Header list of 1k91.pdb file
Complete list - 23 20 Bytes
HEADER METAL TRANSPORT 26-OCT-01 1K91 TITLE SOLUTION STRUCTURE OF CALRETICULIN P-DOMAIN SUBDOMAIN (RESIDUES 221- TITLE 2 256) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALRETICULIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: P-DOMAIN, RESIDUES 221-256; COMPND 5 SYNONYM: CRP55; CALREGULIN; HACBP; ERP60; CALBP; CALCIUM-BINDING COMPND 6 PROTEIN 3; CABP3; COMPND 7 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS HAIRPIN, METAL TRANSPORT EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR L.ELLGAARD,P.BETTENDORFF,D.BRAUN,T.HERRMANN,F.FIORITO,P.GUNTERT, AUTHOR 2 A.HELENIUS,K.WUTHRICH REVDAT 3 23-FEB-22 1K91 1 REMARK SEQADV REVDAT 2 24-FEB-09 1K91 1 VERSN REVDAT 1 12-OCT-02 1K91 0 JRNL AUTH L.ELLGAARD,P.BETTENDORFF,D.BRAUN,T.HERRMANN,F.FIORITO, JRNL AUTH 2 I.JELESAROV,P.GUNTERT,A.HELENIUS,K.WUTHRICH JRNL TITL NMR STRUCTURES OF 36 AND 73-RESIDUE FRAGMENTS OF THE JRNL TITL 2 CALRETICULIN P-DOMAIN JRNL REF J.MOL.BIOL. V. 322 773 2002 JRNL REFN ISSN 0022-2836 JRNL PMID 12270713 JRNL DOI 10.1016/S0022-2836(02)00812-4 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, DYANA 1.82 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1K91 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-01. REMARK 100 THE DEPOSITION ID IS D_1000014711. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 280 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 25 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 5.3 MM CALRETICULIN P-DOMAIN REMARK 210 SUBDOMAIN; 25 MM NACL; 50 MM REMARK 210 SODIUM PHOSPHATE BUFFER;90% H20 REMARK 210 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY; E-COSY; 2D REMARK 210 TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.82 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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 LYS A 232 121.89 -34.39 REMARK 500 1 PRO A 247 -170.80 -68.41 REMARK 500 3 MET A 240 -70.29 -90.57 REMARK 500 3 PRO A 247 -179.12 -66.62 REMARK 500 3 GLU A 253 81.59 -152.30 REMARK 500 3 LYS A 255 -61.60 -133.86 REMARK 500 4 ASP A 241 -80.33 -81.15 REMARK 500 5 ASP A 235 53.10 -92.01 REMARK 500 5 MET A 240 -65.04 -91.37 REMARK 500 7 ASP A 237 74.15 -119.95 REMARK 500 7 MET A 240 -65.04 -109.53 REMARK 500 7 PRO A 247 -178.55 -60.25 REMARK 500 7 GLU A 253 47.82 -155.24 REMARK 500 8 ASP A 237 79.13 -115.30 REMARK 500 8 ASP A 241 -75.84 -115.17 REMARK 500 8 PRO A 247 -174.60 -67.15 REMARK 500 8 GLU A 253 79.89 -152.97 REMARK 500 8 LYS A 255 -83.67 -136.60 REMARK 500 9 LYS A 232 126.54 -37.37 REMARK 500 9 ASP A 241 -74.52 -106.99 REMARK 500 9 PRO A 247 -174.96 -66.53 REMARK 500 10 MET A 240 -62.79 -99.63 REMARK 500 10 GLU A 253 48.83 -150.15 REMARK 500 10 LYS A 255 -58.11 -141.12 REMARK 500 11 PRO A 247 -167.28 -73.91 REMARK 500 12 MET A 240 -67.52 -90.18 REMARK 500 12 PRO A 247 -177.56 -69.83 REMARK 500 13 ASP A 235 33.38 -86.63 REMARK 500 13 MET A 240 -63.80 -91.42 REMARK 500 13 PRO A 247 -175.97 -62.34 REMARK 500 13 PRO A 252 3.88 -69.90 REMARK 500 13 GLU A 253 82.80 -161.23 REMARK 500 14 LYS A 232 142.70 -31.39 REMARK 500 14 ASP A 235 36.45 -73.72 REMARK 500 14 GLU A 238 1.25 -65.14 REMARK 500 14 ASP A 241 -76.18 -83.21 REMARK 500 14 PRO A 247 -175.04 -68.52 REMARK 500 14 LYS A 255 -64.13 -126.86 REMARK 500 15 LYS A 232 151.30 -45.85 REMARK 500 15 ASP A 235 33.76 -84.94 REMARK 500 15 MET A 240 -64.36 -93.07 REMARK 500 15 PRO A 247 -177.46 -63.69 REMARK 500 15 GLU A 253 -58.74 -146.23 REMARK 500 15 TYR A 254 151.61 56.37 REMARK 500 15 LYS A 255 -36.18 -141.37 REMARK 500 16 ASP A 235 33.77 -82.40 REMARK 500 16 MET A 240 -65.75 -100.51 REMARK 500 16 PRO A 247 -173.64 -69.47 REMARK 500 16 GLU A 253 26.57 -150.20 REMARK 500 17 PRO A 247 -173.35 -69.76 REMARK 500 REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LYS A 255 GLY A 256 2 135.52 REMARK 500 GLU A 253 TYR A 254 3 147.31 REMARK 500 LYS A 255 GLY A 256 4 147.31 REMARK 500 GLY A 220 LYS A 221 19 148.47 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 20 TYR A 254 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1HHN RELATED DB: PDB REMARK 900 CALRETICULIN P-DOMAIN REMARK 900 RELATED ID: 1K9C RELATED DB: PDB REMARK 900 CALRETICULIN P-DOMAIN (RESIDUES 189-261) DBREF 1K91 A 221 256 UNP P18418 CRTC_RAT 242 277 SEQADV 1K91 GLY A 220 UNP P18418 CLONING ARTIFACT SEQRES 1 A 37 GLY LYS PRO GLU HIS ILE PRO ASP PRO ASP ALA LYS LYS SEQRES 2 A 37 PRO GLU ASP TRP ASP GLU GLU MET ASP GLY GLU TRP GLU SEQRES 3 A 37 PRO PRO VAL ILE GLN ASN PRO GLU TYR LYS GLY HELIX 1 1 ASP A 237 GLY A 242 1 6 SHEET 1 A 2 HIS A 224 PRO A 226 0 SHEET 2 A 2 VAL A 248 GLN A 250 -1 O ILE A 249 N ILE A 225 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 - 23 20 Bytes