Header list of 1ugk.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 16-JUN-03 1UGK
TITLE SOLUTION STRUCTURE OF THE FIRST C2 DOMAIN OF SYNAPTOTAGMIN IV FROM
TITLE 2 HUMAN FETAL BRAIN (KIAA1342)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNAPTOTAGMIN IV;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C2 DOMAIN;
COMPND 5 SYNONYM: KIAA1342;
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: KAZUSA CDNA FJ00418;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020924-36;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS BETA SANDWICH, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NAGASHIMA,F.HAYASHI,M.SHIROUZU,T.TERADA,T.KIGAWA,M.INOUE,T.YABUKI,
AUTHOR 2 M.AOKI,E.SEKI,T.MATSUDA,H.HIROTA,M.YOSHIDA,A.TANAKA,T.OSANAI,
AUTHOR 3 Y.MATSUO,O.OHARA,T.NAGASE,R.KIKUNO,M.NAKAYAMA,S.YOKOYAMA,RIKEN
AUTHOR 4 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1UGK 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UGK 1 VERSN
REVDAT 1 16-DEC-03 1UGK 0
JRNL AUTH T.NAGASHIMA,F.HAYASHI,M.SHIROUZU,T.TERADA,T.KIGAWA,M.INOUE,
JRNL AUTH 2 T.YABUKI,M.AOKI,E.SEKI,T.MATSUDA,H.HIROTA,M.YOSHIDA,
JRNL AUTH 3 A.TANAKA,T.OSANAI,Y.MATSUO,O.OHARA,T.NAGASE,R.KIKUNO,
JRNL AUTH 4 M.NAKAYAMA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST C2 DOMAIN OF SYNAPTOTAGMIN
JRNL TITL 2 IV FROM HUMAN FETAL BRAIN (KIAA1342)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 1.0.7
REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UGK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000005798.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.1
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.75MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM TRIS-D11; 100MM NACL; 1MM
REMARK 210 DTT; 0.1MM NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.822, CYANA 1.0.7
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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, TARGET
REMARK 210 FUNCTION
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: 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 ILE A 52 H LYS A 56 1.47
REMARK 500 OD1 ASP A 45 H LYS A 67 1.51
REMARK 500 O PRO A 83 H THR A 85 1.56
REMARK 500 O GLN A 86 H GLU A 89 1.58
REMARK 500 O TYR A 84 H ILE A 87 1.60
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 3 106.94 -163.03
REMARK 500 1 SER A 5 104.88 -178.60
REMARK 500 1 LEU A 8 76.96 45.72
REMARK 500 1 ASN A 18 68.87 -68.42
REMARK 500 1 LYS A 22 67.32 38.47
REMARK 500 1 LYS A 29 -139.62 -61.55
REMARK 500 1 GLU A 39 60.74 -107.76
REMARK 500 1 GLN A 40 -68.78 -122.17
REMARK 500 1 ASP A 45 73.67 -118.54
REMARK 500 1 GLU A 55 -61.56 -15.50
REMARK 500 1 LYS A 57 -80.85 -67.01
REMARK 500 1 HIS A 58 92.36 -51.26
REMARK 500 1 ARG A 63 147.02 -38.22
REMARK 500 1 LEU A 65 178.60 -56.31
REMARK 500 1 LYS A 67 97.23 48.56
REMARK 500 1 THR A 68 114.91 174.61
REMARK 500 1 ASP A 74 50.83 39.70
REMARK 500 1 TYR A 84 -56.15 67.34
REMARK 500 1 ALA A 91 129.02 -172.92
REMARK 500 1 ASP A 100 64.76 -165.29
REMARK 500 1 ARG A 101 -170.03 45.08
REMARK 500 1 PHE A 102 25.20 44.98
REMARK 500 1 SER A 103 83.53 40.15
REMARK 500 1 SER A 116 91.29 -64.23
REMARK 500 1 SER A 137 92.49 46.25
REMARK 500 2 SER A 3 -54.90 -156.07
REMARK 500 2 LEU A 8 -91.98 -117.85
REMARK 500 2 LYS A 22 70.27 35.38
REMARK 500 2 LYS A 29 -136.37 -61.12
REMARK 500 2 ALA A 36 157.61 -45.65
REMARK 500 2 GLU A 39 -58.21 -125.06
REMARK 500 2 MET A 42 78.08 -61.94
REMARK 500 2 ASP A 45 72.97 -118.23
REMARK 500 2 GLU A 55 -64.79 -25.62
REMARK 500 2 HIS A 58 94.40 -62.47
REMARK 500 2 LYS A 67 84.94 42.91
REMARK 500 2 THR A 68 119.77 -177.83
REMARK 500 2 ASP A 74 43.95 38.04
REMARK 500 2 TYR A 84 -57.80 67.23
REMARK 500 2 ALA A 91 124.78 -178.00
REMARK 500 2 ASP A 100 48.51 -92.37
REMARK 500 2 ARG A 101 42.18 33.77
REMARK 500 2 PHE A 102 26.19 -153.60
REMARK 500 2 SER A 103 -57.51 73.51
REMARK 500 2 ARG A 104 126.52 -36.98
REMARK 500 2 SER A 116 91.28 -68.10
REMARK 500 3 SER A 6 84.97 -155.72
REMARK 500 3 LYS A 22 69.07 37.18
REMARK 500 3 LYS A 29 -137.77 -62.21
REMARK 500 3 GLU A 39 -109.14 -93.59
REMARK 500
REMARK 500 THIS ENTRY HAS 429 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001316.1 RELATED DB: TARGETDB
DBREF 1UGK A 8 132 UNP Q9H2B2 SYT4_HUMAN 154 278
SEQADV 1UGK GLY A 1 UNP Q9H2B2 CLONING ARTIFACT
SEQADV 1UGK SER A 2 UNP Q9H2B2 CLONING ARTIFACT
SEQADV 1UGK SER A 3 UNP Q9H2B2 CLONING ARTIFACT
SEQADV 1UGK GLY A 4 UNP Q9H2B2 CLONING ARTIFACT
SEQADV 1UGK SER A 5 UNP Q9H2B2 CLONING ARTIFACT
SEQADV 1UGK SER A 6 UNP Q9H2B2 CLONING ARTIFACT
SEQADV 1UGK GLY A 7 UNP Q9H2B2 CLONING ARTIFACT
SEQADV 1UGK SER A 133 UNP Q9H2B2 CLONING ARTIFACT
SEQADV 1UGK GLY A 134 UNP Q9H2B2 CLONING ARTIFACT
SEQADV 1UGK PRO A 135 UNP Q9H2B2 CLONING ARTIFACT
SEQADV 1UGK SER A 136 UNP Q9H2B2 CLONING ARTIFACT
SEQADV 1UGK SER A 137 UNP Q9H2B2 CLONING ARTIFACT
SEQADV 1UGK GLY A 138 UNP Q9H2B2 CLONING ARTIFACT
SEQRES 1 A 138 GLY SER SER GLY SER SER GLY LEU GLY THR LEU PHE PHE
SEQRES 2 A 138 SER LEU GLU TYR ASN PHE GLU ARG LYS ALA PHE VAL VAL
SEQRES 3 A 138 ASN ILE LYS GLU ALA ARG GLY LEU PRO ALA MET ASP GLU
SEQRES 4 A 138 GLN SER MET THR SER ASP PRO TYR ILE LYS MET THR ILE
SEQRES 5 A 138 LEU PRO GLU LYS LYS HIS LYS VAL LYS THR ARG VAL LEU
SEQRES 6 A 138 ARG LYS THR LEU ASP PRO ALA PHE ASP GLU THR PHE THR
SEQRES 7 A 138 PHE TYR GLY ILE PRO TYR THR GLN ILE GLN GLU LEU ALA
SEQRES 8 A 138 LEU HIS PHE THR ILE LEU SER PHE ASP ARG PHE SER ARG
SEQRES 9 A 138 ASP ASP ILE ILE GLY GLU VAL LEU ILE PRO LEU SER GLY
SEQRES 10 A 138 ILE GLU LEU SER GLU GLY LYS MET LEU MET ASN ARG GLU
SEQRES 11 A 138 ILE ILE SER GLY PRO SER SER GLY
HELIX 1 1 PHE A 19 ARG A 21 5 3
HELIX 2 2 GLN A 86 GLU A 89 5 4
SHEET 1 A 4 ALA A 72 TYR A 80 0
SHEET 2 A 4 ALA A 23 ARG A 32 -1 N PHE A 24 O PHE A 79
SHEET 3 A 4 THR A 10 ASN A 18 -1 N THR A 10 O ARG A 32
SHEET 4 A 4 MET A 125 GLU A 130 -1 O MET A 127 N PHE A 13
SHEET 1 B 4 LYS A 59 LYS A 61 0
SHEET 2 B 4 ASP A 45 LEU A 53 -1 N MET A 50 O VAL A 60
SHEET 3 B 4 ALA A 91 PHE A 99 -1 O ALA A 91 N LEU A 53
SHEET 4 B 4 GLY A 109 PRO A 114 -1 O ILE A 113 N LEU A 92
CISPEP 1 LEU A 53 PRO A 54 1 0.00
CISPEP 2 LEU A 53 PRO A 54 2 0.01
CISPEP 3 LEU A 53 PRO A 54 3 -0.01
CISPEP 4 LEU A 53 PRO A 54 4 0.05
CISPEP 5 LEU A 53 PRO A 54 5 0.01
CISPEP 6 LEU A 53 PRO A 54 6 0.00
CISPEP 7 LEU A 53 PRO A 54 7 0.01
CISPEP 8 LEU A 53 PRO A 54 8 -0.06
CISPEP 9 LEU A 53 PRO A 54 9 -0.08
CISPEP 10 LEU A 53 PRO A 54 10 0.06
CISPEP 11 LEU A 53 PRO A 54 11 0.03
CISPEP 12 LEU A 53 PRO A 54 12 0.04
CISPEP 13 LEU A 53 PRO A 54 13 -0.05
CISPEP 14 LEU A 53 PRO A 54 14 0.03
CISPEP 15 LEU A 53 PRO A 54 15 -0.06
CISPEP 16 LEU A 53 PRO A 54 16 0.03
CISPEP 17 LEU A 53 PRO A 54 17 0.04
CISPEP 18 LEU A 53 PRO A 54 18 -0.04
CISPEP 19 LEU A 53 PRO A 54 19 -0.07
CISPEP 20 LEU A 53 PRO A 54 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