Header list of 1uhf.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 03-JUL-03 1UHF
TITLE SOLUTION STRUCTURE OF THE THIRD SH3 DOMAIN OF HUMAN INTERSECTIN
TITLE 2 2(KIAA1256)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERSECTIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: SH3 DOMAIN-CONTAINING PROTEIN 1B, SH3P18, SH3P18-LIKE WASP
COMPND 6 ASSOCIATED PROTEIN;
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 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P021015-61;
SOURCE 7 OTHER_DETAILS: IN VITRO TRANSLATION
KEYWDS BETA BARREL, SH3 DOMAIN, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 2 INITIATIVE, RSGI, STRUCTURAL GENOMICS, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.SUZUKI,H.HATANAKA,S.KOSHIBA,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1UHF 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UHF 1 VERSN
REVDAT 1 10-AUG-04 1UHF 0
JRNL AUTH S.SUZUKI,H.HATANAKA,S.KOSHIBA,M.INOUE,T.KIGAWA,T.TERADA,
JRNL AUTH 2 M.SHIROUZU,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE THIRD SH3 DOMAIN OF HUMAN
JRNL TITL 2 INTERSECTIN 2(KIAA1256)
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 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UHF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000005829.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 0.12
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 6.6MM 13C/15N SH3 DOMAIN, 20MM
REMARK 210 PHOSPHATE BUFFER NA, 100MM NACL,
REMARK 210 0.02% NAN3
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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.771, OLIVIA 1.9.5,
REMARK 210 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 : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 GLN A 37 H THR A 44 1.54
REMARK 500 H GLU A 9 O VAL A 35 1.54
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 2 166.76 61.70
REMARK 500 1 THR A 36 -45.08 -135.85
REMARK 500 1 ASP A 49 28.95 -161.76
REMARK 500 1 LYS A 62 99.51 -56.26
REMARK 500 2 SER A 2 90.46 42.30
REMARK 500 2 SER A 5 94.10 47.83
REMARK 500 2 ASP A 49 21.36 -149.78
REMARK 500 2 LYS A 62 98.10 -54.85
REMARK 500 2 SER A 64 -65.04 72.31
REMARK 500 2 SER A 68 79.84 63.95
REMARK 500 3 SER A 3 125.06 -171.22
REMARK 500 3 SER A 6 110.41 -165.04
REMARK 500 3 ASP A 49 23.86 -152.53
REMARK 500 3 LYS A 62 97.42 -53.45
REMARK 500 3 ASP A 63 102.09 58.54
REMARK 500 3 SER A 67 96.88 -63.06
REMARK 500 3 SER A 68 82.90 51.63
REMARK 500 4 ASP A 49 25.67 -156.27
REMARK 500 4 LYS A 62 97.67 -51.90
REMARK 500 4 SER A 64 164.94 58.78
REMARK 500 4 SER A 68 68.47 60.09
REMARK 500 5 SER A 2 -58.35 -123.94
REMARK 500 5 SER A 3 82.13 54.92
REMARK 500 5 GLU A 31 160.25 -49.27
REMARK 500 5 THR A 36 -44.93 -132.42
REMARK 500 5 ASP A 49 30.19 -163.82
REMARK 500 5 ASN A 57 -45.47 -142.85
REMARK 500 5 TYR A 58 40.48 -85.54
REMARK 500 5 LYS A 62 98.16 -55.08
REMARK 500 5 ASP A 63 107.92 69.44
REMARK 500 5 SER A 64 117.17 -175.92
REMARK 500 6 SER A 5 90.93 -168.51
REMARK 500 6 ASP A 49 26.90 -157.95
REMARK 500 6 LYS A 62 96.46 -50.09
REMARK 500 6 SER A 67 84.62 -150.37
REMARK 500 6 SER A 68 -58.03 -130.92
REMARK 500 7 SER A 6 102.92 59.69
REMARK 500 7 LEU A 25 106.12 -53.48
REMARK 500 7 THR A 36 -44.23 -133.10
REMARK 500 7 ASP A 49 23.79 85.34
REMARK 500 7 LYS A 62 97.51 -51.90
REMARK 500 8 SER A 2 -59.12 74.68
REMARK 500 8 SER A 5 88.91 43.99
REMARK 500 8 SER A 6 -55.02 -144.36
REMARK 500 8 ASP A 49 19.02 -143.16
REMARK 500 8 ASN A 57 -45.69 -141.36
REMARK 500 8 TYR A 58 40.70 -85.84
REMARK 500 8 LYS A 62 97.94 -53.69
REMARK 500 8 ASP A 63 -51.69 -128.17
REMARK 500 8 SER A 68 100.91 54.88
REMARK 500
REMARK 500 THIS ENTRY HAS 121 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002001230.5 RELATED DB: TARGETDB
DBREF 1UHF A 8 63 UNP Q9NZM3 ITSN2_HUMAN 982 1037
SEQADV 1UHF GLY A 1 UNP Q9NZM3 CLONING ARTIFACT
SEQADV 1UHF SER A 2 UNP Q9NZM3 CLONING ARTIFACT
SEQADV 1UHF SER A 3 UNP Q9NZM3 CLONING ARTIFACT
SEQADV 1UHF GLY A 4 UNP Q9NZM3 CLONING ARTIFACT
SEQADV 1UHF SER A 5 UNP Q9NZM3 CLONING ARTIFACT
SEQADV 1UHF SER A 6 UNP Q9NZM3 CLONING ARTIFACT
SEQADV 1UHF GLY A 7 UNP Q9NZM3 CLONING ARTIFACT
SEQADV 1UHF SER A 64 UNP Q9NZM3 CLONING ARTIFACT
SEQADV 1UHF GLY A 65 UNP Q9NZM3 CLONING ARTIFACT
SEQADV 1UHF PRO A 66 UNP Q9NZM3 CLONING ARTIFACT
SEQADV 1UHF SER A 67 UNP Q9NZM3 CLONING ARTIFACT
SEQADV 1UHF SER A 68 UNP Q9NZM3 CLONING ARTIFACT
SEQADV 1UHF GLY A 69 UNP Q9NZM3 CLONING ARTIFACT
SEQRES 1 A 69 GLY SER SER GLY SER SER GLY GLY GLU GLU TYR ILE ALA
SEQRES 2 A 69 LEU TYR PRO TYR SER SER VAL GLU PRO GLY ASP LEU THR
SEQRES 3 A 69 PHE THR GLU GLY GLU GLU ILE LEU VAL THR GLN LYS ASP
SEQRES 4 A 69 GLY GLU TRP TRP THR GLY SER ILE GLY ASP ARG SER GLY
SEQRES 5 A 69 ILE PHE PRO SER ASN TYR VAL LYS PRO LYS ASP SER GLY
SEQRES 6 A 69 PRO SER SER GLY
HELIX 1 1 PRO A 55 VAL A 59 5 5
SHEET 1 A 3 GLU A 32 VAL A 35 0
SHEET 2 A 3 GLU A 9 ILE A 12 -1 N GLU A 9 O VAL A 35
SHEET 3 A 3 LYS A 60 PRO A 61 -1 O LYS A 60 N ILE A 12
SHEET 1 B 3 GLN A 37 ASP A 39 0
SHEET 2 B 3 TRP A 42 GLY A 45 -1 O THR A 44 N GLN A 37
SHEET 3 B 3 GLY A 52 PHE A 54 -1 O PHE A 54 N TRP A 43
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