Header list of 1rjh.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 19-NOV-03 1RJH
TITLE STRUCTURE OF THE CALCIUM FREE FORM OF THE C-TYPE LECTIN-LIKE DOMAIN OF
TITLE 2 TETRANECTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TETRANECTIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TN, PLASMINOGEN-KRINGLE 4 BINDING PROTEIN;
COMPND 5 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: TNA;
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: PT7H6FXATN3
KEYWDS APO, CALCIUM FREE, CTLD, C-TYPE LECTIN-LIKE DOMAIN, PLASMINOGEN
KEYWDS 2 KRINGLE 4 BINDING, TETRANECTIN, TRANS PROLINE, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.NIELBO,J.K.THOMSEN,J.H.GRAVERSEN,M.ETZERODT,F.M.POULSEN,
AUTHOR 2 H.C.THOEGERSEN
REVDAT 3 02-MAR-22 1RJH 1 REMARK
REVDAT 2 24-FEB-09 1RJH 1 VERSN
REVDAT 1 20-JUL-04 1RJH 0
JRNL AUTH S.NIELBO,J.K.THOMSEN,J.H.GRAVERSEN,P.H.JENSEN,M.ETZERODT,
JRNL AUTH 2 F.M.POULSEN,H.C.THOEGERSEN
JRNL TITL STRUCTURE OF THE PLASMINOGEN KRINGLE 4 BINDING CALCIUM-FREE
JRNL TITL 2 FORM OF THE C-TYPE LECTIN-LIKE DOMAIN OF TETRANECTIN.
JRNL REF BIOCHEMISTRY V. 43 8636 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15236571
JRNL DOI 10.1021/BI049570S
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, CNS 1.1
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON 1552 NOE
REMARK 3 -DERIVED DISTANCE RESTRAINTS AND 194 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1RJH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020803.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 1 MM NAN3, 2 MM EDTA
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.6 MM U-15N-13C;
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 : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1, PRONTO 20020313, X
REMARK 210 -PLOR 98.1, CYANA 1.0.6, CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING PROTOCOL
REMARK 210 WITH AN EXPLICIT LAYER OF WATER
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD SPECTRA FROM
REMARK 210 THE VARIAN PROTEIN NMR PACK.
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 OE1 GLU A 109 HZ2 LYS A 166 1.57
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 SER A 103 -55.78 -153.95
REMARK 500 1 GLU A 107 36.95 -94.77
REMARK 500 1 ASP A 116 39.54 -87.52
REMARK 500 1 MET A 117 -135.84 -77.95
REMARK 500 1 ALA A 118 43.84 -81.61
REMARK 500 1 ASN A 160 -41.56 -176.65
REMARK 500 1 ILE A 180 -49.06 -145.09
REMARK 500 2 SER A 103 -57.54 -138.78
REMARK 500 2 THR A 138 34.60 -94.25
REMARK 500 2 LYS A 148 98.91 -67.41
REMARK 500 2 CYS A 152 143.90 83.37
REMARK 500 2 ASN A 160 -34.35 -174.51
REMARK 500 2 PRO A 173 -178.50 -62.58
REMARK 500 3 SER A 103 -64.60 -151.69
REMARK 500 3 ASN A 106 -62.66 172.98
REMARK 500 3 GLU A 107 37.46 -86.30
REMARK 500 3 MET A 117 -162.10 -126.18
REMARK 500 3 CYS A 152 110.80 78.79
REMARK 500 3 ALA A 159 -63.99 -90.75
REMARK 500 3 ASN A 160 -19.92 -177.72
REMARK 500 3 PRO A 173 -177.92 -63.11
REMARK 500 4 SER A 103 -46.66 -149.42
REMARK 500 4 ASN A 160 -25.76 -169.68
REMARK 500 4 LYS A 166 -152.68 -153.69
REMARK 500 4 PRO A 173 -177.68 -67.01
REMARK 500 4 ILE A 180 111.66 -164.82
REMARK 500 5 SER A 85 109.94 -54.09
REMARK 500 5 SER A 103 -54.61 -153.63
REMARK 500 5 THR A 141 -74.98 -110.79
REMARK 500 5 ASP A 145 -56.34 -145.62
REMARK 500 5 LYS A 148 99.44 -62.90
REMARK 500 5 ASN A 160 -29.35 175.61
REMARK 500 5 PHE A 164 -168.01 -127.55
REMARK 500 5 PRO A 173 -178.98 -67.26
REMARK 500 5 ILE A 180 -70.89 -107.04
REMARK 500 6 SER A 103 -62.98 -152.07
REMARK 500 6 ASN A 106 -57.46 173.80
REMARK 500 6 GLU A 107 39.65 -85.81
REMARK 500 6 THR A 138 39.56 -84.06
REMARK 500 6 CYS A 152 100.13 70.94
REMARK 500 6 ASN A 160 -27.67 -177.78
REMARK 500 6 ILE A 180 -24.83 63.15
REMARK 500 7 SER A 103 -58.92 -154.87
REMARK 500 7 ALA A 118 -65.23 -107.49
REMARK 500 7 ALA A 119 50.71 -166.18
REMARK 500 7 ASN A 160 -40.99 178.82
REMARK 500 8 SER A 103 -59.52 -153.18
REMARK 500 8 ASN A 106 -54.69 175.29
REMARK 500 8 GLU A 107 36.48 -78.91
REMARK 500 8 ALA A 119 63.30 65.70
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TN3 RELATED DB: PDB
REMARK 900 XRAY STRUCTURE OF THE C-TYPE LECTIN-LIKE DOMAIN OF HUMAN
REMARK 900 TETRANECTIN (TN3) WITH TWO CALCIUM IONS BOUND.
REMARK 900 RELATED ID: 1HTN RELATED DB: PDB
REMARK 900 XRAY STRUCTURE OF FULL LENGTH TETRANECTIN (TN) WITH TWO CALCIUM
REMARK 900 IONS BOUND IN THE C-TYPE LECTIN-LIKE DOMAIN.
DBREF 1RJH A 64 181 UNP P05452 TETN_HUMAN 85 202
SEQRES 1 A 118 PHE THR GLN THR LYS THR PHE HIS GLU ALA SER GLU ASP
SEQRES 2 A 118 CYS ILE SER ARG GLY GLY THR LEU SER THR PRO GLN THR
SEQRES 3 A 118 GLY SER GLU ASN ASP ALA LEU TYR GLU TYR LEU ARG GLN
SEQRES 4 A 118 SER VAL GLY ASN GLU ALA GLU ILE TRP LEU GLY LEU ASN
SEQRES 5 A 118 ASP MET ALA ALA GLU GLY THR TRP VAL ASP MET THR GLY
SEQRES 6 A 118 ALA ARG ILE ALA TYR LYS ASN TRP GLU THR GLU ILE THR
SEQRES 7 A 118 ALA GLN PRO ASP GLY GLY LYS THR GLU ASN CYS ALA VAL
SEQRES 8 A 118 LEU SER GLY ALA ALA ASN GLY LYS TRP PHE ASP LYS ARG
SEQRES 9 A 118 CYS ARG ASP GLN LEU PRO TYR ILE CYS GLN PHE GLY ILE
SEQRES 10 A 118 VAL
HELIX 1 1 THR A 69 ARG A 80 1 12
HELIX 2 2 THR A 89 GLN A 102 1 14
SHEET 1 A 2 GLY A 82 LEU A 84 0
SHEET 2 A 2 CYS A 176 PHE A 178 -1 O GLN A 177 N THR A 83
SHEET 1 B 3 GLU A 109 TRP A 111 0
SHEET 2 B 3 ALA A 153 SER A 156 -1 O LEU A 155 N ILE A 110
SHEET 3 B 3 TRP A 163 ASP A 165 -1 O PHE A 164 N VAL A 154
SHEET 1 C 2 LEU A 114 ASN A 115 0
SHEET 2 C 2 VAL A 124 ASP A 125 -1 O VAL A 124 N ASN A 115
SSBOND 1 CYS A 77 CYS A 176 1555 1555 2.03
SSBOND 2 CYS A 152 CYS A 168 1555 1555 2.03
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 2 2 Bytes