HEADER HYDROLASE 11-JAN-05 1YIF
TITLE CRYSTAL STRUCTURE OF BETA-1,4-XYLOSIDASE FROM BACILLUS SUBTILIS, NEW
TITLE 2 YORK STRUCTURAL GENOMICS CONSORTIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-1,4-XYLOSIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.2.1.37;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: XYNB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS GLYCOSIDASE, XYLAN, XYLOSIDASE, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, NYSGXRC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PATSKOVSKY,S.C.ALMO,S.K.BURLEY,NEW YORK SGX RESEARCH CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 5 14-FEB-24 1YIF 1 REMARK
REVDAT 4 03-FEB-21 1YIF 1 AUTHOR
REVDAT 3 11-OCT-17 1YIF 1 REMARK
REVDAT 2 24-FEB-09 1YIF 1 VERSN
REVDAT 1 18-JAN-05 1YIF 0
JRNL AUTH Y.PATSKOVSKY,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF BETA-1,4-XYLOSIDASE FROM BACILLUS
JRNL TITL 2 SUBTILIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 236885.370
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 200404
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) : 0.205
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.900
REMARK 3 FREE R VALUE TEST SET COUNT : 5889
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 24072
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 709
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17356
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 2728
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.93000
REMARK 3 B22 (A**2) : -1.20000
REMARK 3 B33 (A**2) : 2.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.170
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) : 1.220 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.770 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.830 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.640 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 29.18
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.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.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 1YIF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031547.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
REMARK 200 NUMBER OF CRYSTALS USED : 2
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 203403
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.19800
REMARK 200 R SYM FOR SHELL (I) : 0.22500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, 0.1M BIS-TRIS, 0.1M AMMONIUM
REMARK 280 ACETATE , PH 5.50, VAPOR DIFFUSION, TEMPERATURE 290K
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 52.30500
REMARK 290 SMTRY3 2 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 300 REMARK: THE BIOLOGICAL ASSEMBLY MOST LIKELY IS A HOMOTETRAMER
REMARK 300 COMPOSED OF FOUR IDENTICAL PROTEIN MONOMERS. THE ASYMMETRIC UNIT
REMARK 300 CONTAINS ONE FULL TETRAMER (CHAINS A,B,C AND D)
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 72590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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 MET B 1
REMARK 465 MET C 1
REMARK 465 MET D 1
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 PRO A 445 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 ASP D 272 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 PRO D 445 C - N - CA ANGL. DEV. = 9.6 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 PHE A 11 94.56 -52.08
REMARK 500 ASN A 12 70.22 -155.47
REMARK 500 PHE A 31 -117.54 51.48
REMARK 500 VAL A 37 117.15 61.26
REMARK 500 LEU A 45 -3.17 68.69
REMARK 500 TRP A 73 -157.60 -89.53
REMARK 500 LYS A 99 57.41 -143.48
REMARK 500 CYS A 108 136.68 -170.46
REMARK 500 LEU A 121 -82.98 -104.35
REMARK 500 THR A 180 -166.17 -113.26
REMARK 500 LYS A 183 -168.26 54.59
REMARK 500 ARG A 207 -144.52 -87.54
REMARK 500 THR A 234 141.46 174.76
REMARK 500 ARG A 346 -43.35 60.53
REMARK 500 HIS A 368 -137.19 -128.61
REMARK 500 PHE A 375 -83.88 -115.64
REMARK 500 HIS A 388 81.26 -150.75
REMARK 500 LYS A 467 -98.81 63.23
REMARK 500 ASN A 477 24.80 -154.87
REMARK 500 LYS A 478 49.18 39.63
REMARK 500 GLU A 479 -62.20 -149.49
REMARK 500 ASP A 485 65.66 -55.68
REMARK 500 PHE A 503 54.48 -140.51
REMARK 500 THR A 505 -111.84 -104.88
REMARK 500 PHE B 11 94.87 -54.59
REMARK 500 ASN B 12 68.71 -155.95
REMARK 500 PHE B 31 -117.63 57.99
REMARK 500 VAL B 37 113.29 53.93
REMARK 500 LEU B 45 -3.09 68.95
REMARK 500 TRP B 73 -155.74 -90.43
REMARK 500 LYS B 99 56.91 -143.61
REMARK 500 CYS B 108 135.69 -172.96
REMARK 500 LEU B 121 -83.51 -104.87
REMARK 500 THR B 180 -166.00 -111.10
REMARK 500 LYS B 183 -167.56 54.94
REMARK 500 ARG B 207 -144.67 -87.33
REMARK 500 THR B 234 142.68 176.04
REMARK 500 ARG B 346 -58.99 69.16
REMARK 500 HIS B 368 -138.21 -130.94
REMARK 500 PHE B 375 -81.33 -113.99
REMARK 500 LYS B 467 -100.07 62.83
REMARK 500 GLU B 479 -63.87 -125.36
REMARK 500 ASP B 485 62.34 -54.51
REMARK 500 PHE B 503 52.79 -142.93
REMARK 500 THR B 505 -114.16 -116.96
REMARK 500 PHE C 11 94.85 -52.18
REMARK 500 ASN C 12 68.38 -156.25
REMARK 500 PHE C 31 -119.77 57.24
REMARK 500 VAL C 37 115.66 62.26
REMARK 500 LEU C 45 -2.51 69.14
REMARK 500
REMARK 500 THIS ENTRY HAS 89 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-T2062 RELATED DB: TARGETDB
DBREF 1YIF A 1 533 UNP P94489 P94489_BACSU 1 533
DBREF 1YIF B 1 533 UNP P94489 P94489_BACSU 1 533
DBREF 1YIF C 1 533 UNP P94489 P94489_BACSU 1 533
DBREF 1YIF D 1 533 UNP P94489 P94489_BACSU 1 533
SEQRES 1 A 533 MET LYS ILE THR ASN PRO VAL LEU LYS GLY PHE ASN PRO
SEQRES 2 A 533 ASP PRO SER ILE CYS ARG ALA GLY GLU ASP TYR TYR ILE
SEQRES 3 A 533 ALA VAL SER THR PHE GLU TRP PHE PRO GLY VAL GLN ILE
SEQRES 4 A 533 HIS HIS SER LYS ASP LEU VAL ASN TRP HIS LEU VAL ALA
SEQRES 5 A 533 HIS PRO LEU GLN ARG VAL SER GLN LEU ASP MET LYS GLY
SEQRES 6 A 533 ASN PRO ASN SER GLY GLY VAL TRP ALA PRO CYS LEU SER
SEQRES 7 A 533 TYR SER ASP GLY LYS PHE TRP LEU ILE TYR THR ASP VAL
SEQRES 8 A 533 LYS VAL VAL ASP GLY ALA TRP LYS ASP CYS HIS ASN TYR
SEQRES 9 A 533 LEU VAL THR CYS GLU THR ILE ASN GLY ASP TRP SER GLU
SEQRES 10 A 533 PRO ILE LYS LEU ASN SER SER GLY PHE ASP ALA SER LEU
SEQRES 11 A 533 PHE HIS ASP THR ASP GLY LYS LYS TYR LEU LEU ASN MET
SEQRES 12 A 533 LEU TRP ASP HIS ARG ILE ASP ARG HIS SER PHE GLY GLY
SEQRES 13 A 533 ILE VAL ILE GLN GLU TYR SER ASP LYS GLU GLN LYS LEU
SEQRES 14 A 533 ILE GLY LYS PRO LYS VAL ILE PHE GLU GLY THR ASP ARG
SEQRES 15 A 533 LYS LEU THR GLU ALA PRO HIS LEU TYR HIS ILE GLY ASN
SEQRES 16 A 533 TYR TYR TYR LEU LEU THR ALA GLU GLY GLY THR ARG TYR
SEQRES 17 A 533 GLU HIS ALA ALA THR ILE ALA ARG SER ALA ASN ILE GLU
SEQRES 18 A 533 GLY PRO TYR GLU VAL HIS PRO ASP ASN PRO ILE LEU THR
SEQRES 19 A 533 SER TRP HIS ASP PRO GLY ASN PRO LEU GLN LYS CYS GLY
SEQRES 20 A 533 HIS ALA SER ILE VAL GLN THR HIS THR ASP GLU TRP TYR
SEQRES 21 A 533 LEU ALA HIS LEU THR GLY ARG PRO ILE HIS PRO ASP ASP
SEQRES 22 A 533 ASP SER ILE PHE GLN GLN ARG GLY TYR CYS PRO LEU GLY
SEQRES 23 A 533 ARG GLU THR ALA ILE GLN LYS LEU TYR TRP LYS ASP GLU
SEQRES 24 A 533 TRP PRO TYR VAL VAL GLY GLY LYS GLU GLY SER LEU GLU
SEQRES 25 A 533 VAL ASP ALA PRO SER ILE PRO GLU THR ILE PHE GLU ALA
SEQRES 26 A 533 THR TYR PRO GLU VAL ASP GLU PHE GLU ASP SER THR LEU
SEQRES 27 A 533 ASN ILE ASN PHE GLN THR LEU ARG ILE PRO PHE THR ASN
SEQRES 28 A 533 GLU LEU GLY SER LEU THR GLN ALA PRO ASN HIS LEU ARG
SEQRES 29 A 533 LEU PHE GLY HIS GLU SER LEU THR SER THR PHE THR GLN
SEQRES 30 A 533 ALA PHE VAL ALA ARG ARG TRP GLN SER LEU HIS PHE GLU
SEQRES 31 A 533 ALA GLU THR ALA VAL GLU PHE TYR PRO GLU ASN PHE GLN
SEQRES 32 A 533 GLN ALA ALA GLY LEU VAL ASN TYR TYR ASN THR GLU ASN
SEQRES 33 A 533 TRP THR ALA LEU GLN VAL THR HIS ASP GLU GLU LEU GLY
SEQRES 34 A 533 ARG ILE LEU GLU LEU THR ILE CYS ASP ASN PHE SER PHE
SEQRES 35 A 533 SER GLN PRO LEU ASN ASN LYS ILE VAL ILE PRO ARG GLU
SEQRES 36 A 533 VAL LYS TYR VAL TYR LEU ARG VAL ASN ILE GLU LYS ASP
SEQRES 37 A 533 LYS TYR TYR TYR PHE TYR SER PHE ASN LYS GLU ASP TRP
SEQRES 38 A 533 HIS LYS ILE ASP ILE ALA LEU GLU SER LYS LYS LEU SER
SEQRES 39 A 533 ASP ASP TYR ILE ARG GLY GLY GLY PHE PHE THR GLY ALA
SEQRES 40 A 533 PHE VAL GLY MET GLN CYS GLN ASP THR GLY GLY ASN HIS
SEQRES 41 A 533 ILE PRO ALA ASP PHE ARG TYR PHE ARG TYR LYS GLU LYS
SEQRES 1 B 533 MET LYS ILE THR ASN PRO VAL LEU LYS GLY PHE ASN PRO
SEQRES 2 B 533 ASP PRO SER ILE CYS ARG ALA GLY GLU ASP TYR TYR ILE
SEQRES 3 B 533 ALA VAL SER THR PHE GLU TRP PHE PRO GLY VAL GLN ILE
SEQRES 4 B 533 HIS HIS SER LYS ASP LEU VAL ASN TRP HIS LEU VAL ALA
SEQRES 5 B 533 HIS PRO LEU GLN ARG VAL SER GLN LEU ASP MET LYS GLY
SEQRES 6 B 533 ASN PRO ASN SER GLY GLY VAL TRP ALA PRO CYS LEU SER
SEQRES 7 B 533 TYR SER ASP GLY LYS PHE TRP LEU ILE TYR THR ASP VAL
SEQRES 8 B 533 LYS VAL VAL ASP GLY ALA TRP LYS ASP CYS HIS ASN TYR
SEQRES 9 B 533 LEU VAL THR CYS GLU THR ILE ASN GLY ASP TRP SER GLU
SEQRES 10 B 533 PRO ILE LYS LEU ASN SER SER GLY PHE ASP ALA SER LEU
SEQRES 11 B 533 PHE HIS ASP THR ASP GLY LYS LYS TYR LEU LEU ASN MET
SEQRES 12 B 533 LEU TRP ASP HIS ARG ILE ASP ARG HIS SER PHE GLY GLY
SEQRES 13 B 533 ILE VAL ILE GLN GLU TYR SER ASP LYS GLU GLN LYS LEU
SEQRES 14 B 533 ILE GLY LYS PRO LYS VAL ILE PHE GLU GLY THR ASP ARG
SEQRES 15 B 533 LYS LEU THR GLU ALA PRO HIS LEU TYR HIS ILE GLY ASN
SEQRES 16 B 533 TYR TYR TYR LEU LEU THR ALA GLU GLY GLY THR ARG TYR
SEQRES 17 B 533 GLU HIS ALA ALA THR ILE ALA ARG SER ALA ASN ILE GLU
SEQRES 18 B 533 GLY PRO TYR GLU VAL HIS PRO ASP ASN PRO ILE LEU THR
SEQRES 19 B 533 SER TRP HIS ASP PRO GLY ASN PRO LEU GLN LYS CYS GLY
SEQRES 20 B 533 HIS ALA SER ILE VAL GLN THR HIS THR ASP GLU TRP TYR
SEQRES 21 B 533 LEU ALA HIS LEU THR GLY ARG PRO ILE HIS PRO ASP ASP
SEQRES 22 B 533 ASP SER ILE PHE GLN GLN ARG GLY TYR CYS PRO LEU GLY
SEQRES 23 B 533 ARG GLU THR ALA ILE GLN LYS LEU TYR TRP LYS ASP GLU
SEQRES 24 B 533 TRP PRO TYR VAL VAL GLY GLY LYS GLU GLY SER LEU GLU
SEQRES 25 B 533 VAL ASP ALA PRO SER ILE PRO GLU THR ILE PHE GLU ALA
SEQRES 26 B 533 THR TYR PRO GLU VAL ASP GLU PHE GLU ASP SER THR LEU
SEQRES 27 B 533 ASN ILE ASN PHE GLN THR LEU ARG ILE PRO PHE THR ASN
SEQRES 28 B 533 GLU LEU GLY SER LEU THR GLN ALA PRO ASN HIS LEU ARG
SEQRES 29 B 533 LEU PHE GLY HIS GLU SER LEU THR SER THR PHE THR GLN
SEQRES 30 B 533 ALA PHE VAL ALA ARG ARG TRP GLN SER LEU HIS PHE GLU
SEQRES 31 B 533 ALA GLU THR ALA VAL GLU PHE TYR PRO GLU ASN PHE GLN
SEQRES 32 B 533 GLN ALA ALA GLY LEU VAL ASN TYR TYR ASN THR GLU ASN
SEQRES 33 B 533 TRP THR ALA LEU GLN VAL THR HIS ASP GLU GLU LEU GLY
SEQRES 34 B 533 ARG ILE LEU GLU LEU THR ILE CYS ASP ASN PHE SER PHE
SEQRES 35 B 533 SER GLN PRO LEU ASN ASN LYS ILE VAL ILE PRO ARG GLU
SEQRES 36 B 533 VAL LYS TYR VAL TYR LEU ARG VAL ASN ILE GLU LYS ASP
SEQRES 37 B 533 LYS TYR TYR TYR PHE TYR SER PHE ASN LYS GLU ASP TRP
SEQRES 38 B 533 HIS LYS ILE ASP ILE ALA LEU GLU SER LYS LYS LEU SER
SEQRES 39 B 533 ASP ASP TYR ILE ARG GLY GLY GLY PHE PHE THR GLY ALA
SEQRES 40 B 533 PHE VAL GLY MET GLN CYS GLN ASP THR GLY GLY ASN HIS
SEQRES 41 B 533 ILE PRO ALA ASP PHE ARG TYR PHE ARG TYR LYS GLU LYS
SEQRES 1 C 533 MET LYS ILE THR ASN PRO VAL LEU LYS GLY PHE ASN PRO
SEQRES 2 C 533 ASP PRO SER ILE CYS ARG ALA GLY GLU ASP TYR TYR ILE
SEQRES 3 C 533 ALA VAL SER THR PHE GLU TRP PHE PRO GLY VAL GLN ILE
SEQRES 4 C 533 HIS HIS SER LYS ASP LEU VAL ASN TRP HIS LEU VAL ALA
SEQRES 5 C 533 HIS PRO LEU GLN ARG VAL SER GLN LEU ASP MET LYS GLY
SEQRES 6 C 533 ASN PRO ASN SER GLY GLY VAL TRP ALA PRO CYS LEU SER
SEQRES 7 C 533 TYR SER ASP GLY LYS PHE TRP LEU ILE TYR THR ASP VAL
SEQRES 8 C 533 LYS VAL VAL ASP GLY ALA TRP LYS ASP CYS HIS ASN TYR
SEQRES 9 C 533 LEU VAL THR CYS GLU THR ILE ASN GLY ASP TRP SER GLU
SEQRES 10 C 533 PRO ILE LYS LEU ASN SER SER GLY PHE ASP ALA SER LEU
SEQRES 11 C 533 PHE HIS ASP THR ASP GLY LYS LYS TYR LEU LEU ASN MET
SEQRES 12 C 533 LEU TRP ASP HIS ARG ILE ASP ARG HIS SER PHE GLY GLY
SEQRES 13 C 533 ILE VAL ILE GLN GLU TYR SER ASP LYS GLU GLN LYS LEU
SEQRES 14 C 533 ILE GLY LYS PRO LYS VAL ILE PHE GLU GLY THR ASP ARG
SEQRES 15 C 533 LYS LEU THR GLU ALA PRO HIS LEU TYR HIS ILE GLY ASN
SEQRES 16 C 533 TYR TYR TYR LEU LEU THR ALA GLU GLY GLY THR ARG TYR
SEQRES 17 C 533 GLU HIS ALA ALA THR ILE ALA ARG SER ALA ASN ILE GLU
SEQRES 18 C 533 GLY PRO TYR GLU VAL HIS PRO ASP ASN PRO ILE LEU THR
SEQRES 19 C 533 SER TRP HIS ASP PRO GLY ASN PRO LEU GLN LYS CYS GLY
SEQRES 20 C 533 HIS ALA SER ILE VAL GLN THR HIS THR ASP GLU TRP TYR
SEQRES 21 C 533 LEU ALA HIS LEU THR GLY ARG PRO ILE HIS PRO ASP ASP
SEQRES 22 C 533 ASP SER ILE PHE GLN GLN ARG GLY TYR CYS PRO LEU GLY
SEQRES 23 C 533 ARG GLU THR ALA ILE GLN LYS LEU TYR TRP LYS ASP GLU
SEQRES 24 C 533 TRP PRO TYR VAL VAL GLY GLY LYS GLU GLY SER LEU GLU
SEQRES 25 C 533 VAL ASP ALA PRO SER ILE PRO GLU THR ILE PHE GLU ALA
SEQRES 26 C 533 THR TYR PRO GLU VAL ASP GLU PHE GLU ASP SER THR LEU
SEQRES 27 C 533 ASN ILE ASN PHE GLN THR LEU ARG ILE PRO PHE THR ASN
SEQRES 28 C 533 GLU LEU GLY SER LEU THR GLN ALA PRO ASN HIS LEU ARG
SEQRES 29 C 533 LEU PHE GLY HIS GLU SER LEU THR SER THR PHE THR GLN
SEQRES 30 C 533 ALA PHE VAL ALA ARG ARG TRP GLN SER LEU HIS PHE GLU
SEQRES 31 C 533 ALA GLU THR ALA VAL GLU PHE TYR PRO GLU ASN PHE GLN
SEQRES 32 C 533 GLN ALA ALA GLY LEU VAL ASN TYR TYR ASN THR GLU ASN
SEQRES 33 C 533 TRP THR ALA LEU GLN VAL THR HIS ASP GLU GLU LEU GLY
SEQRES 34 C 533 ARG ILE LEU GLU LEU THR ILE CYS ASP ASN PHE SER PHE
SEQRES 35 C 533 SER GLN PRO LEU ASN ASN LYS ILE VAL ILE PRO ARG GLU
SEQRES 36 C 533 VAL LYS TYR VAL TYR LEU ARG VAL ASN ILE GLU LYS ASP
SEQRES 37 C 533 LYS TYR TYR TYR PHE TYR SER PHE ASN LYS GLU ASP TRP
SEQRES 38 C 533 HIS LYS ILE ASP ILE ALA LEU GLU SER LYS LYS LEU SER
SEQRES 39 C 533 ASP ASP TYR ILE ARG GLY GLY GLY PHE PHE THR GLY ALA
SEQRES 40 C 533 PHE VAL GLY MET GLN CYS GLN ASP THR GLY GLY ASN HIS
SEQRES 41 C 533 ILE PRO ALA ASP PHE ARG TYR PHE ARG TYR LYS GLU LYS
SEQRES 1 D 533 MET LYS ILE THR ASN PRO VAL LEU LYS GLY PHE ASN PRO
SEQRES 2 D 533 ASP PRO SER ILE CYS ARG ALA GLY GLU ASP TYR TYR ILE
SEQRES 3 D 533 ALA VAL SER THR PHE GLU TRP PHE PRO GLY VAL GLN ILE
SEQRES 4 D 533 HIS HIS SER LYS ASP LEU VAL ASN TRP HIS LEU VAL ALA
SEQRES 5 D 533 HIS PRO LEU GLN ARG VAL SER GLN LEU ASP MET LYS GLY
SEQRES 6 D 533 ASN PRO ASN SER GLY GLY VAL TRP ALA PRO CYS LEU SER
SEQRES 7 D 533 TYR SER ASP GLY LYS PHE TRP LEU ILE TYR THR ASP VAL
SEQRES 8 D 533 LYS VAL VAL ASP GLY ALA TRP LYS ASP CYS HIS ASN TYR
SEQRES 9 D 533 LEU VAL THR CYS GLU THR ILE ASN GLY ASP TRP SER GLU
SEQRES 10 D 533 PRO ILE LYS LEU ASN SER SER GLY PHE ASP ALA SER LEU
SEQRES 11 D 533 PHE HIS ASP THR ASP GLY LYS LYS TYR LEU LEU ASN MET
SEQRES 12 D 533 LEU TRP ASP HIS ARG ILE ASP ARG HIS SER PHE GLY GLY
SEQRES 13 D 533 ILE VAL ILE GLN GLU TYR SER ASP LYS GLU GLN LYS LEU
SEQRES 14 D 533 ILE GLY LYS PRO LYS VAL ILE PHE GLU GLY THR ASP ARG
SEQRES 15 D 533 LYS LEU THR GLU ALA PRO HIS LEU TYR HIS ILE GLY ASN
SEQRES 16 D 533 TYR TYR TYR LEU LEU THR ALA GLU GLY GLY THR ARG TYR
SEQRES 17 D 533 GLU HIS ALA ALA THR ILE ALA ARG SER ALA ASN ILE GLU
SEQRES 18 D 533 GLY PRO TYR GLU VAL HIS PRO ASP ASN PRO ILE LEU THR
SEQRES 19 D 533 SER TRP HIS ASP PRO GLY ASN PRO LEU GLN LYS CYS GLY
SEQRES 20 D 533 HIS ALA SER ILE VAL GLN THR HIS THR ASP GLU TRP TYR
SEQRES 21 D 533 LEU ALA HIS LEU THR GLY ARG PRO ILE HIS PRO ASP ASP
SEQRES 22 D 533 ASP SER ILE PHE GLN GLN ARG GLY TYR CYS PRO LEU GLY
SEQRES 23 D 533 ARG GLU THR ALA ILE GLN LYS LEU TYR TRP LYS ASP GLU
SEQRES 24 D 533 TRP PRO TYR VAL VAL GLY GLY LYS GLU GLY SER LEU GLU
SEQRES 25 D 533 VAL ASP ALA PRO SER ILE PRO GLU THR ILE PHE GLU ALA
SEQRES 26 D 533 THR TYR PRO GLU VAL ASP GLU PHE GLU ASP SER THR LEU
SEQRES 27 D 533 ASN ILE ASN PHE GLN THR LEU ARG ILE PRO PHE THR ASN
SEQRES 28 D 533 GLU LEU GLY SER LEU THR GLN ALA PRO ASN HIS LEU ARG
SEQRES 29 D 533 LEU PHE GLY HIS GLU SER LEU THR SER THR PHE THR GLN
SEQRES 30 D 533 ALA PHE VAL ALA ARG ARG TRP GLN SER LEU HIS PHE GLU
SEQRES 31 D 533 ALA GLU THR ALA VAL GLU PHE TYR PRO GLU ASN PHE GLN
SEQRES 32 D 533 GLN ALA ALA GLY LEU VAL ASN TYR TYR ASN THR GLU ASN
SEQRES 33 D 533 TRP THR ALA LEU GLN VAL THR HIS ASP GLU GLU LEU GLY
SEQRES 34 D 533 ARG ILE LEU GLU LEU THR ILE CYS ASP ASN PHE SER PHE
SEQRES 35 D 533 SER GLN PRO LEU ASN ASN LYS ILE VAL ILE PRO ARG GLU
SEQRES 36 D 533 VAL LYS TYR VAL TYR LEU ARG VAL ASN ILE GLU LYS ASP
SEQRES 37 D 533 LYS TYR TYR TYR PHE TYR SER PHE ASN LYS GLU ASP TRP
SEQRES 38 D 533 HIS LYS ILE ASP ILE ALA LEU GLU SER LYS LYS LEU SER
SEQRES 39 D 533 ASP ASP TYR ILE ARG GLY GLY GLY PHE PHE THR GLY ALA
SEQRES 40 D 533 PHE VAL GLY MET GLN CYS GLN ASP THR GLY GLY ASN HIS
SEQRES 41 D 533 ILE PRO ALA ASP PHE ARG TYR PHE ARG TYR LYS GLU LYS
FORMUL 5 HOH *2728(H2 O)
HELIX 1 1 LYS A 491 SER A 494 5 4
HELIX 2 2 LYS B 491 SER B 494 5 4
HELIX 3 3 LYS C 491 SER C 494 5 4
HELIX 4 4 LYS D 491 SER D 494 5 4
SHEET 1 A 2 ILE A 3 THR A 4 0
SHEET 2 A 2 GLU A 312 VAL A 313 -1 O VAL A 313 N ILE A 3
SHEET 1 B 4 SER A 16 ALA A 20 0
SHEET 2 B 4 ASP A 23 VAL A 28 -1 O ASP A 23 N ALA A 20
SHEET 3 B 4 GLN A 38 SER A 42 -1 O SER A 42 N TYR A 24
SHEET 4 B 4 TRP A 48 ALA A 52 -1 O ALA A 52 N ILE A 39
SHEET 1 C 2 TRP A 33 PHE A 34 0
SHEET 2 C 2 THR A 344 LEU A 345 -1 O THR A 344 N PHE A 34
SHEET 1 D 4 CYS A 76 SER A 80 0
SHEET 2 D 4 LYS A 83 VAL A 91 -1 O ILE A 87 N CYS A 76
SHEET 3 D 4 CYS A 101 CYS A 108 -1 O CYS A 108 N PHE A 84
SHEET 4 D 4 ILE A 119 LYS A 120 -1 O ILE A 119 N LEU A 105
SHEET 1 E 4 SER A 129 HIS A 132 0
SHEET 2 E 4 LYS A 138 TRP A 145 -1 O TYR A 139 N PHE A 131
SHEET 3 E 4 PHE A 154 SER A 163 -1 O GLY A 155 N LEU A 144
SHEET 4 E 4 LYS A 168 LEU A 169 -1 O LYS A 168 N SER A 163
SHEET 1 F 4 SER A 129 HIS A 132 0
SHEET 2 F 4 LYS A 138 TRP A 145 -1 O TYR A 139 N PHE A 131
SHEET 3 F 4 PHE A 154 SER A 163 -1 O GLY A 155 N LEU A 144
SHEET 4 F 4 LYS A 174 PHE A 177 -1 O PHE A 177 N ILE A 157
SHEET 1 G 4 GLU A 186 ILE A 193 0
SHEET 2 G 4 TYR A 196 GLU A 203 -1 O LEU A 200 N HIS A 189
SHEET 3 G 4 ALA A 211 SER A 217 -1 O THR A 213 N THR A 201
SHEET 4 G 4 GLU A 225 VAL A 226 -1 O GLU A 225 N ARG A 216
SHEET 1 H 4 GLU A 186 ILE A 193 0
SHEET 2 H 4 TYR A 196 GLU A 203 -1 O LEU A 200 N HIS A 189
SHEET 3 H 4 ALA A 211 SER A 217 -1 O THR A 213 N THR A 201
SHEET 4 H 4 LEU A 233 THR A 234 -1 O LEU A 233 N ALA A 212
SHEET 1 I 4 GLN A 244 GLN A 253 0
SHEET 2 I 4 TRP A 259 GLY A 266 -1 O ALA A 262 N SER A 250
SHEET 3 I 4 GLU A 288 LYS A 297 -1 O GLN A 292 N LEU A 261
SHEET 4 I 4 TRP A 300 VAL A 303 -1 O TYR A 302 N TYR A 295
SHEET 1 J 4 VAL A 330 ASP A 331 0
SHEET 2 J 4 PRO A 522 GLU A 532 -1 O PHE A 528 N ASP A 331
SHEET 3 J 4 LEU A 363 PHE A 366 -1 N LEU A 363 O PHE A 525
SHEET 4 J 4 GLY A 354 SER A 355 -1 N SER A 355 O ARG A 364
SHEET 1 K 6 VAL A 330 ASP A 331 0
SHEET 2 K 6 PRO A 522 GLU A 532 -1 O PHE A 528 N ASP A 331
SHEET 3 K 6 HIS A 388 GLU A 396 -1 N GLU A 392 O ARG A 529
SHEET 4 K 6 VAL A 459 GLU A 466 -1 O LEU A 461 N THR A 393
SHEET 5 K 6 LYS A 469 SER A 475 -1 O LYS A 469 N GLU A 466
SHEET 6 K 6 HIS A 482 GLU A 489 -1 O HIS A 482 N TYR A 474
SHEET 1 L 6 ALA A 378 ARG A 383 0
SHEET 2 L 6 PHE A 508 ASP A 515 -1 O VAL A 509 N ARG A 382
SHEET 3 L 6 GLN A 404 ASN A 413 -1 N ALA A 405 O GLN A 514
SHEET 4 L 6 ASN A 416 ASP A 425 -1 O VAL A 422 N ALA A 406
SHEET 5 L 6 GLY A 429 ASP A 438 -1 O ILE A 431 N THR A 423
SHEET 6 L 6 SER A 441 SER A 443 -1 O SER A 443 N ILE A 436
SHEET 1 M 6 ALA A 378 ARG A 383 0
SHEET 2 M 6 PHE A 508 ASP A 515 -1 O VAL A 509 N ARG A 382
SHEET 3 M 6 GLN A 404 ASN A 413 -1 N ALA A 405 O GLN A 514
SHEET 4 M 6 ASN A 416 ASP A 425 -1 O VAL A 422 N ALA A 406
SHEET 5 M 6 GLY A 429 ASP A 438 -1 O ILE A 431 N THR A 423
SHEET 6 M 6 ILE A 450 VAL A 451 -1 O ILE A 450 N LEU A 432
SHEET 1 N 2 ILE B 3 THR B 4 0
SHEET 2 N 2 GLU B 312 VAL B 313 -1 O VAL B 313 N ILE B 3
SHEET 1 O 4 SER B 16 ALA B 20 0
SHEET 2 O 4 ASP B 23 VAL B 28 -1 O ASP B 23 N ALA B 20
SHEET 3 O 4 GLN B 38 SER B 42 -1 O SER B 42 N TYR B 24
SHEET 4 O 4 HIS B 49 ALA B 52 -1 O VAL B 51 N ILE B 39
SHEET 1 P 2 TRP B 33 PHE B 34 0
SHEET 2 P 2 THR B 344 LEU B 345 -1 O THR B 344 N PHE B 34
SHEET 1 Q 4 CYS B 76 SER B 80 0
SHEET 2 Q 4 LYS B 83 VAL B 91 -1 O ILE B 87 N CYS B 76
SHEET 3 Q 4 CYS B 101 CYS B 108 -1 O CYS B 108 N PHE B 84
SHEET 4 Q 4 ILE B 119 LYS B 120 -1 O ILE B 119 N LEU B 105
SHEET 1 R 4 SER B 129 HIS B 132 0
SHEET 2 R 4 LYS B 138 TRP B 145 -1 O TYR B 139 N PHE B 131
SHEET 3 R 4 PHE B 154 SER B 163 -1 O GLN B 160 N LEU B 140
SHEET 4 R 4 LYS B 168 LEU B 169 -1 O LYS B 168 N SER B 163
SHEET 1 S 4 SER B 129 HIS B 132 0
SHEET 2 S 4 LYS B 138 TRP B 145 -1 O TYR B 139 N PHE B 131
SHEET 3 S 4 PHE B 154 SER B 163 -1 O GLN B 160 N LEU B 140
SHEET 4 S 4 LYS B 174 PHE B 177 -1 O PHE B 177 N ILE B 157
SHEET 1 T 4 GLU B 186 ILE B 193 0
SHEET 2 T 4 TYR B 196 GLU B 203 -1 O TYR B 198 N TYR B 191
SHEET 3 T 4 ALA B 211 SER B 217 -1 O THR B 213 N THR B 201
SHEET 4 T 4 GLU B 225 VAL B 226 -1 O GLU B 225 N ARG B 216
SHEET 1 U 4 GLU B 186 ILE B 193 0
SHEET 2 U 4 TYR B 196 GLU B 203 -1 O TYR B 198 N TYR B 191
SHEET 3 U 4 ALA B 211 SER B 217 -1 O THR B 213 N THR B 201
SHEET 4 U 4 LEU B 233 THR B 234 -1 O LEU B 233 N ALA B 212
SHEET 1 V 4 GLN B 244 GLN B 253 0
SHEET 2 V 4 TRP B 259 GLY B 266 -1 O GLY B 266 N GLN B 244
SHEET 3 V 4 GLU B 288 LYS B 297 -1 O ALA B 290 N HIS B 263
SHEET 4 V 4 TRP B 300 VAL B 303 -1 O TYR B 302 N TYR B 295
SHEET 1 W 4 VAL B 330 ASP B 331 0
SHEET 2 W 4 PRO B 522 GLU B 532 -1 O PHE B 528 N ASP B 331
SHEET 3 W 4 LEU B 363 PHE B 366 -1 N LEU B 363 O PHE B 525
SHEET 4 W 4 GLY B 354 SER B 355 -1 N SER B 355 O ARG B 364
SHEET 1 X 6 VAL B 330 ASP B 331 0
SHEET 2 X 6 PRO B 522 GLU B 532 -1 O PHE B 528 N ASP B 331
SHEET 3 X 6 HIS B 388 GLU B 396 -1 N GLU B 392 O ARG B 529
SHEET 4 X 6 VAL B 459 GLU B 466 -1 O LEU B 461 N THR B 393
SHEET 5 X 6 LYS B 469 SER B 475 -1 O LYS B 469 N GLU B 466
SHEET 6 X 6 HIS B 482 GLU B 489 -1 O HIS B 482 N TYR B 474
SHEET 1 Y 6 ALA B 378 ARG B 383 0
SHEET 2 Y 6 PHE B 508 ASP B 515 -1 O VAL B 509 N ARG B 382
SHEET 3 Y 6 GLN B 404 ASN B 413 -1 N ALA B 405 O GLN B 514
SHEET 4 Y 6 ASN B 416 ASP B 425 -1 O VAL B 422 N ALA B 406
SHEET 5 Y 6 GLY B 429 ASP B 438 -1 O ILE B 431 N THR B 423
SHEET 6 Y 6 SER B 441 SER B 443 -1 O SER B 443 N ILE B 436
SHEET 1 Z 6 ALA B 378 ARG B 383 0
SHEET 2 Z 6 PHE B 508 ASP B 515 -1 O VAL B 509 N ARG B 382
SHEET 3 Z 6 GLN B 404 ASN B 413 -1 N ALA B 405 O GLN B 514
SHEET 4 Z 6 ASN B 416 ASP B 425 -1 O VAL B 422 N ALA B 406
SHEET 5 Z 6 GLY B 429 ASP B 438 -1 O ILE B 431 N THR B 423
SHEET 6 Z 6 ILE B 450 VAL B 451 -1 O ILE B 450 N LEU B 432
SHEET 1 AA 2 ILE C 3 THR C 4 0
SHEET 2 AA 2 GLU C 312 VAL C 313 -1 O VAL C 313 N ILE C 3
SHEET 1 AB 4 SER C 16 ALA C 20 0
SHEET 2 AB 4 ASP C 23 VAL C 28 -1 O ASP C 23 N ALA C 20
SHEET 3 AB 4 GLN C 38 SER C 42 -1 O SER C 42 N TYR C 24
SHEET 4 AB 4 HIS C 49 ALA C 52 -1 O HIS C 49 N HIS C 41
SHEET 1 AC 8 TRP C 33 PHE C 34 0
SHEET 2 AC 8 GLN C 343 LEU C 345 -1 O THR C 344 N PHE C 34
SHEET 3 AC 8 ALA C 378 ARG C 383 -1 O ALA C 381 N GLN C 343
SHEET 4 AC 8 PHE C 508 ASP C 515 -1 O VAL C 509 N ARG C 382
SHEET 5 AC 8 GLN C 404 ASN C 413 -1 N ALA C 405 O GLN C 514
SHEET 6 AC 8 ASN C 416 ASP C 425 -1 O VAL C 422 N ALA C 406
SHEET 7 AC 8 GLY C 429 ASP C 438 -1 O ILE C 431 N THR C 423
SHEET 8 AC 8 SER C 441 SER C 443 -1 O SER C 443 N ILE C 436
SHEET 1 AD 8 TRP C 33 PHE C 34 0
SHEET 2 AD 8 GLN C 343 LEU C 345 -1 O THR C 344 N PHE C 34
SHEET 3 AD 8 ALA C 378 ARG C 383 -1 O ALA C 381 N GLN C 343
SHEET 4 AD 8 PHE C 508 ASP C 515 -1 O VAL C 509 N ARG C 382
SHEET 5 AD 8 GLN C 404 ASN C 413 -1 N ALA C 405 O GLN C 514
SHEET 6 AD 8 ASN C 416 ASP C 425 -1 O VAL C 422 N ALA C 406
SHEET 7 AD 8 GLY C 429 ASP C 438 -1 O ILE C 431 N THR C 423
SHEET 8 AD 8 ILE C 450 VAL C 451 -1 O ILE C 450 N LEU C 432
SHEET 1 AE 4 CYS C 76 SER C 80 0
SHEET 2 AE 4 LYS C 83 VAL C 91 -1 O ILE C 87 N CYS C 76
SHEET 3 AE 4 CYS C 101 CYS C 108 -1 O CYS C 108 N PHE C 84
SHEET 4 AE 4 ILE C 119 LYS C 120 -1 O ILE C 119 N LEU C 105
SHEET 1 AF 4 SER C 129 HIS C 132 0
SHEET 2 AF 4 LYS C 138 TRP C 145 -1 O TYR C 139 N PHE C 131
SHEET 3 AF 4 PHE C 154 SER C 163 -1 O GLN C 160 N LEU C 140
SHEET 4 AF 4 LYS C 168 LEU C 169 -1 O LYS C 168 N SER C 163
SHEET 1 AG 4 SER C 129 HIS C 132 0
SHEET 2 AG 4 LYS C 138 TRP C 145 -1 O TYR C 139 N PHE C 131
SHEET 3 AG 4 PHE C 154 SER C 163 -1 O GLN C 160 N LEU C 140
SHEET 4 AG 4 LYS C 174 PHE C 177 -1 O PHE C 177 N ILE C 157
SHEET 1 AH 4 GLU C 186 ILE C 193 0
SHEET 2 AH 4 TYR C 196 GLU C 203 -1 O TYR C 198 N TYR C 191
SHEET 3 AH 4 ALA C 211 SER C 217 -1 O THR C 213 N THR C 201
SHEET 4 AH 4 GLU C 225 VAL C 226 -1 O GLU C 225 N ARG C 216
SHEET 1 AI 4 GLU C 186 ILE C 193 0
SHEET 2 AI 4 TYR C 196 GLU C 203 -1 O TYR C 198 N TYR C 191
SHEET 3 AI 4 ALA C 211 SER C 217 -1 O THR C 213 N THR C 201
SHEET 4 AI 4 LEU C 233 THR C 234 -1 O LEU C 233 N ALA C 212
SHEET 1 AJ 4 GLN C 244 GLN C 253 0
SHEET 2 AJ 4 TRP C 259 GLY C 266 -1 O GLY C 266 N GLN C 244
SHEET 3 AJ 4 GLU C 288 LYS C 297 -1 O ALA C 290 N HIS C 263
SHEET 4 AJ 4 TRP C 300 VAL C 303 -1 O TYR C 302 N TYR C 295
SHEET 1 AK 6 VAL C 330 ASP C 331 0
SHEET 2 AK 6 PRO C 522 GLU C 532 -1 O PHE C 528 N ASP C 331
SHEET 3 AK 6 HIS C 388 GLU C 396 -1 N GLU C 392 O ARG C 529
SHEET 4 AK 6 VAL C 459 GLU C 466 -1 O LEU C 461 N THR C 393
SHEET 5 AK 6 LYS C 469 SER C 475 -1 O LYS C 469 N GLU C 466
SHEET 6 AK 6 HIS C 482 LYS C 483 -1 O HIS C 482 N TYR C 474
SHEET 1 AL 7 GLY C 354 SER C 355 0
SHEET 2 AL 7 LEU C 363 PHE C 366 -1 O ARG C 364 N SER C 355
SHEET 3 AL 7 PRO C 522 GLU C 532 -1 O PHE C 525 N LEU C 363
SHEET 4 AL 7 HIS C 388 GLU C 396 -1 N GLU C 392 O ARG C 529
SHEET 5 AL 7 VAL C 459 GLU C 466 -1 O LEU C 461 N THR C 393
SHEET 6 AL 7 LYS C 469 SER C 475 -1 O LYS C 469 N GLU C 466
SHEET 7 AL 7 LEU C 488 GLU C 489 -1 O LEU C 488 N TYR C 470
SHEET 1 AM 2 ILE D 3 THR D 4 0
SHEET 2 AM 2 GLU D 312 VAL D 313 -1 O VAL D 313 N ILE D 3
SHEET 1 AN 4 SER D 16 ALA D 20 0
SHEET 2 AN 4 ASP D 23 VAL D 28 -1 O ASP D 23 N ALA D 20
SHEET 3 AN 4 GLN D 38 SER D 42 -1 O SER D 42 N TYR D 24
SHEET 4 AN 4 HIS D 49 ALA D 52 -1 O HIS D 49 N HIS D 41
SHEET 1 AO 2 TRP D 33 PHE D 34 0
SHEET 2 AO 2 THR D 344 LEU D 345 -1 O THR D 344 N PHE D 34
SHEET 1 AP 4 CYS D 76 SER D 80 0
SHEET 2 AP 4 LYS D 83 VAL D 91 -1 O TRP D 85 N SER D 78
SHEET 3 AP 4 CYS D 101 CYS D 108 -1 O CYS D 108 N PHE D 84
SHEET 4 AP 4 ILE D 119 LYS D 120 -1 O ILE D 119 N LEU D 105
SHEET 1 AQ 4 SER D 129 HIS D 132 0
SHEET 2 AQ 4 LYS D 138 TRP D 145 -1 O TYR D 139 N PHE D 131
SHEET 3 AQ 4 PHE D 154 SER D 163 -1 O GLN D 160 N LEU D 140
SHEET 4 AQ 4 LYS D 168 LEU D 169 -1 O LYS D 168 N SER D 163
SHEET 1 AR 4 SER D 129 HIS D 132 0
SHEET 2 AR 4 LYS D 138 TRP D 145 -1 O TYR D 139 N PHE D 131
SHEET 3 AR 4 PHE D 154 SER D 163 -1 O GLN D 160 N LEU D 140
SHEET 4 AR 4 LYS D 174 PHE D 177 -1 O PHE D 177 N ILE D 157
SHEET 1 AS 4 GLU D 186 ILE D 193 0
SHEET 2 AS 4 TYR D 196 GLU D 203 -1 O TYR D 198 N TYR D 191
SHEET 3 AS 4 ALA D 211 SER D 217 -1 O THR D 213 N THR D 201
SHEET 4 AS 4 GLU D 225 VAL D 226 -1 O GLU D 225 N ARG D 216
SHEET 1 AT 4 GLU D 186 ILE D 193 0
SHEET 2 AT 4 TYR D 196 GLU D 203 -1 O TYR D 198 N TYR D 191
SHEET 3 AT 4 ALA D 211 SER D 217 -1 O THR D 213 N THR D 201
SHEET 4 AT 4 LEU D 233 THR D 234 -1 O LEU D 233 N ALA D 212
SHEET 1 AU 4 GLN D 244 GLN D 253 0
SHEET 2 AU 4 TRP D 259 GLY D 266 -1 O GLY D 266 N GLN D 244
SHEET 3 AU 4 GLU D 288 LYS D 297 -1 O GLN D 292 N LEU D 261
SHEET 4 AU 4 TRP D 300 VAL D 303 -1 O TYR D 302 N TYR D 295
SHEET 1 AV 6 VAL D 330 ASP D 331 0
SHEET 2 AV 6 PRO D 522 GLU D 532 -1 O PHE D 528 N ASP D 331
SHEET 3 AV 6 HIS D 388 GLU D 396 -1 N GLU D 392 O ARG D 529
SHEET 4 AV 6 VAL D 459 GLU D 466 -1 O LEU D 461 N THR D 393
SHEET 5 AV 6 LYS D 469 SER D 475 -1 O LYS D 469 N GLU D 466
SHEET 6 AV 6 HIS D 482 LYS D 483 -1 O HIS D 482 N TYR D 474
SHEET 1 AW 7 GLY D 354 SER D 355 0
SHEET 2 AW 7 LEU D 363 PHE D 366 -1 O ARG D 364 N SER D 355
SHEET 3 AW 7 PRO D 522 GLU D 532 -1 O PHE D 525 N LEU D 363
SHEET 4 AW 7 HIS D 388 GLU D 396 -1 N GLU D 392 O ARG D 529
SHEET 5 AW 7 VAL D 459 GLU D 466 -1 O LEU D 461 N THR D 393
SHEET 6 AW 7 LYS D 469 SER D 475 -1 O LYS D 469 N GLU D 466
SHEET 7 AW 7 LEU D 488 GLU D 489 -1 O LEU D 488 N TYR D 470
SHEET 1 AX 6 ALA D 378 ARG D 383 0
SHEET 2 AX 6 PHE D 508 ASP D 515 -1 O VAL D 509 N ARG D 382
SHEET 3 AX 6 GLN D 404 ASN D 413 -1 N ALA D 405 O GLN D 514
SHEET 4 AX 6 ASN D 416 ASP D 425 -1 O VAL D 422 N ALA D 406
SHEET 5 AX 6 GLY D 429 ASP D 438 -1 O ILE D 431 N THR D 423
SHEET 6 AX 6 SER D 441 SER D 443 -1 O SER D 443 N ILE D 436
SHEET 1 AY 6 ALA D 378 ARG D 383 0
SHEET 2 AY 6 PHE D 508 ASP D 515 -1 O VAL D 509 N ARG D 382
SHEET 3 AY 6 GLN D 404 ASN D 413 -1 N ALA D 405 O GLN D 514
SHEET 4 AY 6 ASN D 416 ASP D 425 -1 O VAL D 422 N ALA D 406
SHEET 5 AY 6 GLY D 429 ASP D 438 -1 O ILE D 431 N THR D 423
SHEET 6 AY 6 ILE D 450 VAL D 451 -1 O ILE D 450 N LEU D 432
CISPEP 1 ASN A 5 PRO A 6 0 -0.12
CISPEP 2 PHE A 34 PRO A 35 0 -0.24
CISPEP 3 GLY A 222 PRO A 223 0 0.24
CISPEP 4 ASN A 230 PRO A 231 0 -0.26
CISPEP 5 ASN B 5 PRO B 6 0 -0.30
CISPEP 6 PHE B 34 PRO B 35 0 -0.32
CISPEP 7 GLY B 222 PRO B 223 0 0.18
CISPEP 8 ASN B 230 PRO B 231 0 -0.16
CISPEP 9 ASN C 5 PRO C 6 0 -0.20
CISPEP 10 PHE C 34 PRO C 35 0 -0.19
CISPEP 11 GLY C 222 PRO C 223 0 0.28
CISPEP 12 ASN C 230 PRO C 231 0 -0.36
CISPEP 13 ASN D 5 PRO D 6 0 -0.17
CISPEP 14 PHE D 34 PRO D 35 0 -0.11
CISPEP 15 GLY D 222 PRO D 223 0 0.06
CISPEP 16 ASN D 230 PRO D 231 0 -0.25
CRYST1 104.230 104.610 114.600 90.00 108.88 90.00 P 1 21 1 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 0.009594 0.000000 0.003281 0.00000
SCALE2 0.000000 0.009559 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009222 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
