Header list of 1ss2.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 23-MAR-04 1SS2 TITLE SOLUTION STRUCTURE OF THE SECOND COMPLEMENT CONTROL PROTEIN (CCP) TITLE 2 MODULE OF THE GABA(B)R1A RECEPTOR, PRO-119 CIS CONFORMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: GAMMA-AMINOBUTYRIC ACID TYPE B RECEPTOR, SUBUNIT 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SUSHI 2 (RESIDUES 96-159); COMPND 5 SYNONYM: GABA-B RECEPTOR 1, GABA-B-R1, GB1; 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: GABBR1; SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: KM71; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZALPHA KEYWDS GABA(B) RECEPTOR, CIS-TRANS ISOMERISATION, CCP MODULE, SUSHI DOMAIN, KEYWDS 2 SHORT CONSENSUS REPEAT, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 24 AUTHOR S.BLEIN,D.UHRIN,B.O.SMITH,J.H.WHITE,P.N.BARLOW REVDAT 4 02-MAR-22 1SS2 1 REMARK SEQADV REVDAT 3 24-FEB-09 1SS2 1 VERSN REVDAT 2 14-DEC-04 1SS2 1 JRNL REVDAT 1 12-OCT-04 1SS2 0 JRNL AUTH S.BLEIN,R.GINHAM,D.UHRIN,B.O.SMITH,D.C.SOARES,S.VELTEL, JRNL AUTH 2 R.A.MCILHINNEY,J.H.WHITE,P.N.BARLOW JRNL TITL STRUCTURAL ANALYSIS OF THE COMPLEMENT CONTROL PROTEIN (CCP) JRNL TITL 2 MODULES OF GABA(B) RECEPTOR 1A: ONLY ONE OF THE TWO CCP JRNL TITL 3 MODULES IS COMPACTLY FOLDED. JRNL REF J.BIOL.CHEM. V. 279 48292 2004 JRNL REFN ISSN 0021-9258 JRNL PMID 15304491 JRNL DOI 10.1074/JBC.M406540200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1, CNS 1.0 REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 1268 UNIQUE RESTRAINTS, 23 DIHEDRAL REMARK 3 ANGLES (HNHA), 11 HYDROGEN BONDS REMARK 4 REMARK 4 1SS2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-04. REMARK 100 THE DEPOSITION ID IS D_1000021953. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 4 REMARK 210 IONIC STRENGTH : 0 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM GABA(B)R1A 2ND CCP MODULE U REMARK 210 -15N,13C; 20 MM DEUTERATED REMARK 210 SODIUM ACETATE, PH 4; 90% H2O, REMARK 210 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; DRX REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AZARA 2.6, ANSIG 3.3, CNS 1.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 120 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST 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 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 ALA A 93 43.87 -174.17 REMARK 500 1 ASP A 117 124.38 -174.93 REMARK 500 1 LEU A 121 -34.94 -168.35 REMARK 500 1 ASP A 122 51.13 36.38 REMARK 500 1 PRO A 132 69.37 -65.87 REMARK 500 1 ASP A 133 -31.59 -173.25 REMARK 500 1 GLN A 148 140.56 -173.12 REMARK 500 1 PRO A 152 -155.68 -67.80 REMARK 500 1 PRO A 154 -146.88 -81.61 REMARK 500 2 GLU A 94 -129.28 -72.23 REMARK 500 2 PHE A 95 133.88 68.27 REMARK 500 2 ILE A 98 43.59 -157.83 REMARK 500 2 CYS A 99 139.18 62.18 REMARK 500 2 LEU A 113 129.96 69.79 REMARK 500 2 ASP A 117 65.81 -159.67 REMARK 500 2 LEU A 118 137.77 -38.39 REMARK 500 2 ASP A 122 109.13 38.37 REMARK 500 2 PRO A 132 157.81 -40.45 REMARK 500 2 ASP A 133 -40.31 80.93 REMARK 500 2 SER A 140 38.81 -70.43 REMARK 500 2 SER A 145 -29.60 -158.72 REMARK 500 2 GLN A 146 48.08 -149.29 REMARK 500 2 PRO A 152 -159.88 -64.01 REMARK 500 2 PRO A 154 -149.45 -79.89 REMARK 500 3 ALA A 93 136.89 -177.21 REMARK 500 3 GLU A 94 135.56 64.90 REMARK 500 3 PHE A 95 109.76 60.48 REMARK 500 3 ARG A 97 44.47 -89.62 REMARK 500 3 ASP A 117 58.10 -151.02 REMARK 500 3 PRO A 132 158.38 -44.44 REMARK 500 3 ASP A 133 -31.89 77.98 REMARK 500 3 SER A 140 4.41 -63.14 REMARK 500 3 SER A 145 -137.32 -150.67 REMARK 500 3 GLN A 148 147.74 69.67 REMARK 500 3 PRO A 154 -143.81 -75.26 REMARK 500 4 VAL A 96 140.84 66.01 REMARK 500 4 LYS A 110 -41.60 -144.02 REMARK 500 4 VAL A 111 136.10 52.02 REMARK 500 4 LEU A 118 133.51 -38.58 REMARK 500 4 PRO A 119 44.69 -92.43 REMARK 500 4 LEU A 121 79.27 -162.45 REMARK 500 4 PRO A 132 155.47 -49.64 REMARK 500 4 ASP A 133 -29.74 79.37 REMARK 500 4 SER A 145 -29.77 -162.80 REMARK 500 4 GLN A 146 57.07 -166.68 REMARK 500 4 GLN A 148 -149.31 -155.33 REMARK 500 4 PRO A 152 156.99 -47.15 REMARK 500 4 PRO A 154 -147.30 -75.02 REMARK 500 5 ALA A 93 -140.15 -66.31 REMARK 500 5 GLU A 94 135.07 -174.29 REMARK 500 REMARK 500 THIS ENTRY HAS 297 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1SRZ RELATED DB: PDB REMARK 900 TRANS PRO-119 CONFORMER DBREF 1SS2 A 96 159 UNP Q9Z0U4 GABR1_RAT 96 159 SEQADV 1SS2 GLU A 92 UNP Q9Z0U4 CLONING ARTIFACT SEQADV 1SS2 ALA A 93 UNP Q9Z0U4 CLONING ARTIFACT SEQADV 1SS2 GLU A 94 UNP Q9Z0U4 CLONING ARTIFACT SEQADV 1SS2 PHE A 95 UNP Q9Z0U4 CLONING ARTIFACT SEQRES 1 A 68 GLU ALA GLU PHE VAL ARG ILE CYS SER LYS SER TYR LEU SEQRES 2 A 68 THR LEU GLU ASN GLY LYS VAL PHE LEU THR GLY GLY ASP SEQRES 3 A 68 LEU PRO ALA LEU ASP GLY ALA ARG VAL GLU PHE ARG CYS SEQRES 4 A 68 ASP PRO ASP PHE HIS LEU VAL GLY SER SER ARG SER VAL SEQRES 5 A 68 CYS SER GLN GLY GLN TRP SER THR PRO LYS PRO HIS CYS SEQRES 6 A 68 GLN VAL ASN HELIX 1 1 LYS A 101 THR A 105 5 5 SHEET 1 A 3 GLY A 109 THR A 114 0 SHEET 2 A 3 ARG A 125 CYS A 130 -1 O ARG A 129 N LYS A 110 SHEET 3 A 3 ARG A 141 VAL A 143 -1 O SER A 142 N VAL A 126 SHEET 1 B 2 PHE A 134 LEU A 136 0 SHEET 2 B 2 CYS A 156 VAL A 158 -1 O GLN A 157 N HIS A 135 SSBOND 1 CYS A 99 CYS A 144 1555 1555 2.03 SSBOND 2 CYS A 130 CYS A 156 1555 1555 2.03 CISPEP 1 LEU A 118 PRO A 119 1 0.26 CISPEP 2 LEU A 118 PRO A 119 2 0.28 CISPEP 3 LEU A 118 PRO A 119 3 0.23 CISPEP 4 LEU A 118 PRO A 119 4 0.46 CISPEP 5 LEU A 118 PRO A 119 5 0.14 CISPEP 6 LEU A 118 PRO A 119 6 0.32 CISPEP 7 LEU A 118 PRO A 119 7 -0.18 CISPEP 8 LEU A 118 PRO A 119 8 0.28 CISPEP 9 LEU A 118 PRO A 119 9 0.54 CISPEP 10 LEU A 118 PRO A 119 10 -0.08 CISPEP 11 LEU A 118 PRO A 119 11 0.24 CISPEP 12 LEU A 118 PRO A 119 12 0.43 CISPEP 13 LEU A 118 PRO A 119 13 0.35 CISPEP 14 LEU A 118 PRO A 119 14 0.46 CISPEP 15 LEU A 118 PRO A 119 15 0.20 CISPEP 16 LEU A 118 PRO A 119 16 0.51 CISPEP 17 LEU A 118 PRO A 119 17 -0.21 CISPEP 18 LEU A 118 PRO A 119 18 0.04 CISPEP 19 LEU A 118 PRO A 119 19 0.16 CISPEP 20 LEU A 118 PRO A 119 20 -0.37 CISPEP 21 LEU A 118 PRO A 119 21 0.07 CISPEP 22 LEU A 118 PRO A 119 22 -0.02 CISPEP 23 LEU A 118 PRO A 119 23 -0.33 CISPEP 24 LEU A 118 PRO A 119 24 0.76 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