Header list of 1co4.pdb file
Complete list - 16 20 Bytes
HEADER TRANSLATION/REGULATION PROTEIN 04-JUN-99 1CO4
TITLE SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-
TITLE 2 REGULATED TRANSCRIPTION FACTORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ACTIVATOR OF METALLOTHIONEIN 1);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-42;
COMPND 5 SYNONYM: AMT1;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: ZINC BINDING DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THIS PROTEIN IS NATURALLY FOUND IN CANDIDA GLABRATA.
KEYWDS METALLOTHIONEIN, AMT, METAL REGULATION, TRANSLATION-REGULATION
KEYWDS 2 PROTEIN COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR R.B.TURNER,D.L.SMITH,M.E.ZAWROTNY,M.F.SUMMERS,M.C.POSEWITZ,D.R.WINGE
REVDAT 3 16-FEB-22 1CO4 1 REMARK
REVDAT 2 24-FEB-09 1CO4 1 VERSN
REVDAT 1 10-JUN-99 1CO4 0
JRNL AUTH R.B.TURNER,D.L.SMITH,M.E.ZAWROTNY,M.F.SUMMERS,M.C.POSEWITZ,
JRNL AUTH 2 D.R.WINGE
JRNL TITL SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST
JRNL TITL 2 COPPER-REGULATED TRANSCRIPTION FACTORS.
JRNL REF NAT.STRUCT.BIOL. V. 5 551 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9665167
JRNL DOI 10.1038/805
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CO4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1000001151.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 25MM NACL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 25MM NAOAC, 0.1MM ZNCL2, 90%
REMARK 210 WATER/10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; HOHAHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX 600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 2.0
REMARK 210 METHOD USED : DYANA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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 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
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 ASN A 5 -86.88 60.76
REMARK 500 1 ALA A 10 166.19 173.16
REMARK 500 1 CYS A 14 -60.75 -145.74
REMARK 500 1 SER A 17 -75.79 -96.78
REMARK 500 1 HIS A 18 -25.12 158.89
REMARK 500 1 ALA A 21 -32.94 -37.19
REMARK 500 1 GLN A 22 39.43 -156.00
REMARK 500 1 GLU A 24 23.07 -154.18
REMARK 500 1 ASN A 26 -73.92 -108.79
REMARK 500 1 ASP A 27 178.88 -50.19
REMARK 500 1 ARG A 28 151.64 79.74
REMARK 500 1 ARG A 36 158.44 58.88
REMARK 500 1 ARG A 38 150.74 86.32
REMARK 500 1 THR A 41 -80.34 -124.43
REMARK 500 2 ASN A 5 -82.65 67.24
REMARK 500 2 CYS A 14 -52.17 -150.41
REMARK 500 2 SER A 17 -79.18 -102.04
REMARK 500 2 HIS A 18 -24.87 158.78
REMARK 500 2 ALA A 21 -32.98 -37.16
REMARK 500 2 GLN A 22 43.72 -155.64
REMARK 500 2 ASP A 27 178.93 -53.65
REMARK 500 2 ARG A 28 150.79 77.28
REMARK 500 2 LEU A 33 174.25 174.73
REMARK 500 2 PRO A 35 -89.04 -75.01
REMARK 500 2 ARG A 36 133.89 61.90
REMARK 500 2 ARG A 38 68.93 69.76
REMARK 500 2 PRO A 40 -82.40 -75.00
REMARK 500 2 THR A 41 -42.67 169.53
REMARK 500 3 ASN A 5 -88.21 60.84
REMARK 500 3 CYS A 14 -55.44 -145.50
REMARK 500 3 SER A 17 -78.47 -100.79
REMARK 500 3 HIS A 18 -24.11 158.54
REMARK 500 3 ALA A 21 -35.37 -35.44
REMARK 500 3 GLN A 22 41.08 -155.45
REMARK 500 3 CYS A 23 152.08 -42.19
REMARK 500 3 GLU A 24 25.71 -158.25
REMARK 500 3 ASN A 26 -65.77 -128.49
REMARK 500 3 ASP A 27 179.26 -50.44
REMARK 500 3 ARG A 28 151.88 75.08
REMARK 500 3 LEU A 33 -179.79 -179.85
REMARK 500 3 PRO A 40 -162.70 -75.00
REMARK 500 3 THR A 41 -92.88 -42.51
REMARK 500 4 ASN A 5 -88.95 60.61
REMARK 500 4 CYS A 14 -58.27 -142.28
REMARK 500 4 SER A 17 -75.28 -95.58
REMARK 500 4 HIS A 18 -25.45 159.48
REMARK 500 4 GLU A 24 30.22 -166.57
REMARK 500 4 ASN A 26 -74.36 -107.61
REMARK 500 4 ASP A 27 179.20 -51.82
REMARK 500 4 ARG A 28 151.82 79.28
REMARK 500
REMARK 500 THIS ENTRY HAS 197 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 43 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 CYS A 14 SG 85.4
REMARK 620 3 CYS A 23 SG 115.5 114.4
REMARK 620 4 HIS A 25 ND1 125.4 101.6 110.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZNB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZN METAL-BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 43
DBREF 1CO4 A 1 42 UNP P41772 AMT1_CANGA 1 42
SEQRES 1 A 42 MET VAL VAL ILE ASN GLY VAL LYS TYR ALA CYS ASP SER
SEQRES 2 A 42 CYS ILE LYS SER HIS LYS ALA ALA GLN CYS GLU HIS ASN
SEQRES 3 A 42 ASP ARG PRO LEU LYS ILE LEU LYS PRO ARG GLY ARG PRO
SEQRES 4 A 42 PRO THR THR
HET ZN A 43 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 H1 ASP A 12 ILE A 15 5 4
HELIX 2 H2 HIS A 18 GLN A 22 5 5
SHEET 1 A 3 VAL A 2 ILE A 4 0
SHEET 2 A 3 VAL A 7 CYS A 11 -1 N TYR A 9 O VAL A 2
SHEET 3 A 3 LEU A 30 LEU A 33 -1 N LEU A 33 O LYS A 8
LINK SG CYS A 11 ZN ZN A 43 1555 1555 2.34
LINK SG CYS A 14 ZN ZN A 43 1555 1555 2.37
LINK SG CYS A 23 ZN ZN A 43 1555 1555 2.30
LINK ND1 HIS A 25 ZN ZN A 43 1555 1555 2.06
SITE 1 ZNB 4 CYS A 11 CYS A 14 CYS A 23 HIS A 25
SITE 1 AC1 4 CYS A 11 CYS A 14 CYS A 23 HIS A 25
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 - 16 20 Bytes