Header list of 1emo.pdb file
Complete list - t 27 2 Bytes
HEADER MATRIX PROTEIN 05-AUG-96 1EMO TITLE NMR STUDY OF A PAIR OF FIBRILLIN CA2+ BINDING EPIDERMAL GROWTH FACTOR- TITLE 2 LIKE DOMAINS, 22 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: FIBRILLIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CA2+ BINDING EPIDERMAL GROWTH FACTOR-LIKE DOMAIN, RESIDUES COMPND 5 2124 - 2205; 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 ORGAN: SKIN; SOURCE 6 TISSUE: SKIN (DERMIS); SOURCE 7 CELL: FIBROBLAST; SOURCE 8 GENE: FBN1; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 11 EXPRESSION_SYSTEM_STRAIN: NM554 (HIS TAG); SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PQE30 (QIAGEN); SOURCE 13 EXPRESSION_SYSTEM_GENE: FBN1 KEYWDS EXTRACELLULAR MATRIX, CALCIUM-BINDING, GLYCOPROTEIN, MULTIGENE KEYWDS 2 FAMILY, DISEASE MUTATION, EGF-LIKE DOMAIN, HUMAN FIBRILLIN-1 KEYWDS 3 FRAGMENT, MATRIX PROTEIN EXPDTA SOLUTION NMR NUMMDL 22 AUTHOR A.K.DOWNING,I.D.CAMPBELL,P.A.HANDFORD REVDAT 3 27-OCT-21 1EMO 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1EMO 1 VERSN REVDAT 1 23-DEC-96 1EMO 0 JRNL AUTH A.K.DOWNING,V.KNOTT,J.M.WERNER,C.M.CARDY,I.D.CAMPBELL, JRNL AUTH 2 P.A.HANDFORD JRNL TITL SOLUTION STRUCTURE OF A PAIR OF CALCIUM-BINDING EPIDERMAL JRNL TITL 2 GROWTH FACTOR-LIKE DOMAINS: IMPLICATIONS FOR THE MARFAN JRNL TITL 3 SYNDROME AND OTHER GENETIC DISORDERS. JRNL REF CELL(CAMBRIDGE,MASS.) V. 85 597 1996 JRNL REFN ISSN 0092-8674 JRNL PMID 8653794 JRNL DOI 10.1016/S0092-8674(00)81259-3 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH V.KNOTT,A.K.DOWNING,C.M.CARDY,P.HANDFORD REMARK 1 TITL CALCIUM BINDING PROPERTIES OF AN EPIDERMAL GROWTH REMARK 1 TITL 2 FACTOR-LIKE DOMAIN PAIR FROM HUMAN FIBRILLIN-1 REMARK 1 REF J.MOL.BIOL. V. 255 22 1996 REMARK 1 REFN ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1EMO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000173086. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-NOESY; COSY; TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : OMEGA; AM REMARK 210 SPECTROMETER MANUFACTURER : GE; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.1 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22 REMARK 210 CONFORMERS, SELECTION CRITERIA : F(NOE) < 165 KJ MOL-1 TORSION REMARK 210 ANGLE CONSTRAINTS VIOLATED BY > REMARK 210 3 DEGREES REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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: 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 GLU A2130 -44.91 81.89 REMARK 500 1 CYS A2137 -90.28 55.99 REMARK 500 1 HIS A2139 42.54 163.26 REMARK 500 1 SER A2148 -160.89 171.56 REMARK 500 1 PRO A2154 -167.03 -66.20 REMARK 500 1 ALA A2160 49.14 -97.02 REMARK 500 1 ASN A2162 -43.70 -172.50 REMARK 500 1 VAL A2165 -166.87 -160.63 REMARK 500 1 ASN A2174 84.92 49.75 REMARK 500 1 ASN A2178 -38.62 -165.10 REMARK 500 1 CYS A2192 177.01 -47.84 REMARK 500 1 GLU A2194 129.36 -32.23 REMARK 500 1 PHE A2196 -162.85 -111.19 REMARK 500 1 PRO A2198 -158.61 -68.71 REMARK 500 1 MET A2201 49.08 -157.84 REMARK 500 1 MET A2202 -89.58 -119.73 REMARK 500 2 ALA A2125 107.34 -59.83 REMARK 500 2 GLU A2130 -46.97 82.14 REMARK 500 2 VAL A2136 -94.09 -101.22 REMARK 500 2 CYS A2137 -72.77 -81.02 REMARK 500 2 LYS A2138 100.54 65.48 REMARK 500 2 ASP A2146 -71.15 -50.64 REMARK 500 2 SER A2148 -162.70 166.83 REMARK 500 2 ARG A2150 112.07 -160.86 REMARK 500 2 PRO A2154 -167.23 -66.06 REMARK 500 2 TYR A2157 -169.87 -108.78 REMARK 500 2 ALA A2160 53.34 -99.58 REMARK 500 2 ASN A2162 -44.85 168.95 REMARK 500 2 VAL A2172 -79.03 -105.38 REMARK 500 2 ASN A2174 101.61 -41.68 REMARK 500 2 ASN A2178 -47.08 -171.48 REMARK 500 2 CYS A2192 177.49 -54.49 REMARK 500 2 GLU A2194 131.58 -35.08 REMARK 500 2 PHE A2196 -163.89 -116.87 REMARK 500 2 PRO A2198 -164.17 -68.69 REMARK 500 2 PRO A2200 -81.86 -65.39 REMARK 500 2 MET A2202 -75.84 -122.10 REMARK 500 2 THR A2203 -173.69 -173.21 REMARK 500 3 VAL A2126 143.99 -170.17 REMARK 500 3 GLU A2130 -41.25 81.52 REMARK 500 3 VAL A2136 -140.17 -109.86 REMARK 500 3 CYS A2137 96.38 -45.70 REMARK 500 3 HIS A2139 48.06 165.40 REMARK 500 3 GLN A2141 72.03 -100.89 REMARK 500 3 CYS A2142 -169.22 -62.90 REMARK 500 3 SER A2148 -158.99 -84.72 REMARK 500 3 TYR A2149 -167.73 -178.82 REMARK 500 3 ARG A2150 115.07 -169.02 REMARK 500 3 CYS A2153 155.57 -47.40 REMARK 500 3 PRO A2154 -168.80 -64.23 REMARK 500 REMARK 500 THIS ENTRY HAS 498 RAMACHANDRAN OUTLIERS. 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 A2150 0.31 SIDE CHAIN REMARK 500 2 ARG A2150 0.18 SIDE CHAIN REMARK 500 3 ARG A2150 0.22 SIDE CHAIN REMARK 500 4 ARG A2150 0.31 SIDE CHAIN REMARK 500 5 ARG A2150 0.20 SIDE CHAIN REMARK 500 6 ARG A2150 0.23 SIDE CHAIN REMARK 500 7 ARG A2150 0.31 SIDE CHAIN REMARK 500 8 ARG A2150 0.32 SIDE CHAIN REMARK 500 9 ARG A2150 0.30 SIDE CHAIN REMARK 500 10 ARG A2150 0.29 SIDE CHAIN REMARK 500 11 ARG A2150 0.31 SIDE CHAIN REMARK 500 12 ARG A2150 0.31 SIDE CHAIN REMARK 500 13 ARG A2150 0.32 SIDE CHAIN REMARK 500 14 ARG A2150 0.29 SIDE CHAIN REMARK 500 15 ARG A2150 0.32 SIDE CHAIN REMARK 500 16 ARG A2150 0.10 SIDE CHAIN REMARK 500 17 ARG A2150 0.19 SIDE CHAIN REMARK 500 18 ARG A2150 0.24 SIDE CHAIN REMARK 500 19 ARG A2150 0.26 SIDE CHAIN REMARK 500 20 ARG A2150 0.28 SIDE CHAIN REMARK 500 21 ARG A2150 0.31 SIDE CHAIN REMARK 500 22 ARG A2150 0.27 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2224 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A2127 OD2 REMARK 620 2 MET A2128 O 87.7 REMARK 620 3 GLU A2130 OE1 143.2 77.1 REMARK 620 4 GLU A2130 OE2 96.3 80.6 48.5 REMARK 620 5 ASN A2144 OD1 105.4 101.5 110.4 158.2 REMARK 620 6 ASN A2144 ND2 138.8 71.3 67.0 113.8 48.7 REMARK 620 7 THR A2145 O 86.8 174.0 106.2 97.8 82.1 114.5 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2225 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A2166 OD2 REMARK 620 2 THR A2167 O 115.0 REMARK 620 3 GLU A2169 OE1 118.5 63.1 REMARK 620 4 GLU A2169 OE2 80.7 107.8 49.9 REMARK 620 5 ASN A2183 OD1 139.2 61.8 96.8 140.1 REMARK 620 6 VAL A2184 O 59.2 119.7 176.7 126.8 86.2 REMARK 620 7 GLY A2187 O 95.4 144.9 87.6 58.2 106.5 90.2 REMARK 620 N 1 2 3 4 5 6 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: CA1 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE FOR EGF-LIKE DOMAIN 32. REMARK 800 REMARK 800 SITE_IDENTIFIER: CA2 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE FOR EGF-LIKE DOMAIN 33. REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2224 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2225 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1EMN RELATED DB: PDB DBREF 1EMO A 2124 2205 UNP P35555 FBN1_HUMAN 2124 2205 SEQADV 1EMO ILE A 2158 UNP P35555 THR 2158 CONFLICT SEQRES 1 A 82 SER ALA VAL ASP MET ASP GLU CYS LYS GLU PRO ASP VAL SEQRES 2 A 82 CYS LYS HIS GLY GLN CYS ILE ASN THR ASP GLY SER TYR SEQRES 3 A 82 ARG CYS GLU CYS PRO PHE GLY TYR ILE LEU ALA GLY ASN SEQRES 4 A 82 GLU CYS VAL ASP THR ASP GLU CYS SER VAL GLY ASN PRO SEQRES 5 A 82 CYS GLY ASN GLY THR CYS LYS ASN VAL ILE GLY GLY PHE SEQRES 6 A 82 GLU CYS THR CYS GLU GLU GLY PHE GLU PRO GLY PRO MET SEQRES 7 A 82 MET THR CYS GLU HET CA A2224 1 HET CA A2225 1 HETNAM CA CALCIUM ION FORMUL 2 CA 2(CA 2+) HELIX 1 H1 GLU A 2169 SER A 2171 5 3 SHEET 1 S1 2 GLN A2141 CYS A2142 0 SHEET 2 S1 2 CYS A2151 GLU A2152 -1 N GLU A2152 O GLN A2141 SHEET 1 S2 2 TYR A2157 ALA A2160 0 SHEET 2 S2 2 GLU A2163 ASP A2166 -1 O VAL A2165 N ILE A2158 SHEET 1 S3 2 CYS A2181 ASN A2183 0 SHEET 2 S3 2 PHE A2188 CYS A2190 -1 O GLU A2189 N LYS A2182 SSBOND 1 CYS A 2131 CYS A 2142 1555 1555 2.02 SSBOND 2 CYS A 2137 CYS A 2151 1555 1555 2.02 SSBOND 3 CYS A 2153 CYS A 2164 1555 1555 2.02 SSBOND 4 CYS A 2170 CYS A 2181 1555 1555 2.02 SSBOND 5 CYS A 2176 CYS A 2190 1555 1555 2.01 SSBOND 6 CYS A 2192 CYS A 2204 1555 1555 2.02 LINK OD2 ASP A2127 CA CA A2224 1555 1555 2.53 LINK O MET A2128 CA CA A2224 1555 1555 2.68 LINK OE1 GLU A2130 CA CA A2224 1555 1555 2.63 LINK OE2 GLU A2130 CA CA A2224 1555 1555 2.61 LINK OD1 ASN A2144 CA CA A2224 1555 1555 2.64 LINK ND2 ASN A2144 CA CA A2224 1555 1555 2.65 LINK O THR A2145 CA CA A2224 1555 1555 2.65 LINK OD2 ASP A2166 CA CA A2225 1555 1555 2.45 LINK O THR A2167 CA CA A2225 1555 1555 2.51 LINK OE1 GLU A2169 CA CA A2225 1555 1555 2.47 LINK OE2 GLU A2169 CA CA A2225 1555 1555 2.63 LINK OD1 ASN A2183 CA CA A2225 1555 1555 2.62 LINK O VAL A2184 CA CA A2225 1555 1555 2.59 LINK O GLY A2187 CA CA A2225 1555 1555 2.68 SITE 1 CA1 6 ASP A2127 ASP A2129 GLU A2130 ASN A2144 SITE 2 CA1 6 TYR A2149 CA A2224 SITE 1 CA2 6 ASP A2166 ASP A2168 GLU A2169 ASN A2183 SITE 2 CA2 6 PHE A2188 CA A2225 SITE 1 AC1 6 ASP A2127 MET A2128 GLU A2130 ASN A2144 SITE 2 AC1 6 THR A2145 SER A2148 SITE 1 AC2 6 ASP A2166 THR A2167 GLU A2169 ASN A2183 SITE 2 AC2 6 VAL A2184 GLY A2187 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 - t 27 2 Bytes