Header list of 1y7n.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN TRANSPORT 09-DEC-04 1Y7N TITLE SOLUTION STRUCTURE OF THE SECOND PDZ DOMAIN OF THE HUMAN NEURONAL TITLE 2 ADAPTOR X11ALPHA COMPND MOL_ID: 1; COMPND 2 MOLECULE: AMYLOID BETA A4 PRECURSOR PROTEIN-BINDING FAMILY A MEMBER COMPND 3 1; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: SECOND PDZ DOMAIN; COMPND 6 SYNONYM: NEURON-SPECIFIC X11 PROTEIN, NEURONAL MUNC18-1-INTERACTING COMPND 7 PROTEIN 1, MINT-1, ADAPTER PROTEIN X11ALPHA; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 TISSUE: BRAIN; SOURCE 6 GENE: APBA1; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) *RP; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET3H KEYWDS COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE, NEURONAL ADAPTOR, PROTEIN KEYWDS 2 TRANSPORT EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.E.DUQUESNE,M.DE RUIJTER,J.BROUWER,J.W.DRIJFHOUT,S.B.NABUURS, AUTHOR 2 C.A.E.M.SPRONK,G.W.VUISTER,M.UBBINK,G.W.CANTERS REVDAT 3 02-MAR-22 1Y7N 1 REMARK SEQADV REVDAT 2 24-FEB-09 1Y7N 1 VERSN REVDAT 1 22-NOV-05 1Y7N 0 JRNL AUTH A.E.DUQUESNE,M.DE RUIJTER,J.BROUWER,J.W.DRIJFHOUT, JRNL AUTH 2 S.B.NABUURS,C.A.E.M.SPRONK,G.W.VUISTER,M.UBBINK,G.W.CANTERS JRNL TITL SOLUTION STRUCTURE OF THE SECOND PDZ DOMAIN OF THE NEURONAL JRNL TITL 2 ADAPTOR X11ALPHA AND ITS INTERACTION WITH THE C-TERMINAL JRNL TITL 3 PEPTIDE OF THE HUMAN COPPER CHAPERONE FOR SUPEROXIDE JRNL TITL 4 DISMUTASE JRNL REF J.BIOMOL.NMR V. 32 209 2005 JRNL REFN ISSN 0925-2738 JRNL PMID 16132821 JRNL DOI 10.1007/S10858-005-7333-1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2002 RELEASE, X-PLOR 2.9.6 REMARK 3 AUTHORS : F. DELAGLIO, S. GRZESIEK, G. W. VUISTER, G. ZHU, REMARK 3 J. PFEIFER AND A. BAX (NMRPIPE), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE FINAL STRUCTURE CALCULATIONS WITH CYANA WERE STARTED FROM 100 REMARK 3 CONFORMERS WITH RANDOM TORSION ANGLE VALUES. SIMULATED ANNEALING REMARK 3 WITH 10,000 TIME STEPS PER CONFORMER WAS DONE USING THE DYANA REMARK 3 TORSION ANGLE DYNAMICS ALGORITHM. USING THE FORMATCONVERTER, REMARK 3 DEVELOPED AS PART OF THE COLLABORATIVE COMPUTING PROJECT FOR THE REMARK 3 NMR COMMUNITY (CCPN), THE DISTANCE AND DIHEDRAL ANGLE RESTRAINTS REMARK 3 WERE CONVERTED TO THE X-PLOR RESTRAINT FORMAT. SUBSEQUENTLY THE REMARK 3 100 GENERATED STRUCTURES WERE REFINED USING A SH REMARK 3 RT RESTRAINED MOLECULAR DYNAMICS SIMULATION IN EXPLICIT SOLVENT IN REMARK 3 THE PROGRAM XPLOR-NIH. OF THESE, THE 20 LOWEST ENERGY STRUCTURES REMARK 3 WERE SELECTED TO FORM THE FINAL ENSEMBLE. REMARK 4 REMARK 4 1Y7N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JAN-05. REMARK 100 THE DEPOSITION ID IS D_1000031218. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 290 REMARK 210 PH : 6.7 REMARK 210 IONIC STRENGTH : 10MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.2MM PDZ2A U-15N,13C; 10MM REMARK 210 SODIUM PHOSPHATE BUFFER; PH 6.7; REMARK 210 95% H2O; 5% 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 : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CARA 1.1.8, CYANA 1.0, VNMR REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR REMARK 210 DYNAMICS SIMULATION, TORSION REMARK 210 ANGLE DYNAMICS, DISTANCE AND REMARK 210 DIHEDRAL ANGLE RESTRAINTS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 HIS A 1 REMARK 465 HIS A 2 REMARK 465 HIS A 3 REMARK 465 HIS A 4 REMARK 465 HIS A 5 REMARK 465 LEU A 6 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 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 THR A 8 77.13 61.22 REMARK 500 1 PRO A 88 28.71 -70.27 REMARK 500 2 PRO A 88 31.31 -74.71 REMARK 500 3 ASP A 21 -175.46 -171.71 REMARK 500 3 PRO A 88 35.64 -74.30 REMARK 500 4 PRO A 88 31.49 -72.74 REMARK 500 5 MET A 9 -46.24 -173.95 REMARK 500 5 PRO A 88 32.42 -68.20 REMARK 500 6 GLN A 25 -168.42 -121.63 REMARK 500 6 PRO A 88 29.50 -71.04 REMARK 500 6 ALA A 89 -2.36 71.00 REMARK 500 7 ASN A 32 12.80 59.86 REMARK 500 7 PRO A 88 29.83 -75.98 REMARK 500 8 THR A 8 93.69 83.29 REMARK 500 8 ASN A 32 -1.14 64.20 REMARK 500 8 PRO A 88 27.52 -73.77 REMARK 500 9 ASN A 11 88.26 63.22 REMARK 500 9 PRO A 88 30.27 -74.84 REMARK 500 10 GLN A 25 -164.46 57.05 REMARK 500 10 PRO A 88 26.26 -69.71 REMARK 500 10 ALA A 89 -1.27 74.86 REMARK 500 11 GLU A 81 108.78 -59.11 REMARK 500 12 THR A 8 140.11 64.93 REMARK 500 12 ASN A 11 92.09 62.19 REMARK 500 12 ASP A 21 -176.89 -176.73 REMARK 500 12 PRO A 88 29.58 -71.29 REMARK 500 13 ASP A 21 -170.49 -173.10 REMARK 500 13 PRO A 88 38.76 -70.79 REMARK 500 14 ASN A 32 11.97 59.39 REMARK 500 14 PRO A 88 24.33 -71.42 REMARK 500 15 GLN A 25 -153.58 54.09 REMARK 500 15 PRO A 88 29.67 -75.51 REMARK 500 16 ASN A 11 86.79 68.91 REMARK 500 16 PRO A 88 26.64 -70.69 REMARK 500 17 ASN A 59 -21.18 73.38 REMARK 500 17 PRO A 88 22.33 -72.94 REMARK 500 18 GLN A 25 -157.27 -97.07 REMARK 500 18 PRO A 88 24.91 -72.10 REMARK 500 19 ASN A 59 -2.72 69.43 REMARK 500 19 PRO A 88 29.68 -78.33 REMARK 500 20 ASN A 11 89.88 63.48 REMARK 500 20 ASN A 59 -18.66 70.84 REMARK 500 20 PRO A 88 30.05 -74.48 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 19 0.08 SIDE CHAIN REMARK 500 3 ARG A 18 0.09 SIDE CHAIN REMARK 500 5 ARG A 19 0.07 SIDE CHAIN REMARK 500 5 ARG A 54 0.08 SIDE CHAIN REMARK 500 8 ARG A 19 0.11 SIDE CHAIN REMARK 500 9 ARG A 50 0.08 SIDE CHAIN REMARK 500 10 ARG A 23 0.13 SIDE CHAIN REMARK 500 11 ARG A 19 0.09 SIDE CHAIN REMARK 500 12 ARG A 40 0.08 SIDE CHAIN REMARK 500 13 ARG A 50 0.08 SIDE CHAIN REMARK 500 13 ARG A 54 0.11 SIDE CHAIN REMARK 500 14 ARG A 23 0.08 SIDE CHAIN REMARK 500 14 ARG A 46 0.09 SIDE CHAIN REMARK 500 15 ARG A 54 0.08 SIDE CHAIN REMARK 500 16 ARG A 18 0.12 SIDE CHAIN REMARK 500 17 ARG A 19 0.07 SIDE CHAIN REMARK 500 18 ARG A 18 0.08 SIDE CHAIN REMARK 500 19 ARG A 18 0.08 SIDE CHAIN REMARK 500 19 ARG A 46 0.10 SIDE CHAIN REMARK 500 20 ARG A 19 0.09 SIDE CHAIN REMARK 500 20 ARG A 50 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1Y7N A 12 90 UNP Q02410 APBA1_HUMAN 745 823 SEQADV 1Y7N HIS A 1 UNP Q02410 EXPRESSION TAG SEQADV 1Y7N HIS A 2 UNP Q02410 EXPRESSION TAG SEQADV 1Y7N HIS A 3 UNP Q02410 EXPRESSION TAG SEQADV 1Y7N HIS A 4 UNP Q02410 EXPRESSION TAG SEQADV 1Y7N HIS A 5 UNP Q02410 EXPRESSION TAG SEQADV 1Y7N LEU A 6 UNP Q02410 EXPRESSION TAG SEQADV 1Y7N GLU A 7 UNP Q02410 EXPRESSION TAG SEQADV 1Y7N THR A 8 UNP Q02410 EXPRESSION TAG SEQADV 1Y7N MET A 9 UNP Q02410 EXPRESSION TAG SEQADV 1Y7N GLY A 10 UNP Q02410 EXPRESSION TAG SEQADV 1Y7N ASN A 11 UNP Q02410 EXPRESSION TAG SEQRES 1 A 90 HIS HIS HIS HIS HIS LEU GLU THR MET GLY ASN VAL THR SEQRES 2 A 90 THR VAL LEU ILE ARG ARG PRO ASP LEU ARG TYR GLN LEU SEQRES 3 A 90 GLY PHE SER VAL GLN ASN GLY ILE ILE CYS SER LEU MET SEQRES 4 A 90 ARG GLY GLY ILE ALA GLU ARG GLY GLY VAL ARG VAL GLY SEQRES 5 A 90 HIS ARG ILE ILE GLU ILE ASN GLY GLN SER VAL VAL ALA SEQRES 6 A 90 THR PRO HIS GLU LYS ILE VAL HIS ILE LEU SER ASN ALA SEQRES 7 A 90 VAL GLY GLU ILE HIS MET LYS THR MET PRO ALA ALA HELIX 1 1 GLY A 42 GLY A 48 1 7 HELIX 2 2 PRO A 67 ALA A 78 1 12 SHEET 1 A 4 THR A 13 ARG A 19 0 SHEET 2 A 4 GLY A 80 MET A 87 -1 O THR A 86 N THR A 13 SHEET 3 A 4 ARG A 54 ILE A 58 -1 N ILE A 56 O LYS A 85 SHEET 4 A 4 GLN A 61 SER A 62 -1 O GLN A 61 N ILE A 58 SHEET 1 B 2 PHE A 28 GLN A 31 0 SHEET 2 B 2 ILE A 34 LEU A 38 -1 O CYS A 36 N SER A 29 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