HEADER HYDROLASE 21-JAN-98 1A3H
TITLE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOGLUCANASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC CORE DOMAIN;
COMPND 5 SYNONYM: CELLULASE;
COMPND 6 EC: 3.2.1.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS AGARADHAERENS;
SOURCE 3 ORGANISM_TAXID: 76935;
SOURCE 4 STRAIN: AC13;
SOURCE 5 ATCC: NCIMB 40482;
SOURCE 6 COLLECTION: NCIMB 40482;
SOURCE 7 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 1423;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: PL2306;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACILLUS, CELLULASE NEGATIVE STRAIN;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PMOL995;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: THERMAMYL-AMYLASE PROMOTER SYSTEM
KEYWDS HYDROLASE, CELLULOSE DEGRADATION, ENDOGLUCANASE, GLYCOSIDE HYDROLASE
KEYWDS 2 FAMILY 5
EXPDTA X-RAY DIFFRACTION
AUTHOR G.J.DAVIES,A.M.BRZOZOWSKI,K.ANDERSEN,M.SCHULEIN
REVDAT 3 07-FEB-24 1A3H 1 REMARK
REVDAT 2 24-FEB-09 1A3H 1 VERSN
REVDAT 1 16-MAR-99 1A3H 0
JRNL AUTH G.J.DAVIES,M.DAUTER,A.M.BRZOZOWSKI,M.E.BJORNVAD,
JRNL AUTH 2 K.V.ANDERSEN,M.SCHULEIN
JRNL TITL STRUCTURE OF THE BACILLUS AGARADHERANS FAMILY 5
JRNL TITL 2 ENDOGLUCANASE AT 1.6 A AND ITS CELLOBIOSE COMPLEX AT 2.0 A
JRNL TITL 3 RESOLUTION
JRNL REF BIOCHEMISTRY V. 37 1926 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9485319
JRNL DOI 10.1021/BI972162M
REMARK 2
REMARK 2 RESOLUTION. 1.57 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.57
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 38663
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.140
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2074
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2377
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 424
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.80
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.010 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.026 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.031 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.012 ; 0.040
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.110 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.174 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.225 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.185 ; 0.300
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 4.900 ; 7.000
REMARK 3 STAGGERED (DEGREES) : 12.700; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 28.700; 20.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.830 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.330 ; 5.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.930 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.460 ; 6.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ESTIMATED COORDINATE ERROR. ESD FROM
REMARK 3 SIGMAA (A) : 0.013 LOW RESOLUTION CUTOFF (A) : 15 FIT/AGREEMENT
REMARK 3 OF MODEL WITH ALL DATA. R VALUE (WORKING + TEST SET, NO CUTOFF) :
REMARK 3 NULL R VALUE (WORKING SET, NO CUTOFF) : 0.12888 FREE R VALUE
REMARK 3 (NO CUTOFF) : 0.16078
REMARK 4
REMARK 4 1A3H 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_1000170345.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : LONG MIRRORS (MSC)
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 222447
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.19600
REMARK 200 R SYM FOR SHELL (I) : 0.19600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIPLE ISOMORPHOUS
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.5
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 27.35500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.52000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.78500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.52000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.35500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.78500
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 400
REMARK 400 COMPOUND
REMARK 400 THE FIRST 3 RESIDUES ARE DISORDERED SO IT STARTS WITH
REMARK 400 RESIDUE SER 4. THIS THE NATURALLY OCCURRING CATALYTIC CORQ
REMARK 400 DOMAIN AFTER LOSS OF THE CELLULOSE-BINDING DOMAIN(S).
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HOH A 429 O HOH A 610 2.12
REMARK 500
REMARK 500 REMARK: NULL
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 CG GLU A 25 O HOH A 721 3845 1.72
REMARK 500 CD GLU A 25 O HOH A 721 3845 2.06
REMARK 500 O HOH A 559 O HOH A 576 4566 2.09
REMARK 500 O HOH A 439 O HOH A 546 3745 2.14
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 ARG A 53 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 54 CB - CG - OD1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ASP A 144 CB - CG - OD1 ANGL. DEV. = 11.9 DEGREES
REMARK 500 ASP A 144 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP A 237 CB - CG - OD1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ASP A 237 CB - CG - OD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ARG A 301 NE - CZ - NH2 ANGL. DEV. = -3.9 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 SER A 68 -159.75 -97.67
REMARK 500 LEU A 103 -78.50 -162.10
REMARK 500 ALA A 137 91.19 -164.52
REMARK 500 ASN A 138 -71.93 -37.80
REMARK 500 ASN A 168 9.76 -151.08
REMARK 500 ASN A 188 60.76 -150.70
REMARK 500 ASP A 237 -158.68 -133.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AVE
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: SITE
DBREF 1A3H A 4 303 UNP O85465 GUN5_BACAG 30 329
SEQRES 1 A 300 SER VAL VAL GLU GLU HIS GLY GLN LEU SER ILE SER ASN
SEQRES 2 A 300 GLY GLU LEU VAL ASN GLU ARG GLY GLU GLN VAL GLN LEU
SEQRES 3 A 300 LYS GLY MET SER SER HIS GLY LEU GLN TRP TYR GLY GLN
SEQRES 4 A 300 PHE VAL ASN TYR GLU SER MET LYS TRP LEU ARG ASP ASP
SEQRES 5 A 300 TRP GLY ILE ASN VAL PHE ARG ALA ALA MET TYR THR SER
SEQRES 6 A 300 SER GLY GLY TYR ILE ASP ASP PRO SER VAL LYS GLU LYS
SEQRES 7 A 300 VAL LYS GLU ALA VAL GLU ALA ALA ILE ASP LEU ASP ILE
SEQRES 8 A 300 TYR VAL ILE ILE ASP TRP HIS ILE LEU SER ASP ASN ASP
SEQRES 9 A 300 PRO ASN ILE TYR LYS GLU GLU ALA LYS ASP PHE PHE ASP
SEQRES 10 A 300 GLU MET SER GLU LEU TYR GLY ASP TYR PRO ASN VAL ILE
SEQRES 11 A 300 TYR GLU ILE ALA ASN GLU PRO ASN GLY SER ASP VAL THR
SEQRES 12 A 300 TRP GLY ASN GLN ILE LYS PRO TYR ALA GLU GLU VAL ILE
SEQRES 13 A 300 PRO ILE ILE ARG ASN ASN ASP PRO ASN ASN ILE ILE ILE
SEQRES 14 A 300 VAL GLY THR GLY THR TRP SER GLN ASP VAL HIS HIS ALA
SEQRES 15 A 300 ALA ASP ASN GLN LEU ALA ASP PRO ASN VAL MET TYR ALA
SEQRES 16 A 300 PHE HIS PHE TYR ALA GLY THR HIS GLY GLN ASN LEU ARG
SEQRES 17 A 300 ASP GLN VAL ASP TYR ALA LEU ASP GLN GLY ALA ALA ILE
SEQRES 18 A 300 PHE VAL SER GLU TRP GLY THR SER ALA ALA THR GLY ASP
SEQRES 19 A 300 GLY GLY VAL PHE LEU ASP GLU ALA GLN VAL TRP ILE ASP
SEQRES 20 A 300 PHE MET ASP GLU ARG ASN LEU SER TRP ALA ASN TRP SER
SEQRES 21 A 300 LEU THR HIS LYS ASP GLU SER SER ALA ALA LEU MET PRO
SEQRES 22 A 300 GLY ALA ASN PRO THR GLY GLY TRP THR GLU ALA GLU LEU
SEQRES 23 A 300 SER PRO SER GLY THR PHE VAL ARG GLU LYS ILE ARG GLU
SEQRES 24 A 300 SER
FORMUL 2 HOH *424(H2 O)
HELIX 1 1 VAL A 5 HIS A 9 1 5
HELIX 2 2 LEU A 37 PHE A 43 1 7
HELIX 3 3 TYR A 46 ASP A 55 1 10
HELIX 4 4 PRO A 76 LEU A 92 5 17
HELIX 5 5 LYS A 112 TYR A 126 1 15
HELIX 6 6 ILE A 151 ASN A 165 1 15
HELIX 7 7 GLY A 176 SER A 179 1 4
HELIX 8 8 VAL A 182 ALA A 186 1 5
HELIX 9 9 GLN A 208 GLN A 220 1 13
HELIX 10 10 LEU A 242 GLU A 254 1 13
HELIX 11 11 GLU A 286 GLU A 288 5 3
HELIX 12 12 PRO A 291 ARG A 301 1 11
SHEET 1 A 2 SER A 13 SER A 15 0
SHEET 2 A 2 GLU A 18 VAL A 20 -1 N VAL A 20 O SER A 13
SHEET 1 B 5 TRP A 259 ASN A 261 0
SHEET 2 B 5 LYS A 30 SER A 33 1 N GLY A 31 O TRP A 259
SHEET 3 B 5 VAL A 60 TYR A 66 1 N VAL A 60 O MET A 32
SHEET 4 B 5 TYR A 95 HIS A 101 1 N TYR A 95 O PHE A 61
SHEET 5 B 5 VAL A 132 GLU A 135 1 N ILE A 133 O VAL A 96
SHEET 1 C 2 ILE A 171 VAL A 173 0
SHEET 2 C 2 VAL A 195 TYR A 197 1 N MET A 196 O ILE A 171
SHEET 1 D 2 HIS A 200 TYR A 202 0
SHEET 2 D 2 GLU A 228 GLY A 230 1 N GLU A 228 O PHE A 201
CISPEP 1 TRP A 262 SER A 263 0 3.65
SITE 1 AVE 2 GLU A 139 GLU A 228
CRYST1 54.710 69.570 77.040 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 0.018278 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014374 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012980 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
