HEADER HYDROLASE 10-MAY-12 4ATW
TITLE THE CRYSTAL STRUCTURE OF ARABINOFURANOSIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-L-ARABINOFURANOSIDASE DOMAIN PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: RESIDUES 2-482;
COMPND 5 SYNONYM: ALPHA-L-ARABINOFURANOSIDASE;
COMPND 6 EC: 3.2.1.55;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA MSB8;
SOURCE 3 ORGANISM_TAXID: 243274;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: MC1061
KEYWDS HYDROLASE, TAF, ARABINOFURANOSIDASE, THERMOSTABLE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DUMBREPATIL,H.-N.SONG,T.-Y.JUNG,T.-J.KIM,E.-J.WOO
REVDAT 2 09-JAN-13 4ATW 1 JRNL
REVDAT 1 23-MAY-12 4ATW 0
JRNL AUTH A.DUMBREPATIL,J.PARK,T.-Y.JUNG,H.-N.SONG,M.JANG,N.S.HAN,
JRNL AUTH 2 T.-J.KIM,E.-J.WOO
JRNL TITL STRUCTURAL ANALYSIS OF ALPHA-L-ARABINOFURANOSIDASE FROM
JRNL TITL 2 THERMOTOGA MARITIMA REVEALS CHARACTERISTICS FOR
JRNL TITL 3 THERMOSTABILITY AND SUBSTRATE SPECIFICITY.
JRNL REF J.MICROBIOL.BIOTECH. V. 22 1724 2012
JRNL REFN ISSN 1017-7825
JRNL PMID 23221536
JRNL DOI 10.4014/JMB.1208.08043
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 98388.92
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.00
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.5
REMARK 3 NUMBER OF REFLECTIONS : 60127
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) : 0.227
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.4
REMARK 3 FREE R VALUE TEST SET COUNT : 4430
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.3
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9196
REMARK 3 BIN R VALUE (WORKING SET) : 0.334
REMARK 3 BIN FREE R VALUE : 0.414
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.0
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 285
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23256
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.8
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.32
REMARK 3 B22 (A**2) : -7.62
REMARK 3 B33 (A**2) : 13.94
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -1.30
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.56
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) : 0.55
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.75
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.020
REMARK 3 BOND ANGLES (DEGREES) : 2.1
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.7
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.70
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) : 6.41 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 9.58 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 9.33 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 12.37 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.3
REMARK 3 BSOL : 15.4997
REMARK 3
REMARK 3 NCS MODEL : NONE
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.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 4ATW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAY-12.
REMARK 100 THE PDBE ID CODE IS EBI-52445.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 6C1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 210)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60127
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.00
REMARK 200 RESOLUTION RANGE LOW (A) : 29.94
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 6.2
REMARK 200 R MERGE (I) : 0.13
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.28
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.
REMARK 200 R MERGE FOR SHELL (I) : 0.64
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.45
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: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 0.1 M SODIUM
REMARK 280 CACODYLATE (PH 6.5), 0.2 M MAGNESIUM ACEATE
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 80.76900
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 HIS A 1
REMARK 465 HIS B 1
REMARK 465 HIS C 1
REMARK 465 HIS D 1
REMARK 465 HIS E 1
REMARK 465 HIS F 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH2 ARG A 50 O GLU A 337 2.15
REMARK 500 O GLY A 239 O MET A 377 1.67
REMARK 500 O VAL A 328 O ILE A 334 2.17
REMARK 500 CG LYS A 419 CG2 THR A 470 1.92
REMARK 500 O GLY B 239 O MET B 377 2.02
REMARK 500 CG1 VAL B 410 CZ TYR B 412 2.00
REMARK 500 CA TYR C 286 O PHE C 378 2.19
REMARK 500 CB TYR C 286 O PHE C 378 2.00
REMARK 500 CG LYS C 419 CG2 THR C 470 1.83
REMARK 500 NH2 ARG D 50 O GLU D 337 2.18
REMARK 500 ND2 ASN D 411 N ARG D 413 2.19
REMARK 500 CG LYS D 419 CG2 THR D 470 1.89
REMARK 500 CD2 PHE E 24 CB ALA E 325 1.90
REMARK 500 NH2 ARG E 50 O GLU E 337 2.16
REMARK 500 CG LYS E 419 CG2 THR E 470 1.80
REMARK 500 CD2 PHE F 24 CB ALA F 325 1.98
REMARK 500 O GLY F 239 O MET F 377 1.84
REMARK 500 O LEU F 327 N ALA F 333 1.85
REMARK 500 O VAL F 328 O ILE F 334 2.19
REMARK 500 CG LYS F 419 CG2 THR F 470 1.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CE LYS C 144 CE LYS E 431 1556 1.60
REMARK 500 CE LYS C 144 NZ LYS E 431 1556 1.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 26 C HIS A 27 N -0.160
REMARK 500 VAL A 328 CA VAL A 328 CB -0.390
REMARK 500 VAL A 328 CB VAL A 328 CG1 -0.402
REMARK 500 VAL A 328 CB VAL A 328 CG2 -0.312
REMARK 500 VAL A 328 C VAL A 328 O -0.189
REMARK 500 MET A 377 CG MET A 377 SD -0.177
REMARK 500 MET A 377 C MET A 377 O -0.253
REMARK 500 PHE A 378 CD1 PHE A 378 CE1 -0.253
REMARK 500 PHE A 378 CD2 PHE A 378 CE2 -0.234
REMARK 500 PHE A 378 CE1 PHE A 378 CZ -0.187
REMARK 500 PHE A 378 CE2 PHE A 378 CZ -0.313
REMARK 500 PHE A 378 CG PHE A 378 CD1 -0.147
REMARK 500 PHE A 378 CG PHE A 378 CD2 -0.127
REMARK 500 PHE A 378 C PHE A 378 O -0.151
REMARK 500 GLU A 415 CG GLU A 415 CD 0.112
REMARK 500 GLU B 26 C HIS B 27 N -0.186
REMARK 500 HIS B 158 C PRO B 159 N 1.156
REMARK 500 VAL B 328 CA VAL B 328 CB -0.183
REMARK 500 VAL B 328 CB VAL B 328 CG1 -0.253
REMARK 500 VAL B 328 CB VAL B 328 CG2 -0.302
REMARK 500 VAL B 328 C VAL B 328 O -0.181
REMARK 500 GLU C 26 C HIS C 27 N -0.261
REMARK 500 THR C 147 CA THR C 147 CB -0.176
REMARK 500 THR C 147 CB THR C 147 CG2 -0.310
REMARK 500 THR C 147 C THR C 147 O -0.231
REMARK 500 THR C 147 N THR C 147 CA -0.218
REMARK 500 HIS C 158 C PRO C 159 N 1.281
REMARK 500 VAL C 328 CA VAL C 328 CB -0.280
REMARK 500 VAL C 328 CB VAL C 328 CG1 -0.232
REMARK 500 VAL C 328 CB VAL C 328 CG2 -0.280
REMARK 500 VAL C 328 N VAL C 328 CA -0.138
REMARK 500 ASN C 329 CA ASN C 329 C -0.176
REMARK 500 ASN C 329 CG ASN C 329 ND2 -0.167
REMARK 500 ASN C 329 CG ASN C 329 OD1 -0.205
REMARK 500 ASN C 329 C ASN C 329 O -0.187
REMARK 500 SER C 368 CA SER C 368 CB -0.098
REMARK 500 SER C 368 CB SER C 368 OG -0.096
REMARK 500 SER C 368 C SER C 368 O -0.228
REMARK 500 LYS C 414 CA LYS C 414 CB -0.136
REMARK 500 LYS C 414 CB LYS C 414 CG -0.269
REMARK 500 LYS C 414 CD LYS C 414 CE -0.205
REMARK 500 LYS C 414 CE LYS C 414 NZ -0.200
REMARK 500 LYS C 414 C LYS C 414 O -0.169
REMARK 500 GLU D 26 C HIS D 27 N -0.394
REMARK 500 HIS D 158 C PRO D 159 N 1.220
REMARK 500 LEU D 327 CG LEU D 327 CD1 -0.325
REMARK 500 LEU D 327 CG LEU D 327 CD2 -0.320
REMARK 500 LEU D 327 C LEU D 327 O -0.183
REMARK 500 VAL D 328 CA VAL D 328 CB -0.220
REMARK 500 VAL D 328 CB VAL D 328 CG1 -0.325
REMARK 500
REMARK 500 THIS ENTRY HAS 101 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 9 CA - N - CD ANGL. DEV. = -13.8 DEGREES
REMARK 500 PRO A 15 C - N - CD ANGL. DEV. = -19.8 DEGREES
REMARK 500 PRO A 15 CA - N - CD ANGL. DEV. = -12.1 DEGREES
REMARK 500 THR A 25 O - C - N ANGL. DEV. = -10.8 DEGREES
REMARK 500 GLU A 26 C - N - CA ANGL. DEV. = 15.1 DEGREES
REMARK 500 ILE A 60 N - CA - C ANGL. DEV. = -24.8 DEGREES
REMARK 500 LYS A 61 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 GLY A 70 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 ASN A 142 N - CA - C ANGL. DEV. = 19.9 DEGREES
REMARK 500 TRP A 282 CB - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 ASN A 283 N - CA - CB ANGL. DEV. = -12.5 DEGREES
REMARK 500 GLN A 326 CB - CA - C ANGL. DEV. = 16.8 DEGREES
REMARK 500 ASN A 329 N - CA - CB ANGL. DEV. = 12.0 DEGREES
REMARK 500 LEU A 341 CB - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 GLU A 369 N - CA - C ANGL. DEV. = -31.0 DEGREES
REMARK 500 MET A 377 N - CA - C ANGL. DEV. = 25.0 DEGREES
REMARK 500 MET A 377 O - C - N ANGL. DEV. = -11.1 DEGREES
REMARK 500 ILE A 379 CB - CA - C ANGL. DEV. = -25.9 DEGREES
REMARK 500 ILE A 379 N - CA - C ANGL. DEV. = 17.3 DEGREES
REMARK 500 ASN A 380 N - CA - C ANGL. DEV. = -21.9 DEGREES
REMARK 500 ARG A 413 CB - CA - C ANGL. DEV. = 17.8 DEGREES
REMARK 500 VAL A 420 N - CA - CB ANGL. DEV. = -14.5 DEGREES
REMARK 500 CYS A 476 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 PRO B 9 CA - N - CD ANGL. DEV. = -13.5 DEGREES
REMARK 500 ILE B 60 N - CA - C ANGL. DEV. = -26.6 DEGREES
REMARK 500 LYS B 61 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 GLY B 70 N - CA - C ANGL. DEV. = -16.1 DEGREES
REMARK 500 ASN B 142 N - CA - C ANGL. DEV. = 22.8 DEGREES
REMARK 500 HIS B 158 O - C - N ANGL. DEV. = -54.8 DEGREES
REMARK 500 PRO B 159 C - N - CA ANGL. DEV. = -35.1 DEGREES
REMARK 500 PRO B 159 C - N - CD ANGL. DEV. = 20.7 DEGREES
REMARK 500 VAL B 328 N - CA - CB ANGL. DEV. = -22.7 DEGREES
REMARK 500 ASN B 329 N - CA - C ANGL. DEV. = 41.1 DEGREES
REMARK 500 ASN B 329 N - CA - CB ANGL. DEV. = -21.9 DEGREES
REMARK 500 ASN B 329 C - N - CA ANGL. DEV. = -20.0 DEGREES
REMARK 500 LEU B 341 CB - CA - C ANGL. DEV. = -14.0 DEGREES
REMARK 500 GLU B 369 CB - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 GLU B 369 N - CA - C ANGL. DEV. = -20.2 DEGREES
REMARK 500 THR B 370 N - CA - CB ANGL. DEV. = -18.9 DEGREES
REMARK 500 GLU B 415 CB - CA - C ANGL. DEV. = -16.1 DEGREES
REMARK 500 LYS B 419 CB - CA - C ANGL. DEV. = -22.7 DEGREES
REMARK 500 CYS B 476 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 PRO C 9 C - N - CD ANGL. DEV. = -16.7 DEGREES
REMARK 500 PRO C 9 CA - N - CD ANGL. DEV. = -14.7 DEGREES
REMARK 500 PRO C 15 C - N - CD ANGL. DEV. = -22.7 DEGREES
REMARK 500 PRO C 15 CA - N - CD ANGL. DEV. = -12.3 DEGREES
REMARK 500 THR C 25 O - C - N ANGL. DEV. = -14.4 DEGREES
REMARK 500 GLU C 26 C - N - CA ANGL. DEV. = 20.0 DEGREES
REMARK 500 GLY C 70 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 ASN C 142 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 133 ANGLE DEVIATIONS.
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 ARG A 4 136.73 -178.50
REMARK 500 ILE A 32 -74.44 -91.23
REMARK 500 GLU A 38 89.59 -151.16
REMARK 500 LYS A 61 76.94 -64.53
REMARK 500 ASN A 75 18.64 -145.16
REMARK 500 LYS A 85 -164.43 -79.12
REMARK 500 ASP A 86 -52.15 72.28
REMARK 500 ASN A 142 -73.70 -93.85
REMARK 500 GLU A 172 41.37 33.45
REMARK 500 TRP A 197 -162.70 -77.70
REMARK 500 MET A 198 -61.02 67.51
REMARK 500 CYS A 212 -158.41 -165.56
REMARK 500 GLU A 281 104.50 -167.05
REMARK 500 TRP A 282 107.84 -162.31
REMARK 500 TRP A 285 104.95 -167.35
REMARK 500 TYR A 286 -27.29 -146.50
REMARK 500 SER A 289 55.54 -144.41
REMARK 500 ASP A 290 -143.43 -118.53
REMARK 500 SER A 316 -9.18 -51.89
REMARK 500 LEU A 327 50.49 -148.03
REMARK 500 VAL A 328 -72.49 -160.25
REMARK 500 ASN A 329 -49.51 -139.12
REMARK 500 LEU A 331 28.26 49.64
REMARK 500 ILE A 342 131.52 -170.78
REMARK 500 LYS A 363 114.24 -33.89
REMARK 500 MET A 377 -77.29 -113.23
REMARK 500 ILE A 379 -8.99 84.90
REMARK 500 MET A 382 129.27 -39.50
REMARK 500 TYR A 412 53.89 -95.93
REMARK 500 GLU A 415 36.91 -78.48
REMARK 500 LYS A 419 40.34 -102.73
REMARK 500 GLU A 425 112.96 -38.84
REMARK 500 LYS A 431 69.29 -114.23
REMARK 500 THR A 438 -164.94 -161.23
REMARK 500 VAL A 442 11.80 -67.06
REMARK 500 PRO A 451 14.69 -66.08
REMARK 500 GLU A 459 138.25 -177.81
REMARK 500 PHE A 467 -166.14 -163.30
REMARK 500 PHE A 474 55.60 33.08
REMARK 500 VAL A 481 -167.58 -115.54
REMARK 500 ILE B 32 -75.31 -92.14
REMARK 500 ASP B 45 -159.42 -90.46
REMARK 500 LYS B 61 87.12 -63.32
REMARK 500 SER B 74 3.82 -66.11
REMARK 500 ASN B 75 21.67 -147.75
REMARK 500 LYS B 85 -167.11 -72.89
REMARK 500 ASP B 86 -49.00 73.05
REMARK 500 ASN B 102 18.87 57.34
REMARK 500 ASN B 142 -72.04 -86.44
REMARK 500 GLU B 172 39.95 33.29
REMARK 500
REMARK 500 THIS ENTRY HAS 218 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU F 369 THR F 370 -135.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 251 0.07 SIDE CHAIN
REMARK 500 TYR C 251 0.08 SIDE CHAIN
REMARK 500 TYR D 251 0.07 SIDE CHAIN
REMARK 500 TYR E 251 0.08 SIDE CHAIN
REMARK 500 TYR F 251 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 MET A 377 -21.11
REMARK 500 HIS B 158 39.52
REMARK 500 HIS C 158 38.06
REMARK 500 HIS D 158 37.76
REMARK 500 LEU D 327 10.24
REMARK 500 HIS E 158 38.32
REMARK 500 HIS F 158 38.24
REMARK 500 GLU F 369 -11.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ILE A 60 47.9 L L OUTSIDE RANGE
REMARK 500 ASN A 142 21.6 L L OUTSIDE RANGE
REMARK 500 VAL A 328 21.6 L L OUTSIDE RANGE
REMARK 500 GLU A 369 50.9 L L OUTSIDE RANGE
REMARK 500 THR A 370 46.8 L L OUTSIDE RANGE
REMARK 500 MET A 377 5.6 L L EXPECTING SP3
REMARK 500 PHE A 378 23.4 L L OUTSIDE RANGE
REMARK 500 ILE B 60 48.0 L L OUTSIDE RANGE
REMARK 500 ASN B 142 18.7 L L OUTSIDE RANGE
REMARK 500 VAL B 328 45.6 L L OUTSIDE RANGE
REMARK 500 ASN B 329 15.3 L L OUTSIDE RANGE
REMARK 500 THR B 370 45.4 L L OUTSIDE RANGE
REMARK 500 LEU C 327 19.5 L L OUTSIDE RANGE
REMARK 500 PHE C 378 21.0 L L OUTSIDE RANGE
REMARK 500 ASN D 142 21.8 L L OUTSIDE RANGE
REMARK 500 ALA D 325 47.5 L L OUTSIDE RANGE
REMARK 500 LEU D 327 21.6 L L OUTSIDE RANGE
REMARK 500 ASN D 329 24.1 L L OUTSIDE RANGE
REMARK 500 GLU D 369 47.6 L L OUTSIDE RANGE
REMARK 500 MET D 377 19.2 L L OUTSIDE RANGE
REMARK 500 ILE D 379 23.1 L L OUTSIDE RANGE
REMARK 500 ASN E 142 20.1 L L OUTSIDE RANGE
REMARK 500 ASN E 329 23.7 L L OUTSIDE RANGE
REMARK 500 MET E 377 19.2 L L OUTSIDE RANGE
REMARK 500 PHE E 378 51.2 L L OUTSIDE RANGE
REMARK 500 ILE E 379 23.1 L L OUTSIDE RANGE
REMARK 500 ILE F 60 48.0 L L OUTSIDE RANGE
REMARK 500 ASN F 142 21.3 L L OUTSIDE RANGE
REMARK 500 ARG F 287 24.7 L L OUTSIDE RANGE
REMARK 500 VAL F 328 49.4 L L OUTSIDE RANGE
REMARK 500 THR F 370 47.6 L L OUTSIDE RANGE
REMARK 500 PHE F 378 22.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
DBREF 4ATW A 2 482 UNP G4FHJ5 G4FHJ5_THEMA 2 482
DBREF 4ATW B 2 482 UNP G4FHJ5 G4FHJ5_THEMA 2 482
DBREF 4ATW C 2 482 UNP G4FHJ5 G4FHJ5_THEMA 2 482
DBREF 4ATW D 2 482 UNP G4FHJ5 G4FHJ5_THEMA 2 482
DBREF 4ATW E 2 482 UNP G4FHJ5 G4FHJ5_THEMA 2 482
DBREF 4ATW F 2 482 UNP G4FHJ5 G4FHJ5_THEMA 2 482
SEQADV 4ATW HIS A 1 UNP G4FHJ5 EXPRESSION TAG
SEQADV 4ATW HIS B 1 UNP G4FHJ5 EXPRESSION TAG
SEQADV 4ATW HIS C 1 UNP G4FHJ5 EXPRESSION TAG
SEQADV 4ATW HIS D 1 UNP G4FHJ5 EXPRESSION TAG
SEQADV 4ATW HIS E 1 UNP G4FHJ5 EXPRESSION TAG
SEQADV 4ATW HIS F 1 UNP G4FHJ5 EXPRESSION TAG
SEQRES 1 A 482 HIS SER TYR ARG ILE VAL VAL ASP PRO LYS GLU VAL VAL
SEQRES 2 A 482 LYS PRO ILE SER ARG HIS ILE TYR GLY HIS PHE THR GLU
SEQRES 3 A 482 HIS LEU GLY ARG CYS ILE TYR GLY GLY ILE TYR GLU GLU
SEQRES 4 A 482 GLY SER PRO LEU SER ASP GLU ARG GLY PHE ARG LYS ASP
SEQRES 5 A 482 VAL LEU GLU ALA VAL LYS ARG ILE LYS VAL PRO ASN LEU
SEQRES 6 A 482 ARG TRP PRO GLY GLY ASN PHE VAL SER ASN TYR HIS TRP
SEQRES 7 A 482 GLU ASP GLY ILE GLY PRO LYS ASP GLN ARG PRO VAL ARG
SEQRES 8 A 482 PHE ASP LEU ALA TRP GLN GLN GLU GLU THR ASN ARG PHE
SEQRES 9 A 482 GLY THR ASP GLU PHE ILE GLU TYR CYS ARG GLU ILE GLY
SEQRES 10 A 482 ALA GLU PRO TYR ILE SER ILE ASN MET GLY THR GLY THR
SEQRES 11 A 482 LEU ASP GLU ALA LEU HIS TRP LEU GLU TYR CYS ASN GLY
SEQRES 12 A 482 LYS GLY ASN THR TYR TYR ALA GLN LEU ARG ARG LYS TYR
SEQRES 13 A 482 GLY HIS PRO GLU PRO TYR ASN VAL LYS PHE TRP GLY ILE
SEQRES 14 A 482 GLY ASN GLU MET TYR GLY GLU TRP GLN VAL GLY HIS MET
SEQRES 15 A 482 THR ALA ASP GLU TYR ALA ARG ALA ALA LYS GLU TYR THR
SEQRES 16 A 482 LYS TRP MET LYS VAL PHE ASP PRO THR ILE LYS ALA ILE
SEQRES 17 A 482 ALA VAL GLY CYS ASP ASP PRO ILE TRP ASN LEU ARG VAL
SEQRES 18 A 482 LEU GLN GLU ALA GLY ASP VAL ILE ASP PHE ILE SER TYR
SEQRES 19 A 482 HIS PHE TYR THR GLY SER ASP ASP TYR TYR GLU THR VAL
SEQRES 20 A 482 SER THR VAL TYR LEU LEU LYS GLU ARG LEU ILE GLY VAL
SEQRES 21 A 482 LYS LYS LEU ILE ASP MET VAL ASP THR ALA ARG LYS ARG
SEQRES 22 A 482 GLY VAL LYS ILE ALA LEU ASP GLU TRP ASN VAL TRP TYR
SEQRES 23 A 482 ARG VAL SER ASP ASN LYS LEU GLU GLU PRO TYR ASP LEU
SEQRES 24 A 482 LYS ASP GLY ILE PHE ALA CYS GLY VAL LEU VAL LEU LEU
SEQRES 25 A 482 GLN LYS MET SER ASP ILE VAL PRO LEU ALA ASN LEU ALA
SEQRES 26 A 482 GLN LEU VAL ASN ALA LEU GLY ALA ILE HIS THR GLU LYS
SEQRES 27 A 482 ASP GLY LEU ILE LEU THR PRO VAL TYR LYS ALA PHE GLU
SEQRES 28 A 482 LEU ILE VAL ASN HIS SER GLY GLU LYS LEU VAL LYS THR
SEQRES 29 A 482 HIS VAL GLU SER GLU THR TYR ASN ILE GLU GLY VAL MET
SEQRES 30 A 482 PHE ILE ASN LYS MET PRO PHE SER VAL GLU ASN ALA PRO
SEQRES 31 A 482 PHE LEU ASP ALA ALA ALA SER ILE SER GLU ASP GLY LYS
SEQRES 32 A 482 LYS LEU PHE ILE ALA VAL VAL ASN TYR ARG LYS GLU ASP
SEQRES 33 A 482 ALA LEU LYS VAL PRO ILE ARG VAL GLU GLY LEU GLY GLN
SEQRES 34 A 482 LYS LYS ALA THR VAL TYR THR LEU THR GLY PRO ASP VAL
SEQRES 35 A 482 ASN ALA ARG ASN THR MET GLU ASN PRO ASN VAL VAL ASP
SEQRES 36 A 482 ILE THR SER GLU THR ILE THR VAL ASP THR GLU PHE GLU
SEQRES 37 A 482 HIS THR PHE LYS PRO PHE SER CYS SER VAL ILE GLU VAL
SEQRES 38 A 482 GLU
SEQRES 1 B 482 HIS SER TYR ARG ILE VAL VAL ASP PRO LYS GLU VAL VAL
SEQRES 2 B 482 LYS PRO ILE SER ARG HIS ILE TYR GLY HIS PHE THR GLU
SEQRES 3 B 482 HIS LEU GLY ARG CYS ILE TYR GLY GLY ILE TYR GLU GLU
SEQRES 4 B 482 GLY SER PRO LEU SER ASP GLU ARG GLY PHE ARG LYS ASP
SEQRES 5 B 482 VAL LEU GLU ALA VAL LYS ARG ILE LYS VAL PRO ASN LEU
SEQRES 6 B 482 ARG TRP PRO GLY GLY ASN PHE VAL SER ASN TYR HIS TRP
SEQRES 7 B 482 GLU ASP GLY ILE GLY PRO LYS ASP GLN ARG PRO VAL ARG
SEQRES 8 B 482 PHE ASP LEU ALA TRP GLN GLN GLU GLU THR ASN ARG PHE
SEQRES 9 B 482 GLY THR ASP GLU PHE ILE GLU TYR CYS ARG GLU ILE GLY
SEQRES 10 B 482 ALA GLU PRO TYR ILE SER ILE ASN MET GLY THR GLY THR
SEQRES 11 B 482 LEU ASP GLU ALA LEU HIS TRP LEU GLU TYR CYS ASN GLY
SEQRES 12 B 482 LYS GLY ASN THR TYR TYR ALA GLN LEU ARG ARG LYS TYR
SEQRES 13 B 482 GLY HIS PRO GLU PRO TYR ASN VAL LYS PHE TRP GLY ILE
SEQRES 14 B 482 GLY ASN GLU MET TYR GLY GLU TRP GLN VAL GLY HIS MET
SEQRES 15 B 482 THR ALA ASP GLU TYR ALA ARG ALA ALA LYS GLU TYR THR
SEQRES 16 B 482 LYS TRP MET LYS VAL PHE ASP PRO THR ILE LYS ALA ILE
SEQRES 17 B 482 ALA VAL GLY CYS ASP ASP PRO ILE TRP ASN LEU ARG VAL
SEQRES 18 B 482 LEU GLN GLU ALA GLY ASP VAL ILE ASP PHE ILE SER TYR
SEQRES 19 B 482 HIS PHE TYR THR GLY SER ASP ASP TYR TYR GLU THR VAL
SEQRES 20 B 482 SER THR VAL TYR LEU LEU LYS GLU ARG LEU ILE GLY VAL
SEQRES 21 B 482 LYS LYS LEU ILE ASP MET VAL ASP THR ALA ARG LYS ARG
SEQRES 22 B 482 GLY VAL LYS ILE ALA LEU ASP GLU TRP ASN VAL TRP TYR
SEQRES 23 B 482 ARG VAL SER ASP ASN LYS LEU GLU GLU PRO TYR ASP LEU
SEQRES 24 B 482 LYS ASP GLY ILE PHE ALA CYS GLY VAL LEU VAL LEU LEU
SEQRES 25 B 482 GLN LYS MET SER ASP ILE VAL PRO LEU ALA ASN LEU ALA
SEQRES 26 B 482 GLN LEU VAL ASN ALA LEU GLY ALA ILE HIS THR GLU LYS
SEQRES 27 B 482 ASP GLY LEU ILE LEU THR PRO VAL TYR LYS ALA PHE GLU
SEQRES 28 B 482 LEU ILE VAL ASN HIS SER GLY GLU LYS LEU VAL LYS THR
SEQRES 29 B 482 HIS VAL GLU SER GLU THR TYR ASN ILE GLU GLY VAL MET
SEQRES 30 B 482 PHE ILE ASN LYS MET PRO PHE SER VAL GLU ASN ALA PRO
SEQRES 31 B 482 PHE LEU ASP ALA ALA ALA SER ILE SER GLU ASP GLY LYS
SEQRES 32 B 482 LYS LEU PHE ILE ALA VAL VAL ASN TYR ARG LYS GLU ASP
SEQRES 33 B 482 ALA LEU LYS VAL PRO ILE ARG VAL GLU GLY LEU GLY GLN
SEQRES 34 B 482 LYS LYS ALA THR VAL TYR THR LEU THR GLY PRO ASP VAL
SEQRES 35 B 482 ASN ALA ARG ASN THR MET GLU ASN PRO ASN VAL VAL ASP
SEQRES 36 B 482 ILE THR SER GLU THR ILE THR VAL ASP THR GLU PHE GLU
SEQRES 37 B 482 HIS THR PHE LYS PRO PHE SER CYS SER VAL ILE GLU VAL
SEQRES 38 B 482 GLU
SEQRES 1 C 482 HIS SER TYR ARG ILE VAL VAL ASP PRO LYS GLU VAL VAL
SEQRES 2 C 482 LYS PRO ILE SER ARG HIS ILE TYR GLY HIS PHE THR GLU
SEQRES 3 C 482 HIS LEU GLY ARG CYS ILE TYR GLY GLY ILE TYR GLU GLU
SEQRES 4 C 482 GLY SER PRO LEU SER ASP GLU ARG GLY PHE ARG LYS ASP
SEQRES 5 C 482 VAL LEU GLU ALA VAL LYS ARG ILE LYS VAL PRO ASN LEU
SEQRES 6 C 482 ARG TRP PRO GLY GLY ASN PHE VAL SER ASN TYR HIS TRP
SEQRES 7 C 482 GLU ASP GLY ILE GLY PRO LYS ASP GLN ARG PRO VAL ARG
SEQRES 8 C 482 PHE ASP LEU ALA TRP GLN GLN GLU GLU THR ASN ARG PHE
SEQRES 9 C 482 GLY THR ASP GLU PHE ILE GLU TYR CYS ARG GLU ILE GLY
SEQRES 10 C 482 ALA GLU PRO TYR ILE SER ILE ASN MET GLY THR GLY THR
SEQRES 11 C 482 LEU ASP GLU ALA LEU HIS TRP LEU GLU TYR CYS ASN GLY
SEQRES 12 C 482 LYS GLY ASN THR TYR TYR ALA GLN LEU ARG ARG LYS TYR
SEQRES 13 C 482 GLY HIS PRO GLU PRO TYR ASN VAL LYS PHE TRP GLY ILE
SEQRES 14 C 482 GLY ASN GLU MET TYR GLY GLU TRP GLN VAL GLY HIS MET
SEQRES 15 C 482 THR ALA ASP GLU TYR ALA ARG ALA ALA LYS GLU TYR THR
SEQRES 16 C 482 LYS TRP MET LYS VAL PHE ASP PRO THR ILE LYS ALA ILE
SEQRES 17 C 482 ALA VAL GLY CYS ASP ASP PRO ILE TRP ASN LEU ARG VAL
SEQRES 18 C 482 LEU GLN GLU ALA GLY ASP VAL ILE ASP PHE ILE SER TYR
SEQRES 19 C 482 HIS PHE TYR THR GLY SER ASP ASP TYR TYR GLU THR VAL
SEQRES 20 C 482 SER THR VAL TYR LEU LEU LYS GLU ARG LEU ILE GLY VAL
SEQRES 21 C 482 LYS LYS LEU ILE ASP MET VAL ASP THR ALA ARG LYS ARG
SEQRES 22 C 482 GLY VAL LYS ILE ALA LEU ASP GLU TRP ASN VAL TRP TYR
SEQRES 23 C 482 ARG VAL SER ASP ASN LYS LEU GLU GLU PRO TYR ASP LEU
SEQRES 24 C 482 LYS ASP GLY ILE PHE ALA CYS GLY VAL LEU VAL LEU LEU
SEQRES 25 C 482 GLN LYS MET SER ASP ILE VAL PRO LEU ALA ASN LEU ALA
SEQRES 26 C 482 GLN LEU VAL ASN ALA LEU GLY ALA ILE HIS THR GLU LYS
SEQRES 27 C 482 ASP GLY LEU ILE LEU THR PRO VAL TYR LYS ALA PHE GLU
SEQRES 28 C 482 LEU ILE VAL ASN HIS SER GLY GLU LYS LEU VAL LYS THR
SEQRES 29 C 482 HIS VAL GLU SER GLU THR TYR ASN ILE GLU GLY VAL MET
SEQRES 30 C 482 PHE ILE ASN LYS MET PRO PHE SER VAL GLU ASN ALA PRO
SEQRES 31 C 482 PHE LEU ASP ALA ALA ALA SER ILE SER GLU ASP GLY LYS
SEQRES 32 C 482 LYS LEU PHE ILE ALA VAL VAL ASN TYR ARG LYS GLU ASP
SEQRES 33 C 482 ALA LEU LYS VAL PRO ILE ARG VAL GLU GLY LEU GLY GLN
SEQRES 34 C 482 LYS LYS ALA THR VAL TYR THR LEU THR GLY PRO ASP VAL
SEQRES 35 C 482 ASN ALA ARG ASN THR MET GLU ASN PRO ASN VAL VAL ASP
SEQRES 36 C 482 ILE THR SER GLU THR ILE THR VAL ASP THR GLU PHE GLU
SEQRES 37 C 482 HIS THR PHE LYS PRO PHE SER CYS SER VAL ILE GLU VAL
SEQRES 38 C 482 GLU
SEQRES 1 D 482 HIS SER TYR ARG ILE VAL VAL ASP PRO LYS GLU VAL VAL
SEQRES 2 D 482 LYS PRO ILE SER ARG HIS ILE TYR GLY HIS PHE THR GLU
SEQRES 3 D 482 HIS LEU GLY ARG CYS ILE TYR GLY GLY ILE TYR GLU GLU
SEQRES 4 D 482 GLY SER PRO LEU SER ASP GLU ARG GLY PHE ARG LYS ASP
SEQRES 5 D 482 VAL LEU GLU ALA VAL LYS ARG ILE LYS VAL PRO ASN LEU
SEQRES 6 D 482 ARG TRP PRO GLY GLY ASN PHE VAL SER ASN TYR HIS TRP
SEQRES 7 D 482 GLU ASP GLY ILE GLY PRO LYS ASP GLN ARG PRO VAL ARG
SEQRES 8 D 482 PHE ASP LEU ALA TRP GLN GLN GLU GLU THR ASN ARG PHE
SEQRES 9 D 482 GLY THR ASP GLU PHE ILE GLU TYR CYS ARG GLU ILE GLY
SEQRES 10 D 482 ALA GLU PRO TYR ILE SER ILE ASN MET GLY THR GLY THR
SEQRES 11 D 482 LEU ASP GLU ALA LEU HIS TRP LEU GLU TYR CYS ASN GLY
SEQRES 12 D 482 LYS GLY ASN THR TYR TYR ALA GLN LEU ARG ARG LYS TYR
SEQRES 13 D 482 GLY HIS PRO GLU PRO TYR ASN VAL LYS PHE TRP GLY ILE
SEQRES 14 D 482 GLY ASN GLU MET TYR GLY GLU TRP GLN VAL GLY HIS MET
SEQRES 15 D 482 THR ALA ASP GLU TYR ALA ARG ALA ALA LYS GLU TYR THR
SEQRES 16 D 482 LYS TRP MET LYS VAL PHE ASP PRO THR ILE LYS ALA ILE
SEQRES 17 D 482 ALA VAL GLY CYS ASP ASP PRO ILE TRP ASN LEU ARG VAL
SEQRES 18 D 482 LEU GLN GLU ALA GLY ASP VAL ILE ASP PHE ILE SER TYR
SEQRES 19 D 482 HIS PHE TYR THR GLY SER ASP ASP TYR TYR GLU THR VAL
SEQRES 20 D 482 SER THR VAL TYR LEU LEU LYS GLU ARG LEU ILE GLY VAL
SEQRES 21 D 482 LYS LYS LEU ILE ASP MET VAL ASP THR ALA ARG LYS ARG
SEQRES 22 D 482 GLY VAL LYS ILE ALA LEU ASP GLU TRP ASN VAL TRP TYR
SEQRES 23 D 482 ARG VAL SER ASP ASN LYS LEU GLU GLU PRO TYR ASP LEU
SEQRES 24 D 482 LYS ASP GLY ILE PHE ALA CYS GLY VAL LEU VAL LEU LEU
SEQRES 25 D 482 GLN LYS MET SER ASP ILE VAL PRO LEU ALA ASN LEU ALA
SEQRES 26 D 482 GLN LEU VAL ASN ALA LEU GLY ALA ILE HIS THR GLU LYS
SEQRES 27 D 482 ASP GLY LEU ILE LEU THR PRO VAL TYR LYS ALA PHE GLU
SEQRES 28 D 482 LEU ILE VAL ASN HIS SER GLY GLU LYS LEU VAL LYS THR
SEQRES 29 D 482 HIS VAL GLU SER GLU THR TYR ASN ILE GLU GLY VAL MET
SEQRES 30 D 482 PHE ILE ASN LYS MET PRO PHE SER VAL GLU ASN ALA PRO
SEQRES 31 D 482 PHE LEU ASP ALA ALA ALA SER ILE SER GLU ASP GLY LYS
SEQRES 32 D 482 LYS LEU PHE ILE ALA VAL VAL ASN TYR ARG LYS GLU ASP
SEQRES 33 D 482 ALA LEU LYS VAL PRO ILE ARG VAL GLU GLY LEU GLY GLN
SEQRES 34 D 482 LYS LYS ALA THR VAL TYR THR LEU THR GLY PRO ASP VAL
SEQRES 35 D 482 ASN ALA ARG ASN THR MET GLU ASN PRO ASN VAL VAL ASP
SEQRES 36 D 482 ILE THR SER GLU THR ILE THR VAL ASP THR GLU PHE GLU
SEQRES 37 D 482 HIS THR PHE LYS PRO PHE SER CYS SER VAL ILE GLU VAL
SEQRES 38 D 482 GLU
SEQRES 1 E 482 HIS SER TYR ARG ILE VAL VAL ASP PRO LYS GLU VAL VAL
SEQRES 2 E 482 LYS PRO ILE SER ARG HIS ILE TYR GLY HIS PHE THR GLU
SEQRES 3 E 482 HIS LEU GLY ARG CYS ILE TYR GLY GLY ILE TYR GLU GLU
SEQRES 4 E 482 GLY SER PRO LEU SER ASP GLU ARG GLY PHE ARG LYS ASP
SEQRES 5 E 482 VAL LEU GLU ALA VAL LYS ARG ILE LYS VAL PRO ASN LEU
SEQRES 6 E 482 ARG TRP PRO GLY GLY ASN PHE VAL SER ASN TYR HIS TRP
SEQRES 7 E 482 GLU ASP GLY ILE GLY PRO LYS ASP GLN ARG PRO VAL ARG
SEQRES 8 E 482 PHE ASP LEU ALA TRP GLN GLN GLU GLU THR ASN ARG PHE
SEQRES 9 E 482 GLY THR ASP GLU PHE ILE GLU TYR CYS ARG GLU ILE GLY
SEQRES 10 E 482 ALA GLU PRO TYR ILE SER ILE ASN MET GLY THR GLY THR
SEQRES 11 E 482 LEU ASP GLU ALA LEU HIS TRP LEU GLU TYR CYS ASN GLY
SEQRES 12 E 482 LYS GLY ASN THR TYR TYR ALA GLN LEU ARG ARG LYS TYR
SEQRES 13 E 482 GLY HIS PRO GLU PRO TYR ASN VAL LYS PHE TRP GLY ILE
SEQRES 14 E 482 GLY ASN GLU MET TYR GLY GLU TRP GLN VAL GLY HIS MET
SEQRES 15 E 482 THR ALA ASP GLU TYR ALA ARG ALA ALA LYS GLU TYR THR
SEQRES 16 E 482 LYS TRP MET LYS VAL PHE ASP PRO THR ILE LYS ALA ILE
SEQRES 17 E 482 ALA VAL GLY CYS ASP ASP PRO ILE TRP ASN LEU ARG VAL
SEQRES 18 E 482 LEU GLN GLU ALA GLY ASP VAL ILE ASP PHE ILE SER TYR
SEQRES 19 E 482 HIS PHE TYR THR GLY SER ASP ASP TYR TYR GLU THR VAL
SEQRES 20 E 482 SER THR VAL TYR LEU LEU LYS GLU ARG LEU ILE GLY VAL
SEQRES 21 E 482 LYS LYS LEU ILE ASP MET VAL ASP THR ALA ARG LYS ARG
SEQRES 22 E 482 GLY VAL LYS ILE ALA LEU ASP GLU TRP ASN VAL TRP TYR
SEQRES 23 E 482 ARG VAL SER ASP ASN LYS LEU GLU GLU PRO TYR ASP LEU
SEQRES 24 E 482 LYS ASP GLY ILE PHE ALA CYS GLY VAL LEU VAL LEU LEU
SEQRES 25 E 482 GLN LYS MET SER ASP ILE VAL PRO LEU ALA ASN LEU ALA
SEQRES 26 E 482 GLN LEU VAL ASN ALA LEU GLY ALA ILE HIS THR GLU LYS
SEQRES 27 E 482 ASP GLY LEU ILE LEU THR PRO VAL TYR LYS ALA PHE GLU
SEQRES 28 E 482 LEU ILE VAL ASN HIS SER GLY GLU LYS LEU VAL LYS THR
SEQRES 29 E 482 HIS VAL GLU SER GLU THR TYR ASN ILE GLU GLY VAL MET
SEQRES 30 E 482 PHE ILE ASN LYS MET PRO PHE SER VAL GLU ASN ALA PRO
SEQRES 31 E 482 PHE LEU ASP ALA ALA ALA SER ILE SER GLU ASP GLY LYS
SEQRES 32 E 482 LYS LEU PHE ILE ALA VAL VAL ASN TYR ARG LYS GLU ASP
SEQRES 33 E 482 ALA LEU LYS VAL PRO ILE ARG VAL GLU GLY LEU GLY GLN
SEQRES 34 E 482 LYS LYS ALA THR VAL TYR THR LEU THR GLY PRO ASP VAL
SEQRES 35 E 482 ASN ALA ARG ASN THR MET GLU ASN PRO ASN VAL VAL ASP
SEQRES 36 E 482 ILE THR SER GLU THR ILE THR VAL ASP THR GLU PHE GLU
SEQRES 37 E 482 HIS THR PHE LYS PRO PHE SER CYS SER VAL ILE GLU VAL
SEQRES 38 E 482 GLU
SEQRES 1 F 482 HIS SER TYR ARG ILE VAL VAL ASP PRO LYS GLU VAL VAL
SEQRES 2 F 482 LYS PRO ILE SER ARG HIS ILE TYR GLY HIS PHE THR GLU
SEQRES 3 F 482 HIS LEU GLY ARG CYS ILE TYR GLY GLY ILE TYR GLU GLU
SEQRES 4 F 482 GLY SER PRO LEU SER ASP GLU ARG GLY PHE ARG LYS ASP
SEQRES 5 F 482 VAL LEU GLU ALA VAL LYS ARG ILE LYS VAL PRO ASN LEU
SEQRES 6 F 482 ARG TRP PRO GLY GLY ASN PHE VAL SER ASN TYR HIS TRP
SEQRES 7 F 482 GLU ASP GLY ILE GLY PRO LYS ASP GLN ARG PRO VAL ARG
SEQRES 8 F 482 PHE ASP LEU ALA TRP GLN GLN GLU GLU THR ASN ARG PHE
SEQRES 9 F 482 GLY THR ASP GLU PHE ILE GLU TYR CYS ARG GLU ILE GLY
SEQRES 10 F 482 ALA GLU PRO TYR ILE SER ILE ASN MET GLY THR GLY THR
SEQRES 11 F 482 LEU ASP GLU ALA LEU HIS TRP LEU GLU TYR CYS ASN GLY
SEQRES 12 F 482 LYS GLY ASN THR TYR TYR ALA GLN LEU ARG ARG LYS TYR
SEQRES 13 F 482 GLY HIS PRO GLU PRO TYR ASN VAL LYS PHE TRP GLY ILE
SEQRES 14 F 482 GLY ASN GLU MET TYR GLY GLU TRP GLN VAL GLY HIS MET
SEQRES 15 F 482 THR ALA ASP GLU TYR ALA ARG ALA ALA LYS GLU TYR THR
SEQRES 16 F 482 LYS TRP MET LYS VAL PHE ASP PRO THR ILE LYS ALA ILE
SEQRES 17 F 482 ALA VAL GLY CYS ASP ASP PRO ILE TRP ASN LEU ARG VAL
SEQRES 18 F 482 LEU GLN GLU ALA GLY ASP VAL ILE ASP PHE ILE SER TYR
SEQRES 19 F 482 HIS PHE TYR THR GLY SER ASP ASP TYR TYR GLU THR VAL
SEQRES 20 F 482 SER THR VAL TYR LEU LEU LYS GLU ARG LEU ILE GLY VAL
SEQRES 21 F 482 LYS LYS LEU ILE ASP MET VAL ASP THR ALA ARG LYS ARG
SEQRES 22 F 482 GLY VAL LYS ILE ALA LEU ASP GLU TRP ASN VAL TRP TYR
SEQRES 23 F 482 ARG VAL SER ASP ASN LYS LEU GLU GLU PRO TYR ASP LEU
SEQRES 24 F 482 LYS ASP GLY ILE PHE ALA CYS GLY VAL LEU VAL LEU LEU
SEQRES 25 F 482 GLN LYS MET SER ASP ILE VAL PRO LEU ALA ASN LEU ALA
SEQRES 26 F 482 GLN LEU VAL ASN ALA LEU GLY ALA ILE HIS THR GLU LYS
SEQRES 27 F 482 ASP GLY LEU ILE LEU THR PRO VAL TYR LYS ALA PHE GLU
SEQRES 28 F 482 LEU ILE VAL ASN HIS SER GLY GLU LYS LEU VAL LYS THR
SEQRES 29 F 482 HIS VAL GLU SER GLU THR TYR ASN ILE GLU GLY VAL MET
SEQRES 30 F 482 PHE ILE ASN LYS MET PRO PHE SER VAL GLU ASN ALA PRO
SEQRES 31 F 482 PHE LEU ASP ALA ALA ALA SER ILE SER GLU ASP GLY LYS
SEQRES 32 F 482 LYS LEU PHE ILE ALA VAL VAL ASN TYR ARG LYS GLU ASP
SEQRES 33 F 482 ALA LEU LYS VAL PRO ILE ARG VAL GLU GLY LEU GLY GLN
SEQRES 34 F 482 LYS LYS ALA THR VAL TYR THR LEU THR GLY PRO ASP VAL
SEQRES 35 F 482 ASN ALA ARG ASN THR MET GLU ASN PRO ASN VAL VAL ASP
SEQRES 36 F 482 ILE THR SER GLU THR ILE THR VAL ASP THR GLU PHE GLU
SEQRES 37 F 482 HIS THR PHE LYS PRO PHE SER CYS SER VAL ILE GLU VAL
SEQRES 38 F 482 GLU
HELIX 1 1 SER A 17 TYR A 21 5 5
HELIX 2 2 ARG A 50 ARG A 59 1 10
HELIX 3 3 GLY A 70 TYR A 76 5 7
HELIX 4 4 HIS A 77 ILE A 82 5 6
HELIX 5 5 GLY A 105 GLY A 117 1 13
HELIX 6 6 THR A 130 ASN A 142 1 13
HELIX 7 7 THR A 147 GLY A 157 1 11
HELIX 8 8 THR A 183 TRP A 197 1 15
HELIX 9 9 ASP A 214 GLY A 226 1 13
HELIX 10 10 ASP A 242 SER A 248 1 7
HELIX 11 11 THR A 249 MET A 266 1 18
HELIX 12 12 VAL A 267 ARG A 273 1 7
HELIX 13 13 ASP A 298 LYS A 314 1 17
HELIX 14 14 THR A 344 HIS A 356 1 13
HELIX 15 15 SER B 17 TYR B 21 5 5
HELIX 16 16 ARG B 50 ARG B 59 1 10
HELIX 17 17 GLY B 70 TYR B 76 5 7
HELIX 18 18 HIS B 77 ILE B 82 5 6
HELIX 19 19 GLY B 105 GLY B 117 1 13
HELIX 20 20 THR B 130 ASN B 142 1 13
HELIX 21 21 THR B 147 TYR B 156 1 10
HELIX 22 22 THR B 183 TRP B 197 1 15
HELIX 23 23 ASP B 214 GLY B 226 1 13
HELIX 24 24 ASP B 242 SER B 248 1 7
HELIX 25 25 THR B 249 MET B 266 1 18
HELIX 26 26 VAL B 267 ARG B 273 1 7
HELIX 27 27 ASP B 298 LYS B 314 1 17
HELIX 28 28 THR B 344 HIS B 356 1 13
HELIX 29 29 SER C 17 TYR C 21 5 5
HELIX 30 30 ARG C 50 ILE C 60 1 11
HELIX 31 31 GLY C 70 TYR C 76 5 7
HELIX 32 32 HIS C 77 ILE C 82 5 6
HELIX 33 33 GLY C 105 GLY C 117 1 13
HELIX 34 34 THR C 130 ASN C 142 1 13
HELIX 35 35 THR C 147 GLY C 157 1 11
HELIX 36 36 THR C 183 TRP C 197 1 15
HELIX 37 37 ASP C 214 GLY C 226 1 13
HELIX 38 38 ASP C 242 SER C 248 1 7
HELIX 39 39 THR C 249 MET C 266 1 18
HELIX 40 40 VAL C 267 ARG C 273 1 7
HELIX 41 41 ASP C 298 LYS C 314 1 17
HELIX 42 42 THR C 344 HIS C 356 1 13
HELIX 43 43 SER D 17 TYR D 21 5 5
HELIX 44 44 ARG D 50 ARG D 59 1 10
HELIX 45 45 GLY D 70 TYR D 76 5 7
HELIX 46 46 HIS D 77 ILE D 82 5 6
HELIX 47 47 GLY D 105 GLY D 117 1 13
HELIX 48 48 THR D 130 ASN D 142 1 13
HELIX 49 49 THR D 147 GLY D 157 1 11
HELIX 50 50 THR D 183 TRP D 197 1 15
HELIX 51 51 ASP D 214 GLY D 226 1 13
HELIX 52 52 ASP D 242 SER D 248 1 7
HELIX 53 53 THR D 249 MET D 266 1 18
HELIX 54 54 VAL D 267 ARG D 273 1 7
HELIX 55 55 ASP D 298 LYS D 314 1 17
HELIX 56 56 THR D 344 HIS D 356 1 13
HELIX 57 57 SER E 17 TYR E 21 5 5
HELIX 58 58 ARG E 50 ARG E 59 1 10
HELIX 59 59 GLY E 70 TYR E 76 5 7
HELIX 60 60 HIS E 77 ILE E 82 5 6
HELIX 61 61 GLY E 105 GLY E 117 1 13
HELIX 62 62 THR E 130 ASN E 142 1 13
HELIX 63 63 THR E 147 GLY E 157 1 11
HELIX 64 64 THR E 183 TRP E 197 1 15
HELIX 65 65 ASP E 214 GLY E 226 1 13
HELIX 66 66 ASP E 242 SER E 248 1 7
HELIX 67 67 THR E 249 MET E 266 1 18
HELIX 68 68 VAL E 267 ARG E 273 1 7
HELIX 69 69 ASP E 298 LYS E 314 1 17
HELIX 70 70 THR E 344 HIS E 356 1 13
HELIX 71 71 SER F 17 TYR F 21 5 5
HELIX 72 72 ARG F 50 ARG F 59 1 10
HELIX 73 73 GLY F 70 TYR F 76 5 7
HELIX 74 74 HIS F 77 ILE F 82 5 6
HELIX 75 75 GLY F 105 GLY F 117 1 13
HELIX 76 76 THR F 130 ASN F 142 1 13
HELIX 77 77 THR F 147 GLY F 157 1 11
HELIX 78 78 THR F 183 TRP F 197 1 15
HELIX 79 79 ASP F 214 GLY F 226 1 13
HELIX 80 80 ASP F 242 SER F 248 1 7
HELIX 81 81 THR F 249 MET F 266 1 18
HELIX 82 82 VAL F 267 ARG F 273 1 7
HELIX 83 83 ASP F 298 LYS F 314 1 17
HELIX 84 84 THR F 344 HIS F 356 1 13
SHEET 1 AA 9 ASP A 455 THR A 457 0
SHEET 2 AA 9 THR A 433 THR A 438 -1 O THR A 436 N THR A 457
SHEET 3 AA 9 SER A 475 VAL A 481 -1 O CYS A 476 N LEU A 437
SHEET 4 AA 9 LEU A 405 ASN A 411 -1 O LEU A 405 N VAL A 481
SHEET 5 AA 9 LEU A 392 ILE A 398 -1 O ASP A 393 N VAL A 410
SHEET 6 AA 9 LYS A 360 GLU A 367 -1 O LYS A 360 N ILE A 398
SHEET 7 AA 9 ARG A 4 PRO A 15 -1 O ARG A 4 N GLU A 367
SHEET 8 AA 9 PRO A 421 VAL A 424 1 O PRO A 421 N ILE A 5
SHEET 9 AA 9 GLU A 466 GLU A 468 -1 O PHE A 467 N ILE A 422
SHEET 1 AB 8 HIS A 23 PHE A 24 0
SHEET 2 AB 8 ASN A 64 TRP A 67 1 O ASN A 64 N HIS A 23
SHEET 3 AB 8 GLU A 119 SER A 123 1 O GLU A 119 N LEU A 65
SHEET 4 AB 8 PHE A 166 ILE A 169 1 O PHE A 166 N ILE A 122
SHEET 5 AB 8 LYS A 206 ALA A 209 1 O LYS A 206 N TRP A 167
SHEET 6 AB 8 PHE A 231 THR A 238 1 O PHE A 231 N ALA A 209
SHEET 7 AB 8 LYS A 276 VAL A 284 1 O LYS A 276 N ILE A 232
SHEET 8 AB 8 LEU A 321 ALA A 322 1 O LEU A 321 N LEU A 279
SHEET 1 AC 2 ARG A 91 ASP A 93 0
SHEET 2 AC 2 GLN A 98 GLU A 100 -1 O GLN A 98 N ASP A 93
SHEET 1 AD 2 ILE A 334 GLU A 337 0
SHEET 2 AD 2 GLY A 340 LEU A 343 -1 O GLY A 340 N GLU A 337
SHEET 1 AE 2 THR A 370 VAL A 376 0
SHEET 2 AE 2 PRO A 383 PRO A 390 -1 O PHE A 384 N GLY A 375
SHEET 1 BA 9 ASP B 455 THR B 457 0
SHEET 2 BA 9 THR B 433 THR B 438 -1 O THR B 436 N THR B 457
SHEET 3 BA 9 SER B 475 VAL B 481 -1 O CYS B 476 N LEU B 437
SHEET 4 BA 9 LEU B 405 ASN B 411 -1 O LEU B 405 N VAL B 481
SHEET 5 BA 9 LEU B 392 ILE B 398 -1 O ASP B 393 N VAL B 410
SHEET 6 BA 9 LYS B 360 GLU B 367 -1 O LYS B 360 N ILE B 398
SHEET 7 BA 9 ARG B 4 PRO B 15 -1 O ARG B 4 N GLU B 367
SHEET 8 BA 9 PRO B 421 VAL B 424 1 O PRO B 421 N ILE B 5
SHEET 9 BA 9 GLU B 466 GLU B 468 -1 O PHE B 467 N ILE B 422
SHEET 1 BB 9 GLY B 22 PHE B 24 0
SHEET 2 BB 9 LEU B 321 LEU B 324 1 O ALA B 322 N GLY B 22
SHEET 3 BB 9 LYS B 276 VAL B 284 1 O ILE B 277 N LEU B 321
SHEET 4 BB 9 PHE B 231 THR B 238 1 O ILE B 232 N ALA B 278
SHEET 5 BB 9 LYS B 206 ALA B 209 1 O ALA B 209 N SER B 233
SHEET 6 BB 9 PHE B 166 ILE B 169 1 O TRP B 167 N ILE B 208
SHEET 7 BB 9 GLU B 119 SER B 123 1 O PRO B 120 N PHE B 166
SHEET 8 BB 9 ASN B 64 TRP B 67 1 O LEU B 65 N TYR B 121
SHEET 9 BB 9 GLY B 22 PHE B 24 1 O HIS B 23 N ARG B 66
SHEET 1 BC 2 ARG B 91 ASP B 93 0
SHEET 2 BC 2 GLN B 98 GLU B 100 -1 O GLN B 98 N ASP B 93
SHEET 1 BD 2 ILE B 334 GLU B 337 0
SHEET 2 BD 2 GLY B 340 LEU B 343 -1 O GLY B 340 N GLU B 337
SHEET 1 BE 2 THR B 370 VAL B 376 0
SHEET 2 BE 2 PRO B 383 PRO B 390 -1 O PHE B 384 N GLY B 375
SHEET 1 CA 9 ASP C 455 THR C 457 0
SHEET 2 CA 9 THR C 433 THR C 438 -1 O THR C 436 N THR C 457
SHEET 3 CA 9 SER C 475 VAL C 481 -1 O CYS C 476 N LEU C 437
SHEET 4 CA 9 LEU C 405 ASN C 411 -1 O LEU C 405 N VAL C 481
SHEET 5 CA 9 LEU C 392 ILE C 398 -1 O ASP C 393 N VAL C 410
SHEET 6 CA 9 LYS C 360 GLU C 367 -1 O LYS C 360 N ILE C 398
SHEET 7 CA 9 ARG C 4 PRO C 15 -1 O ARG C 4 N GLU C 367
SHEET 8 CA 9 PRO C 421 VAL C 424 1 O PRO C 421 N ILE C 5
SHEET 9 CA 9 GLU C 466 GLU C 468 -1 O PHE C 467 N ILE C 422
SHEET 1 CB 8 HIS C 23 PHE C 24 0
SHEET 2 CB 8 ASN C 64 TRP C 67 1 O ASN C 64 N HIS C 23
SHEET 3 CB 8 GLU C 119 SER C 123 1 O GLU C 119 N LEU C 65
SHEET 4 CB 8 PHE C 166 ILE C 169 1 O PHE C 166 N ILE C 122
SHEET 5 CB 8 LYS C 206 ALA C 209 1 O LYS C 206 N TRP C 167
SHEET 6 CB 8 PHE C 231 THR C 238 1 O PHE C 231 N ALA C 209
SHEET 7 CB 8 LYS C 276 VAL C 284 1 O LYS C 276 N ILE C 232
SHEET 8 CB 8 LEU C 321 LEU C 324 1 O LEU C 321 N LEU C 279
SHEET 1 CC 2 ARG C 91 ASP C 93 0
SHEET 2 CC 2 GLN C 98 GLU C 100 -1 O GLN C 98 N ASP C 93
SHEET 1 CD 2 ILE C 334 GLU C 337 0
SHEET 2 CD 2 GLY C 340 LEU C 343 -1 O GLY C 340 N GLU C 337
SHEET 1 CE 2 THR C 370 MET C 377 0
SHEET 2 CE 2 MET C 382 PRO C 390 -1 O MET C 382 N MET C 377
SHEET 1 DA 9 ASP D 455 THR D 457 0
SHEET 2 DA 9 THR D 433 THR D 438 -1 O THR D 436 N THR D 457
SHEET 3 DA 9 SER D 475 VAL D 481 -1 O CYS D 476 N LEU D 437
SHEET 4 DA 9 LEU D 405 ASN D 411 -1 O LEU D 405 N VAL D 481
SHEET 5 DA 9 LEU D 392 ILE D 398 -1 O ASP D 393 N VAL D 410
SHEET 6 DA 9 LYS D 360 GLU D 367 -1 O LYS D 360 N ILE D 398
SHEET 7 DA 9 ARG D 4 PRO D 15 -1 O ARG D 4 N GLU D 367
SHEET 8 DA 9 PRO D 421 VAL D 424 1 O PRO D 421 N ILE D 5
SHEET 9 DA 9 GLU D 466 GLU D 468 -1 O PHE D 467 N ILE D 422
SHEET 1 DB 8 HIS D 23 PHE D 24 0
SHEET 2 DB 8 ASN D 64 TRP D 67 1 O ASN D 64 N HIS D 23
SHEET 3 DB 8 GLU D 119 SER D 123 1 O GLU D 119 N LEU D 65
SHEET 4 DB 8 PHE D 166 ILE D 169 1 O PHE D 166 N ILE D 122
SHEET 5 DB 8 LYS D 206 ALA D 209 1 O LYS D 206 N TRP D 167
SHEET 6 DB 8 PHE D 231 THR D 238 1 O PHE D 231 N ALA D 209
SHEET 7 DB 8 LYS D 276 VAL D 284 1 O LYS D 276 N ILE D 232
SHEET 8 DB 8 LEU D 321 LEU D 324 1 O LEU D 321 N LEU D 279
SHEET 1 DC 2 ARG D 91 ASP D 93 0
SHEET 2 DC 2 GLN D 98 GLU D 100 -1 O GLN D 98 N ASP D 93
SHEET 1 DD 2 ILE D 334 GLU D 337 0
SHEET 2 DD 2 GLY D 340 LEU D 343 -1 O GLY D 340 N GLU D 337
SHEET 1 DE 2 THR D 370 VAL D 376 0
SHEET 2 DE 2 PRO D 383 PRO D 390 -1 O PHE D 384 N GLY D 375
SHEET 1 EA 9 ASP E 455 THR E 457 0
SHEET 2 EA 9 THR E 433 THR E 438 -1 O THR E 436 N THR E 457
SHEET 3 EA 9 SER E 475 VAL E 481 -1 O CYS E 476 N LEU E 437
SHEET 4 EA 9 LEU E 405 ASN E 411 -1 O LEU E 405 N VAL E 481
SHEET 5 EA 9 LEU E 392 ILE E 398 -1 O ASP E 393 N VAL E 410
SHEET 6 EA 9 LYS E 360 GLU E 367 -1 O LYS E 360 N ILE E 398
SHEET 7 EA 9 ARG E 4 PRO E 15 -1 O ARG E 4 N GLU E 367
SHEET 8 EA 9 PRO E 421 VAL E 424 1 O PRO E 421 N ILE E 5
SHEET 9 EA 9 GLU E 466 GLU E 468 -1 O PHE E 467 N ILE E 422
SHEET 1 EB 8 HIS E 23 PHE E 24 0
SHEET 2 EB 8 ASN E 64 TRP E 67 1 O ASN E 64 N HIS E 23
SHEET 3 EB 8 GLU E 119 SER E 123 1 O GLU E 119 N LEU E 65
SHEET 4 EB 8 PHE E 166 ILE E 169 1 O PHE E 166 N ILE E 122
SHEET 5 EB 8 LYS E 206 ALA E 209 1 O LYS E 206 N TRP E 167
SHEET 6 EB 8 PHE E 231 THR E 238 1 O PHE E 231 N ALA E 209
SHEET 7 EB 8 LYS E 276 VAL E 284 1 O LYS E 276 N ILE E 232
SHEET 8 EB 8 LEU E 321 ALA E 322 1 O LEU E 321 N LEU E 279
SHEET 1 EC 2 ARG E 91 ASP E 93 0
SHEET 2 EC 2 GLN E 98 GLU E 100 -1 O GLN E 98 N ASP E 93
SHEET 1 ED 2 ILE E 334 GLU E 337 0
SHEET 2 ED 2 GLY E 340 LEU E 343 -1 O GLY E 340 N GLU E 337
SHEET 1 EE 2 THR E 370 VAL E 376 0
SHEET 2 EE 2 PRO E 383 PRO E 390 -1 O PHE E 384 N GLY E 375
SHEET 1 FA 9 ASP F 455 THR F 457 0
SHEET 2 FA 9 THR F 433 THR F 438 -1 O THR F 436 N THR F 457
SHEET 3 FA 9 SER F 475 VAL F 481 -1 O CYS F 476 N LEU F 437
SHEET 4 FA 9 LEU F 405 ASN F 411 -1 O LEU F 405 N VAL F 481
SHEET 5 FA 9 LEU F 392 ILE F 398 -1 O ASP F 393 N VAL F 410
SHEET 6 FA 9 LYS F 360 GLU F 367 -1 O LYS F 360 N ILE F 398
SHEET 7 FA 9 ARG F 4 PRO F 15 -1 O ARG F 4 N GLU F 367
SHEET 8 FA 9 LEU F 418 VAL F 424 1 O PRO F 421 N ILE F 5
SHEET 9 FA 9 GLU F 466 PHE F 471 -1 O PHE F 467 N ILE F 422
SHEET 1 FB 8 HIS F 23 PHE F 24 0
SHEET 2 FB 8 ASN F 64 TRP F 67 1 O ASN F 64 N HIS F 23
SHEET 3 FB 8 GLU F 119 SER F 123 1 O GLU F 119 N LEU F 65
SHEET 4 FB 8 PHE F 166 ILE F 169 1 O PHE F 166 N ILE F 122
SHEET 5 FB 8 LYS F 206 ALA F 209 1 O LYS F 206 N TRP F 167
SHEET 6 FB 8 PHE F 231 THR F 238 1 O PHE F 231 N ALA F 209
SHEET 7 FB 8 LYS F 276 VAL F 284 1 O LYS F 276 N ILE F 232
SHEET 8 FB 8 LEU F 321 ALA F 322 1 O LEU F 321 N LEU F 279
SHEET 1 FC 2 ARG F 91 ASP F 93 0
SHEET 2 FC 2 GLN F 98 GLU F 100 -1 O GLN F 98 N ASP F 93
SHEET 1 FD 2 ILE F 334 GLU F 337 0
SHEET 2 FD 2 GLY F 340 LEU F 343 -1 O GLY F 340 N GLU F 337
SHEET 1 FE 2 TYR F 371 VAL F 376 0
SHEET 2 FE 2 PRO F 383 ALA F 389 -1 O PHE F 384 N GLY F 375
SSBOND 1 CYS A 306 CYS A 476 1555 1555 2.06
SSBOND 2 CYS B 306 CYS B 476 1555 1555 2.06
SSBOND 3 CYS C 306 CYS C 476 1555 1555 2.07
SSBOND 4 CYS D 306 CYS D 476 1555 1555 2.06
SSBOND 5 CYS E 306 CYS E 476 1555 1555 2.04
SSBOND 6 CYS F 306 CYS F 476 1555 1555 2.05
CISPEP 1 TRP A 67 PRO A 68 0 0.36
CISPEP 2 TRP B 67 PRO B 68 0 0.25
CISPEP 3 ALA B 325 GLN B 326 0 -2.13
CISPEP 4 TRP C 67 PRO C 68 0 0.21
CISPEP 5 TRP D 67 PRO D 68 0 0.45
CISPEP 6 TRP E 67 PRO E 68 0 0.30
CISPEP 7 ALA E 325 GLN E 326 0 0.13
CISPEP 8 TRP F 67 PRO F 68 0 0.15
CISPEP 9 ALA F 325 GLN F 326 0 -0.06
CRYST1 103.710 161.538 112.602 90.00 106.30 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 0.009642 0.000000 0.002820 0.00000
SCALE2 0.000000 0.006190 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009253 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
