HEADER HYDROLASE 28-JAN-00 1EDQ
TITLE CRYSTAL STRUCTURE OF CHITINASE A FROM S. MARCESCENS AT 1.55 ANGSTROMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHITINASE A;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.14;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SERRATIA MARCESCENS;
SOURCE 3 ORGANISM_TAXID: 615;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR: PBR322
KEYWDS BETA-ALPHA (TIM) BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PAPANIKOLAU,K.PETRATOS
REVDAT 6 09-AUG-23 1EDQ 1 REMARK SEQADV
REVDAT 5 24-FEB-09 1EDQ 1 VERSN
REVDAT 4 11-FEB-03 1EDQ 1 JRNL REMARK MASTER
REVDAT 3 26-SEP-01 1EDQ 1 SOURCE JRNL REMARK DBREF
REVDAT 2 02-MAR-00 1EDQ 3 ATOM HEADER COMPND DBREF
REVDAT 1 18-FEB-00 1EDQ 0
JRNL AUTH Y.PAPANIKOLAU,G.TAVLAS,C.E.VORGIAS,K.PETRATOS
JRNL TITL DE NOVO PURIFICATION SCHEME AND CRYSTALLIZATION CONDITIONS
JRNL TITL 2 YIELD HIGH-RESOLUTION STRUCTURES OF CHITINASE A AND ITS
JRNL TITL 3 COMPLEX WITH THE INHIBITOR ALLOSAMIDIN.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 59 400 2003
JRNL REFN ISSN 0907-4449
JRNL PMID 12554965
JRNL DOI 10.1107/S0907444902021923
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.PERRAKIS,I.TEWS,Z.DAUTER,A.B.OPPENHEIM,I.CHET,K.S.WILSON,
REMARK 1 AUTH 2 C.E.VORGIAS
REMARK 1 TITL CRYSTAL STRUCTURE OF A BACTERIAL CHITINASE AT 2.3 ANGSTROM
REMARK 1 TITL 2 RESOLUTION
REMARK 1 REF STRUCTURE V. 2 1169 1994
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.PAPANIKOLAU,G.PRAG,G.TAVLAS,C.E.VORGIAS,A.B.OPPENHEIM,
REMARK 1 AUTH 2 K.PETRATOS
REMARK 1 TITL HIGH RESOLUTION STRUCTURAL ANALYSES OF MUTANT CHITINASE A
REMARK 1 TITL 2 COMPLEXES WITH SUBSTRATES PROVIDE NEW INSIGHT INTO THE
REMARK 1 TITL 3 MECHANISM OF CATALYSIS
REMARK 1 REF BIOCHEMISTRY V. 40 11338 2001
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI010505H
REMARK 2
REMARK 2 RESOLUTION. 1.55 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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 112857
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4137
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 909
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.20
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): 0.072
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.074
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.049
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.328
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) : 0.023 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.030 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.010 ; 0.030
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.093 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.171 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.241 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.196 ; 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) : 6.500 ; 7.000
REMARK 3 STAGGERED (DEGREES) : 11.900; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 25.200; 20.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.090 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.570 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.500 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.270 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EDQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010470.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9116
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 112857
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.03200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.21600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1CTN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.75 M CITRATE-NA PH 7.2, 20% (V/V)
REMARK 280 METHANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.68400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 29.68400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 99.74850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.91250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 99.74850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.91250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 29.68400
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 99.74850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.91250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 29.68400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 99.74850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.91250
REMARK 290 SMTRY3 8 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 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 107 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ASP A 132 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 134 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 290 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG A 290 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ASP A 291 CB - CG - OD1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ASP A 291 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG A 292 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 343 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 343 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 355 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 TYR A 357 CB - CG - CD1 ANGL. DEV. = -4.2 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 LYS A 142 75.15 -119.89
REMARK 500 GLU A 147 -131.37 49.93
REMARK 500 TYR A 170 -108.11 -93.06
REMARK 500 LYS A 250 -149.24 -110.30
REMARK 500 ASP A 313 68.52 -112.31
REMARK 500 THR A 405 26.20 -147.75
REMARK 500 LYS A 413 76.80 -151.00
REMARK 500 MET A 443 31.71 -97.02
REMARK 500 GLU A 500 69.74 62.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CTN RELATED DB: PDB
REMARK 900 1CTN CONTAINS THE SAME PROTEIN STRUCTURE AT 2.3 ANGSTROM
REMARK 900 RESOLUTION. DIFFERENT CRYSTALLIZATION SOLUTIONS.
DBREF 1EDQ A 24 563 UNP O83008 O83008_SERMA 24 563
SEQADV 1EDQ GLY A 475 UNP O83008 ARG 475 CONFLICT
SEQRES 1 A 540 ALA ALA PRO GLY LYS PRO THR ILE ALA TRP GLY ASN THR
SEQRES 2 A 540 LYS PHE ALA ILE VAL GLU VAL ASP GLN ALA ALA THR ALA
SEQRES 3 A 540 TYR ASN ASN LEU VAL LYS VAL LYS ASN ALA ALA ASP VAL
SEQRES 4 A 540 SER VAL SER TRP ASN LEU TRP ASN GLY ASP THR GLY THR
SEQRES 5 A 540 THR ALA LYS VAL LEU LEU ASN GLY LYS GLU ALA TRP SER
SEQRES 6 A 540 GLY PRO SER THR GLY SER SER GLY THR ALA ASN PHE LYS
SEQRES 7 A 540 VAL ASN LYS GLY GLY ARG TYR GLN MET GLN VAL ALA LEU
SEQRES 8 A 540 CYS ASN ALA ASP GLY CYS THR ALA SER ASP ALA THR GLU
SEQRES 9 A 540 ILE VAL VAL ALA ASP THR ASP GLY SER HIS LEU ALA PRO
SEQRES 10 A 540 LEU LYS GLU PRO LEU LEU GLU LYS ASN LYS PRO TYR LYS
SEQRES 11 A 540 GLN ASN SER GLY LYS VAL VAL GLY SER TYR PHE VAL GLU
SEQRES 12 A 540 TRP GLY VAL TYR GLY ARG ASN PHE THR VAL ASP LYS ILE
SEQRES 13 A 540 PRO ALA GLN ASN LEU THR HIS LEU LEU TYR GLY PHE ILE
SEQRES 14 A 540 PRO ILE CYS GLY GLY ASN GLY ILE ASN ASP SER LEU LYS
SEQRES 15 A 540 GLU ILE GLU GLY SER PHE GLN ALA LEU GLN ARG SER CYS
SEQRES 16 A 540 GLN GLY ARG GLU ASP PHE LYS VAL SER ILE HIS ASP PRO
SEQRES 17 A 540 PHE ALA ALA LEU GLN LYS ALA GLN LYS GLY VAL THR ALA
SEQRES 18 A 540 TRP ASP ASP PRO TYR LYS GLY ASN PHE GLY GLN LEU MET
SEQRES 19 A 540 ALA LEU LYS GLN ALA HIS PRO ASP LEU LYS ILE LEU PRO
SEQRES 20 A 540 SER ILE GLY GLY TRP THR LEU SER ASP PRO PHE PHE PHE
SEQRES 21 A 540 MET GLY ASP LYS VAL LYS ARG ASP ARG PHE VAL GLY SER
SEQRES 22 A 540 VAL LYS GLU PHE LEU GLN THR TRP LYS PHE PHE ASP GLY
SEQRES 23 A 540 VAL ASP ILE ASP TRP GLU PHE PRO GLY GLY LYS GLY ALA
SEQRES 24 A 540 ASN PRO ASN LEU GLY SER PRO GLN ASP GLY GLU THR TYR
SEQRES 25 A 540 VAL LEU LEU MET LYS GLU LEU ARG ALA MET LEU ASP GLN
SEQRES 26 A 540 LEU SER VAL GLU THR GLY ARG LYS TYR GLU LEU THR SER
SEQRES 27 A 540 ALA ILE SER ALA GLY LYS ASP LYS ILE ASP LYS VAL ALA
SEQRES 28 A 540 TYR ASN VAL ALA GLN ASN SER MET ASP HIS ILE PHE LEU
SEQRES 29 A 540 MET SER TYR ASP PHE TYR GLY ALA PHE ASP LEU LYS ASN
SEQRES 30 A 540 LEU GLY HIS GLN THR ALA LEU ASN ALA PRO ALA TRP LYS
SEQRES 31 A 540 PRO ASP THR ALA TYR THR THR VAL ASN GLY VAL ASN ALA
SEQRES 32 A 540 LEU LEU ALA GLN GLY VAL LYS PRO GLY LYS ILE VAL VAL
SEQRES 33 A 540 GLY THR ALA MET TYR GLY ARG GLY TRP THR GLY VAL ASN
SEQRES 34 A 540 GLY TYR GLN ASN ASN ILE PRO PHE THR GLY THR ALA THR
SEQRES 35 A 540 GLY PRO VAL LYS GLY THR TRP GLU ASN GLY ILE VAL ASP
SEQRES 36 A 540 TYR ARG GLN ILE ALA GLY GLN PHE MET SER GLY GLU TRP
SEQRES 37 A 540 GLN TYR THR TYR ASP ALA THR ALA GLU ALA PRO TYR VAL
SEQRES 38 A 540 PHE LYS PRO SER THR GLY ASP LEU ILE THR PHE ASP ASP
SEQRES 39 A 540 ALA ARG SER VAL GLN ALA LYS GLY LYS TYR VAL LEU ASP
SEQRES 40 A 540 LYS GLN LEU GLY GLY LEU PHE SER TRP GLU ILE ASP ALA
SEQRES 41 A 540 ASP ASN GLY ASP ILE LEU ASN SER MET ASN ALA SER LEU
SEQRES 42 A 540 GLY ASN SER ALA GLY VAL GLN
FORMUL 2 HOH *909(H2 O)
HELIX 1 1 ALA A 49 LEU A 53 1 5
HELIX 2 2 TRP A 167 TYR A 170 5 4
HELIX 3 3 THR A 175 ILE A 179 5 5
HELIX 4 4 PRO A 180 LEU A 184 5 5
HELIX 5 5 ASN A 201 ILE A 207 5 7
HELIX 6 6 GLY A 209 CYS A 218 1 10
HELIX 7 7 ASP A 230 GLN A 236 1 7
HELIX 8 8 LYS A 250 HIS A 263 1 14
HELIX 9 9 SER A 278 MET A 284 5 7
HELIX 10 10 ASP A 286 TRP A 304 1 19
HELIX 11 11 GLN A 330 GLY A 354 1 25
HELIX 12 12 GLY A 366 ASP A 371 1 6
HELIX 13 13 ALA A 374 GLN A 379 1 6
HELIX 14 14 ASN A 380 MET A 382 5 3
HELIX 15 15 THR A 419 GLY A 431 1 13
HELIX 16 16 LYS A 433 GLY A 435 5 3
HELIX 17 17 ILE A 458 GLY A 462 5 5
HELIX 18 18 TYR A 479 PHE A 486 1 8
HELIX 19 19 ASP A 517 GLN A 532 1 16
HELIX 20 20 GLU A 540 ASP A 544 5 5
HELIX 21 21 GLY A 546 LEU A 556 1 11
SHEET 1 A 3 THR A 30 ILE A 31 0
SHEET 2 A 3 ALA A 60 ASN A 67 -1 O ASN A 67 N THR A 30
SHEET 3 A 3 SER A 95 VAL A 102 -1 N GLY A 96 O TRP A 66
SHEET 1 B 5 LYS A 37 ALA A 39 0
SHEET 2 B 5 THR A 126 ALA A 131 1 O VAL A 129 N PHE A 38
SHEET 3 B 5 GLY A 106 ASN A 116 -1 O GLY A 106 N VAL A 130
SHEET 4 B 5 THR A 76 LEU A 81 -1 O THR A 76 N CYS A 115
SHEET 5 B 5 LYS A 84 PRO A 90 -1 O LYS A 84 N LEU A 81
SHEET 1 C 4 LYS A 37 ALA A 39 0
SHEET 2 C 4 THR A 126 ALA A 131 1 O VAL A 129 N PHE A 38
SHEET 3 C 4 GLY A 106 ASN A 116 -1 O GLY A 106 N VAL A 130
SHEET 4 C 4 GLY A 119 ALA A 122 -1 O GLY A 119 N ASN A 116
SHEET 1 D 2 VAL A 41 VAL A 43 0
SHEET 2 D 2 VAL A 54 VAL A 56 -1 O LYS A 55 N GLU A 42
SHEET 1 E 9 VAL A 159 VAL A 165 0
SHEET 2 E 9 HIS A 186 ILE A 192 1 N HIS A 186 O VAL A 160
SHEET 3 E 9 LYS A 267 GLY A 273 1 O LYS A 267 N LEU A 187
SHEET 4 E 9 GLY A 309 ASP A 313 1 O ASP A 311 N ILE A 272
SHEET 5 E 9 GLU A 358 SER A 364 1 O GLU A 358 N VAL A 310
SHEET 6 E 9 HIS A 384 MET A 388 1 O HIS A 384 N SER A 361
SHEET 7 E 9 ILE A 437 ALA A 442 1 N VAL A 438 O ILE A 385
SHEET 8 E 9 GLY A 535 TRP A 539 1 O GLY A 535 N VAL A 439
SHEET 9 E 9 VAL A 159 VAL A 165 1 O VAL A 159 N LEU A 536
SHEET 1 F 5 GLN A 492 ASP A 496 0
SHEET 2 F 5 ALA A 501 LYS A 506 -1 O ALA A 501 N ASP A 496
SHEET 3 F 5 ASP A 511 THR A 514 -1 O ASP A 511 N LYS A 506
SHEET 4 F 5 TYR A 444 THR A 449 -1 O ARG A 446 N THR A 514
SHEET 5 F 5 GLY A 466 PRO A 467 -1 O GLY A 466 N THR A 449
SHEET 1 G 5 GLN A 492 ASP A 496 0
SHEET 2 G 5 ALA A 501 LYS A 506 -1 O ALA A 501 N ASP A 496
SHEET 3 G 5 ASP A 511 THR A 514 -1 O ASP A 511 N LYS A 506
SHEET 4 G 5 TYR A 444 THR A 449 -1 O ARG A 446 N THR A 514
SHEET 5 G 5 ILE A 476 ASP A 478 -1 O VAL A 477 N GLY A 445
SSBOND 1 CYS A 115 CYS A 120 1555 1555 2.05
SSBOND 2 CYS A 195 CYS A 218 1555 1555 2.06
CISPEP 1 GLY A 190 PHE A 191 0 0.26
CISPEP 2 GLU A 315 PHE A 316 0 -3.69
CISPEP 3 TRP A 539 GLU A 540 0 -6.70
CRYST1 199.497 131.825 59.368 90.00 90.00 90.00 C 2 2 21 8
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 0.005013 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007586 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016844 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
