HEADER CELLULOSE DEGRADATION 07-JUL-95 1EDG
TITLE SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF
TITLE 2 CELCCA CARRIED OUT AT 15 DEGREE C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOGLUCANASE A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, C TERMINUS TRUNCATED;
COMPND 5 SYNONYM: ENDO-(1,4)-BETA-GLUCANASE, CELCCA;
COMPND 6 EC: 3.2.1.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: FAMILY 5 OF GLYCOSYL HYDROLASES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM CELLULOLYTICUM;
SOURCE 3 ORGANISM_TAXID: 394503;
SOURCE 4 STRAIN: H10;
SOURCE 5 ATCC: 35319;
SOURCE 6 GENE: CELCCA;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PJF118EH;
SOURCE 11 EXPRESSION_SYSTEM_GENE: CELCCA
KEYWDS FAMILY A, CELLULASES, XYLANASES, FAMILY 5 OF GLYCOSYL HYDROLASE,
KEYWDS 2 CELLULOSE DEGRADATION
EXPDTA X-RAY DIFFRACTION
AUTHOR V.DUCROS,M.CZJZEK,R.HASER
REVDAT 4 07-FEB-24 1EDG 1 REMARK
REVDAT 3 13-JUL-11 1EDG 1 VERSN
REVDAT 2 24-FEB-09 1EDG 1 VERSN
REVDAT 1 17-AUG-96 1EDG 0
JRNL AUTH V.DUCROS,M.CZJZEK,A.BELAICH,C.GAUDIN,H.P.FIEROBE,
JRNL AUTH 2 J.P.BELAICH,G.J.DAVIES,R.HASER
JRNL TITL CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A BACTERIAL
JRNL TITL 2 CELLULASE BELONGING TO FAMILY 5.
JRNL REF STRUCTURE V. 3 939 1995
JRNL REFN ISSN 0969-2126
JRNL PMID 8535787
JRNL DOI 10.1016/S0969-2126(01)00228-3
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.P.FIEROBE,C.GAUDIN,A.BELAICH,M.LOUTFI,E.FAURE,C.BAGNARA,
REMARK 1 AUTH 2 D.BATY,J.P.BELAICH
REMARK 1 TITL CHARACTERIZATION OF ENDOGLUCANASE A FROM CLOSTRIDIUM
REMARK 1 TITL 2 CELLULOLYTICUM
REMARK 1 REF J.BACTERIOL. V. 173 7956 1991
REMARK 1 REFN ISSN 0021-9193
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 53913
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3035
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 375
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.130
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE SIDE CHAIN ATOMS OF TRP 181 AND ARG 358 WERE MODELED
REMARK 3 WITH PARTIAL OCCUPATION OF 0.7. THE SIDE CHAIN ATOMS OF
REMARK 3 ASN 46 WERE MODELED WITH PARTIAL OCCUPATION OF 0.6.
REMARK 4
REMARK 4 1EDG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173021.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-94; 17-NOV-94
REMARK 200 TEMPERATURE (KELVIN) : 288; NULL
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG; EMBL/DESY,
REMARK 200 HAMBURG
REMARK 200 BEAMLINE : X31; BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.870; 0.998
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE AREA
REMARK 200 DETECTOR
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59967
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.06900
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN AT 4 DEGREES C AND
REMARK 280 PH 6.0, TEMPERATURE 277K
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 26.20000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.75000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.10000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.75000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.20000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.10000
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 630 O HOH A 639 4455 0.00
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 ARG A 30 -64.20 63.97
REMARK 500 THR A 38 -98.21 -115.90
REMARK 500 HIS A 122 -99.20 -111.98
REMARK 500 ASN A 169 -83.16 -89.58
REMARK 500 LEU A 184 -9.48 -56.64
REMARK 500 TYR A 296 -66.65 -126.57
REMARK 500 ASN A 315 58.71 -140.05
REMARK 500 PHE A 354 -54.42 -128.55
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1EDG A 2 376 UNP P17901 GUNA_CLOCE 27 401
SEQRES 1 A 380 MET TYR ASP ALA SER LEU ILE PRO ASN LEU GLN ILE PRO
SEQRES 2 A 380 GLN LYS ASN ILE PRO ASN ASN ASP GLY MET ASN PHE VAL
SEQRES 3 A 380 LYS GLY LEU ARG LEU GLY TRP ASN LEU GLY ASN THR PHE
SEQRES 4 A 380 ASP ALA PHE ASN GLY THR ASN ILE THR ASN GLU LEU ASP
SEQRES 5 A 380 TYR GLU THR SER TRP SER GLY ILE LYS THR THR LYS GLN
SEQRES 6 A 380 MET ILE ASP ALA ILE LYS GLN LYS GLY PHE ASN THR VAL
SEQRES 7 A 380 ARG ILE PRO VAL SER TRP HIS PRO HIS VAL SER GLY SER
SEQRES 8 A 380 ASP TYR LYS ILE SER ASP VAL TRP MET ASN ARG VAL GLN
SEQRES 9 A 380 GLU VAL VAL ASN TYR CYS ILE ASP ASN LYS MET TYR VAL
SEQRES 10 A 380 ILE LEU ASN THR HIS HIS ASP VAL ASP LYS VAL LYS GLY
SEQRES 11 A 380 TYR PHE PRO SER SER GLN TYR MET ALA SER SER LYS LYS
SEQRES 12 A 380 TYR ILE THR SER VAL TRP ALA GLN ILE ALA ALA ARG PHE
SEQRES 13 A 380 ALA ASN TYR ASP GLU HIS LEU ILE PHE GLU GLY MET ASN
SEQRES 14 A 380 GLU PRO ARG LEU VAL GLY HIS ALA ASN GLU TRP TRP PRO
SEQRES 15 A 380 GLU LEU THR ASN SER ASP VAL VAL ASP SER ILE ASN CYS
SEQRES 16 A 380 ILE ASN GLN LEU ASN GLN ASP PHE VAL ASN THR VAL ARG
SEQRES 17 A 380 ALA THR GLY GLY LYS ASN ALA SER ARG TYR LEU MET CYS
SEQRES 18 A 380 PRO GLY TYR VAL ALA SER PRO ASP GLY ALA THR ASN ASP
SEQRES 19 A 380 TYR PHE ARG MET PRO ASN ASP ILE SER GLY ASN ASN ASN
SEQRES 20 A 380 LYS ILE ILE VAL SER VAL HIS ALA TYR CYS PRO TRP ASN
SEQRES 21 A 380 PHE ALA GLY LEU ALA MET ALA ASP GLY GLY THR ASN ALA
SEQRES 22 A 380 TRP ASN ILE ASN ASP SER LYS ASP GLN SER GLU VAL THR
SEQRES 23 A 380 TRP PHE MET ASP ASN ILE TYR ASN LYS TYR THR SER ARG
SEQRES 24 A 380 GLY ILE PRO VAL ILE ILE GLY GLU CYS GLY ALA VAL ASP
SEQRES 25 A 380 LYS ASN ASN LEU LYS THR ARG VAL GLU TYR MET SER TYR
SEQRES 26 A 380 TYR VAL ALA GLN ALA LYS ALA ARG GLY ILE LEU CYS ILE
SEQRES 27 A 380 LEU TRP ASP ASN ASN ASN PHE SER GLY THR GLY GLU LEU
SEQRES 28 A 380 PHE GLY PHE PHE ASP ARG ARG SER CYS GLN PHE LYS PHE
SEQRES 29 A 380 PRO GLU ILE ILE ASP GLY MET VAL LYS TYR ALA PHE GLY
SEQRES 30 A 380 LEU ILE ASN
FORMUL 2 HOH *375(H2 O)
HELIX 1 1 ALA A 4 LEU A 6 5 3
HELIX 2 2 ASP A 21 LEU A 29 1 9
HELIX 3 3 GLU A 50 SER A 56 5 7
HELIX 4 4 LYS A 64 LYS A 73 1 10
HELIX 5 5 HIS A 85 HIS A 87 5 3
HELIX 6 6 ASP A 97 ASN A 113 1 17
HELIX 7 7 SER A 135 ARG A 155 5 21
HELIX 8 8 SER A 187 THR A 210 1 24
HELIX 9 9 GLY A 212 ALA A 215 5 4
HELIX 10 10 TYR A 224 ALA A 226 5 3
HELIX 11 11 PRO A 228 THR A 232 1 5
HELIX 12 12 TRP A 259 ALA A 262 1 4
HELIX 13 13 MET A 266 ASP A 268 5 3
HELIX 14 14 SER A 279 LYS A 295 1 17
HELIX 15 15 THR A 297 ARG A 299 5 3
HELIX 16 16 LEU A 316 ARG A 333 1 18
HELIX 17 17 PRO A 365 TYR A 374 1 10
SHEET 1 A 4 GLY A 32 ASN A 34 0
SHEET 2 A 4 THR A 77 ILE A 80 1 N THR A 77 O TRP A 33
SHEET 3 A 4 TYR A 116 ASN A 120 1 N TYR A 116 O VAL A 78
SHEET 4 A 4 LEU A 163 GLU A 166 1 N ILE A 164 O VAL A 117
SHEET 1 B 4 LEU A 219 PRO A 222 0
SHEET 2 B 4 ILE A 249 HIS A 254 1 N ILE A 250 O LEU A 219
SHEET 3 B 4 VAL A 303 GLU A 307 1 N ILE A 304 O VAL A 251
SHEET 4 B 4 LEU A 336 LEU A 339 1 N ILE A 338 O ILE A 305
CISPEP 1 CYS A 257 PRO A 258 0 -0.51
CRYST1 52.400 76.200 113.500 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 0.019084 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013123 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008811 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
