Header list of 2a5m.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL PROTEIN 30-JUN-05 2A5M TITLE NMR STRUCTURE OF MURINE GAMMA-S CRYSTALLIN FROM JOINT REFINEMENT WITH TITLE 2 SAXS DATA COMPND MOL_ID: 1; COMPND 2 MOLECULE: GAMMA CRYSTALLIN S; COMPND 3 CHAIN: A; COMPND 4 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 GENE: CRYGS; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET17B KEYWDS SAXS, SMALL-ANGLE X-RAY SCATTERING, ALIGNMENT, DEUTERATION, LIQUID KEYWDS 2 CRYSTAL, PF1, RDC, RESIDUAL DIPOLAR COUPLING, MOLECULAR FRAGMENT KEYWDS 3 REPLACEMENT, MFR, STRUCTURAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.GRISHAEV,J.WU,J.TREWHELLA,A.BAX REVDAT 4 09-MAR-22 2A5M 1 REMARK REVDAT 3 24-FEB-09 2A5M 1 VERSN REVDAT 2 06-DEC-05 2A5M 1 JRNL REVDAT 1 19-JUL-05 2A5M 0 JRNL AUTH A.GRISHAEV,J.WU,J.TREWHELLA,A.BAX JRNL TITL REFINEMENT OF MULTIDOMAIN PROTEIN STRUCTURES BY COMBINATION JRNL TITL 2 OF SOLUTION SMALL-ANGLE X-RAY SCATTERING AND NMR DATA. JRNL REF J.AM.CHEM.SOC. V. 127 16621 2005 JRNL REFN ISSN 0002-7863 JRNL PMID 16305251 JRNL DOI 10.1021/JA054342M REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH Z.WU,F.DELAGLIO,K.WYATT,G.WISTOW,A.BAX REMARK 1 TITL SOLUTION STRUCTURE OF GAMMA-S CRYSTALLIN BY MOLECULAR REMARK 1 TITL 2 FRAGMENT REPLACEMENT NMR REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 WITH AN ADDITIONAL SAXS DATA FITTING REMARK 3 MODULE REMARK 3 AUTHORS : BRUNGER,ADAMS,BONVIN,CLORE,DELANO,GROS,GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: EXPERIMENTAL NMR DATA IS THE SAME AS REMARK 3 THOSE IN THE PDB DEPOSITION 1ZWM. SAXS DATA OVER THE RANGE Q = REMARK 3 0.02 TO 0.22 A-1 WAS FITTED BY AN IN-HOUSE WRITTEN CNS MODULE. REMARK 4 REMARK 4 2A5M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-05. REMARK 100 THE DEPOSITION ID IS D_1000033516. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 291.4 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 25 MM IMIDAZOLE, 10 MM KCL, REMARK 210 0.04% NAN3 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 0.22 MM GAMMA-S CRYSTALLIN, 25 REMARK 210 MM IMIDAZOLE, PH 6.0, 10 MM KCL, REMARK 210 0.04% NAN3, 10 MM DTT, FOR SAXS REMARK 210 DATA. ALL NMR CONDITIONS AS REMARK 210 REPORTED FOR 1ZWM REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX600 WITH PFG-CRYOPROBE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES REMARK 210 SUBMITTED REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: SAXS DATA WAS COLLECTED ON A HOME-BUILT INSTRUMENT USING A REMARK 210 SEALED-SOURCE X-RAY TUBE AND A ONE-DIMENSIONAL POSITION REMARK 210 SENSITIVE DETECTOR. ALL NMR RESTRAINTS WERE TAKEN FROM ENTRY REMARK 210 1ZWM. 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 LYS A 2 98.91 -65.99 REMARK 500 1 THR A 3 -140.47 -104.33 REMARK 500 1 SER A 89 -155.43 -102.51 REMARK 500 1 CYS A 129 147.28 -170.64 REMARK 500 1 GLU A 133 -63.30 -148.03 REMARK 500 1 LYS A 153 35.57 -72.83 REMARK 500 2 THR A 3 -129.03 -138.58 REMARK 500 2 SER A 89 -155.47 -102.99 REMARK 500 2 GLU A 133 -67.39 -146.42 REMARK 500 2 LYS A 153 37.45 -71.64 REMARK 500 3 THR A 3 -141.28 -101.30 REMARK 500 3 SER A 89 -155.40 -102.79 REMARK 500 3 GLU A 133 -68.24 -147.21 REMARK 500 3 ASP A 152 -110.46 -111.38 REMARK 500 3 LYS A 153 31.08 -151.16 REMARK 500 3 LYS A 154 -165.42 -109.73 REMARK 500 4 THR A 3 -141.69 -101.10 REMARK 500 4 SER A 89 -155.00 -103.28 REMARK 500 4 GLU A 133 -64.88 -150.82 REMARK 500 4 ASP A 152 -163.27 -108.50 REMARK 500 4 LYS A 153 40.99 -75.12 REMARK 500 5 THR A 3 -140.06 -107.04 REMARK 500 5 SER A 89 -154.65 -103.77 REMARK 500 5 GLU A 133 -63.00 -147.65 REMARK 500 5 LYS A 153 41.88 -78.53 REMARK 500 6 LYS A 2 101.31 -49.83 REMARK 500 6 THR A 3 -139.02 -106.42 REMARK 500 6 SER A 89 -155.68 -102.75 REMARK 500 6 CYS A 129 144.33 -170.28 REMARK 500 6 GLU A 133 -70.04 -146.83 REMARK 500 6 LYS A 153 38.95 -71.52 REMARK 500 7 THR A 3 -140.70 -102.78 REMARK 500 7 SER A 89 -155.41 -102.74 REMARK 500 7 GLU A 133 -69.79 -146.71 REMARK 500 7 LYS A 153 40.64 -71.67 REMARK 500 8 THR A 3 -130.09 -137.35 REMARK 500 8 SER A 89 -155.43 -102.96 REMARK 500 8 GLU A 133 -58.31 -151.67 REMARK 500 8 ASP A 152 -116.94 -106.91 REMARK 500 8 LYS A 153 26.31 -141.29 REMARK 500 8 LYS A 154 -166.81 -110.35 REMARK 500 9 LYS A 2 97.45 -50.85 REMARK 500 9 THR A 3 -139.31 -104.91 REMARK 500 9 SER A 89 -154.73 -104.02 REMARK 500 9 GLU A 133 -69.10 -147.02 REMARK 500 9 LYS A 153 39.79 -71.65 REMARK 500 10 THR A 3 -129.04 -138.24 REMARK 500 10 GLU A 133 -66.38 -146.97 REMARK 500 10 LYS A 153 36.36 -75.28 REMARK 500 11 THR A 3 -139.00 -106.25 REMARK 500 REMARK 500 THIS ENTRY HAS 98 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1ZWM RELATED DB: PDB REMARK 900 RELATED ID: 1ZWO RELATED DB: PDB REMARK 900 RELATED ID: 1AMM RELATED DB: PDB REMARK 900 RELATED ID: 1HK0 RELATED DB: PDB REMARK 900 RELATED ID: 1A7H RELATED DB: PDB REMARK 900 RELATED ID: 1A45 RELATED DB: PDB REMARK 900 RELATED ID: 1AG4 RELATED DB: PDB REMARK 900 RELATED ID: 1A5D RELATED DB: PDB DBREF 2A5M A 1 177 UNP O35486 CRBS_MOUSE 1 177 SEQRES 1 A 177 SER LYS THR GLY GLY LYS ILE SER PHE TYR GLU ASP ARG SEQRES 2 A 177 ASN PHE GLN GLY ARG ARG TYR ASP CYS ASP CYS ASP CYS SEQRES 3 A 177 ALA ASP PHE ARG SER TYR LEU SER ARG CYS ASN SER ILE SEQRES 4 A 177 ARG VAL GLU GLY GLY THR TRP ALA VAL TYR GLU ARG PRO SEQRES 5 A 177 ASN PHE SER GLY HIS MET TYR ILE LEU PRO GLN GLY GLU SEQRES 6 A 177 TYR PRO GLU TYR GLN ARG TRP MET GLY LEU ASN ASP ARG SEQRES 7 A 177 LEU GLY SER CYS ARG ALA VAL HIS LEU SER SER GLY GLY SEQRES 8 A 177 GLN ALA LYS ILE GLN VAL PHE GLU LYS GLY ASP PHE ASN SEQRES 9 A 177 GLY GLN MET TYR GLU THR THR GLU ASP CYS PRO SER ILE SEQRES 10 A 177 MET GLU GLN PHE HIS LEU ARG GLU ILE HIS SER CYS LYS SEQRES 11 A 177 VAL VAL GLU GLY THR TRP ILE PHE TYR GLU LEU PRO ASN SEQRES 12 A 177 TYR ARG GLY ARG GLN TYR LEU LEU ASP LYS LYS GLU TYR SEQRES 13 A 177 ARG LYS PRO VAL ASP TRP GLY ALA ALA SER PRO ALA ILE SEQRES 14 A 177 GLN SER PHE ARG ARG ILE VAL GLU HELIX 1 1 GLU A 68 MET A 73 5 6 HELIX 2 2 SER A 116 HIS A 122 1 7 HELIX 3 3 LYS A 158 GLY A 163 5 6 SHEET 1 A 4 ARG A 19 CYS A 22 0 SHEET 2 A 4 LYS A 6 TYR A 10 -1 N PHE A 9 O TYR A 20 SHEET 3 A 4 SER A 38 GLY A 43 -1 O ARG A 40 N SER A 8 SHEET 4 A 4 GLY A 64 TYR A 66 -1 O GLY A 64 N VAL A 41 SHEET 1 B 3 SER A 55 LEU A 61 0 SHEET 2 B 3 THR A 45 ARG A 51 -1 N TRP A 46 O LEU A 61 SHEET 3 B 3 SER A 81 VAL A 85 -1 O ARG A 83 N ALA A 47 SHEET 1 C 4 ASN A 104 THR A 110 0 SHEET 2 C 4 ILE A 95 LYS A 100 -1 N LYS A 100 O ASN A 104 SHEET 3 C 4 SER A 128 VAL A 131 -1 O LYS A 130 N GLN A 96 SHEET 4 C 4 GLU A 155 TYR A 156 -1 O TYR A 156 N CYS A 129 SHEET 1 D 3 ARG A 145 LEU A 151 0 SHEET 2 D 3 TRP A 136 LEU A 141 -1 N TRP A 136 O LEU A 151 SHEET 3 D 3 SER A 171 ARG A 174 -1 O SER A 171 N TYR A 139 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 9 2 Bytes