Header list of 1uhp.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 09-JUL-03 1UHP TITLE SOLUTION STRUCTURE OF RSGI RUH-005, A PDZ DOMAIN IN HUMAN CDNA, TITLE 2 KIAA1095 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN KIAA1095; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PDZ DOMAIN; COMPND 5 SYNONYM: RSGI RUH-005, A PDZ DOMAIN IN HUMAN CDNA; 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: KIAA1095; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021030-36; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS PDZ DOMAIN, SEMAPHORIN CYTOPLASMIC DOMAIN ASSOCIATED PROTEIN, KEYWDS 2 STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 3 INITIATIVE, RSGI, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.HAMADA,Y.MUTO,H.HIROTA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1UHP 1 REMARK SEQADV REVDAT 2 24-FEB-09 1UHP 1 VERSN REVDAT 1 09-JAN-04 1UHP 0 JRNL AUTH T.HAMADA,Y.MUTO,H.HIROTA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF RSGI RUH-005, A PDZ DOMAIN IN HUMAN JRNL TITL 2 CDNA, KIAA1095 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 1UHP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUL-03. REMARK 100 THE DEPOSITION ID IS D_1000005839. 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 : 100MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.1MM PDZ DOMAIN U-15N,13C; 20MM REMARK 210 TRIS-HCL BUFFER (PH 7.0); 100MM REMARK 210 NACL; 0.02% NAN3; 90% H2O, 10% REMARK 210 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 21_2, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.811, 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, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY, TARGET REMARK 210 FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING 3D NMR TECHNIQUES 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 LEU A 12 O VAL A 95 1.50 REMARK 500 O GLU A 84 H THR A 88 1.51 REMARK 500 O GLN A 81 H ALA A 85 1.55 REMARK 500 O THR A 78 H ALA A 82 1.57 REMARK 500 H ILE A 67 O GLN A 96 1.57 REMARK 500 H ASN A 70 O VAL A 94 1.58 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 2 105.16 -160.75 REMARK 500 1 SER A 5 -61.16 -161.98 REMARK 500 1 SER A 18 84.46 172.11 REMARK 500 1 VAL A 32 64.06 -107.59 REMARK 500 1 ASP A 36 -53.47 -168.78 REMARK 500 1 SER A 40 153.63 63.01 REMARK 500 1 LYS A 56 -83.73 -64.78 REMARK 500 1 LEU A 60 174.25 -49.78 REMARK 500 1 ASN A 70 16.38 59.32 REMARK 500 1 ARG A 100 -178.21 -56.85 REMARK 500 1 THR A 101 154.99 -47.56 REMARK 500 1 SER A 105 164.41 57.27 REMARK 500 1 SER A 106 93.21 63.29 REMARK 500 2 SER A 3 122.68 66.78 REMARK 500 2 SER A 6 111.85 176.87 REMARK 500 2 SER A 18 77.82 70.43 REMARK 500 2 SER A 20 103.65 -170.82 REMARK 500 2 PHE A 23 -178.53 -170.48 REMARK 500 2 ASP A 33 144.72 179.16 REMARK 500 2 ASN A 34 -54.92 -121.59 REMARK 500 2 HIS A 35 -64.80 -172.67 REMARK 500 2 GLU A 41 172.01 54.75 REMARK 500 2 ASP A 50 -76.22 -60.05 REMARK 500 2 LYS A 56 -83.01 -51.15 REMARK 500 2 LEU A 60 172.44 -47.16 REMARK 500 2 ASN A 70 18.07 57.70 REMARK 500 2 ARG A 100 172.20 -48.33 REMARK 500 2 SER A 102 -49.68 -159.26 REMARK 500 3 SER A 5 111.28 58.35 REMARK 500 3 SER A 18 79.17 54.28 REMARK 500 3 SER A 20 114.70 -179.01 REMARK 500 3 PHE A 23 -174.80 -174.32 REMARK 500 3 ARG A 29 163.90 60.59 REMARK 500 3 SER A 31 -48.81 -151.77 REMARK 500 3 VAL A 32 -75.70 66.75 REMARK 500 3 ASP A 33 150.73 -41.15 REMARK 500 3 ASN A 34 113.75 73.93 REMARK 500 3 ASP A 36 146.26 -179.92 REMARK 500 3 SER A 38 -69.26 -175.31 REMARK 500 3 SER A 40 -74.77 -148.47 REMARK 500 3 LYS A 56 -83.28 -41.54 REMARK 500 3 LEU A 60 172.18 -50.26 REMARK 500 3 ILE A 62 156.52 -39.53 REMARK 500 3 ASN A 70 16.88 58.64 REMARK 500 3 ARG A 100 -172.96 -53.40 REMARK 500 3 SER A 102 89.10 57.27 REMARK 500 3 SER A 105 -62.44 -128.67 REMARK 500 3 SER A 106 166.28 66.46 REMARK 500 4 SER A 2 106.72 64.95 REMARK 500 4 ASP A 17 74.42 -105.04 REMARK 500 REMARK 500 THIS ENTRY HAS 310 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK002001069.1 RELATED DB: TARGETDB DBREF 1UHP A 8 101 UNP Q9UPQ7 PZRN3_HUMAN 278 371 SEQADV 1UHP GLY A 1 UNP Q9UPQ7 CLONING ARTIFACT SEQADV 1UHP SER A 2 UNP Q9UPQ7 CLONING ARTIFACT SEQADV 1UHP SER A 3 UNP Q9UPQ7 CLONING ARTIFACT SEQADV 1UHP GLY A 4 UNP Q9UPQ7 CLONING ARTIFACT SEQADV 1UHP SER A 5 UNP Q9UPQ7 CLONING ARTIFACT SEQADV 1UHP SER A 6 UNP Q9UPQ7 CLONING ARTIFACT SEQADV 1UHP GLY A 7 UNP Q9UPQ7 CLONING ARTIFACT SEQADV 1UHP SER A 102 UNP Q9UPQ7 CLONING ARTIFACT SEQADV 1UHP GLY A 103 UNP Q9UPQ7 CLONING ARTIFACT SEQADV 1UHP PRO A 104 UNP Q9UPQ7 CLONING ARTIFACT SEQADV 1UHP SER A 105 UNP Q9UPQ7 CLONING ARTIFACT SEQADV 1UHP SER A 106 UNP Q9UPQ7 CLONING ARTIFACT SEQADV 1UHP GLY A 107 UNP Q9UPQ7 CLONING ARTIFACT SEQRES 1 A 107 GLY SER SER GLY SER SER GLY LYS SER LEU THR LEU VAL SEQRES 2 A 107 LEU HIS ARG ASP SER GLY SER LEU GLY PHE ASN ILE ILE SEQRES 3 A 107 GLY GLY ARG PRO SER VAL ASP ASN HIS ASP GLY SER SER SEQRES 4 A 107 SER GLU GLY ILE PHE VAL SER LYS ILE VAL ASP SER GLY SEQRES 5 A 107 PRO ALA ALA LYS GLU GLY GLY LEU GLN ILE HIS ASP ARG SEQRES 6 A 107 ILE ILE GLU VAL ASN GLY ARG ASP LEU SER ARG ALA THR SEQRES 7 A 107 HIS ASP GLN ALA VAL GLU ALA PHE LYS THR ALA LYS GLU SEQRES 8 A 107 PRO ILE VAL VAL GLN VAL LEU ARG ARG THR SER GLY PRO SEQRES 9 A 107 SER SER GLY HELIX 1 1 GLY A 52 GLU A 57 1 6 HELIX 2 2 THR A 78 ALA A 89 1 12 SHEET 1 A 4 LYS A 8 LEU A 14 0 SHEET 2 A 4 ILE A 93 ARG A 99 -1 O VAL A 95 N LEU A 12 SHEET 3 A 4 ARG A 65 VAL A 69 -1 N GLU A 68 O GLN A 96 SHEET 4 A 4 ARG A 72 ASP A 73 -1 O ARG A 72 N VAL A 69 SHEET 1 B 2 PHE A 23 ILE A 26 0 SHEET 2 B 2 PHE A 44 ILE A 48 -1 O PHE A 44 N ILE A 26 CISPEP 1 GLU A 91 PRO A 92 1 0.03 CISPEP 2 GLU A 91 PRO A 92 2 -0.05 CISPEP 3 GLU A 91 PRO A 92 3 -0.02 CISPEP 4 GLU A 91 PRO A 92 4 0.02 CISPEP 5 GLU A 91 PRO A 92 5 -0.04 CISPEP 6 GLU A 91 PRO A 92 6 0.00 CISPEP 7 GLU A 91 PRO A 92 7 -0.07 CISPEP 8 GLU A 91 PRO A 92 8 -0.03 CISPEP 9 GLU A 91 PRO A 92 9 0.06 CISPEP 10 GLU A 91 PRO A 92 10 0.01 CISPEP 11 GLU A 91 PRO A 92 11 -0.03 CISPEP 12 GLU A 91 PRO A 92 12 -0.08 CISPEP 13 GLU A 91 PRO A 92 13 -0.06 CISPEP 14 GLU A 91 PRO A 92 14 -0.01 CISPEP 15 GLU A 91 PRO A 92 15 0.03 CISPEP 16 GLU A 91 PRO A 92 16 0.00 CISPEP 17 GLU A 91 PRO A 92 17 -0.01 CISPEP 18 GLU A 91 PRO A 92 18 -0.04 CISPEP 19 GLU A 91 PRO A 92 19 -0.02 CISPEP 20 GLU A 91 PRO A 92 20 0.03 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