HEADER HYDROLASE 13-JUL-05 2CZN
TITLE SOLUTION STRUCTURE OF THE CHITIN-BINDING DOMAIN OF HYPERTHERMOPHILIC
TITLE 2 CHITINASE FROM PYROCOCCUS FURIOSUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHITINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CHITIN BINDING DOMAIN;
COMPND 5 EC: 3.2.1.14;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET32
KEYWDS CHITIN BINDING, PYROCOCCUS FURIOSUS, CHITINASE, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 38
AUTHOR T.UEGAKI,T.IKEGAMI,T.NAKAMURA,Y.HAGIHARA,S.MINE,T.INOUE,H.MATSUMURA,
AUTHOR 2 M.ATAKA,K.ISHIKAWA
REVDAT 4 09-MAR-22 2CZN 1 REMARK SEQADV
REVDAT 3 26-MAY-09 2CZN 1 JRNL
REVDAT 2 24-FEB-09 2CZN 1 VERSN
REVDAT 1 18-JUL-06 2CZN 0
JRNL AUTH T.NAKAMURA,S.MINE,Y.HAGIHARA,K.ISHIKAWA,T.IKEGAMI,K.UEGAKI
JRNL TITL TERTIARY STRUCTURE AND CARBOHYDRATE RECOGNITION BY THE
JRNL TITL 2 CHITIN-BINDING DOMAIN OF A HYPERTHERMOPHILIC CHITINASE FROM
JRNL TITL 3 PYROCOCCUS FURIOSUS.
JRNL REF J.MOL.BIOL. V. 381 670 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18582475
JRNL DOI 10.1016/J.JMB.2008.06.006
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.841, X-PLOR 3.841
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CZN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000024804.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : 25MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : UNIFORM (RANDOM) LABELING WITH
REMARK 210 15N; NON LABELING; UNIFORM
REMARK 210 (RANDOM) LABELING WITH 13C, 15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, SPARKY
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 38
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY, STRUCTURES WITH THE
REMARK 210 LEAST RESTRAINT VIOLATIONS,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 ILE A 353 H GLN A 356 1.50
REMARK 500 H ILE A 353 O GLN A 356 1.51
REMARK 500 H GLY A 305 O ILE A 337 1.52
REMARK 500 H ALA A 299 O LYS A 345 1.55
REMARK 500 H LEU A 298 O GLY A 317 1.55
REMARK 500 H LEU A 286 O PRO A 330 1.56
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 SER A 264 74.33 179.32
REMARK 500 1 ASP A 287 34.87 -89.80
REMARK 500 1 PRO A 300 77.28 -67.82
REMARK 500 1 ALA A 310 144.33 -174.98
REMARK 500 1 ASN A 316 82.33 57.43
REMARK 500 1 VAL A 324 -125.67 -64.39
REMARK 500 1 ASN A 354 32.35 39.17
REMARK 500 2 SER A 264 96.18 179.40
REMARK 500 2 ASP A 287 39.13 -89.04
REMARK 500 2 PRO A 300 84.59 -68.73
REMARK 500 2 ALA A 310 140.68 -174.08
REMARK 500 2 ASN A 316 89.42 58.50
REMARK 500 2 VAL A 324 -117.55 -66.80
REMARK 500 2 ASN A 327 33.21 -87.43
REMARK 500 2 PRO A 341 -158.75 -68.86
REMARK 500 2 ASP A 344 140.45 66.85
REMARK 500 2 ASN A 354 37.56 38.94
REMARK 500 3 VAL A 263 29.51 -140.31
REMARK 500 3 SER A 264 76.94 178.96
REMARK 500 3 ASP A 287 36.64 -89.79
REMARK 500 3 ALA A 299 176.00 -56.47
REMARK 500 3 PRO A 300 79.87 -68.99
REMARK 500 3 ALA A 310 148.84 -174.57
REMARK 500 3 ASN A 316 90.92 66.23
REMARK 500 3 VAL A 324 -120.37 -64.29
REMARK 500 3 ASN A 327 38.67 -90.96
REMARK 500 3 PRO A 341 -158.28 -71.44
REMARK 500 3 ASP A 344 134.93 65.77
REMARK 500 3 ASN A 354 31.22 38.36
REMARK 500 4 SER A 264 97.69 179.44
REMARK 500 4 ASP A 287 34.59 -94.04
REMARK 500 4 ASP A 291 97.02 -64.88
REMARK 500 4 PRO A 300 83.20 -67.24
REMARK 500 4 ALA A 310 143.41 -174.27
REMARK 500 4 ASN A 316 92.25 60.86
REMARK 500 4 VAL A 324 -129.37 -73.22
REMARK 500 4 PRO A 341 -151.70 -68.01
REMARK 500 5 SER A 264 55.43 168.49
REMARK 500 5 ASP A 287 31.28 -91.64
REMARK 500 5 PRO A 300 84.61 -68.40
REMARK 500 5 ALA A 310 145.44 -175.90
REMARK 500 5 ASN A 316 91.06 58.52
REMARK 500 5 VAL A 324 -113.89 -64.12
REMARK 500 5 PRO A 341 -169.42 -72.14
REMARK 500 5 ASP A 344 140.81 61.10
REMARK 500 6 SER A 264 102.85 -163.24
REMARK 500 6 ASP A 287 36.02 -91.94
REMARK 500 6 PRO A 300 79.06 -68.24
REMARK 500 6 ALA A 310 142.56 -174.47
REMARK 500 6 ASN A 316 77.50 -160.93
REMARK 500
REMARK 500 THIS ENTRY HAS 362 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2CZN A 258 358 UNP Q8U1H5 Q8U1H5_PYRFU 258 358
SEQADV 2CZN GLY A 256 UNP Q8U1H5 EXPRESSION TAG
SEQADV 2CZN PRO A 257 UNP Q8U1H5 EXPRESSION TAG
SEQRES 1 A 103 GLY PRO THR THR PRO VAL PRO VAL SER GLY SER LEU GLU
SEQRES 2 A 103 VAL LYS VAL ASN ASP TRP GLY SER GLY ALA GLU TYR ASP
SEQRES 3 A 103 VAL THR LEU ASN LEU ASP GLY GLN TYR ASP TRP THR VAL
SEQRES 4 A 103 LYS VAL LYS LEU ALA PRO GLY ALA THR VAL GLY SER PHE
SEQRES 5 A 103 TRP SER ALA ASN LYS GLN GLU GLY ASN GLY TYR VAL ILE
SEQRES 6 A 103 PHE THR PRO VAL SER TRP ASN LYS GLY PRO THR ALA THR
SEQRES 7 A 103 PHE GLY PHE ILE VAL ASN GLY PRO GLN GLY ASP LYS VAL
SEQRES 8 A 103 GLU GLU ILE THR LEU GLU ILE ASN GLY GLN VAL ILE
SHEET 1 A 4 SER A 266 ASP A 273 0
SHEET 2 A 4 ALA A 278 ASN A 285 -1 O THR A 283 N GLU A 268
SHEET 3 A 4 THR A 331 ASN A 339 -1 O PHE A 334 N VAL A 282
SHEET 4 A 4 THR A 303 TRP A 308 -1 N THR A 303 O ASN A 339
SHEET 1 B 5 ASN A 311 LYS A 312 0
SHEET 2 B 5 TYR A 318 THR A 322 -1 O THR A 322 N ASN A 311
SHEET 3 B 5 TRP A 292 LEU A 298 -1 N VAL A 296 O VAL A 319
SHEET 4 B 5 VAL A 346 ILE A 353 -1 O GLU A 352 N THR A 293
SHEET 5 B 5 GLN A 356 VAL A 357 -1 O GLN A 356 N ILE A 353
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
(ATOM LINES ARE NOT SHOWN.)
END
