HEADER HYDROLASE 28-FEB-06 2DFB
TITLE XYLANASE II FROM TRICODERMA REESEI AT 100K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: XYLANASE 2, 1,4-BETA-D-XYLAN XYLANOHYDROLASE 2;
COMPND 5 EC: 3.2.1.8
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HYPOCREA JECORINA;
SOURCE 3 ORGANISM_TAXID: 51453
KEYWDS BENT BETA SHEET, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.HARATA,T.AKIBA
REVDAT 4 25-OCT-23 2DFB 1 REMARK
REVDAT 3 25-DEC-19 2DFB 1 SEQADV SEQRES LINK
REVDAT 2 24-FEB-09 2DFB 1 VERSN
REVDAT 1 11-JUL-06 2DFB 0
JRNL AUTH N.WATANABE,T.AKIBA,R.KANAI,K.HARATA
JRNL TITL STRUCTURE OF AN ORTHORHOMBIC FORM OF XYLANASE II FROM
JRNL TITL 2 TRICHODERMA REESEI AND ANALYSIS OF THERMAL DISPLACEMENT.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 62 784 2006
JRNL REFN ISSN 0907-4449
JRNL PMID 16790934
JRNL DOI 10.1107/S0907444906017379
REMARK 2
REMARK 2 RESOLUTION. 1.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.108
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.121
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3875
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 80022
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1480
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 292
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 ANGLE DISTANCES (A) : 0.028
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.036
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.099
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.101
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DFB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025350.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-18B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.15
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : TRUNCATE, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77541
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.110
REMARK 200 RESOLUTION RANGE LOW (A) : 19.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.11
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.20300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1ENX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M AMMONIUM SULFATE, 0.1M BICINE,
REMARK 280 0.15M SODIUM IODIDE, 1.6% PROTEIN, PH 9.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 24.48500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.90000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.25500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 34.90000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.48500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.25500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 39 NE1 TRP A 39 CE2 -0.087
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TRP A 39 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 TRP A 39 CD1 - NE1 - CE2 ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 122 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 TRP A 138 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 TRP A 138 CD1 - NE1 - CE2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 ASN A 154 OD1 - CG - ND2 ANGL. DEV. = -16.8 DEGREES
REMARK 500 ASN A 154 CB - CG - ND2 ANGL. DEV. = 18.0 DEGREES
REMARK 500 HIS A 155 CG - ND1 - CE1 ANGL. DEV. = 8.8 DEGREES
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 ASN A 57 20.86 -142.34
REMARK 500 ASP A 170 -143.37 -99.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 192
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 193
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 194
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 195
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 196
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 197
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DFC RELATED DB: PDB
DBREF 2DFB A 1 190 UNP P36217 XYN2_TRIRE 33 222
SEQRES 1 A 190 PCA THR ILE GLN PRO GLY THR GLY TYR ASN ASN GLY TYR
SEQRES 2 A 190 PHE TYR SER TYR TRP ASN ASP GLY HIS GLY GLY VAL THR
SEQRES 3 A 190 TYR THR ASN GLY PRO GLY GLY GLN PHE SER VAL ASN TRP
SEQRES 4 A 190 SER ASN SER GLY ASN PHE VAL GLY GLY LYS GLY TRP GLN
SEQRES 5 A 190 PRO GLY THR LYS ASN LYS VAL ILE ASN PHE SER GLY SER
SEQRES 6 A 190 TYR ASN PRO ASN GLY ASN SER TYR LEU SER VAL TYR GLY
SEQRES 7 A 190 TRP SER ARG ASN PRO LEU ILE GLU TYR TYR ILE VAL GLU
SEQRES 8 A 190 ASN PHE GLY THR TYR ASN PRO SER THR GLY ALA THR LYS
SEQRES 9 A 190 LEU GLY GLU VAL THR SER ASP GLY SER VAL TYR ASP ILE
SEQRES 10 A 190 TYR ARG THR GLN ARG VAL ASN GLN PRO SER ILE ILE GLY
SEQRES 11 A 190 THR ALA THR PHE TYR GLN TYR TRP SER VAL ARG ARG ASN
SEQRES 12 A 190 HIS ARG SER SER GLY SER VAL ASN THR ALA ASN HIS PHE
SEQRES 13 A 190 ASN ALA TRP ALA GLN GLN GLY LEU THR LEU GLY THR MET
SEQRES 14 A 190 ASP TYR GLN ILE VAL ALA VAL GLU GLY TYR PHE SER SER
SEQRES 15 A 190 GLY SER ALA SER ILE THR VAL SER
MODRES 2DFB PCA A 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 8
HET SO4 A 191 5
HET IOD A 192 1
HET IOD A 193 1
HET IOD A 194 1
HET IOD A 195 1
HET IOD A 196 1
HET IOD A 197 1
HETNAM PCA PYROGLUTAMIC ACID
HETNAM SO4 SULFATE ION
HETNAM IOD IODIDE ION
FORMUL 1 PCA C5 H7 N O3
FORMUL 2 SO4 O4 S 2-
FORMUL 3 IOD 6(I 1-)
FORMUL 9 HOH *292(H2 O)
HELIX 1 1 THR A 152 GLN A 162 1 11
SHEET 1 A 6 THR A 2 ILE A 3 0
SHEET 2 A 6 VAL A 25 ASN A 29 -1 O TYR A 27 N ILE A 3
SHEET 3 A 6 GLN A 34 TRP A 39 -1 O ASN A 38 N THR A 26
SHEET 4 A 6 SER A 182 SER A 190 -1 O GLY A 183 N TRP A 39
SHEET 5 A 6 VAL A 59 ASN A 69 -1 N ASN A 67 O SER A 184
SHEET 6 A 6 GLY A 148 ASN A 151 -1 O VAL A 150 N ILE A 60
SHEET 1 B 9 GLY A 6 ASN A 10 0
SHEET 2 B 9 TYR A 13 ASN A 19 -1 O TYR A 15 N GLY A 8
SHEET 3 B 9 ASN A 44 TRP A 51 -1 O GLY A 50 N PHE A 14
SHEET 4 B 9 THR A 168 TYR A 179 -1 O GLN A 172 N TRP A 51
SHEET 5 B 9 SER A 72 ARG A 81 -1 N TYR A 77 O ILE A 173
SHEET 6 B 9 ILE A 85 PHE A 93 -1 O TYR A 87 N GLY A 78
SHEET 7 B 9 ALA A 132 ARG A 141 1 O SER A 139 N VAL A 90
SHEET 8 B 9 SER A 113 GLN A 125 -1 N ARG A 122 O PHE A 134
SHEET 9 B 9 THR A 103 SER A 110 -1 N LEU A 105 O ILE A 117
LINK C PCA A 1 N THR A 2 1555 1555 1.33
CISPEP 1 GLN A 52 PRO A 53 0 -0.62
CISPEP 2 ASN A 82 PRO A 83 0 6.07
SITE 1 AC1 9 GLN A 4 PRO A 5 ASN A 19 HOH A 220
SITE 2 AC1 9 HOH A 244 HOH A 267 HOH A 285 HOH A 290
SITE 3 AC1 9 HOH A 452
SITE 1 AC2 2 ASN A 82 SER A 146
SITE 1 AC3 1 ARG A 119
SITE 1 AC4 1 PRO A 68
SITE 1 AC5 2 SER A 65 SER A 184
SITE 1 AC6 2 VAL A 123 GLN A 125
SITE 1 AC7 3 GLY A 30 GLN A 34 SER A 36
CRYST1 48.970 58.510 69.800 90.00 90.00 90.00 P 21 21 21 4
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 0.020421 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017091 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014327 0.00000
HETATM 1 N PCA A 1 30.995 46.351 -10.751 1.00 14.52 N
ANISOU 1 N PCA A 1 1599 1981 1937 -183 -55 265 N
HETATM 2 CA PCA A 1 30.372 45.180 -10.223 1.00 14.49 C
ANISOU 2 CA PCA A 1 1526 1906 2075 -171 -92 362 C
HETATM 3 CB PCA A 1 30.170 45.483 -8.734 1.00 16.71 C
ANISOU 3 CB PCA A 1 2267 2111 1971 -222 -145 443 C
HETATM 4 CG PCA A 1 30.722 46.845 -8.510 1.00 16.54 C
ANISOU 4 CG PCA A 1 2236 2108 1942 -134 91 227 C
HETATM 5 CD PCA A 1 31.205 47.292 -9.870 1.00 13.80 C
ANISOU 5 CD PCA A 1 1461 2190 1591 -417 -373 241 C
HETATM 6 OE PCA A 1 31.810 48.351 -10.064 1.00 15.23 O
ANISOU 6 OE PCA A 1 1752 1807 2228 -38 60 119 O
HETATM 7 C PCA A 1 29.067 44.832 -10.895 1.00 14.99 C
ANISOU 7 C PCA A 1 1688 1856 2152 -250 -122 468 C
HETATM 8 O PCA A 1 28.616 43.686 -10.904 1.00 17.67 O
ANISOU 8 O PCA A 1 1523 1756 3434 -196 -209 99 O
(ATOM LINES ARE NOT SHOWN.)
END
