Header list of 1x52.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 15-MAY-05 1X52 TITLE SOLUTION STRUCTURES OF THE C-TERMINAL DOMAIN OF THE HUMAN PELOTA TITLE 2 HOMOLOG (CGI-17) COMPND MOL_ID: 1; COMPND 2 MOLECULE: PELOTA HOMOLOG; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ERF1_3 DOMAIN; COMPND 5 SYNONYM: CGI-17; 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: PELO; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040830-12; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS ERF1_3 DOMAIN, PELO, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.NAMEKI,M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1X52 1 REMARK SEQADV REVDAT 2 24-FEB-09 1X52 1 VERSN REVDAT 1 15-NOV-05 1X52 0 JRNL AUTH N.NAMEKI,M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURES OF THE C-TERMINAL DOMAIN OF THE HUMAN JRNL TITL 2 PELOTA HOMOLOG (CGI-17) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, OPALP 1.2 REMARK 3 AUTHORS : BRUKER (XWINNMR), KORADI, R., BILLETER, M., REMARK 3 GUNTERT, P. (OPALP) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1X52 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_1000024388. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 296 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.3MM ERF1_3 DOMAIN; 20MM D-TRIS REMARK 210 -HCL; 100MM NACL; 1MM D-DTT; REMARK 210 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 : 900 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 0.9295, CYANA 1.0.7 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 RESTRAINED 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: 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 OD2 ASP A 56 HG1 THR A 57 1.53 REMARK 500 OD2 ASP A 69 HG1 THR A 72 1.57 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 4 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 5 ARG A 78 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 5 PHE A 93 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 6 ARG A 66 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 8 ARG A 114 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 9 PHE A 93 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 18 ARG A 114 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES 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 -65.31 -154.16 REMARK 500 1 SER A 5 97.79 63.05 REMARK 500 1 SER A 6 90.68 35.20 REMARK 500 1 ALA A 10 41.11 -77.79 REMARK 500 1 HIS A 34 -85.55 -64.97 REMARK 500 1 MET A 53 14.91 51.96 REMARK 500 1 ALA A 87 19.34 57.26 REMARK 500 1 THR A 107 18.40 56.99 REMARK 500 1 PRO A 121 -73.64 -80.33 REMARK 500 2 ALA A 10 100.10 -169.69 REMARK 500 2 GLN A 105 4.03 -66.00 REMARK 500 3 SER A 3 -170.72 57.51 REMARK 500 3 SER A 5 103.58 67.33 REMARK 500 3 ARG A 12 -66.42 -148.97 REMARK 500 3 LEU A 13 -163.55 44.01 REMARK 500 3 ASP A 15 105.41 63.12 REMARK 500 3 SER A 95 9.83 -62.40 REMARK 500 3 THR A 107 -12.12 77.57 REMARK 500 3 SER A 119 -74.98 -158.90 REMARK 500 3 SER A 123 -164.33 -167.38 REMARK 500 4 SER A 2 141.14 61.68 REMARK 500 4 SER A 6 -164.91 61.12 REMARK 500 4 SER A 14 83.52 47.03 REMARK 500 4 ASP A 15 96.26 74.05 REMARK 500 4 PRO A 118 98.87 -65.12 REMARK 500 4 SER A 123 53.92 -95.63 REMARK 500 5 SER A 5 -97.57 -93.34 REMARK 500 5 VAL A 9 67.99 -114.41 REMARK 500 5 MET A 53 19.96 58.31 REMARK 500 5 THR A 107 -14.93 75.11 REMARK 500 5 SER A 122 -62.96 -135.67 REMARK 500 6 SER A 2 121.16 62.45 REMARK 500 6 SER A 5 113.81 110.65 REMARK 500 6 VAL A 9 21.70 -149.36 REMARK 500 6 SER A 11 -58.53 -132.53 REMARK 500 6 ARG A 12 91.75 49.42 REMARK 500 6 SER A 14 -53.05 -144.64 REMARK 500 6 ASN A 86 44.10 -100.71 REMARK 500 6 ALA A 87 5.04 58.45 REMARK 500 6 PRO A 118 49.06 -77.03 REMARK 500 6 SER A 119 89.30 -152.88 REMARK 500 6 SER A 122 -43.85 -162.30 REMARK 500 6 SER A 123 -64.13 68.08 REMARK 500 7 SER A 2 -20.74 64.55 REMARK 500 7 SER A 5 -67.59 -165.74 REMARK 500 7 ARG A 12 -156.89 -106.08 REMARK 500 7 MET A 53 14.15 55.49 REMARK 500 7 SER A 122 89.89 -153.22 REMARK 500 8 SER A 5 -82.19 -149.07 REMARK 500 8 SER A 14 -58.44 -155.06 REMARK 500 REMARK 500 THIS ENTRY HAS 137 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER A 123 GLY A 124 20 -145.42 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 38 0.08 SIDE CHAIN REMARK 500 1 ARG A 66 0.08 SIDE CHAIN REMARK 500 1 ARG A 75 0.12 SIDE CHAIN REMARK 500 2 TYR A 29 0.10 SIDE CHAIN REMARK 500 3 ARG A 12 0.08 SIDE CHAIN REMARK 500 3 TYR A 29 0.09 SIDE CHAIN REMARK 500 5 ARG A 78 0.11 SIDE CHAIN REMARK 500 6 TYR A 29 0.08 SIDE CHAIN REMARK 500 6 ARG A 66 0.07 SIDE CHAIN REMARK 500 6 ARG A 75 0.09 SIDE CHAIN REMARK 500 9 TYR A 41 0.09 SIDE CHAIN REMARK 500 10 TYR A 29 0.11 SIDE CHAIN REMARK 500 11 ARG A 38 0.08 SIDE CHAIN REMARK 500 11 ARG A 73 0.09 SIDE CHAIN REMARK 500 12 TYR A 29 0.08 SIDE CHAIN REMARK 500 14 ARG A 114 0.10 SIDE CHAIN REMARK 500 15 TYR A 29 0.07 SIDE CHAIN REMARK 500 18 TYR A 29 0.07 SIDE CHAIN REMARK 500 19 TYR A 29 0.08 SIDE CHAIN REMARK 500 20 ARG A 66 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSI002005867.1 RELATED DB: TARGETDB DBREF 1X52 A 8 118 UNP Q9BRX2 PELO_HUMAN 261 371 SEQADV 1X52 GLY A 1 UNP Q9BRX2 CLONING ARTIFACT SEQADV 1X52 SER A 2 UNP Q9BRX2 CLONING ARTIFACT SEQADV 1X52 SER A 3 UNP Q9BRX2 CLONING ARTIFACT SEQADV 1X52 GLY A 4 UNP Q9BRX2 CLONING ARTIFACT SEQADV 1X52 SER A 5 UNP Q9BRX2 CLONING ARTIFACT SEQADV 1X52 SER A 6 UNP Q9BRX2 CLONING ARTIFACT SEQADV 1X52 GLY A 7 UNP Q9BRX2 CLONING ARTIFACT SEQADV 1X52 SER A 119 UNP Q9BRX2 CLONING ARTIFACT SEQADV 1X52 GLY A 120 UNP Q9BRX2 CLONING ARTIFACT SEQADV 1X52 PRO A 121 UNP Q9BRX2 CLONING ARTIFACT SEQADV 1X52 SER A 122 UNP Q9BRX2 CLONING ARTIFACT SEQADV 1X52 SER A 123 UNP Q9BRX2 CLONING ARTIFACT SEQADV 1X52 GLY A 124 UNP Q9BRX2 CLONING ARTIFACT SEQRES 1 A 124 GLY SER SER GLY SER SER GLY THR VAL ALA SER ARG LEU SEQRES 2 A 124 SER ASP THR LYS ALA ALA GLY GLU VAL LYS ALA LEU ASP SEQRES 3 A 124 ASP PHE TYR LYS MET LEU GLN HIS GLU PRO ASP ARG ALA SEQRES 4 A 124 PHE TYR GLY LEU LYS GLN VAL GLU LYS ALA ASN GLU ALA SEQRES 5 A 124 MET ALA ILE ASP THR LEU LEU ILE SER ASP GLU LEU PHE SEQRES 6 A 124 ARG HIS GLN ASP VAL ALA THR ARG SER ARG TYR VAL ARG SEQRES 7 A 124 LEU VAL ASP SER VAL LYS GLU ASN ALA GLY THR VAL ARG SEQRES 8 A 124 ILE PHE SER SER LEU HIS VAL SER GLY GLU GLN LEU SER SEQRES 9 A 124 GLN LEU THR GLY VAL ALA ALA ILE LEU ARG PHE PRO VAL SEQRES 10 A 124 PRO SER GLY PRO SER SER GLY HELIX 1 1 ASP A 15 HIS A 34 1 20 HELIX 2 2 GLU A 35 ASP A 37 5 3 HELIX 3 3 GLY A 42 ALA A 52 1 11 HELIX 4 4 ASP A 62 ARG A 66 1 5 HELIX 5 5 ASP A 69 ASN A 86 1 18 HELIX 6 6 HIS A 97 GLN A 105 1 9 SHEET 1 A 4 ALA A 39 TYR A 41 0 SHEET 2 A 4 VAL A 109 LEU A 113 -1 O ALA A 111 N PHE A 40 SHEET 3 A 4 ILE A 55 SER A 61 -1 N THR A 57 O ILE A 112 SHEET 4 A 4 THR A 89 PHE A 93 1 O PHE A 93 N ILE A 60 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