Header list of 2mfn.pdb file
Complete list - r 16 2 Bytes
HEADER CELL ADHESION PROTEIN 11-FEB-98 2MFN TITLE SOLUTION NMR STRUCTURE OF LINKED CELL ATTACHMENT MODULES OF MOUSE TITLE 2 FIBRONECTIN CONTAINING THE RGD AND SYNERGY REGIONS, 10 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: FIBRONECTIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: 184 AMINO ACID FRAGMENT, 9TH AND 10TH TYPE-III REPEATS; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 CELL_LINE: BL21; SOURCE 6 GENE: POTENTIAL; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS; SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PRSET; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: BL21 KEYWDS CELL ADHESION PROTEIN, RGD, EXTRACELLULAR MATRIX EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR V.COPIE,Y.TOMITA,S.K.AKIYAMA,S.AOTA,K.M.YAMADA,R.M.VENABLE, AUTHOR 2 R.W.PASTOR,S.KRUEGER,D.A.TORCHIA REVDAT 3 16-MAR-22 2MFN 1 REMARK REVDAT 2 24-FEB-09 2MFN 1 VERSN REVDAT 1 29-APR-98 2MFN 0 JRNL AUTH V.COPIE,Y.TOMITA,S.K.AKIYAMA,S.AOTA,K.M.YAMADA,R.M.VENABLE, JRNL AUTH 2 R.W.PASTOR,S.KRUEGER,D.A.TORCHIA JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF LINKED CELL ATTACHMENT JRNL TITL 2 MODULES OF MOUSE FIBRONECTIN CONTAINING THE RGD AND SYNERGY JRNL TITL 3 REGIONS: COMPARISON WITH THE HUMAN FIBRONECTIN CRYSTAL JRNL TITL 4 STRUCTURE. JRNL REF J.MOL.BIOL. V. 277 663 1998 JRNL REFN ISSN 0022-2836 JRNL PMID 9533887 JRNL DOI 10.1006/JMBI.1998.1616 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE. REMARK 4 REMARK 4 2MFN 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_1000178351. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 4.2 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE FOR ASSIGNMENT REMARK 210 OF PROTEIN: CBCA(CO)NH; CBCANH; REMARK 210 HBHA(CO)NH; C (CO)NH; H(CCO)NH; REMARK 210 HCCH-TOCSY; HOHAHA; 15N; 13C- REMARK 210 HSQC; 2D; 3D; 4D-NOESY. REMARK 210 QUANTITATIVE J CORRELATION FOR REMARK 210 COUPLING CONSTANTS; HNHA; HNHB; REMARK 210 HAHB; CCO-SED; CN-SED; LRCC; REMARK 210 LRCH. REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX500; AMX500; AMX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : TORSION-ANGLE MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 40 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATIONS GREATER THAN REMARK 210 0.5 A,NO DIHEDRAL ANGLE REMARK 210 RESTRAINT VIOLATIONS > 5, RMSD REMARK 210 FOR BOND DEVIATIONS FROM REMARK 210 IDEALITY < 0.05 A, RMSD FOR REMARK 210 ANGLE DEVIATIONS FROM IDEALITY < REMARK 210 5 AND RMSD FOR IMPROPER ANGLES REMARK 210 DEVIATIONS FROM IDEALITY < 5 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: 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 HG SER A 103 OH TYR A 182 1.32 REMARK 500 O VAL A 140 H GLY A 142 1.38 REMARK 500 O GLY A 130 H ASN A 132 1.42 REMARK 500 OG1 THR A 129 H GLY A 130 1.43 REMARK 500 H THR A 125 O THR A 161 1.50 REMARK 500 H ASN A 63 OH TYR A 68 1.50 REMARK 500 O SER A 133 H VAL A 135 1.57 REMARK 500 H ARG A 123 O TYR A 163 1.57 REMARK 500 OG1 THR A 104 O SER A 107 2.16 REMARK 500 OG SER A 10 OE1 GLN A 88 2.18 REMARK 500 OG1 THR A 14 O SER A 17 2.18 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 6 -153.29 -150.57 REMARK 500 1 PRO A 25 176.15 -59.17 REMARK 500 1 VAL A 91 171.68 -43.47 REMARK 500 1 PRO A 95 -165.97 -58.45 REMARK 500 1 PRO A 115 -162.18 -60.87 REMARK 500 1 THR A 129 -89.10 -21.37 REMARK 500 1 PRO A 134 44.33 -65.91 REMARK 500 1 PRO A 141 44.23 -59.80 REMARK 500 1 ASN A 151 44.98 77.15 REMARK 500 1 THR A 166 -65.30 -108.52 REMARK 500 1 PRO A 172 99.03 -66.34 REMARK 500 2 PRO A 5 72.65 -58.81 REMARK 500 2 THR A 6 -153.73 -79.55 REMARK 500 2 ASN A 76 38.45 -140.49 REMARK 500 2 PRO A 95 -170.37 -58.78 REMARK 500 2 ASP A 97 36.22 72.60 REMARK 500 2 PRO A 115 -160.65 -60.63 REMARK 500 2 THR A 129 -35.39 -28.91 REMARK 500 2 THR A 166 -65.38 -123.13 REMARK 500 3 PRO A 5 79.91 -59.04 REMARK 500 3 THR A 6 -159.56 -85.90 REMARK 500 3 VAL A 91 171.26 -37.21 REMARK 500 3 PRO A 95 -158.61 -61.70 REMARK 500 3 ASP A 97 35.08 74.96 REMARK 500 3 PRO A 115 -163.42 -63.31 REMARK 500 3 PRO A 141 50.56 -58.87 REMARK 500 3 ARG A 168 -109.98 -114.87 REMARK 500 3 PRO A 172 82.61 -65.74 REMARK 500 3 LYS A 176 100.10 -39.07 REMARK 500 4 THR A 6 -144.36 -156.20 REMARK 500 4 PRO A 25 -179.50 -59.79 REMARK 500 4 GLU A 39 -97.27 -72.66 REMARK 500 4 PRO A 45 95.47 -61.75 REMARK 500 4 VAL A 91 166.62 -45.72 REMARK 500 4 PRO A 115 -178.22 -60.22 REMARK 500 4 PRO A 134 87.15 -57.21 REMARK 500 4 PRO A 172 98.57 -62.06 REMARK 500 5 THR A 6 -150.65 -143.54 REMARK 500 5 PRO A 25 -164.57 -61.58 REMARK 500 5 VAL A 91 155.97 -41.71 REMARK 500 5 ASP A 93 14.61 58.62 REMARK 500 5 PRO A 115 -166.33 -60.03 REMARK 500 5 THR A 129 157.95 -33.08 REMARK 500 5 ASN A 151 49.74 71.69 REMARK 500 5 PRO A 172 87.66 -64.02 REMARK 500 6 THR A 6 -155.75 -120.00 REMARK 500 6 SER A 11 -162.32 -172.75 REMARK 500 6 PRO A 25 179.28 -58.69 REMARK 500 6 VAL A 91 170.21 -55.33 REMARK 500 6 PRO A 95 81.31 -63.68 REMARK 500 REMARK 500 THIS ENTRY HAS 90 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 A 26 0.10 SIDE CHAIN REMARK 500 1 ARG A 35 0.32 SIDE CHAIN REMARK 500 1 ARG A 44 0.20 SIDE CHAIN REMARK 500 1 ARG A 46 0.31 SIDE CHAIN REMARK 500 1 ARG A 54 0.18 SIDE CHAIN REMARK 500 1 ARG A 78 0.17 SIDE CHAIN REMARK 500 1 ARG A 96 0.31 SIDE CHAIN REMARK 500 1 ARG A 123 0.24 SIDE CHAIN REMARK 500 1 ARG A 168 0.30 SIDE CHAIN REMARK 500 2 ARG A 26 0.18 SIDE CHAIN REMARK 500 2 ARG A 35 0.14 SIDE CHAIN REMARK 500 2 ARG A 44 0.24 SIDE CHAIN REMARK 500 2 ARG A 46 0.09 SIDE CHAIN REMARK 500 2 ARG A 49 0.20 SIDE CHAIN REMARK 500 2 ARG A 54 0.16 SIDE CHAIN REMARK 500 2 ARG A 78 0.13 SIDE CHAIN REMARK 500 2 ARG A 120 0.26 SIDE CHAIN REMARK 500 2 ARG A 123 0.21 SIDE CHAIN REMARK 500 2 ARG A 168 0.18 SIDE CHAIN REMARK 500 3 ARG A 26 0.18 SIDE CHAIN REMARK 500 3 ARG A 35 0.22 SIDE CHAIN REMARK 500 3 ARG A 44 0.18 SIDE CHAIN REMARK 500 3 ARG A 46 0.32 SIDE CHAIN REMARK 500 3 ARG A 54 0.24 SIDE CHAIN REMARK 500 3 ARG A 78 0.26 SIDE CHAIN REMARK 500 3 ARG A 96 0.18 SIDE CHAIN REMARK 500 3 ARG A 120 0.30 SIDE CHAIN REMARK 500 3 ARG A 123 0.27 SIDE CHAIN REMARK 500 4 ARG A 46 0.18 SIDE CHAIN REMARK 500 4 ARG A 49 0.20 SIDE CHAIN REMARK 500 4 ARG A 54 0.12 SIDE CHAIN REMARK 500 4 ARG A 78 0.31 SIDE CHAIN REMARK 500 4 ARG A 96 0.32 SIDE CHAIN REMARK 500 4 ARG A 120 0.28 SIDE CHAIN REMARK 500 4 ARG A 123 0.15 SIDE CHAIN REMARK 500 4 ARG A 168 0.14 SIDE CHAIN REMARK 500 5 ARG A 26 0.24 SIDE CHAIN REMARK 500 5 ARG A 35 0.30 SIDE CHAIN REMARK 500 5 ARG A 44 0.17 SIDE CHAIN REMARK 500 5 ARG A 46 0.12 SIDE CHAIN REMARK 500 5 ARG A 49 0.32 SIDE CHAIN REMARK 500 5 ARG A 54 0.27 SIDE CHAIN REMARK 500 5 ARG A 78 0.26 SIDE CHAIN REMARK 500 5 ARG A 96 0.09 SIDE CHAIN REMARK 500 5 ARG A 120 0.26 SIDE CHAIN REMARK 500 5 ARG A 123 0.20 SIDE CHAIN REMARK 500 5 ARG A 168 0.32 SIDE CHAIN REMARK 500 6 ARG A 26 0.31 SIDE CHAIN REMARK 500 6 ARG A 35 0.31 SIDE CHAIN REMARK 500 6 ARG A 44 0.26 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 95 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: RGD REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CELL ADHESION SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: SGY REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CELL ADHESION SYNERGETIC SITE. DBREF 2MFN A 1 184 UNP P11276 FINC_MOUSE 1447 1630 SEQRES 1 A 184 GLY LEU ASP SER PRO THR GLY PHE ASP SER SER ASP ILE SEQRES 2 A 184 THR ALA ASN SER PHE THR VAL HIS TRP VAL ALA PRO ARG SEQRES 3 A 184 ALA PRO ILE THR GLY TYR ILE ILE ARG HIS HIS ALA GLU SEQRES 4 A 184 HIS SER VAL GLY ARG PRO ARG GLN ASP ARG VAL PRO PRO SEQRES 5 A 184 SER ARG ASN SER ILE THR LEU THR ASN LEU ASN PRO GLY SEQRES 6 A 184 THR GLU TYR VAL VAL SER ILE ILE ALA VAL ASN GLY ARG SEQRES 7 A 184 GLU GLU SER PRO PRO LEU ILE GLY GLN GLN ALA THR VAL SEQRES 8 A 184 SER ASP ILE PRO ARG ASP LEU GLU VAL ILE ALA SER THR SEQRES 9 A 184 PRO THR SER LEU LEU ILE SER TRP GLU PRO PRO ALA VAL SEQRES 10 A 184 SER VAL ARG TYR TYR ARG ILE THR TYR GLY GLU THR GLY SEQRES 11 A 184 GLY ASN SER PRO VAL GLN GLU PHE THR VAL PRO GLY SER SEQRES 12 A 184 LYS SER THR ALA THR ILE ASN ASN ILE LYS PRO GLY ALA SEQRES 13 A 184 ASP TYR THR ILE THR LEU TYR ALA VAL THR GLY ARG GLY SEQRES 14 A 184 ASP SER PRO ALA SER SER LYS PRO VAL SER ILE ASN TYR SEQRES 15 A 184 LYS THR SHEET 1 A 3 SER A 56 LEU A 59 0 SHEET 2 A 3 PHE A 18 HIS A 21 -1 N VAL A 20 O ILE A 57 SHEET 3 A 3 ASP A 9 ILE A 13 -1 N ASP A 12 O THR A 19 SHEET 1 B 4 ARG A 46 VAL A 50 0 SHEET 2 B 4 GLY A 31 ALA A 38 -1 N HIS A 36 O ARG A 46 SHEET 3 B 4 THR A 66 VAL A 75 -1 N VAL A 75 O GLY A 31 SHEET 4 B 4 LEU A 84 THR A 90 -1 N THR A 90 O THR A 66 SHEET 1 C 3 THR A 146 ILE A 149 0 SHEET 2 C 3 SER A 107 SER A 111 -1 N ILE A 110 O ALA A 147 SHEET 3 C 3 GLU A 99 THR A 104 -1 N THR A 104 O SER A 107 SHEET 1 D 4 GLN A 136 VAL A 140 0 SHEET 2 D 4 TYR A 121 TYR A 126 -1 N TYR A 126 O GLN A 136 SHEET 3 D 4 ASP A 157 VAL A 165 -1 N VAL A 165 O TYR A 121 SHEET 4 D 4 VAL A 178 LYS A 183 -1 N TYR A 182 O TYR A 158 SITE 1 RGD 3 ARG A 168 GLY A 169 ASP A 170 SITE 1 SGY 5 PRO A 51 PRO A 52 SER A 53 ARG A 54 SITE 2 SGY 5 ASN A 55 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 16 2 Bytes