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HEADER HYDROLASE 26-MAY-26 27CT
TITLE CRYSTAL STRUCTURE OF DE NOVO DESIGNED ESTERASE RPA1511-2297
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RPA1511_2297;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLYASE, DE NOVO DESIGNED, THERMOSTABLE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.WANG,R.LIU
REVDAT 1 08-JUL-26 27CT 0
JRNL AUTH R.LIU,S.LI,P.ZHENG
JRNL TITL ENHANCED EFFICIENCY AND THERMOSTABILITY OF AN ESTERASE
JRNL TITL 2 RPA1511 FOR POLYLACTIC ACID DEPOLYMERIZATION BY PLACER AND
JRNL TITL 3 PROTEINMPNN.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 2.1_6048
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 28090
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.272
REMARK 3 R VALUE (WORKING SET) : 0.269
REMARK 3 FREE R VALUE : 0.303
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.520
REMARK 3 FREE R VALUE TEST SET COUNT : 2113
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.7200 - 7.7400 0.94 1753 141 0.3403 0.3400
REMARK 3 2 7.7400 - 6.2100 0.99 1791 145 0.3098 0.3382
REMARK 3 3 6.2100 - 5.4400 1.00 1783 145 0.2912 0.3131
REMARK 3 4 5.4400 - 4.9500 0.98 1736 141 0.2678 0.2683
REMARK 3 5 4.9500 - 4.6000 1.00 1770 147 0.2584 0.2733
REMARK 3 6 4.6000 - 4.3300 0.99 1765 139 0.2582 0.2989
REMARK 3 7 4.3300 - 4.1200 1.00 1714 141 0.2696 0.3180
REMARK 3 8 4.1200 - 3.9400 1.00 1785 146 0.2545 0.3112
REMARK 3 9 3.9400 - 3.7900 1.00 1728 141 0.2275 0.2911
REMARK 3 10 3.7900 - 3.6600 1.00 1752 139 0.2511 0.3007
REMARK 3 11 3.6600 - 3.5500 0.99 1738 138 0.2482 0.2873
REMARK 3 12 3.5500 - 3.4500 0.99 1691 137 0.2294 0.2784
REMARK 3 13 3.4500 - 3.3600 0.98 1754 146 0.2157 0.2677
REMARK 3 14 3.3600 - 3.2700 1.00 1717 143 0.2198 0.2962
REMARK 3 15 3.2700 - 3.2000 0.88 1500 124 0.2376 0.2935
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.399
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.444
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.22
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 14041
REMARK 3 ANGLE : 0.532 19095
REMARK 3 CHIRALITY : 0.043 2116
REMARK 3 PLANARITY : 0.005 2500
REMARK 3 DIHEDRAL : 11.559 5295
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : chain "A"
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "B" and resid 3 through 295)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "C" and resid 3 through 295)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "D" and resid 3 through 295)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "E" and resid 3 through 295)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 6
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "F" and resid 3 through 295)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 27CT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 29-MAY-26.
REMARK 100 THE DEPOSITION ID IS D_1300074773.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-26
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97861
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28090
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 19.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.13900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M MGCL2, 0.1M HEPES PH 8.0, 31%
REMARK 280 PEG550 MONOETHYLETHER, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 22.42500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 MET A 1
REMARK 465 LYS A 2
REMARK 465 LEU A 296
REMARK 465 GLU A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 LEU B 296
REMARK 465 GLU B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 LEU C 296
REMARK 465 GLU C 297
REMARK 465 HIS C 298
REMARK 465 HIS C 299
REMARK 465 HIS C 300
REMARK 465 HIS C 301
REMARK 465 HIS C 302
REMARK 465 HIS C 303
REMARK 465 LEU D 296
REMARK 465 GLU D 297
REMARK 465 HIS D 298
REMARK 465 HIS D 299
REMARK 465 HIS D 300
REMARK 465 HIS D 301
REMARK 465 HIS D 302
REMARK 465 HIS D 303
REMARK 465 LEU E 296
REMARK 465 GLU E 297
REMARK 465 HIS E 298
REMARK 465 HIS E 299
REMARK 465 HIS E 300
REMARK 465 HIS E 301
REMARK 465 HIS E 302
REMARK 465 HIS E 303
REMARK 465 LEU F 296
REMARK 465 GLU F 297
REMARK 465 HIS F 298
REMARK 465 HIS F 299
REMARK 465 HIS F 300
REMARK 465 HIS F 301
REMARK 465 HIS F 302
REMARK 465 HIS F 303
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 GLU A 8 -67.13 -91.87
REMARK 500 ALA A 50 -144.51 -98.99
REMARK 500 SER A 51 -177.06 -176.52
REMARK 500 SER A 114 -124.41 60.97
REMARK 500 LEU A 271 46.83 -101.84
REMARK 500 GLU B 8 -67.28 -92.47
REMARK 500 ALA B 50 -144.18 -98.93
REMARK 500 SER B 51 -177.10 -176.44
REMARK 500 SER B 114 -124.61 61.29
REMARK 500 LEU B 271 46.43 -101.64
REMARK 500 GLU C 8 -66.85 -92.61
REMARK 500 ALA C 50 -144.31 -99.08
REMARK 500 SER C 51 -177.11 -176.39
REMARK 500 SER C 114 -124.04 60.66
REMARK 500 LEU C 271 46.72 -101.87
REMARK 500 GLU D 8 -67.50 -92.00
REMARK 500 ALA D 50 -144.14 -99.15
REMARK 500 SER D 51 -177.13 -176.51
REMARK 500 SER D 114 -124.10 61.05
REMARK 500 LEU D 271 46.72 -101.93
REMARK 500 GLU E 8 -67.46 -92.00
REMARK 500 ALA E 50 -144.54 -99.23
REMARK 500 SER E 51 -177.48 -176.63
REMARK 500 SER E 114 -124.14 61.12
REMARK 500 LEU E 271 46.58 -101.78
REMARK 500 GLU F 8 -67.15 -92.01
REMARK 500 ALA F 50 -143.86 -98.85
REMARK 500 SER F 51 -177.19 -175.94
REMARK 500 SER F 114 -124.11 60.80
REMARK 500 LEU F 271 46.42 -101.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 21DL RELATED DB: PDB
REMARK 900 21DL WAS DESIGNED BASED ON THE SAME TEMPLATE
DBREF 27CT A 1 303 PDB 27CT 27CT 1 303
DBREF 27CT B 1 303 PDB 27CT 27CT 1 303
DBREF 27CT C 1 303 PDB 27CT 27CT 1 303
DBREF 27CT D 1 303 PDB 27CT 27CT 1 303
DBREF 27CT E 1 303 PDB 27CT 27CT 1 303
DBREF 27CT F 1 303 PDB 27CT 27CT 1 303
SEQRES 1 A 303 MET LYS ASN LEU ASN TRP GLU GLU ASP GLY LYS ASP TRP
SEQRES 2 A 303 PRO LEU ARG GLU ARG SER ARG PHE ILE GLU ALA GLY GLY
SEQRES 3 A 303 ILE ARG TRP HIS VAL GLN LEU LEU GLY ASP PRO SER ALA
SEQRES 4 A 303 PRO ALA LEU LEU LEU ILE HIS GLY THR GLY ALA SER SER
SEQRES 5 A 303 HIS SER TRP ARG GLY LEU ALA PRO LEU LEU SER GLU ARG
SEQRES 6 A 303 TYR TYR VAL VAL ALA PRO ASP LEU PRO GLY HIS GLY PHE
SEQRES 7 A 303 THR GLU THR PRO GLU GLU GLU LYS LEU SER LEU PRO GLY
SEQRES 8 A 303 MET ALA GLU LEU LEU ALA GLU LEU LEU LYS VAL LEU GLY
SEQRES 9 A 303 VAL GLN PRO GLU ILE VAL ILE GLY HIS SER ALA GLY ALA
SEQRES 10 A 303 ALA ILE ALA ALA ARG MET ALA LEU ASP GLY LEU ILE ASP
SEQRES 11 A 303 PRO LYS ILE ILE PHE ALA LEU ASN GLY ALA PHE LEU PRO
SEQRES 12 A 303 TYR GLY GLY GLU ALA TYR LYS GLU PHE LYS PRO VAL ALA
SEQRES 13 A 303 LYS LYS LEU ALA ALA ASN PRO GLN THR PRO VAL ALA PHE
SEQRES 14 A 303 ALA GLU GLU ALA SER LYS PRO GLY ALA ILE GLU ARG LEU
SEQRES 15 A 303 ILE ALA SER THR GLY SER ARG ILE ASP ALA GLU GLY LEU
SEQRES 16 A 303 GLU HIS TYR ARG LYS LEU TRP SER SER PRO GLU HIS VAL
SEQRES 17 A 303 LYS ALA ALA LEU THR MET MET ALA ASN TRP ASP LEU GLU
SEQRES 18 A 303 PRO LEU LEU GLU ARG LEU PRO GLU LEU LYS PRO LEU LEU
SEQRES 19 A 303 VAL LEU VAL ALA ALA GLU GLN ASP ARG ALA VAL PRO PRO
SEQRES 20 A 303 SER VAL ALA GLU LYS VAL LYS GLU LEU LEU PRO ARG ALA
SEQRES 21 A 303 GLU ILE GLU ARG ILE PRO ALA LEU GLY HIS LEU ALA HIS
SEQRES 22 A 303 GLU GLU ASP PRO GLU LEU ILE ALA GLU LEU ILE GLU ARG
SEQRES 23 A 303 HIS VAL GLU ARG LEU GLN ALA GLU GLN LEU GLU HIS HIS
SEQRES 24 A 303 HIS HIS HIS HIS
SEQRES 1 B 303 MET LYS ASN LEU ASN TRP GLU GLU ASP GLY LYS ASP TRP
SEQRES 2 B 303 PRO LEU ARG GLU ARG SER ARG PHE ILE GLU ALA GLY GLY
SEQRES 3 B 303 ILE ARG TRP HIS VAL GLN LEU LEU GLY ASP PRO SER ALA
SEQRES 4 B 303 PRO ALA LEU LEU LEU ILE HIS GLY THR GLY ALA SER SER
SEQRES 5 B 303 HIS SER TRP ARG GLY LEU ALA PRO LEU LEU SER GLU ARG
SEQRES 6 B 303 TYR TYR VAL VAL ALA PRO ASP LEU PRO GLY HIS GLY PHE
SEQRES 7 B 303 THR GLU THR PRO GLU GLU GLU LYS LEU SER LEU PRO GLY
SEQRES 8 B 303 MET ALA GLU LEU LEU ALA GLU LEU LEU LYS VAL LEU GLY
SEQRES 9 B 303 VAL GLN PRO GLU ILE VAL ILE GLY HIS SER ALA GLY ALA
SEQRES 10 B 303 ALA ILE ALA ALA ARG MET ALA LEU ASP GLY LEU ILE ASP
SEQRES 11 B 303 PRO LYS ILE ILE PHE ALA LEU ASN GLY ALA PHE LEU PRO
SEQRES 12 B 303 TYR GLY GLY GLU ALA TYR LYS GLU PHE LYS PRO VAL ALA
SEQRES 13 B 303 LYS LYS LEU ALA ALA ASN PRO GLN THR PRO VAL ALA PHE
SEQRES 14 B 303 ALA GLU GLU ALA SER LYS PRO GLY ALA ILE GLU ARG LEU
SEQRES 15 B 303 ILE ALA SER THR GLY SER ARG ILE ASP ALA GLU GLY LEU
SEQRES 16 B 303 GLU HIS TYR ARG LYS LEU TRP SER SER PRO GLU HIS VAL
SEQRES 17 B 303 LYS ALA ALA LEU THR MET MET ALA ASN TRP ASP LEU GLU
SEQRES 18 B 303 PRO LEU LEU GLU ARG LEU PRO GLU LEU LYS PRO LEU LEU
SEQRES 19 B 303 VAL LEU VAL ALA ALA GLU GLN ASP ARG ALA VAL PRO PRO
SEQRES 20 B 303 SER VAL ALA GLU LYS VAL LYS GLU LEU LEU PRO ARG ALA
SEQRES 21 B 303 GLU ILE GLU ARG ILE PRO ALA LEU GLY HIS LEU ALA HIS
SEQRES 22 B 303 GLU GLU ASP PRO GLU LEU ILE ALA GLU LEU ILE GLU ARG
SEQRES 23 B 303 HIS VAL GLU ARG LEU GLN ALA GLU GLN LEU GLU HIS HIS
SEQRES 24 B 303 HIS HIS HIS HIS
SEQRES 1 C 303 MET LYS ASN LEU ASN TRP GLU GLU ASP GLY LYS ASP TRP
SEQRES 2 C 303 PRO LEU ARG GLU ARG SER ARG PHE ILE GLU ALA GLY GLY
SEQRES 3 C 303 ILE ARG TRP HIS VAL GLN LEU LEU GLY ASP PRO SER ALA
SEQRES 4 C 303 PRO ALA LEU LEU LEU ILE HIS GLY THR GLY ALA SER SER
SEQRES 5 C 303 HIS SER TRP ARG GLY LEU ALA PRO LEU LEU SER GLU ARG
SEQRES 6 C 303 TYR TYR VAL VAL ALA PRO ASP LEU PRO GLY HIS GLY PHE
SEQRES 7 C 303 THR GLU THR PRO GLU GLU GLU LYS LEU SER LEU PRO GLY
SEQRES 8 C 303 MET ALA GLU LEU LEU ALA GLU LEU LEU LYS VAL LEU GLY
SEQRES 9 C 303 VAL GLN PRO GLU ILE VAL ILE GLY HIS SER ALA GLY ALA
SEQRES 10 C 303 ALA ILE ALA ALA ARG MET ALA LEU ASP GLY LEU ILE ASP
SEQRES 11 C 303 PRO LYS ILE ILE PHE ALA LEU ASN GLY ALA PHE LEU PRO
SEQRES 12 C 303 TYR GLY GLY GLU ALA TYR LYS GLU PHE LYS PRO VAL ALA
SEQRES 13 C 303 LYS LYS LEU ALA ALA ASN PRO GLN THR PRO VAL ALA PHE
SEQRES 14 C 303 ALA GLU GLU ALA SER LYS PRO GLY ALA ILE GLU ARG LEU
SEQRES 15 C 303 ILE ALA SER THR GLY SER ARG ILE ASP ALA GLU GLY LEU
SEQRES 16 C 303 GLU HIS TYR ARG LYS LEU TRP SER SER PRO GLU HIS VAL
SEQRES 17 C 303 LYS ALA ALA LEU THR MET MET ALA ASN TRP ASP LEU GLU
SEQRES 18 C 303 PRO LEU LEU GLU ARG LEU PRO GLU LEU LYS PRO LEU LEU
SEQRES 19 C 303 VAL LEU VAL ALA ALA GLU GLN ASP ARG ALA VAL PRO PRO
SEQRES 20 C 303 SER VAL ALA GLU LYS VAL LYS GLU LEU LEU PRO ARG ALA
SEQRES 21 C 303 GLU ILE GLU ARG ILE PRO ALA LEU GLY HIS LEU ALA HIS
SEQRES 22 C 303 GLU GLU ASP PRO GLU LEU ILE ALA GLU LEU ILE GLU ARG
SEQRES 23 C 303 HIS VAL GLU ARG LEU GLN ALA GLU GLN LEU GLU HIS HIS
SEQRES 24 C 303 HIS HIS HIS HIS
SEQRES 1 D 303 MET LYS ASN LEU ASN TRP GLU GLU ASP GLY LYS ASP TRP
SEQRES 2 D 303 PRO LEU ARG GLU ARG SER ARG PHE ILE GLU ALA GLY GLY
SEQRES 3 D 303 ILE ARG TRP HIS VAL GLN LEU LEU GLY ASP PRO SER ALA
SEQRES 4 D 303 PRO ALA LEU LEU LEU ILE HIS GLY THR GLY ALA SER SER
SEQRES 5 D 303 HIS SER TRP ARG GLY LEU ALA PRO LEU LEU SER GLU ARG
SEQRES 6 D 303 TYR TYR VAL VAL ALA PRO ASP LEU PRO GLY HIS GLY PHE
SEQRES 7 D 303 THR GLU THR PRO GLU GLU GLU LYS LEU SER LEU PRO GLY
SEQRES 8 D 303 MET ALA GLU LEU LEU ALA GLU LEU LEU LYS VAL LEU GLY
SEQRES 9 D 303 VAL GLN PRO GLU ILE VAL ILE GLY HIS SER ALA GLY ALA
SEQRES 10 D 303 ALA ILE ALA ALA ARG MET ALA LEU ASP GLY LEU ILE ASP
SEQRES 11 D 303 PRO LYS ILE ILE PHE ALA LEU ASN GLY ALA PHE LEU PRO
SEQRES 12 D 303 TYR GLY GLY GLU ALA TYR LYS GLU PHE LYS PRO VAL ALA
SEQRES 13 D 303 LYS LYS LEU ALA ALA ASN PRO GLN THR PRO VAL ALA PHE
SEQRES 14 D 303 ALA GLU GLU ALA SER LYS PRO GLY ALA ILE GLU ARG LEU
SEQRES 15 D 303 ILE ALA SER THR GLY SER ARG ILE ASP ALA GLU GLY LEU
SEQRES 16 D 303 GLU HIS TYR ARG LYS LEU TRP SER SER PRO GLU HIS VAL
SEQRES 17 D 303 LYS ALA ALA LEU THR MET MET ALA ASN TRP ASP LEU GLU
SEQRES 18 D 303 PRO LEU LEU GLU ARG LEU PRO GLU LEU LYS PRO LEU LEU
SEQRES 19 D 303 VAL LEU VAL ALA ALA GLU GLN ASP ARG ALA VAL PRO PRO
SEQRES 20 D 303 SER VAL ALA GLU LYS VAL LYS GLU LEU LEU PRO ARG ALA
SEQRES 21 D 303 GLU ILE GLU ARG ILE PRO ALA LEU GLY HIS LEU ALA HIS
SEQRES 22 D 303 GLU GLU ASP PRO GLU LEU ILE ALA GLU LEU ILE GLU ARG
SEQRES 23 D 303 HIS VAL GLU ARG LEU GLN ALA GLU GLN LEU GLU HIS HIS
SEQRES 24 D 303 HIS HIS HIS HIS
SEQRES 1 E 303 MET LYS ASN LEU ASN TRP GLU GLU ASP GLY LYS ASP TRP
SEQRES 2 E 303 PRO LEU ARG GLU ARG SER ARG PHE ILE GLU ALA GLY GLY
SEQRES 3 E 303 ILE ARG TRP HIS VAL GLN LEU LEU GLY ASP PRO SER ALA
SEQRES 4 E 303 PRO ALA LEU LEU LEU ILE HIS GLY THR GLY ALA SER SER
SEQRES 5 E 303 HIS SER TRP ARG GLY LEU ALA PRO LEU LEU SER GLU ARG
SEQRES 6 E 303 TYR TYR VAL VAL ALA PRO ASP LEU PRO GLY HIS GLY PHE
SEQRES 7 E 303 THR GLU THR PRO GLU GLU GLU LYS LEU SER LEU PRO GLY
SEQRES 8 E 303 MET ALA GLU LEU LEU ALA GLU LEU LEU LYS VAL LEU GLY
SEQRES 9 E 303 VAL GLN PRO GLU ILE VAL ILE GLY HIS SER ALA GLY ALA
SEQRES 10 E 303 ALA ILE ALA ALA ARG MET ALA LEU ASP GLY LEU ILE ASP
SEQRES 11 E 303 PRO LYS ILE ILE PHE ALA LEU ASN GLY ALA PHE LEU PRO
SEQRES 12 E 303 TYR GLY GLY GLU ALA TYR LYS GLU PHE LYS PRO VAL ALA
SEQRES 13 E 303 LYS LYS LEU ALA ALA ASN PRO GLN THR PRO VAL ALA PHE
SEQRES 14 E 303 ALA GLU GLU ALA SER LYS PRO GLY ALA ILE GLU ARG LEU
SEQRES 15 E 303 ILE ALA SER THR GLY SER ARG ILE ASP ALA GLU GLY LEU
SEQRES 16 E 303 GLU HIS TYR ARG LYS LEU TRP SER SER PRO GLU HIS VAL
SEQRES 17 E 303 LYS ALA ALA LEU THR MET MET ALA ASN TRP ASP LEU GLU
SEQRES 18 E 303 PRO LEU LEU GLU ARG LEU PRO GLU LEU LYS PRO LEU LEU
SEQRES 19 E 303 VAL LEU VAL ALA ALA GLU GLN ASP ARG ALA VAL PRO PRO
SEQRES 20 E 303 SER VAL ALA GLU LYS VAL LYS GLU LEU LEU PRO ARG ALA
SEQRES 21 E 303 GLU ILE GLU ARG ILE PRO ALA LEU GLY HIS LEU ALA HIS
SEQRES 22 E 303 GLU GLU ASP PRO GLU LEU ILE ALA GLU LEU ILE GLU ARG
SEQRES 23 E 303 HIS VAL GLU ARG LEU GLN ALA GLU GLN LEU GLU HIS HIS
SEQRES 24 E 303 HIS HIS HIS HIS
SEQRES 1 F 303 MET LYS ASN LEU ASN TRP GLU GLU ASP GLY LYS ASP TRP
SEQRES 2 F 303 PRO LEU ARG GLU ARG SER ARG PHE ILE GLU ALA GLY GLY
SEQRES 3 F 303 ILE ARG TRP HIS VAL GLN LEU LEU GLY ASP PRO SER ALA
SEQRES 4 F 303 PRO ALA LEU LEU LEU ILE HIS GLY THR GLY ALA SER SER
SEQRES 5 F 303 HIS SER TRP ARG GLY LEU ALA PRO LEU LEU SER GLU ARG
SEQRES 6 F 303 TYR TYR VAL VAL ALA PRO ASP LEU PRO GLY HIS GLY PHE
SEQRES 7 F 303 THR GLU THR PRO GLU GLU GLU LYS LEU SER LEU PRO GLY
SEQRES 8 F 303 MET ALA GLU LEU LEU ALA GLU LEU LEU LYS VAL LEU GLY
SEQRES 9 F 303 VAL GLN PRO GLU ILE VAL ILE GLY HIS SER ALA GLY ALA
SEQRES 10 F 303 ALA ILE ALA ALA ARG MET ALA LEU ASP GLY LEU ILE ASP
SEQRES 11 F 303 PRO LYS ILE ILE PHE ALA LEU ASN GLY ALA PHE LEU PRO
SEQRES 12 F 303 TYR GLY GLY GLU ALA TYR LYS GLU PHE LYS PRO VAL ALA
SEQRES 13 F 303 LYS LYS LEU ALA ALA ASN PRO GLN THR PRO VAL ALA PHE
SEQRES 14 F 303 ALA GLU GLU ALA SER LYS PRO GLY ALA ILE GLU ARG LEU
SEQRES 15 F 303 ILE ALA SER THR GLY SER ARG ILE ASP ALA GLU GLY LEU
SEQRES 16 F 303 GLU HIS TYR ARG LYS LEU TRP SER SER PRO GLU HIS VAL
SEQRES 17 F 303 LYS ALA ALA LEU THR MET MET ALA ASN TRP ASP LEU GLU
SEQRES 18 F 303 PRO LEU LEU GLU ARG LEU PRO GLU LEU LYS PRO LEU LEU
SEQRES 19 F 303 VAL LEU VAL ALA ALA GLU GLN ASP ARG ALA VAL PRO PRO
SEQRES 20 F 303 SER VAL ALA GLU LYS VAL LYS GLU LEU LEU PRO ARG ALA
SEQRES 21 F 303 GLU ILE GLU ARG ILE PRO ALA LEU GLY HIS LEU ALA HIS
SEQRES 22 F 303 GLU GLU ASP PRO GLU LEU ILE ALA GLU LEU ILE GLU ARG
SEQRES 23 F 303 HIS VAL GLU ARG LEU GLN ALA GLU GLN LEU GLU HIS HIS
SEQRES 24 F 303 HIS HIS HIS HIS
FORMUL 7 HOH *22(H2 O)
HELIX 1 AA1 ASN A 5 GLY A 10 1 6
HELIX 2 AA2 LEU A 15 GLU A 17 5 3
HELIX 3 AA3 SER A 51 ARG A 56 5 6
HELIX 4 AA4 GLY A 57 SER A 63 1 7
HELIX 5 AA5 GLU A 83 LEU A 87 5 5
HELIX 6 AA6 SER A 88 GLY A 104 1 17
HELIX 7 AA7 ALA A 115 ASP A 126 1 12
HELIX 8 AA8 GLY A 145 GLU A 147 5 3
HELIX 9 AA9 ALA A 148 ASN A 162 1 15
HELIX 10 AB1 PRO A 163 LYS A 175 1 13
HELIX 11 AB2 GLY A 177 THR A 186 1 10
HELIX 12 AB3 ASP A 191 SER A 203 1 13
HELIX 13 AB4 SER A 204 ASN A 217 1 14
HELIX 14 AB5 LEU A 220 LEU A 227 1 8
HELIX 15 AB6 PRO A 228 LEU A 230 5 3
HELIX 16 AB7 PRO A 246 LEU A 257 1 12
HELIX 17 AB8 LEU A 271 ASP A 276 1 6
HELIX 18 AB9 ASP A 276 GLN A 295 1 20
HELIX 19 AC1 ASN B 5 GLY B 10 1 6
HELIX 20 AC2 LEU B 15 GLU B 17 5 3
HELIX 21 AC3 SER B 51 ARG B 56 5 6
HELIX 22 AC4 GLY B 57 SER B 63 1 7
HELIX 23 AC5 GLU B 83 LEU B 87 5 5
HELIX 24 AC6 SER B 88 GLY B 104 1 17
HELIX 25 AC7 ALA B 115 ASP B 126 1 12
HELIX 26 AC8 GLY B 145 GLU B 147 5 3
HELIX 27 AC9 ALA B 148 ASN B 162 1 15
HELIX 28 AD1 PRO B 163 LYS B 175 1 13
HELIX 29 AD2 GLY B 177 THR B 186 1 10
HELIX 30 AD3 ASP B 191 SER B 203 1 13
HELIX 31 AD4 SER B 204 ASN B 217 1 14
HELIX 32 AD5 LEU B 220 LEU B 227 1 8
HELIX 33 AD6 PRO B 228 LEU B 230 5 3
HELIX 34 AD7 PRO B 246 LEU B 257 1 12
HELIX 35 AD8 LEU B 271 ASP B 276 1 6
HELIX 36 AD9 ASP B 276 GLN B 295 1 20
HELIX 37 AE1 ASN C 5 GLY C 10 1 6
HELIX 38 AE2 LEU C 15 GLU C 17 5 3
HELIX 39 AE3 SER C 51 ARG C 56 5 6
HELIX 40 AE4 GLY C 57 SER C 63 1 7
HELIX 41 AE5 GLU C 83 LEU C 87 5 5
HELIX 42 AE6 SER C 88 GLY C 104 1 17
HELIX 43 AE7 ALA C 115 ASP C 126 1 12
HELIX 44 AE8 GLY C 145 GLU C 147 5 3
HELIX 45 AE9 ALA C 148 ASN C 162 1 15
HELIX 46 AF1 PRO C 163 LYS C 175 1 13
HELIX 47 AF2 GLY C 177 THR C 186 1 10
HELIX 48 AF3 ASP C 191 SER C 203 1 13
HELIX 49 AF4 SER C 204 ASN C 217 1 14
HELIX 50 AF5 LEU C 220 LEU C 227 1 8
HELIX 51 AF6 PRO C 228 LEU C 230 5 3
HELIX 52 AF7 PRO C 246 LEU C 257 1 12
HELIX 53 AF8 LEU C 271 ASP C 276 1 6
HELIX 54 AF9 ASP C 276 GLN C 295 1 20
HELIX 55 AG1 ASN D 5 GLY D 10 1 6
HELIX 56 AG2 LEU D 15 GLU D 17 5 3
HELIX 57 AG3 SER D 51 ARG D 56 5 6
HELIX 58 AG4 GLY D 57 SER D 63 1 7
HELIX 59 AG5 GLU D 83 LEU D 87 5 5
HELIX 60 AG6 SER D 88 GLY D 104 1 17
HELIX 61 AG7 ALA D 115 ASP D 126 1 12
HELIX 62 AG8 GLY D 145 GLU D 147 5 3
HELIX 63 AG9 ALA D 148 ASN D 162 1 15
HELIX 64 AH1 PRO D 163 LYS D 175 1 13
HELIX 65 AH2 GLY D 177 THR D 186 1 10
HELIX 66 AH3 ASP D 191 SER D 203 1 13
HELIX 67 AH4 SER D 204 ASN D 217 1 14
HELIX 68 AH5 LEU D 220 LEU D 227 1 8
HELIX 69 AH6 PRO D 228 LEU D 230 5 3
HELIX 70 AH7 PRO D 246 LEU D 257 1 12
HELIX 71 AH8 LEU D 271 ASP D 276 1 6
HELIX 72 AH9 ASP D 276 GLN D 295 1 20
HELIX 73 AI1 ASN E 5 GLY E 10 1 6
HELIX 74 AI2 LEU E 15 GLU E 17 5 3
HELIX 75 AI3 SER E 51 ARG E 56 5 6
HELIX 76 AI4 GLY E 57 SER E 63 1 7
HELIX 77 AI5 GLU E 83 LEU E 87 5 5
HELIX 78 AI6 SER E 88 GLY E 104 1 17
HELIX 79 AI7 ALA E 115 ASP E 126 1 12
HELIX 80 AI8 GLY E 145 GLU E 147 5 3
HELIX 81 AI9 ALA E 148 ASN E 162 1 15
HELIX 82 AJ1 PRO E 163 LYS E 175 1 13
HELIX 83 AJ2 GLY E 177 THR E 186 1 10
HELIX 84 AJ3 ASP E 191 SER E 203 1 13
HELIX 85 AJ4 SER E 204 ASN E 217 1 14
HELIX 86 AJ5 LEU E 220 LEU E 227 1 8
HELIX 87 AJ6 PRO E 228 LEU E 230 5 3
HELIX 88 AJ7 PRO E 247 LEU E 257 1 11
HELIX 89 AJ8 LEU E 271 ASP E 276 1 6
HELIX 90 AJ9 ASP E 276 GLN E 295 1 20
HELIX 91 AK1 ASN F 5 GLY F 10 1 6
HELIX 92 AK2 LEU F 15 GLU F 17 5 3
HELIX 93 AK3 SER F 51 ARG F 56 5 6
HELIX 94 AK4 GLY F 57 SER F 63 1 7
HELIX 95 AK5 GLU F 83 LEU F 87 5 5
HELIX 96 AK6 SER F 88 GLY F 104 1 17
HELIX 97 AK7 SER F 114 ASP F 126 1 13
HELIX 98 AK8 GLY F 145 GLU F 147 5 3
HELIX 99 AK9 ALA F 148 ASN F 162 1 15
HELIX 100 AL1 PRO F 163 LYS F 175 1 13
HELIX 101 AL2 GLY F 177 THR F 186 1 10
HELIX 102 AL3 ASP F 191 SER F 203 1 13
HELIX 103 AL4 SER F 204 ASN F 217 1 14
HELIX 104 AL5 LEU F 220 LEU F 227 1 8
HELIX 105 AL6 PRO F 228 LEU F 230 5 3
HELIX 106 AL7 PRO F 246 LEU F 257 1 12
HELIX 107 AL8 LEU F 271 ASP F 276 1 6
HELIX 108 AL9 ASP F 276 GLN F 295 1 20
SHEET 1 AA1 8 SER A 19 ALA A 24 0
SHEET 2 AA1 8 ILE A 27 LEU A 34 -1 O TRP A 29 N ILE A 22
SHEET 3 AA1 8 TYR A 67 PRO A 71 -1 O ALA A 70 N GLN A 32
SHEET 4 AA1 8 ALA A 41 ILE A 45 1 N LEU A 44 O VAL A 69
SHEET 5 AA1 8 ILE A 109 HIS A 113 1 O ILE A 111 N LEU A 43
SHEET 6 AA1 8 ILE A 133 LEU A 137 1 O PHE A 135 N VAL A 110
SHEET 7 AA1 8 LEU A 233 ALA A 239 1 O VAL A 235 N ILE A 134
SHEET 8 AA1 8 GLU A 261 ILE A 265 1 O GLU A 263 N ALA A 238
SHEET 1 AA2 8 SER B 19 ALA B 24 0
SHEET 2 AA2 8 ILE B 27 LEU B 34 -1 O TRP B 29 N ILE B 22
SHEET 3 AA2 8 TYR B 67 PRO B 71 -1 O ALA B 70 N GLN B 32
SHEET 4 AA2 8 ALA B 41 ILE B 45 1 N LEU B 44 O VAL B 69
SHEET 5 AA2 8 ILE B 109 HIS B 113 1 O ILE B 111 N LEU B 43
SHEET 6 AA2 8 ILE B 133 LEU B 137 1 O PHE B 135 N VAL B 110
SHEET 7 AA2 8 LEU B 233 ALA B 239 1 O LEU B 233 N ILE B 134
SHEET 8 AA2 8 GLU B 261 ILE B 265 1 O GLU B 263 N ALA B 238
SHEET 1 AA3 8 SER C 19 ALA C 24 0
SHEET 2 AA3 8 ILE C 27 LEU C 34 -1 O TRP C 29 N ILE C 22
SHEET 3 AA3 8 TYR C 67 PRO C 71 -1 O ALA C 70 N GLN C 32
SHEET 4 AA3 8 ALA C 41 ILE C 45 1 N LEU C 44 O VAL C 69
SHEET 5 AA3 8 ILE C 109 HIS C 113 1 O ILE C 111 N LEU C 43
SHEET 6 AA3 8 ILE C 133 LEU C 137 1 O PHE C 135 N VAL C 110
SHEET 7 AA3 8 LEU C 233 ALA C 239 1 O VAL C 235 N ALA C 136
SHEET 8 AA3 8 GLU C 261 ILE C 265 1 O GLU C 263 N ALA C 238
SHEET 1 AA4 8 SER D 19 ALA D 24 0
SHEET 2 AA4 8 ILE D 27 LEU D 34 -1 O TRP D 29 N ILE D 22
SHEET 3 AA4 8 TYR D 67 PRO D 71 -1 O ALA D 70 N GLN D 32
SHEET 4 AA4 8 ALA D 41 ILE D 45 1 N LEU D 44 O VAL D 69
SHEET 5 AA4 8 ILE D 109 HIS D 113 1 O ILE D 111 N LEU D 43
SHEET 6 AA4 8 ILE D 133 LEU D 137 1 O PHE D 135 N VAL D 110
SHEET 7 AA4 8 LEU D 233 ALA D 239 1 O VAL D 235 N ALA D 136
SHEET 8 AA4 8 GLU D 261 ILE D 265 1 O GLU D 263 N ALA D 238
SHEET 1 AA5 8 SER E 19 ALA E 24 0
SHEET 2 AA5 8 ILE E 27 LEU E 34 -1 O TRP E 29 N ILE E 22
SHEET 3 AA5 8 TYR E 67 PRO E 71 -1 O ALA E 70 N GLN E 32
SHEET 4 AA5 8 ALA E 41 ILE E 45 1 N LEU E 44 O VAL E 69
SHEET 5 AA5 8 ILE E 109 HIS E 113 1 O ILE E 111 N LEU E 43
SHEET 6 AA5 8 ILE E 133 LEU E 137 1 O PHE E 135 N VAL E 110
SHEET 7 AA5 8 LEU E 233 ALA E 239 1 O VAL E 235 N ALA E 136
SHEET 8 AA5 8 GLU E 261 ILE E 265 1 O GLU E 263 N ALA E 238
SHEET 1 AA6 8 SER F 19 ALA F 24 0
SHEET 2 AA6 8 ILE F 27 LEU F 34 -1 O TRP F 29 N ILE F 22
SHEET 3 AA6 8 TYR F 67 PRO F 71 -1 O ALA F 70 N GLN F 32
SHEET 4 AA6 8 ALA F 41 ILE F 45 1 N LEU F 44 O VAL F 69
SHEET 5 AA6 8 ILE F 109 HIS F 113 1 O ILE F 111 N LEU F 43
SHEET 6 AA6 8 ILE F 133 LEU F 137 1 O PHE F 135 N VAL F 110
SHEET 7 AA6 8 LEU F 233 ALA F 239 1 O VAL F 235 N ALA F 136
SHEET 8 AA6 8 GLU F 261 ILE F 265 1 O GLU F 263 N ALA F 238
CRYST1 128.230 44.850 161.890 90.00 113.31 90.00 P 1 21 1 12
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 0.007798 0.000000 0.003360 0.00000
SCALE2 0.000000 0.022297 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006726 0.00000
MTRIX1 1 0.988569 0.150663 0.005705 44.27981 1
MTRIX2 1 -0.150098 0.987024 -0.057046 4.96439 1
MTRIX3 1 -0.014226 0.055538 0.998355 -0.95066 1
MTRIX1 2 0.992349 0.123395 -0.004179 -41.16641 1
MTRIX2 2 -0.123463 0.991527 -0.040398 2.25691 1
MTRIX3 2 -0.000841 0.040605 0.999175 -0.64682 1
MTRIX1 3 -0.985235 -0.171207 -0.000467 46.88195 1
MTRIX2 3 -0.170898 0.983288 0.062755 1.10549 1
MTRIX3 3 -0.010285 0.061908 -0.998029 75.01937 1
MTRIX1 4 -0.991704 -0.128248 -0.008691 5.25852 1
MTRIX2 4 -0.128467 0.986528 0.101284 -2.93321 1
MTRIX3 4 -0.004416 0.101560 -0.994820 74.26281 1
MTRIX1 5 -0.999936 0.010971 0.002906 91.61589 1
MTRIX2 5 0.011315 0.983557 0.180243 -7.11444 1
MTRIX3 5 -0.000881 0.180264 -0.983618 73.43541 1
TER 2271 GLN A 295
TER 4559 GLN B 295
TER 6847 GLN C 295
TER 9135 GLN D 295
TER 11423 GLN E 295
TER 13711 GLN F 295
MASTER 368 0 0 108 48 0 0 2113727 6 0 144
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