Header list of 2cup.pdb file
Complete list - r 9 2 Bytes
HEADER METAL BINDING PROTEIN 27-MAY-05 2CUP
TITLE SOLUTION STRUCTURE OF THE SKELETAL MUSCLE LIM-PROTEIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SKELETAL MUSCLE LIM-PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ONE AND A HALF LIM DOMAIN;
COMPND 5 SYNONYM: SLIM 1, SLIM, FOUR AND A HALF LIM DOMAINS PROTEIN 1, FHL-1;
COMPND 6 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: FHL 1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: 040816-01;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS FOUR AND HALF LIM DOMAINS PROTEIN 1, LIM DOMAIN, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.N.NIRAULA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CUP 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2CUP 1 VERSN
REVDAT 1 27-NOV-05 2CUP 0
JRNL AUTH T.N.NIRAULA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SKELETAL MUSCLE LIM-PROTEIN 1
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 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CUP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024640.
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 : 1.40MM PROTEIN U-13C 15N; 20MM D
REMARK 210 -TRIS-HCL(PH 7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 0.01MM
REMARK 210 ZNCL2; 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 : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.913, 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 LEAST RESTRAINT 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 3 -47.61 -133.07
REMARK 500 1 PHE A 34 104.98 -59.61
REMARK 500 1 THR A 62 175.23 -48.11
REMARK 500 1 SER A 66 161.62 -44.25
REMARK 500 1 TYR A 85 -77.07 -126.34
REMARK 500 1 LYS A 92 -36.93 -38.43
REMARK 500 1 SER A 96 78.84 -108.43
REMARK 500 1 PRO A 98 2.55 -69.74
REMARK 500 2 ARG A 12 32.73 37.60
REMARK 500 2 ARG A 63 128.90 -35.60
REMARK 500 2 SER A 66 145.82 -33.95
REMARK 500 2 PRO A 67 -179.42 -69.70
REMARK 500 2 PHE A 73 51.49 73.74
REMARK 500 2 TYR A 85 -72.02 -98.13
REMARK 500 2 LYS A 92 -29.38 -36.54
REMARK 500 2 SER A 96 -60.41 -123.23
REMARK 500 2 SER A 100 145.40 -35.64
REMARK 500 3 ARG A 12 28.53 46.32
REMARK 500 3 ASP A 65 51.06 39.10
REMARK 500 3 PHE A 73 51.41 71.78
REMARK 500 3 LYS A 92 -36.59 -36.69
REMARK 500 4 ARG A 12 37.99 30.99
REMARK 500 4 PHE A 34 99.51 -59.39
REMARK 500 4 ASP A 65 76.57 -100.68
REMARK 500 4 LYS A 92 -31.96 -34.45
REMARK 500 4 SER A 96 55.80 -97.73
REMARK 500 4 SER A 99 39.26 37.73
REMARK 500 5 SER A 5 -62.75 -100.28
REMARK 500 5 SER A 6 102.66 -55.14
REMARK 500 5 ARG A 12 37.94 39.94
REMARK 500 5 PHE A 34 98.74 -55.70
REMARK 500 5 CYS A 36 172.60 -59.05
REMARK 500 5 THR A 61 -31.63 -38.08
REMARK 500 5 ARG A 63 115.52 -39.40
REMARK 500 5 ASP A 65 39.58 -85.81
REMARK 500 5 TYR A 85 -80.80 -123.61
REMARK 500 6 SER A 5 44.30 -100.67
REMARK 500 6 ASP A 65 44.67 73.77
REMARK 500 6 SER A 66 139.91 -37.48
REMARK 500 6 PHE A 73 49.00 74.22
REMARK 500 6 GLN A 81 147.59 -39.79
REMARK 500 6 TYR A 85 -77.34 -114.24
REMARK 500 6 HIS A 91 158.14 -49.73
REMARK 500 6 SER A 99 144.91 -171.77
REMARK 500 7 PHE A 34 97.01 -58.48
REMARK 500 7 ASP A 65 87.28 -57.83
REMARK 500 7 SER A 66 157.27 -37.50
REMARK 500 7 PRO A 67 -175.87 -69.79
REMARK 500 7 LYS A 92 -31.47 -34.74
REMARK 500 8 ARG A 12 42.63 31.50
REMARK 500
REMARK 500 THIS ENTRY HAS 125 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 8 SG
REMARK 620 2 CYS A 11 SG 95.5
REMARK 620 3 HIS A 30 ND1 110.9 87.1
REMARK 620 4 CYS A 33 SG 117.6 120.1 119.6
REMARK 620 N 1 2 3
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 36 SG
REMARK 620 2 CYS A 39 SG 102.5
REMARK 620 3 CYS A 57 SG 114.9 101.7
REMARK 620 4 CYS A 60 SG 115.5 117.3 104.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 69 SG
REMARK 620 2 CYS A 72 SG 108.0
REMARK 620 3 HIS A 91 ND1 106.1 86.7
REMARK 620 4 CYS A 94 SG 117.0 116.9 117.8
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 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001003796.2 RELATED DB: TARGETDB
DBREF 2CUP A 8 95 UNP Q13642 FHL1_HUMAN 39 126
SEQADV 2CUP GLY A 1 UNP Q13642 CLONING ARTIFACT
SEQADV 2CUP SER A 2 UNP Q13642 CLONING ARTIFACT
SEQADV 2CUP SER A 3 UNP Q13642 CLONING ARTIFACT
SEQADV 2CUP GLY A 4 UNP Q13642 CLONING ARTIFACT
SEQADV 2CUP SER A 5 UNP Q13642 CLONING ARTIFACT
SEQADV 2CUP SER A 6 UNP Q13642 CLONING ARTIFACT
SEQADV 2CUP GLY A 7 UNP Q13642 CLONING ARTIFACT
SEQADV 2CUP SER A 96 UNP Q13642 CLONING ARTIFACT
SEQADV 2CUP GLY A 97 UNP Q13642 CLONING ARTIFACT
SEQADV 2CUP PRO A 98 UNP Q13642 CLONING ARTIFACT
SEQADV 2CUP SER A 99 UNP Q13642 CLONING ARTIFACT
SEQADV 2CUP SER A 100 UNP Q13642 CLONING ARTIFACT
SEQADV 2CUP GLY A 101 UNP Q13642 CLONING ARTIFACT
SEQRES 1 A 101 GLY SER SER GLY SER SER GLY CYS VAL GLU CYS ARG LYS
SEQRES 2 A 101 PRO ILE GLY ALA ASP SER LYS GLU VAL HIS TYR LYS ASN
SEQRES 3 A 101 ARG PHE TRP HIS ASP THR CYS PHE ARG CYS ALA LYS CYS
SEQRES 4 A 101 LEU HIS PRO LEU ALA ASN GLU THR PHE VAL ALA LYS ASP
SEQRES 5 A 101 ASN LYS ILE LEU CYS ASN LYS CYS THR THR ARG GLU ASP
SEQRES 6 A 101 SER PRO LYS CYS LYS GLY CYS PHE LYS ALA ILE VAL ALA
SEQRES 7 A 101 GLY ASP GLN ASN VAL GLU TYR LYS GLY THR VAL TRP HIS
SEQRES 8 A 101 LYS ASP CYS PHE SER GLY PRO SER SER GLY
HET ZN A 201 1
HET ZN A 401 1
HET ZN A 601 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 3(ZN 2+)
HELIX 1 1 CYS A 57 THR A 62 1 6
SHEET 1 A 2 GLU A 21 TYR A 24 0
SHEET 2 A 2 ARG A 27 HIS A 30 -1 O TRP A 29 N VAL A 22
SHEET 1 B 2 VAL A 49 LYS A 51 0
SHEET 2 B 2 LYS A 54 LEU A 56 -1 O LEU A 56 N VAL A 49
SHEET 1 C 2 ASN A 82 GLU A 84 0
SHEET 2 C 2 VAL A 89 HIS A 91 -1 O TRP A 90 N VAL A 83
LINK SG CYS A 8 ZN ZN A 201 1555 1555 2.37
LINK SG CYS A 11 ZN ZN A 201 1555 1555 2.32
LINK ND1 HIS A 30 ZN ZN A 201 1555 1555 2.32
LINK SG CYS A 33 ZN ZN A 201 1555 1555 2.31
LINK SG CYS A 36 ZN ZN A 401 1555 1555 2.37
LINK SG CYS A 39 ZN ZN A 401 1555 1555 2.33
LINK SG CYS A 57 ZN ZN A 401 1555 1555 2.33
LINK SG CYS A 60 ZN ZN A 401 1555 1555 2.34
LINK SG CYS A 69 ZN ZN A 601 1555 1555 2.33
LINK SG CYS A 72 ZN ZN A 601 1555 1555 2.33
LINK ND1 HIS A 91 ZN ZN A 601 1555 1555 2.34
LINK SG CYS A 94 ZN ZN A 601 1555 1555 2.34
SITE 1 AC1 4 CYS A 8 CYS A 11 HIS A 30 CYS A 33
SITE 1 AC2 4 CYS A 36 CYS A 39 CYS A 57 CYS A 60
SITE 1 AC3 4 CYS A 69 CYS A 72 HIS A 91 CYS A 94
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