VERSN
REVDAT 1 12-FEB-08 2EPQ 0
JRNL AUTH W.TANABE,S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,
JRNL AUTH 2 M.SHIROUZU,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE THIRD ZINC FINGER DOMAIN OF ZINC
JRNL TITL 2 FINGER PROTEIN 278
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EPQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000026955.
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 : 0.97MM 13C-15N PROTEIN; 20MM D
REMARK 210 -TRIS-HCL (PH7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 0.05MM
REMARK 210 ZNCL2, 1MM IDA; 90% H2O, 10% D2O
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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20060702, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9820, CYANA 2.1
REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS,
REMARK 210 SIMULATED ANNEALING
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 375 -70.14 -60.18
REMARK 500 1 LYS A 381 73.69 59.63
REMARK 500 1 CYS A 385 74.29 -113.66
REMARK 500 1 LEU A 390 108.64 -168.06
REMARK 500 1 VAL A 409 147.36 -172.16
REMARK 500 2 SER A 377 44.44 -103.48
REMARK 500 2 TYR A 383 76.27 -111.42
REMARK 500 2 LEU A 390 106.06 -168.53
REMARK 500 3 LYS A 381 73.74 -154.56
REMARK 500 3 CYS A 385 74.75 -113.51
REMARK 500 3 LEU A 390 109.81 -167.72
REMARK 500 4 CYS A 385 74.70 -113.87
REMARK 500 4 LEU A 390 105.70 -168.73
REMARK 500 4 SER A 408 72.54 -116.74
REMARK 500 5 SER A 377 66.31 -114.50
REMARK 500 5 LYS A 381 74.03 -160.70
REMARK 500 5 CYS A 385 75.05 -113.48
REMARK 500 5 LEU A 390 112.42 -169.03
REMARK 500 5 LYS A 411 99.13 -59.69
REMARK 500 5 PRO A 414 93.79 -69.76
REMARK 500 6 TYR A 383 68.33 -112.46
REMARK 500 6 LEU A 390 106.33 -168.98
REMARK 500 7 SER A 375 -68.70 -131.78
REMARK 500 7 LYS A 381 73.71 56.79
REMARK 500 7 CYS A 385 74.65 -113.54
REMARK 500 7 LEU A 390 112.97 -168.61
REMARK 500 7 HIS A 405 46.68 -91.24
REMARK 500 8 CYS A 385 74.94 -117.44
REMARK 500 8 LEU A 390 104.11 -168.01
REMARK 500 8 SER A 412 -60.22 -103.99
REMARK 500 8 PRO A 414 -175.32 -69.79
REMARK 500 9 LYS A 381 73.57 -168.46
REMARK 500 9 CYS A 385 75.25 -113.37
REMARK 500 9 LEU A 390 110.88 -168.43
REMARK 500 10 LEU A 390 108.40 -165.81
REMARK 500 11 SER A 378 68.29 -100.40
REMARK 500 11 TYR A 383 77.02 -101.59
REMARK 500 11 CYS A 385 75.87 -113.36
REMARK 500 11 LEU A 390 106.69 -167.57
REMARK 500 11 SER A 415 62.36 -102.11
REMARK 500 12 CYS A 385 74.23 -114.75
REMARK 500 12 LEU A 390 110.30 -166.68
REMARK 500 13 SER A 378 -65.29 -97.66
REMARK 500 13 CYS A 385 74.16 -113.66
REMARK 500 13 LEU A 390 104.71 -167.23
REMARK 500 14 CYS A 385 74.25 -115.17
REMARK 500 14 LEU A 390 113.36 -166.83
REMARK 500 14 PRO A 414 91.82 -69.75
REMARK 500 15 CYS A 385 74.37 -113.63
REMARK 500 15 LEU A 390 109.51 -166.58
REMARK 500
REMARK 500 THIS ENTRY HAS 68 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 385 SG
REMARK 620 2 CYS A 388 SG 108.3
REMARK 620 3 HIS A 401 NE2 112.4 119.0
REMARK 620 4 HIS A 405 NE2 99.3 101.8 113.8
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 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002013231.2 RELATED DB: TARGETDB
DBREF 2EPQ A 380 411 UNP Q9HBE1 PATZ1_HUMAN 380 411
SEQADV 2EPQ GLY A 373 UNP Q9HBE1 EXPRESSION TAG
SEQADV 2EPQ SER A 374 UNP Q9HBE1 EXPRESSION TAG
SEQADV 2EPQ SER A 375 UNP Q9HBE1 EXPRESSION TAG
SEQADV 2EPQ GLY A 376 UNP Q9HBE1 EXPRESSION TAG
SEQADV 2EPQ SER A 377 UNP Q9HBE1 EXPRESSION TAG
SEQADV 2EPQ SER A 378 UNP Q9HBE1 EXPRESSION TAG
SEQADV 2EPQ GLY A 379 UNP Q9HBE1 EXPRESSION TAG
SEQADV 2EPQ SER A 412 UNP Q9HBE1 EXPRESSION TAG
SEQADV 2EPQ GLY A 413 UNP Q9HBE1 EXPRESSION TAG
SEQADV 2EPQ PRO A 414 UNP Q9HBE1 EXPRESSION TAG
SEQADV 2EPQ SER A 415 UNP Q9HBE1 EXPRESSION TAG
SEQADV 2EPQ SER A 416 UNP Q9HBE1 EXPRESSION TAG
SEQADV 2EPQ GLY A 417 UNP Q9HBE1 EXPRESSION TAG
SEQRES 1 A 45 GLY SER SER GLY SER SER GLY GLU LYS PRO TYR SER CYS
SEQRES 2 A 45 PRO VAL CYS GLY LEU ARG PHE LYS ARG LYS ASP ARG MET
SEQRES 3 A 45 SER TYR HIS VAL ARG SER HIS ASP GLY SER VAL GLY LYS
SEQRES 4 A 45 SER GLY PRO SER SER GLY
HET ZN A 201 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ARG A 394 ASP A 406 1 13
SHEET 1 A 2 SER A 384 CYS A 385 0
SHEET 2 A 2 LEU A 390 ARG A 391 -1 O LEU A 390 N CYS A 385
LINK ZN ZN A 201 SG CYS A 385 1555 1555 2.27
LINK ZN ZN A 201 SG CYS A 388 1555 1555 2.19
LINK ZN ZN A 201 NE2 HIS A 401 1555 1555 2.10
LINK ZN ZN A 201 NE2 HIS A 405 1555 1555 2.09
SITE 1 AC1 4 CYS A 385 CYS A 388 HIS A 401 HIS A 405
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
(ATOM LINES ARE NOT SHOWN.)
END