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HEADER HYDROLASE 14-APR-09 3H2H
TITLE CRYSTAL STRUCTURE OF G231F MUTANT OF THE RICE CELL WALL
TITLE 2 DEGRADING ESTERASE LIPA FROM XANTHOMONAS ORYZAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES IN UNP 45-441;
COMPND 5 SYNONYM: PUTATIVE UNCHARACTERIZED PROTEIN;
COMPND 6 EC: 3.1.1.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOMONAS ORYZAE PV. ORYZAE;
SOURCE 3 ORGANISM_TAXID: 64187;
SOURCE 4 STRAIN: BXO43;
SOURCE 5 GENE: LIPA;
SOURCE 6 EXPRESSION_SYSTEM: XANTHOMONAS ORYZAE PV. ORYZAE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 64187;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BXO43;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BROAD HOST RANGE VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHM1
KEYWDS CRYSTAL STRUCTURE, XANTHOMONAS ORYZAE PV. ORYZAE, ESTERASE,
KEYWDS 2 CELL WALL DEGRADING ENZYME, RICE, VIRULENCE, INNATE IMMUNE
KEYWDS 3 RESPONSES, PATHOGENESIS, GLYCOSIDE BINDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.APARNA,A.CHATTERJEE,R.V.SONTI,R.SANKARANARAYANAN
REVDAT 1 18-AUG-09 3H2H 0
JRNL AUTH G.APARNA,A.CHATTERJEE,R.V.SONTI,R.SANKARANARAYANAN
JRNL TITL A CELL WALL-DEGRADING ESTERASE OF XANTHOMONAS
JRNL TITL 2 ORYZAE REQUIRES A UNIQUE SUBSTRATE RECOGNITION
JRNL TITL 3 MODULE FOR PATHOGENESIS ON RICE
JRNL REF PLANT CELL V. 21 1860 2009
JRNL REFN ISSN 1040-4651
JRNL PMID 19525415
JRNL DOI 10.1105/TPC.109.066886
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1771400.750
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 21553
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 SET) : 0.179
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1087
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1878
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 98
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2948
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.80000
REMARK 3 B22 (A**2) : 0.85000
REMARK 3 B33 (A**2) : -0.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.70000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.14
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.110 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.600 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.010 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.790 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 46.11
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3H2H COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052608.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.7
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21553
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 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 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: MOLREP
REMARK 200 STARTING MODEL: 3H2G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 6000, 0.10M MES, PH 6.7,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 51.80000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.35000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.80000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.35000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 GLY A 28
REMARK 465 SER A 29
REMARK 465 GLN A 30
REMARK 465 PRO A 31
REMARK 465 ALA A 32
REMARK 465 SER A 33
REMARK 465 GLY A 34
REMARK 465 SER A 35
REMARK 465 GLN A 36
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 CYS A 75 50.90 -145.59
REMARK 500 TYR A 125 159.89 81.77
REMARK 500 SER A 176 -118.35 64.03
REMARK 500 HIS A 192 -29.87 -143.61
REMARK 500 TYR A 293 -60.43 -94.31
REMARK 500 LEU A 392 -57.02 -129.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 550 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH A 583 DISTANCE = 5.41 ANGSTROMS
REMARK 525 HOH A 632 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH A 710 DISTANCE = 5.59 ANGSTROMS
REMARK 525 HOH A 717 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 724 DISTANCE = 5.59 ANGSTROMS
REMARK 525 HOH A 728 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH A 730 DISTANCE = 5.70 ANGSTROMS
REMARK 525 HOH A 762 DISTANCE = 5.05 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3H2G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A RICE CELL WALL DEGRADING ESTERASE
REMARK 900 LIPA FROM XANTHOMONAS ORYZAE
REMARK 900 RELATED ID: 3H2I RELATED DB: PDB
REMARK 900 RELATED ID: 3H2J RELATED DB: PDB
REMARK 900 RELATED ID: 3H2K RELATED DB: PDB
DBREF 3H2H A 1 397 UNP Q5H5J0 Q5H5J0_XANOR 45 441
SEQADV 3H2H PHE A 231 UNP Q5H5J0 GLY 275 ENGINEERED
SEQRES 1 A 397 ALA PRO ALA ARG GLY THR LEU LEU THR SER ASN PHE LEU
SEQRES 2 A 397 THR SER TYR THR ARG ASP ALA ILE SER ALA MET LEU ALA
SEQRES 3 A 397 SER GLY SER GLN PRO ALA SER GLY SER GLN PRO GLU GLN
SEQRES 4 A 397 ALA LYS CYS ASN VAL ARG VAL ALA GLU PHE THR TYR ALA
SEQRES 5 A 397 THR ILE GLY VAL GLU GLY GLU PRO ALA THR ALA SER GLY
SEQRES 6 A 397 VAL LEU LEU ILE PRO GLY GLY GLU ARG CYS SER GLY PRO
SEQRES 7 A 397 TYR PRO LEU LEU GLY TRP GLY HIS PRO THR GLU ALA LEU
SEQRES 8 A 397 ARG ALA GLN GLU GLN ALA LYS GLU ILE ARG ASP ALA LYS
SEQRES 9 A 397 GLY ASP ASP PRO LEU VAL THR ARG LEU ALA SER GLN GLY
SEQRES 10 A 397 TYR VAL VAL VAL GLY SER ASP TYR LEU GLY LEU GLY LYS
SEQRES 11 A 397 SER ASN TYR ALA TYR HIS PRO TYR LEU HIS SER ALA SER
SEQRES 12 A 397 GLU ALA SER ALA THR ILE ASP ALA MET ARG ALA ALA ARG
SEQRES 13 A 397 SER VAL LEU GLN HIS LEU LYS THR PRO LEU SER GLY LYS
SEQRES 14 A 397 VAL MET LEU SER GLY TYR SER GLN GLY GLY HIS THR ALA
SEQRES 15 A 397 MET ALA THR GLN ARG GLU ILE GLU ALA HIS LEU SER LYS
SEQRES 16 A 397 GLU PHE HIS LEU VAL ALA SER ALA PRO ILE SER GLY PRO
SEQRES 17 A 397 TYR ALA LEU GLU GLN THR PHE LEU ASP SER TRP SER GLY
SEQRES 18 A 397 SER ASN ALA VAL GLY GLU ASN THR PHE PHE ILE LEU LEU
SEQRES 19 A 397 GLY SER TYR ALA ILE VAL ALA MET GLN HIS THR TYR LYS
SEQRES 20 A 397 ASN ILE TYR LEU GLU PRO GLY GLN VAL PHE GLN ASP PRO
SEQRES 21 A 397 TRP ALA ALA LYS VAL GLU PRO LEU PHE PRO GLY LYS GLN
SEQRES 22 A 397 SER LEU THR ASP MET PHE LEU ASN ASP THR LEU PRO SER
SEQRES 23 A 397 ILE ASP LYS VAL LYS SER TYR PHE GLN PRO GLY PHE TYR
SEQRES 24 A 397 SER ASP PHE PRO SER ASN PRO ALA ASN PRO PHE ARG GLN
SEQRES 25 A 397 ASP LEU ALA ARG ASN ASN LEU LEU GLU TRP ALA PRO GLN
SEQRES 26 A 397 THR PRO THR LEU LEU CYS GLY SER SER ASN ASP ALA THR
SEQRES 27 A 397 VAL PRO LEU LYS ASN ALA GLN THR ALA ILE ALA SER PHE
SEQRES 28 A 397 GLN GLN ARG GLY SER ASN GLN VAL ALA LEU VAL ASP THR
SEQRES 29 A 397 GLY THR GLY ASN ALA SER ASP ASN SER ALA PHE ALA HIS
SEQRES 30 A 397 MET LEU THR LYS GLU SER CYS ILE VAL VAL VAL ARG ASP
SEQRES 31 A 397 GLN LEU LEU ASP LYS GLN ARG
FORMUL 2 HOH *380(H2 O)
HELIX 1 1 THR A 17 ALA A 26 1 10
HELIX 2 2 GLU A 95 ALA A 103 1 9
HELIX 3 3 ASP A 107 ARG A 112 1 6
HELIX 4 4 LEU A 113 GLY A 117 5 5
HELIX 5 5 HIS A 140 LYS A 163 1 24
HELIX 6 6 SER A 176 LEU A 193 1 18
HELIX 7 7 ALA A 210 TRP A 219 1 10
HELIX 8 8 PHE A 230 LYS A 247 1 18
HELIX 9 9 GLU A 252 VAL A 256 5 5
HELIX 10 10 VAL A 265 PHE A 269 5 5
HELIX 11 11 SER A 274 ASN A 281 1 8
HELIX 12 12 SER A 286 TYR A 293 5 8
HELIX 13 13 GLN A 295 ASN A 305 1 11
HELIX 14 14 ASN A 308 ARG A 316 1 9
HELIX 15 15 LEU A 341 ARG A 354 1 14
HELIX 16 16 ASN A 368 ASN A 372 5 5
HELIX 17 17 SER A 373 ALA A 374 5 2
HELIX 18 18 PHE A 375 LEU A 392 1 18
HELIX 19 19 LEU A 392 ARG A 397 1 6
SHEET 1 A 7 LEU A 7 TYR A 16 0
SHEET 2 A 7 ASN A 43 ILE A 54 -1 O VAL A 46 N THR A 14
SHEET 3 A 7 PRO A 60 GLY A 71 -1 O GLY A 71 N ASN A 43
SHEET 4 A 7 VAL A 119 SER A 123 -1 O GLY A 122 N VAL A 66
SHEET 5 A 7 TYR A 79 GLY A 85 1 N LEU A 82 O VAL A 119
SHEET 6 A 7 LEU A 166 TYR A 175 1 O MET A 171 N GLY A 83
SHEET 7 A 7 HIS A 198 ILE A 205 1 O HIS A 198 N VAL A 170
SHEET 1 B 2 THR A 328 GLY A 332 0
SHEET 2 B 2 VAL A 359 ASP A 363 1 O ALA A 360 N THR A 328
SSBOND 1 CYS A 42 CYS A 75 1555 1555 2.03
SSBOND 2 CYS A 331 CYS A 384 1555 1555 2.03
CISPEP 1 GLY A 77 PRO A 78 0 -0.11
CISPEP 2 ASP A 259 PRO A 260 0 0.02
CISPEP 3 PHE A 269 PRO A 270 0 -0.21
CRYST1 103.600 54.700 66.300 90.00 92.70 90.00 C 1 2 1 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 0.009653 0.000000 0.000455 0.00000
SCALE2 0.000000 0.018282 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015100 0.00000
TER 2949 ARG A 397
MASTER 284 0 0 19 9 0 0 6 3328 1 4 31
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