Header list of 1ngl.pdb file
Complete list - 23 20 Bytes
HEADER TRANSPORT PROTEIN 23-FEB-99 1NGL TITLE HUMAN NEUTROPHIL GELATINASE-ASSOCIATED LIPOCALIN (HNGAL), REGULARISED TITLE 2 AVERAGE NMR STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (NGAL); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: MATURE SEQUENCE; COMPND 5 SYNONYM: HNGAL, HNL; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: METHIONINE PRECEDES MATURE PROTEIN SEQUENCE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 CELL: NEUTROPHIL; SOURCE 6 CELLULAR_LOCATION: EXTRACELLULAR MATRIX; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21[DE3]; SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET11A KEYWDS TRANSPORT PROTEIN, MMP-9 COMPONENT, LIPOCALIN EXPDTA SOLUTION NMR AUTHOR M.COLES,T.DIERCKS,B.MUEHLENWEG,S.BARTSCH,V.ZOELZER,H.TSCHESCHE, AUTHOR 2 H.KESSLER REVDAT 5 23-FEB-22 1NGL 1 REMARK REVDAT 4 24-FEB-09 1NGL 1 VERSN REVDAT 3 01-APR-03 1NGL 1 JRNL REVDAT 2 07-JUN-99 1NGL 1 REMARK REVDAT 1 26-MAY-99 1NGL 0 JRNL AUTH M.COLES,T.DIERCKS,B.MUEHLENWEG,S.BARTSCH,V.ZOLZER, JRNL AUTH 2 H.TSCHESCHE,H.KESSLER JRNL TITL THE SOLUTION STRUCTURE AND DYNAMICS OF HUMAN NEUTROPHIL JRNL TITL 2 GELATINASE-ASSOCIATED LIPOCALIN. JRNL REF J.MOL.BIOL. V. 289 139 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10339412 JRNL DOI 10.1006/JMBI.1999.2755 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: NULL REMARK 4 REMARK 4 1NGL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-99. REMARK 100 THE DEPOSITION ID IS D_1000000528. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.1 REMARK 210 IONIC STRENGTH : 50 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-NOESY; 13C-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX750 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: MEAN STRUCTURE. STRUCTURE DETERMINED USING TRIPLE REMARK 210 -RESONANCE NMR SPECTROSCOPY ON 15N AND 13C/15N LABELLED HNGAL. 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 O ASN A 115 H GLN A 118 1.46 REMARK 500 O LYS A 60 H ASP A 62 1.48 REMARK 500 H GLY A 87 O GLU A 92 1.50 REMARK 500 O ALA A 54 H VAL A 70 1.51 REMARK 500 H TYR A 65 O PHE A 84 1.55 REMARK 500 O PHE A 93 H VAL A 109 1.57 REMARK 500 O SER A 157 H GLY A 161 1.58 REMARK 500 H ARG A 73 O LYS A 76 1.58 REMARK 500 H ILE A 56 O THR A 68 1.60 REMARK 500 O ALA A 38 H ILE A 136 1.60 REMARK 500 O LEU A 37 O VAL A 168 2.19 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 SER A 6 75.27 -106.26 REMARK 500 VAL A 17 39.57 -145.04 REMARK 500 GLN A 21 -150.03 -63.11 REMARK 500 ASN A 22 33.03 -85.63 REMARK 500 GLU A 61 38.26 -63.08 REMARK 500 ASP A 62 59.05 -149.06 REMARK 500 LYS A 63 60.20 25.94 REMARK 500 LYS A 75 40.61 -143.06 REMARK 500 ASN A 97 56.10 -151.60 REMARK 500 PRO A 102 -77.03 -76.51 REMARK 500 TYR A 116 -7.89 -49.46 REMARK 500 GLN A 118 -69.01 -141.57 REMARK 500 GLN A 129 -50.15 -19.76 REMARK 500 ASN A 130 39.46 -146.17 REMARK 500 LEU A 145 -143.50 -118.11 REMARK 500 LEU A 162 -159.76 36.91 REMARK 500 PRO A 163 48.41 -94.57 REMARK 500 ASN A 165 -125.33 -141.89 REMARK 500 HIS A 166 55.74 -97.76 REMARK 500 PRO A 170 32.76 -83.02 REMARK 500 PRO A 172 -160.83 -74.09 REMARK 500 ILE A 173 -87.65 -95.53 REMARK 500 REMARK 500 REMARK: NULL DBREF 1NGL A 2 179 UNP P80188 NGAL_HUMAN 21 198 SEQADV 1NGL MET A 1 UNP P80188 SEE REMARK 999 SEQRES 1 A 179 MET GLN ASP SER THR SER ASP LEU ILE PRO ALA PRO PRO SEQRES 2 A 179 LEU SER LYS VAL PRO LEU GLN GLN ASN PHE GLN ASP ASN SEQRES 3 A 179 GLN PHE GLN GLY LYS TRP TYR VAL VAL GLY LEU ALA GLY SEQRES 4 A 179 ASN ALA ILE LEU ARG GLU ASP LYS ASP PRO GLN LYS MET SEQRES 5 A 179 TYR ALA THR ILE TYR GLU LEU LYS GLU ASP LYS SER TYR SEQRES 6 A 179 ASN VAL THR SER VAL LEU PHE ARG LYS LYS LYS CYS ASP SEQRES 7 A 179 TYR TRP ILE ARG THR PHE VAL PRO GLY CYS GLN PRO GLY SEQRES 8 A 179 GLU PHE THR LEU GLY ASN ILE LYS SER TYR PRO GLY LEU SEQRES 9 A 179 THR SER TYR LEU VAL ARG VAL VAL SER THR ASN TYR ASN SEQRES 10 A 179 GLN HIS ALA MET VAL PHE PHE LYS LYS VAL SER GLN ASN SEQRES 11 A 179 ARG GLU TYR PHE LYS ILE THR LEU TYR GLY ARG THR LYS SEQRES 12 A 179 GLU LEU THR SER GLU LEU LYS GLU ASN PHE ILE ARG PHE SEQRES 13 A 179 SER LYS SER LEU GLY LEU PRO GLU ASN HIS ILE VAL PHE SEQRES 14 A 179 PRO VAL PRO ILE ASP GLN CYS ILE ASP GLY HELIX 1 1 LEU A 14 LYS A 16 5 3 HELIX 2 2 ASP A 25 PHE A 28 1 4 HELIX 3 3 SER A 147 GLY A 161 5 15 SHEET 1 A 8 PHE A 93 LEU A 95 0 SHEET 2 A 8 CYS A 77 PRO A 86 -1 N VAL A 85 O THR A 94 SHEET 3 A 8 SER A 64 PHE A 72 -1 N LEU A 71 O ASP A 78 SHEET 4 A 8 ALA A 54 LYS A 60 -1 N LYS A 60 O SER A 64 SHEET 5 A 8 LYS A 31 GLY A 39 -1 N TRP A 32 O THR A 55 SHEET 6 A 8 ARG A 131 GLY A 140 -1 N GLY A 140 O TYR A 33 SHEET 7 A 8 ALA A 120 SER A 128 -1 N SER A 128 O ARG A 131 SHEET 8 A 8 LEU A 104 VAL A 111 -1 N ARG A 110 O PHE A 123 SHEET 1 B 2 LEU A 37 GLY A 39 0 SHEET 2 B 2 HIS A 166 VAL A 168 -1 N VAL A 168 O LEU A 37 SSBOND 1 CYS A 77 CYS A 176 1555 1555 2.02 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
Complete list - 23 20 Bytes