Header list of 1xxe.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 04-NOV-04 1XXE
TITLE RDC REFINED SOLUTION STRUCTURE OF THE AALPXC/TU-514 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-3-O-[3-HYDROXYMYRISTOYL] N-ACETYLGLUCOSAMINE
COMPND 3 DEACETYLASE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: UDP-3-O-ACYL-GLCNAC DEACETYLASE;
COMPND 6 EC: 3.5.1.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: COMPLEXED WITH TU-514
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 GENE: LPXC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS LPXC; TU-514; LPS; LIPID A; LIPOPOLYSACCHARIDE UDP-3-O-ACYL-N-
KEYWDS 2 ACETYLGLUCOSAMINE DEACETYLASE; METALLOAMIDASE; ZINC METALLOAMIDASE,
KEYWDS 3 HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR B.E.COGGINS,A.L.MCCLERREN,L.JIANG,X.LI,J.RUDOLPH,O.HINDSGAUL,
AUTHOR 2 C.R.H.RAETZ,P.ZHOU
REVDAT 4 02-MAR-22 1XXE 1 REMARK LINK
REVDAT 3 24-FEB-09 1XXE 1 VERSN
REVDAT 2 08-FEB-05 1XXE 1 JRNL
REVDAT 1 23-NOV-04 1XXE 0
SPRSDE 23-NOV-04 1XXE 1NZT
JRNL AUTH B.E.COGGINS,A.L.MCCLERREN,L.JIANG,X.LI,J.RUDOLPH,
JRNL AUTH 2 O.HINDSGAUL,C.R.H.RAETZ,P.ZHOU
JRNL TITL REFINED SOLUTION STRUCTURE OF THE LPXC-TU-514 COMPLEX AND
JRNL TITL 2 PK(A) ANALYSIS OF AN ACTIVE SITE HISTIDINE: INSIGHTS INTO
JRNL TITL 3 THE MECHANISM AND INHIBITOR DESIGN
JRNL REF BIOCHEMISTRY V. 44 1114 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15667205
JRNL DOI 10.1021/BI047820Z
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, XPLOR-NIH 2.9.7
REMARK 3 AUTHORS : GUNTERT P., MUMENTHALER C., WUTHRICH K. (DYANA),
REMARK 3 SCHWIETERS C.D., KUSZEWSKI J.J., TJANDRA N.,
REMARK 3 MARIUS CLORE G. (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XXE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030875.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 323
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM U-15N/13C AALPXC/TU-514;
REMARK 210 0.5 MM DEUTERATED, 15N/13C, VIL-
REMARK 210 METHYL PROTONATED AALPXC WITH TU-
REMARK 210 514; 13C-TU514/15N AALPXC; 0.5
REMARK 210 MM U-15N AALPXC/TU-514
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; RDC; HNCO-
REMARK 210 BASED RDC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-25
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 ARG A 271
REMARK 465 ASP A 272
REMARK 465 LEU A 273
REMARK 465 PRO A 274
REMARK 465 HIS A 275
REMARK 465 LEU A 276
REMARK 465 PRO A 277
REMARK 465 SER A 278
REMARK 465 VAL A 279
REMARK 465 GLN A 280
REMARK 465 ALA A 281
REMARK 465 LEU A 282
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 HIS A 50 H VAL A 53 1.44
REMARK 500 OD1 ASN A 221 HH21 ARG A 225 1.52
REMARK 500 OE2 GLU A 168 HZ1 LYS A 243 1.52
REMARK 500 H LEU A 147 OE2 GLU A 168 1.55
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 GLU A 33 152.20 -47.68
REMARK 500 1 ASN A 57 -154.26 -166.68
REMARK 500 1 LEU A 99 -126.13 57.59
REMARK 500 1 GLN A 117 -166.69 -108.29
REMARK 500 1 ASN A 118 70.70 -116.73
REMARK 500 1 ASP A 134 147.99 -174.17
REMARK 500 1 ASP A 209 16.16 -147.76
REMARK 500 1 GLU A 220 -16.24 -46.50
REMARK 500 2 ASN A 57 -153.89 -166.63
REMARK 500 2 HIS A 58 -11.40 -48.59
REMARK 500 2 THR A 71 70.35 52.41
REMARK 500 2 THR A 85 -74.63 -104.28
REMARK 500 2 LEU A 99 -113.49 58.35
REMARK 500 2 GLN A 117 -161.19 -102.66
REMARK 500 2 ASN A 157 -167.97 -70.43
REMARK 500 2 ASP A 209 10.39 -149.96
REMARK 500 2 GLU A 220 -16.67 -45.47
REMARK 500 3 LYS A 41 126.69 -176.06
REMARK 500 3 ASN A 57 -154.32 -166.00
REMARK 500 3 HIS A 58 -12.16 -48.32
REMARK 500 3 THR A 85 -76.68 -106.34
REMARK 500 3 LEU A 99 -105.68 55.32
REMARK 500 3 SER A 102 -166.78 -123.98
REMARK 500 3 GLU A 120 167.40 -47.88
REMARK 500 3 ASN A 157 -166.64 -70.15
REMARK 500 3 GLU A 220 -10.15 -49.34
REMARK 500 3 ASN A 221 35.95 -143.11
REMARK 500 4 LYS A 41 143.75 -170.70
REMARK 500 4 GLU A 51 -15.62 -45.26
REMARK 500 4 ASN A 57 -154.71 -166.47
REMARK 500 4 HIS A 58 -11.95 -48.03
REMARK 500 4 GLU A 83 60.72 63.41
REMARK 500 4 LEU A 99 -111.72 55.24
REMARK 500 4 SER A 102 -166.78 -109.93
REMARK 500 4 GLN A 117 -163.03 -103.86
REMARK 500 4 ASP A 134 137.93 -175.26
REMARK 500 4 ASN A 157 -169.40 -73.74
REMARK 500 4 ASP A 209 11.44 -152.56
REMARK 500 4 LEU A 269 -84.39 -57.36
REMARK 500 5 LYS A 41 139.46 -170.00
REMARK 500 5 GLU A 51 -16.33 -45.55
REMARK 500 5 ASN A 57 -154.30 -166.07
REMARK 500 5 HIS A 58 -12.10 -47.81
REMARK 500 5 LEU A 99 -110.87 57.06
REMARK 500 5 SER A 102 -168.84 -119.04
REMARK 500 5 ASN A 113 32.18 -144.37
REMARK 500 5 GLN A 117 -162.36 -105.41
REMARK 500 5 GLU A 135 19.74 56.61
REMARK 500 5 ASN A 157 -169.94 -76.35
REMARK 500 5 ASP A 209 10.12 -150.49
REMARK 500
REMARK 500 THIS ENTRY HAS 279 RAMACHANDRAN OUTLIERS.
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 ZN A 319 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 74 NE2
REMARK 620 2 HIS A 226 NE2 76.1
REMARK 620 3 ASP A 230 OD2 81.1 85.5
REMARK 620 4 TUX A 320 OYH 104.8 116.1 158.3
REMARK 620 5 TUX A 320 OXH 81.0 155.0 100.8 60.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TUX A 320
DBREF 1XXE A 1 282 UNP O67648 LPXC_AQUAE 1 282
SEQRES 1 A 282 MET GLY LEU GLU LYS THR VAL LYS GLU LYS LEU SER PHE
SEQRES 2 A 282 GLU GLY VAL GLY ILE HIS THR GLY GLU TYR SER LYS LEU
SEQRES 3 A 282 ILE ILE HIS PRO GLU LYS GLU GLY THR GLY ILE ARG PHE
SEQRES 4 A 282 PHE LYS ASN GLY VAL TYR ILE PRO ALA ARG HIS GLU PHE
SEQRES 5 A 282 VAL VAL HIS THR ASN HIS SER THR ASP LEU GLY PHE LYS
SEQRES 6 A 282 GLY GLN ARG ILE LYS THR VAL GLU HIS ILE LEU SER VAL
SEQRES 7 A 282 LEU HIS LEU LEU GLU ILE THR ASN VAL THR ILE GLU VAL
SEQRES 8 A 282 ILE GLY ASN GLU ILE PRO ILE LEU ASP GLY SER GLY TRP
SEQRES 9 A 282 GLU PHE TYR GLU ALA ILE ARG LYS ASN ILE LEU ASN GLN
SEQRES 10 A 282 ASN ARG GLU ILE ASP TYR PHE VAL VAL GLU GLU PRO ILE
SEQRES 11 A 282 ILE VAL GLU ASP GLU GLY ARG LEU ILE LYS ALA GLU PRO
SEQRES 12 A 282 SER ASP THR LEU GLU VAL THR TYR GLU GLY GLU PHE LYS
SEQRES 13 A 282 ASN PHE LEU GLY ARG GLN LYS PHE THR PHE VAL GLU GLY
SEQRES 14 A 282 ASN GLU GLU GLU ILE VAL LEU ALA ARG THR PHE CYS PHE
SEQRES 15 A 282 ASP TRP GLU ILE GLU HIS ILE LYS LYS VAL GLY LEU GLY
SEQRES 16 A 282 LYS GLY GLY SER LEU LYS ASN THR LEU VAL LEU GLY LYS
SEQRES 17 A 282 ASP LYS VAL TYR ASN PRO GLU GLY LEU ARG TYR GLU ASN
SEQRES 18 A 282 GLU PRO VAL ARG HIS LYS VAL PHE ASP LEU ILE GLY ASP
SEQRES 19 A 282 LEU TYR LEU LEU GLY SER PRO VAL LYS GLY LYS PHE TYR
SEQRES 20 A 282 SER PHE ARG GLY GLY HIS SER LEU ASN VAL LYS LEU VAL
SEQRES 21 A 282 LYS GLU LEU ALA LYS LYS GLN LYS LEU THR ARG ASP LEU
SEQRES 22 A 282 PRO HIS LEU PRO SER VAL GLN ALA LEU
HET ZN A 319 1
HET TUX A 320 71
HETNAM ZN ZINC ION
HETNAM TUX 1,5-ANHYDRO-2-C-(CARBOXYMETHYL-N-HYDROXYAMIDE)-2-DEOXY-
HETNAM 2 TUX 3-O-MYRISTOYL-D-GLUCITOL
HETSYN TUX TU-514
FORMUL 2 ZN ZN 2+
FORMUL 3 TUX C22 H41 N O7
HELIX 1 1 GLU A 73 LEU A 82 1 10
HELIX 2 2 GLY A 103 LYS A 112 1 10
HELIX 3 3 GLU A 171 ILE A 174 5 4
HELIX 4 4 ASP A 183 LYS A 191 1 9
HELIX 5 5 GLU A 222 LEU A 235 1 14
HELIX 6 6 HIS A 253 LYS A 266 1 14
SHEET 1 A 2 LYS A 5 VAL A 7 0
SHEET 2 A 2 ILE A 114 ASN A 116 -1 O LEU A 115 N THR A 6
SHEET 1 B 5 LEU A 11 VAL A 16 0
SHEET 2 B 5 TYR A 23 PRO A 30 -1 O ILE A 28 N LEU A 11
SHEET 3 B 5 ASN A 86 ILE A 92 -1 O GLU A 90 N ILE A 27
SHEET 4 B 5 GLY A 36 LYS A 41 1 N ARG A 38 O ILE A 89
SHEET 5 B 5 VAL A 44 PRO A 47 -1 O ILE A 46 N PHE A 39
SHEET 1 C 3 VAL A 53 THR A 56 0
SHEET 2 C 3 THR A 60 PHE A 64 -1 O ASP A 61 N VAL A 54
SHEET 3 C 3 GLN A 67 ILE A 69 -1 O ILE A 69 N LEU A 62
SHEET 1 D 2 PHE A 124 VAL A 125 0
SHEET 2 D 2 VAL A 242 LYS A 243 1 O LYS A 243 N PHE A 124
SHEET 1 E 5 ILE A 130 ASP A 134 0
SHEET 2 E 5 ARG A 137 GLU A 142 -1 O ARG A 137 N ASP A 134
SHEET 3 E 5 LYS A 245 PHE A 249 -1 O LYS A 245 N GLU A 142
SHEET 4 E 5 GLU A 148 GLU A 154 1 N GLU A 148 O PHE A 246
SHEET 5 E 5 ARG A 161 VAL A 167 -1 O PHE A 166 N VAL A 149
SHEET 1 F 2 PHE A 180 PHE A 182 0
SHEET 2 F 2 LEU A 204 LEU A 206 1 O LEU A 206 N CYS A 181
LINK NE2 HIS A 74 ZN ZN A 319 1555 1555 2.51
LINK NE2 HIS A 226 ZN ZN A 319 1555 1555 2.51
LINK OD2 ASP A 230 ZN ZN A 319 1555 1555 2.45
LINK ZN ZN A 319 OYH TUX A 320 1555 1555 2.63
LINK ZN ZN A 319 OXH TUX A 320 1555 1555 2.67
SITE 1 AC1 5 HIS A 74 THR A 179 HIS A 226 ASP A 230
SITE 2 AC1 5 TUX A 320
SITE 1 AC2 15 HIS A 58 SER A 59 GLU A 73 HIS A 74
SITE 2 AC2 15 THR A 179 PHE A 180 CYS A 181 GLU A 185
SITE 3 AC2 15 ILE A 186 ILE A 189 GLY A 195 GLY A 198
SITE 4 AC2 15 TYR A 212 LYS A 227 ZN A 319
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 2 2 Bytes