Header list of 1um7.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 24-SEP-03 1UM7 TITLE SOLUTION STRUCTURE OF THE THIRD PDZ DOMAIN OF SYNAPSE-ASSOCIATED TITLE 2 PROTEIN 102 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SYNAPSE-ASSOCIATED PROTEIN 102; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PDZ DOMAIN; COMPND 5 SYNONYM: KIAA1232 PROTEIN; 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 KIAA1232; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021030-42; SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS KEYWDS PDZ, DISCS LARGE HOMOLOG 3, DLG3-HUMAN PRESYNAPTIC PROTEIN, RIKEN KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL KEYWDS 3 GENOMICS, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR X.-R.QIN,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1UM7 1 REMARK SEQADV REVDAT 2 24-FEB-09 1UM7 1 VERSN REVDAT 1 24-MAR-04 1UM7 0 JRNL AUTH X.-R.QIN,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE THIRD PDZ DOMAIN OF JRNL TITL 2 SYNAPSE-ASSOCIATED PROTEIN 102 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 1UM7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-SEP-03. REMARK 100 THE DEPOSITION ID IS D_1000005981. 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 : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.05MM 13C, 15N-LABELED PROTEIN; REMARK 210 20MM PHOSPHATE BUFFER; 100MM REMARK 210 NACL; 1MM D10-DTT; 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 : 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 0.854 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 H ASN A 68 O THR A 92 1.50 REMARK 500 O GLU A 78 H ALA A 82 1.56 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 ASP A 12 83.24 40.32 REMARK 500 1 ALA A 13 59.66 -94.98 REMARK 500 1 GLU A 15 173.85 -55.45 REMARK 500 1 SER A 25 -64.28 177.18 REMARK 500 1 GLU A 57 -65.70 -130.09 REMARK 500 1 ASN A 68 -56.01 79.47 REMARK 500 1 ALA A 87 -142.37 -65.84 REMARK 500 1 TYR A 97 95.15 -52.13 REMARK 500 1 SER A 108 137.85 63.48 REMARK 500 1 SER A 111 79.01 -179.04 REMARK 500 2 SER A 2 98.14 -179.55 REMARK 500 2 SER A 5 -60.36 -142.50 REMARK 500 2 SER A 6 97.55 54.49 REMARK 500 2 ALA A 13 76.69 69.75 REMARK 500 2 SER A 25 -60.46 -173.19 REMARK 500 2 ASP A 37 27.10 45.94 REMARK 500 2 GLU A 57 -75.25 -97.00 REMARK 500 2 ASP A 62 166.68 -47.63 REMARK 500 2 ALA A 87 -142.31 -65.79 REMARK 500 2 TYR A 97 96.84 -58.42 REMARK 500 2 SER A 107 -60.95 -95.79 REMARK 500 2 SER A 108 151.02 67.66 REMARK 500 2 SER A 111 82.02 -169.12 REMARK 500 2 SER A 112 132.67 63.31 REMARK 500 3 LYS A 23 111.90 -39.98 REMARK 500 3 SER A 25 -38.82 -175.81 REMARK 500 3 PHE A 45 165.33 178.77 REMARK 500 3 ASP A 62 153.24 -42.53 REMARK 500 3 ASN A 68 19.43 52.28 REMARK 500 3 ALA A 87 -141.10 -69.05 REMARK 500 3 TYR A 97 97.08 -56.53 REMARK 500 3 SER A 111 165.81 178.14 REMARK 500 4 SER A 5 160.74 -40.63 REMARK 500 4 ARG A 14 -44.42 -131.10 REMARK 500 4 LYS A 23 118.56 -39.73 REMARK 500 4 SER A 25 -59.49 -176.66 REMARK 500 4 GLU A 57 -74.36 -75.51 REMARK 500 4 ASP A 62 173.96 -48.19 REMARK 500 4 ASN A 68 29.15 39.63 REMARK 500 4 ALA A 87 -142.27 -66.05 REMARK 500 4 TYR A 97 93.78 -60.78 REMARK 500 4 SER A 111 84.84 64.79 REMARK 500 5 SER A 2 157.32 60.65 REMARK 500 5 SER A 5 171.83 67.91 REMARK 500 5 ALA A 13 85.60 61.18 REMARK 500 5 ARG A 14 -44.83 -134.43 REMARK 500 5 LYS A 23 101.54 -38.27 REMARK 500 5 THR A 26 23.21 47.51 REMARK 500 5 PHE A 30 148.24 -170.23 REMARK 500 5 PHE A 45 166.56 177.93 REMARK 500 REMARK 500 THIS ENTRY HAS 236 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK002001206.1 RELATED DB: TARGETDB DBREF 1UM7 A 8 107 UNP Q92796 DLG3_HUMAN 47 146 SEQADV 1UM7 GLY A 1 UNP Q92796 CLONING ARTIFACT SEQADV 1UM7 SER A 2 UNP Q92796 CLONING ARTIFACT SEQADV 1UM7 SER A 3 UNP Q92796 CLONING ARTIFACT SEQADV 1UM7 GLY A 4 UNP Q92796 CLONING ARTIFACT SEQADV 1UM7 SER A 5 UNP Q92796 CLONING ARTIFACT SEQADV 1UM7 SER A 6 UNP Q92796 CLONING ARTIFACT SEQADV 1UM7 GLY A 7 UNP Q92796 CLONING ARTIFACT SEQADV 1UM7 SER A 108 UNP Q92796 CLONING ARTIFACT SEQADV 1UM7 GLY A 109 UNP Q92796 CLONING ARTIFACT SEQADV 1UM7 PRO A 110 UNP Q92796 CLONING ARTIFACT SEQADV 1UM7 SER A 111 UNP Q92796 CLONING ARTIFACT SEQADV 1UM7 SER A 112 UNP Q92796 CLONING ARTIFACT SEQADV 1UM7 GLY A 113 UNP Q92796 CLONING ARTIFACT SEQRES 1 A 113 GLY SER SER GLY SER SER GLY ARG PRO GLY GLY ASP ALA SEQRES 2 A 113 ARG GLU PRO ARG LYS ILE ILE LEU HIS LYS GLY SER THR SEQRES 3 A 113 GLY LEU GLY PHE ASN ILE VAL GLY GLY GLU ASP GLY GLU SEQRES 4 A 113 GLY ILE PHE VAL SER PHE ILE LEU ALA GLY GLY PRO ALA SEQRES 5 A 113 ASP LEU SER GLY GLU LEU ARG ARG GLY ASP ARG ILE LEU SEQRES 6 A 113 SER VAL ASN GLY VAL ASN LEU ARG ASN ALA THR HIS GLU SEQRES 7 A 113 GLN ALA ALA ALA ALA LEU LYS ARG ALA GLY GLN SER VAL SEQRES 8 A 113 THR ILE VAL ALA GLN TYR ARG PRO GLU GLU TYR SER ARG SEQRES 9 A 113 PHE GLU SER SER GLY PRO SER SER GLY HELIX 1 1 GLY A 50 SER A 55 1 6 HELIX 2 2 THR A 76 ARG A 86 1 11 HELIX 3 3 ARG A 98 SER A 108 1 11 SHEET 1 A 3 PRO A 16 HIS A 22 0 SHEET 2 A 3 SER A 90 GLN A 96 -1 O ALA A 95 N ARG A 17 SHEET 3 A 3 ARG A 63 VAL A 67 -1 N SER A 66 O VAL 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 2 2 Bytes