Header list of 1x50.pdb file
Complete list - r 2 2 Bytes
HEADER SUGAR BINDING PROTEIN 15-MAY-05 1X50
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL GAL-BIND LECTIN DOMAIN FROM HUMAN
TITLE 2 GALECTIN-4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GALECTIN-4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GAL-BINDING_LECTIN DOMAIN;
COMPND 5 SYNONYM: LACTOSE-BINDING LECTIN 4, L-36 LACTOSE BINDING PROTEIN,
COMPND 6 L36LBP, ANTIGEN NY-CO-27;
COMPND 7 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: LGALS4;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040607-12;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS GAL-BIND LECTIN, GALECTIN, SUGAR BINDING, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 SUGAR BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,K.SAITO,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X50 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X50 1 VERSN
REVDAT 1 15-NOV-05 1X50 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,K.SAITO,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL GAL-BIND LECTIN DOMAIN
JRNL TITL 2 FROM HUMAN GALECTIN-4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X50 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024386.
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 : 2.20MM GAL-BINDING LECTIN U-15N,
REMARK 210 13C; 20MM D-TRIS-HCL; 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 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 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR 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 LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 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 PRO A 15 -176.57 -69.72
REMARK 500 1 MET A 17 43.53 -98.76
REMARK 500 1 SER A 64 -71.54 -68.50
REMARK 500 1 SER A 65 -71.34 -83.70
REMARK 500 1 ASN A 88 102.14 -41.10
REMARK 500 1 LYS A 97 105.87 -171.89
REMARK 500 1 PHE A 103 108.65 -35.33
REMARK 500 1 ARG A 119 -178.20 -173.50
REMARK 500 1 HIS A 128 95.71 -57.79
REMARK 500 1 HIS A 134 98.80 -62.40
REMARK 500 1 VAL A 142 104.72 -50.30
REMARK 500 2 PRO A 15 -164.91 -69.77
REMARK 500 2 PRO A 21 -175.37 -69.74
REMARK 500 2 LEU A 37 107.14 -54.81
REMARK 500 2 TYR A 48 117.04 -170.20
REMARK 500 2 SER A 64 -72.86 -66.47
REMARK 500 2 SER A 65 -74.68 -79.34
REMARK 500 2 ASN A 88 101.67 -38.28
REMARK 500 2 LYS A 97 105.95 -171.54
REMARK 500 2 PHE A 103 108.41 -41.01
REMARK 500 2 VAL A 142 106.93 -41.24
REMARK 500 3 SER A 3 107.08 -174.16
REMARK 500 3 HIS A 8 81.55 -59.51
REMARK 500 3 MET A 17 31.05 -96.86
REMARK 500 3 PRO A 26 -176.93 -69.69
REMARK 500 3 LEU A 37 100.00 -52.43
REMARK 500 3 LYS A 54 -64.56 -133.75
REMARK 500 3 SER A 64 -71.81 -67.15
REMARK 500 3 ASN A 88 101.59 -38.42
REMARK 500 3 LYS A 97 108.37 -175.79
REMARK 500 3 HIS A 128 101.53 -51.58
REMARK 500 3 VAL A 142 104.35 -46.52
REMARK 500 4 ASN A 12 -64.28 -108.59
REMARK 500 4 PRO A 15 -163.67 -69.78
REMARK 500 4 PRO A 21 -179.62 -69.80
REMARK 500 4 LEU A 37 106.48 -50.85
REMARK 500 4 ARG A 40 43.61 -105.03
REMARK 500 4 SER A 64 -75.26 -70.22
REMARK 500 4 SER A 65 -71.93 -77.64
REMARK 500 4 ASN A 88 102.23 -41.08
REMARK 500 4 LYS A 97 106.52 -170.58
REMARK 500 4 PHE A 103 109.72 -41.51
REMARK 500 4 HIS A 128 101.43 -55.46
REMARK 500 4 HIS A 134 104.62 -58.72
REMARK 500 4 VAL A 142 102.92 -49.23
REMARK 500 5 LEU A 14 155.95 -38.54
REMARK 500 5 PRO A 15 -170.70 -69.78
REMARK 500 5 PRO A 26 -178.43 -69.76
REMARK 500 5 GLN A 34 99.74 -64.83
REMARK 500 5 SER A 64 -72.33 -62.26
REMARK 500
REMARK 500 THIS ENTRY HAS 286 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001002278.1 RELATED DB: TARGETDB
DBREF 1X50 A 8 158 UNP P56470 LEG4_HUMAN 173 323
SEQADV 1X50 GLY A 1 UNP P56470 CLONING ARTIFACT
SEQADV 1X50 SER A 2 UNP P56470 CLONING ARTIFACT
SEQADV 1X50 SER A 3 UNP P56470 CLONING ARTIFACT
SEQADV 1X50 GLY A 4 UNP P56470 CLONING ARTIFACT
SEQADV 1X50 SER A 5 UNP P56470 CLONING ARTIFACT
SEQADV 1X50 SER A 6 UNP P56470 CLONING ARTIFACT
SEQADV 1X50 GLY A 7 UNP P56470 CLONING ARTIFACT
SEQADV 1X50 SER A 159 UNP P56470 CLONING ARTIFACT
SEQADV 1X50 GLY A 160 UNP P56470 CLONING ARTIFACT
SEQADV 1X50 PRO A 161 UNP P56470 CLONING ARTIFACT
SEQADV 1X50 SER A 162 UNP P56470 CLONING ARTIFACT
SEQADV 1X50 SER A 163 UNP P56470 CLONING ARTIFACT
SEQADV 1X50 GLY A 164 UNP P56470 CLONING ARTIFACT
SEQRES 1 A 164 GLY SER SER GLY SER SER GLY HIS GLN GLN LEU ASN SER
SEQRES 2 A 164 LEU PRO THR MET GLU GLY PRO PRO THR PHE ASN PRO PRO
SEQRES 3 A 164 VAL PRO TYR PHE GLY ARG LEU GLN GLY GLY LEU THR ALA
SEQRES 4 A 164 ARG ARG THR ILE ILE ILE LYS GLY TYR VAL PRO PRO THR
SEQRES 5 A 164 GLY LYS SER PHE ALA ILE ASN PHE LYS VAL GLY SER SER
SEQRES 6 A 164 GLY ASP ILE ALA LEU HIS ILE ASN PRO ARG MET GLY ASN
SEQRES 7 A 164 GLY THR VAL VAL ARG ASN SER LEU LEU ASN GLY SER TRP
SEQRES 8 A 164 GLY SER GLU GLU LYS LYS ILE THR HIS ASN PRO PHE GLY
SEQRES 9 A 164 PRO GLY GLN PHE PHE ASP LEU SER ILE ARG CYS GLY LEU
SEQRES 10 A 164 ASP ARG PHE LYS VAL TYR ALA ASN GLY GLN HIS LEU PHE
SEQRES 11 A 164 ASP PHE ALA HIS ARG LEU SER ALA PHE GLN ARG VAL ASP
SEQRES 12 A 164 THR LEU GLU ILE GLN GLY ASP VAL THR LEU SER TYR VAL
SEQRES 13 A 164 GLN ILE SER GLY PRO SER SER GLY
HELIX 1 1 ALA A 138 VAL A 142 5 5
SHEET 1 A 6 THR A 22 PHE A 23 0
SHEET 2 A 6 THR A 152 SER A 159 -1 O VAL A 156 N THR A 22
SHEET 3 A 6 ARG A 41 TYR A 48 -1 N LYS A 46 O SER A 154
SHEET 4 A 6 PHE A 108 CYS A 115 -1 O LEU A 111 N ILE A 45
SHEET 5 A 6 ARG A 119 ALA A 124 -1 O TYR A 123 N SER A 112
SHEET 6 A 6 HIS A 128 ALA A 133 -1 O PHE A 130 N VAL A 122
SHEET 1 B 6 TYR A 29 ARG A 32 0
SHEET 2 B 6 THR A 144 GLY A 149 -1 O LEU A 145 N GLY A 31
SHEET 3 B 6 PHE A 56 LYS A 61 -1 N ASN A 59 O GLU A 146
SHEET 4 B 6 LEU A 70 ASN A 73 -1 O ILE A 72 N ILE A 58
SHEET 5 B 6 VAL A 82 ASN A 84 -1 O ASN A 84 N HIS A 71
SHEET 6 B 6 GLU A 95 LYS A 96 -1 O GLU A 95 N ARG A 83
SHEET 1 C 2 LEU A 86 LEU A 87 0
SHEET 2 C 2 SER A 90 TRP A 91 -1 O SER A 90 N LEU A 87
CISPEP 1 VAL A 27 PRO A 28 1 -0.08
CISPEP 2 VAL A 27 PRO A 28 2 -0.07
CISPEP 3 VAL A 27 PRO A 28 3 0.01
CISPEP 4 VAL A 27 PRO A 28 4 -0.08
CISPEP 5 VAL A 27 PRO A 28 5 0.01
CISPEP 6 VAL A 27 PRO A 28 6 -0.11
CISPEP 7 VAL A 27 PRO A 28 7 -0.02
CISPEP 8 VAL A 27 PRO A 28 8 -0.03
CISPEP 9 VAL A 27 PRO A 28 9 -0.07
CISPEP 10 VAL A 27 PRO A 28 10 -0.14
CISPEP 11 VAL A 27 PRO A 28 11 -0.06
CISPEP 12 VAL A 27 PRO A 28 12 -0.08
CISPEP 13 VAL A 27 PRO A 28 13 -0.03
CISPEP 14 VAL A 27 PRO A 28 14 -0.05
CISPEP 15 VAL A 27 PRO A 28 15 -0.07
CISPEP 16 VAL A 27 PRO A 28 16 -0.03
CISPEP 17 VAL A 27 PRO A 28 17 -0.06
CISPEP 18 VAL A 27 PRO A 28 18 -0.06
CISPEP 19 VAL A 27 PRO A 28 19 -0.09
CISPEP 20 VAL A 27 PRO A 28 20 -0.02
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