Header list of 1m9o.pdb file
Complete list - t 27 2 Bytes
HEADER METAL BINDING PROTEIN 29-JUL-02 1M9O
TITLE NMR STRUCTURE OF THE FIRST ZINC BINDING DOMAIN OF NUP475/TTP/TIS11
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRISTETRAPROLINE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC BINDING DOMAIN (RESIDUES 91-163);
COMPND 5 SYNONYM: TTP, TIS11A PROTEIN, TIS11, ZFP-36, GROWTH FACTOR-INDUCIBLE
COMPND 6 NUCLEAR PROTEIN NUP475, TPA INDUCED SEQUENCE 11;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: 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: NUP475;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B, PMW55
KEYWDS CYS3HIS TYPE ZINC FINGER, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 23
AUTHOR B.T.AMANN,M.T.WORTHINGTON,J.M.BERG
REVDAT 3 27-OCT-21 1M9O 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1M9O 1 VERSN
REVDAT 1 03-JUN-03 1M9O 0
JRNL AUTH B.T.AMANN,M.T.WORTHINGTON,J.M.BERG
JRNL TITL A CYS3HIS ZINC-BINDING DOMAIN FROM NUP475/TRISTETRAPROLINE:
JRNL TITL 2 A NOVEL FOLD WITH A DISKLIKE STRUCTURE
JRNL REF BIOCHEMISTRY V. 42 217 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12515557
JRNL DOI 10.1021/BI026988M
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 98, CNS 1.0
REMARK 3 AUTHORS : BIOSYM/MOLECULAR SIMULATION (FELIX), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 442 NOE RESTRAINTS, 15 TORSIONAL ANGLE RESTRAINTS.
REMARK 3 15 ZINC SITE RESTRAINTS, 64 CARBON CHEMICAL SHIFTS, AND
REMARK 3 174 PROTON CHEMICAL RESTRAINTS.
REMARK 4
REMARK 4 1M9O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016770.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : NO SALT ADDED
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.7MM NUP475 WITH 2.2 EQUIVALENT
REMARK 210 ZNCL2, 50MM D-TRIS PH 5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 3D_13C-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNCACB; 15N-
REMARK 210 HSQC-TOCSY; 13C-HCCH-TOCSY;
REMARK 210 HSQCJ_WEX
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.0, VNMR 6.1B
REMARK 210 METHOD USED : CNS, DYNAMICAL ANNEALING
REMARK 210 PROTOCAL WITH MOLECULAR DYNAMIC
REMARK 210 SCHEME OF TORSION,TORSION,
REMARK 210 CARTESIAN. INITIALLY ONLY
REMARK 210 DISTANCE RESTRAINTS FROM THE
REMARK 210 THREE CYS TO THE ZINC WERE
REMARK 210 RESTRAINED. EVENTUALLY THE HIS
REMARK 210 WAS ALSO RESTRAINED AND ANGLE
REMARK 210 RESTRAINTS ADDED TO MAKE THE
REMARK 210 SITE TETRAHEDRAL.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-23
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 ARG A 44
REMARK 465 HIS A 45
REMARK 465 PRO A 46
REMARK 465 LYS A 47
REMARK 465 TYR A 48
REMARK 465 LYS A 49
REMARK 465 THR A 50
REMARK 465 GLU A 51
REMARK 465 LEU A 52
REMARK 465 CYS A 53
REMARK 465 HIS A 54
REMARK 465 LYS A 55
REMARK 465 PHE A 56
REMARK 465 LYS A 57
REMARK 465 LEU A 58
REMARK 465 GLN A 59
REMARK 465 GLY A 60
REMARK 465 ARG A 61
REMARK 465 CYS A 62
REMARK 465 PRO A 63
REMARK 465 TYR A 64
REMARK 465 GLY A 65
REMARK 465 SER A 66
REMARK 465 ARG A 67
REMARK 465 CYS A 68
REMARK 465 HIS A 69
REMARK 465 PHE A 70
REMARK 465 ILE A 71
REMARK 465 HIS A 72
REMARK 465 ASN A 73
REMARK 465 PRO A 74
REMARK 465 THR A 75
REMARK 465 GLU A 76
REMARK 465 ASP A 77
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 O ALA A 33 HD1 HIS A 34 1.47
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 THR A 5 -168.86 57.38
REMARK 500 1 SER A 7 46.54 -104.21
REMARK 500 1 SER A 8 -71.21 -177.18
REMARK 500 1 ARG A 9 151.47 61.70
REMARK 500 1 TYR A 10 -162.84 -63.95
REMARK 500 1 LYS A 11 -166.20 -67.97
REMARK 500 1 ARG A 16 -101.41 -78.07
REMARK 500 1 GLU A 20 32.96 -97.39
REMARK 500 1 CYS A 24 83.97 65.17
REMARK 500 1 ALA A 28 -14.97 75.70
REMARK 500 1 PHE A 32 -85.79 -157.75
REMARK 500 1 ALA A 33 105.57 -33.26
REMARK 500 1 HIS A 34 -139.67 -161.99
REMARK 500 1 LEU A 36 -75.19 -63.14
REMARK 500 1 GLN A 41 12.86 -152.03
REMARK 500 1 ALA A 42 -22.45 178.74
REMARK 500 2 THR A 5 -52.11 -135.58
REMARK 500 2 SER A 7 -40.75 -163.28
REMARK 500 2 ARG A 9 -175.43 -68.11
REMARK 500 2 TYR A 10 -165.33 -76.99
REMARK 500 2 LYS A 11 -167.53 -71.21
REMARK 500 2 ARG A 16 -97.71 -70.04
REMARK 500 2 SER A 21 18.63 158.64
REMARK 500 2 ARG A 23 -57.15 -133.36
REMARK 500 2 CYS A 24 79.85 72.46
REMARK 500 2 TYR A 26 49.90 -140.91
REMARK 500 2 ALA A 28 -14.35 70.96
REMARK 500 2 PHE A 32 -138.79 -153.71
REMARK 500 2 ALA A 33 -158.94 51.75
REMARK 500 2 HIS A 34 -147.10 83.59
REMARK 500 2 LEU A 36 -77.12 -37.22
REMARK 500 2 GLU A 38 46.30 -85.51
REMARK 500 2 ARG A 40 39.87 -93.15
REMARK 500 2 GLN A 41 -58.14 -153.73
REMARK 500 2 ALA A 42 -177.81 56.69
REMARK 500 3 SER A 8 71.37 60.14
REMARK 500 3 TYR A 10 -164.25 -73.72
REMARK 500 3 LYS A 11 -166.70 -69.67
REMARK 500 3 ARG A 16 -100.06 -79.48
REMARK 500 3 SER A 21 -0.72 150.53
REMARK 500 3 ARG A 23 -60.27 -178.26
REMARK 500 3 CYS A 24 80.78 67.26
REMARK 500 3 ALA A 28 -25.81 78.21
REMARK 500 3 PHE A 32 -84.38 -158.62
REMARK 500 3 ALA A 33 107.12 -33.26
REMARK 500 3 HIS A 34 -116.16 -163.27
REMARK 500 3 GLN A 41 72.48 -151.09
REMARK 500 3 ALA A 42 178.57 -51.05
REMARK 500 4 THR A 5 -78.96 -146.66
REMARK 500 4 SER A 8 93.31 -161.58
REMARK 500
REMARK 500 THIS ENTRY HAS 363 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 78 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 15 SG
REMARK 620 2 CYS A 24 SG 110.9
REMARK 620 3 CYS A 30 SG 119.2 123.8
REMARK 620 4 HIS A 34 NE2 94.0 98.0 102.1
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 78
DBREF 1M9O A 5 77 UNP P22893 TTP_MOUSE 91 163
SEQADV 1M9O GLY A 1 UNP P22893 CLONING ARTIFACT
SEQADV 1M9O SER A 2 UNP P22893 CLONING ARTIFACT
SEQADV 1M9O HIS A 3 UNP P22893 CLONING ARTIFACT
SEQADV 1M9O MET A 4 UNP P22893 CLONING ARTIFACT
SEQADV 1M9O LYS A 57 UNP P22893 TYR 143 ENGINEERED MUTATION
SEQRES 1 A 77 GLY SER HIS MET THR THR SER SER ARG TYR LYS THR GLU
SEQRES 2 A 77 LEU CYS ARG THR TYR SER GLU SER GLY ARG CYS ARG TYR
SEQRES 3 A 77 GLY ALA LYS CYS GLN PHE ALA HIS GLY LEU GLY GLU LEU
SEQRES 4 A 77 ARG GLN ALA ASN ARG HIS PRO LYS TYR LYS THR GLU LEU
SEQRES 5 A 77 CYS HIS LYS PHE LYS LEU GLN GLY ARG CYS PRO TYR GLY
SEQRES 6 A 77 SER ARG CYS HIS PHE ILE HIS ASN PRO THR GLU ASP
HET ZN A 78 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ARG A 16 SER A 21 5 6
HELIX 2 2 GLU A 38 ALA A 42 5 5
LINK SG CYS A 15 ZN ZN A 78 1555 1555 2.35
LINK SG CYS A 24 ZN ZN A 78 1555 1555 2.31
LINK SG CYS A 30 ZN ZN A 78 1555 1555 2.29
LINK NE2 HIS A 34 ZN ZN A 78 1555 1555 1.99
SITE 1 AC1 4 CYS A 15 CYS A 24 CYS A 30 HIS A 34
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 - t 27 2 Bytes