Header list of 1rh8.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 14-NOV-03 1RH8 TITLE THREE-DIMENSIONAL STRUCTURE OF THE CALCIUM-FREE PICCOLO C2A-DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PICCOLO PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C2A-DOMAIN; COMPND 5 SYNONYM: MULTIDOMAIN PRESYNAPTIC CYTOMATRIX PROTEIN; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 GENE: PCLO; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-KG KEYWDS BETA-SANDWICH, METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.GARCIA,S.H.GERBER,S.SUGITA,T.C.SUDHOF,J.RIZO REVDAT 3 02-MAR-22 1RH8 1 REMARK REVDAT 2 24-FEB-09 1RH8 1 VERSN REVDAT 1 13-JAN-04 1RH8 0 JRNL AUTH J.GARCIA,S.H.GERBER,S.SUGITA,T.C.SUDHOF,J.RIZO JRNL TITL A CONFORMATIONAL SWITCH IN THE PICCOLO C2A DOMAIN REGULATED JRNL TITL 2 BY ALTERNATIVE SPLICING. JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 45 2004 JRNL REFN ISSN 1545-9993 JRNL PMID 14718922 JRNL DOI 10.1038/NSMB707 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CNS 0.9 REMARK 3 AUTHORS : VARIAN ASSOCIATES (VNMR), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE FINAL STRUCTURES WERE CALCULATED REMARK 3 WITH A TOTAL OF 2316 EXPERIMENTAL RESTRAINTS, INCLUDING 1994 NOE REMARK 3 DISTANCE RESTRAINTS, 116 H-BOND RESTRAINTS AND 206 TORSION ANGLE REMARK 3 RESTRAINTS. REMARK 4 REMARK 4 1RH8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-03. REMARK 100 THE DEPOSITION ID IS D_1000020744. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 150MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.8MM PICCOLO C2A-DOMAIN U-15N, REMARK 210 20MM ACETATE (PH 6.0), 150MM REMARK 210 NACL, 1MM EDTA, 95% H2O, 5% D2O; REMARK 210 0.8MM PICCOLO C2A-DOMAIN U-15N, REMARK 210 13C, 20MM ACETATE (PH 6.0), REMARK 210 150MM NACL, 1MM EDTA, 95% H2O, 5% REMARK 210 D2O; 0.8MM PICCOLO C2A-DOMAIN U- REMARK 210 15N, 20 MM ACETATE (PH 6.0), 150 REMARK 210 MM NACL, 1 MM EDTA, 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_TOCSY; HNCACB; REMARK 210 CBCACONH; 2D TOCSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.2, NMRVIEW 4.1.2, CNS REMARK 210 0.9 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000 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: THIS STRUCTURE WAS DETERMINED USING ADDITIONAL TRIPLE REMARK 210 RESONANCE EXPERIMENTS. 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 LYS A 4699 H LYS A 4703 1.57 REMARK 500 O LEU A 4659 H TRP A 4713 1.59 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 LEU A4659 -70.84 -123.76 REMARK 500 1 ASN A4669 95.20 60.13 REMARK 500 1 TYR A4672 -45.98 -156.78 REMARK 500 1 PRO A4683 55.67 -95.18 REMARK 500 1 ALA A4694 -176.69 -67.20 REMARK 500 1 SER A4695 99.89 -45.84 REMARK 500 1 TYR A4704 -72.04 -42.13 REMARK 500 1 TRP A4713 -47.53 -145.08 REMARK 500 1 SER A4721 27.05 86.19 REMARK 500 1 SER A4743 -32.32 175.04 REMARK 500 1 SER A4744 171.23 -46.84 REMARK 500 1 LEU A4748 -33.16 -140.44 REMARK 500 1 SER A4757 16.08 -142.44 REMARK 500 1 THR A4758 90.33 -50.44 REMARK 500 1 ASP A4762 49.04 -69.99 REMARK 500 1 ASN A4763 80.24 39.90 REMARK 500 2 LEU A4659 -83.94 -93.16 REMARK 500 2 ASN A4669 98.24 60.55 REMARK 500 2 TYR A4672 -34.86 -156.56 REMARK 500 2 PRO A4683 45.57 -85.77 REMARK 500 2 SER A4695 105.79 -41.45 REMARK 500 2 GLN A4706 -62.39 -97.39 REMARK 500 2 TRP A4713 -45.70 -150.17 REMARK 500 2 SER A4721 26.75 90.11 REMARK 500 2 LEU A4748 -25.79 -140.44 REMARK 500 2 THR A4758 67.28 -67.80 REMARK 500 2 LEU A4761 -106.15 -62.72 REMARK 500 2 ASP A4762 17.85 41.30 REMARK 500 2 GLU A4775 95.17 -69.80 REMARK 500 3 SER A4636 -168.74 -63.97 REMARK 500 3 HIS A4637 79.07 -106.61 REMARK 500 3 LEU A4659 -84.68 -89.55 REMARK 500 3 TYR A4672 -48.96 -165.92 REMARK 500 3 PRO A4683 46.75 -91.74 REMARK 500 3 SER A4695 96.34 -42.24 REMARK 500 3 TYR A4704 -72.25 -84.04 REMARK 500 3 TRP A4713 -45.24 -152.34 REMARK 500 3 SER A4721 28.33 85.23 REMARK 500 3 ASP A4740 -178.13 -67.34 REMARK 500 3 SER A4743 -47.94 177.87 REMARK 500 3 SER A4744 -169.18 -59.62 REMARK 500 3 LEU A4748 -33.09 -136.69 REMARK 500 3 SER A4757 16.51 -143.32 REMARK 500 3 THR A4758 89.30 -50.56 REMARK 500 3 ASP A4762 50.32 -69.99 REMARK 500 4 LEU A4659 -83.80 -92.97 REMARK 500 4 TYR A4672 -46.95 -134.63 REMARK 500 4 LEU A4682 -73.84 -56.99 REMARK 500 4 PRO A4683 -167.99 -78.14 REMARK 500 4 ARG A4685 -73.49 -59.34 REMARK 500 REMARK 500 THIS ENTRY HAS 308 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1RH8 A 4635 4776 UNP Q9JKS6 PCLO_RAT 4635 4776 SEQRES 1 A 142 ALA SER HIS PRO ILE THR GLY GLU ILE GLN LEU GLN ILE SEQRES 2 A 142 ASN TYR ASP LEU GLY ASN LEU ILE ILE HIS ILE LEU GLN SEQRES 3 A 142 ALA ARG ASN LEU VAL PRO ARG ASP ASN ASN GLY TYR SER SEQRES 4 A 142 ASP PRO PHE VAL LYS VAL TYR LEU LEU PRO GLY ARG GLY SEQRES 5 A 142 GLN VAL MET VAL VAL GLN ASN ALA SER ALA GLU TYR LYS SEQRES 6 A 142 ARG ARG THR LYS TYR VAL GLN LYS SER LEU ASN PRO GLU SEQRES 7 A 142 TRP ASN GLN THR VAL ILE TYR LYS SER ILE SER MET GLU SEQRES 8 A 142 GLN LEU MET LYS LYS THR LEU GLU VAL THR VAL TRP ASP SEQRES 9 A 142 TYR ASP ARG PHE SER SER ASN ASP PHE LEU GLY GLU VAL SEQRES 10 A 142 LEU ILE ASP LEU SER SER THR SER HIS LEU ASP ASN THR SEQRES 11 A 142 PRO ARG TRP TYR PRO LEU LYS GLU GLN THR GLU SER HELIX 1 1 SER A 4695 ARG A 4700 1 6 HELIX 2 2 VAL A 4705 ASN A 4710 1 6 HELIX 3 3 SER A 4723 MET A 4728 1 6 HELIX 4 4 THR A 4758 ASP A 4762 5 5 SHEET 1 A 4 GLU A4712 TYR A4719 0 SHEET 2 A 4 ASN A4653 ARG A4662 -1 N ILE A4656 O VAL A4717 SHEET 3 A 4 GLU A4642 ASP A4650 -1 N GLN A4644 O GLN A4660 SHEET 4 A 4 ARG A4766 PRO A4769 -1 O TYR A4768 N ILE A4643 SHEET 1 B 4 MET A4689 VAL A4690 0 SHEET 2 B 4 PHE A4676 LEU A4681 -1 N VAL A4679 O MET A4689 SHEET 3 B 4 THR A4731 TYR A4739 -1 O TRP A4737 N PHE A4676 SHEET 4 B 4 ASN A4745 ASP A4754 -1 O ASP A4746 N ASP A4738 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