HEADER OXIDOREDUCTASE 13-NOV-06 2E2G
TITLE CRYSTAL STRUCTURE OF ARCHAEAL PEROXIREDOXIN, THIOREDOXIN PEROXIDASE
TITLE 2 FROM AEROPYRUM PERNIX K1 (PRE-OXIDATION FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE PEROXIREDOXIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 SYNONYM: THIOREDOXIN PEROXIDASE;
COMPND 5 EC: 1.11.1.15;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;
SOURCE 3 ORGANISM_TAXID: 272557;
SOURCE 4 STRAIN: K1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS THIOREDOXIN PEROXIDASE, CYSTEINE SULFENIC ACID, CYSTEINE SULFINIC
KEYWDS 2 ACID, CYSTEINE SULFONIC ACID, HYPERVALENT SULFUR COMPOUND,
KEYWDS 3 PEROXIDATIC CYSTEINE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.NAKAMURA,T.YAMAMOTO,M.ABE,H.MATSUMURA,Y.HAGIHARA,T.GOTO,
AUTHOR 2 T.YAMAGUCHI,T.INOUE
REVDAT 6 25-OCT-23 2E2G 1 REMARK
REVDAT 5 10-NOV-21 2E2G 1 SEQADV
REVDAT 4 13-JUL-11 2E2G 1 VERSN
REVDAT 3 24-FEB-09 2E2G 1 VERSN
REVDAT 2 27-MAY-08 2E2G 1 JRNL
REVDAT 1 20-NOV-07 2E2G 0
JRNL AUTH T.NAKAMURA,T.YAMAMOTO,M.ABE,H.MATSUMURA,Y.HAGIHARA,T.GOTO,
JRNL AUTH 2 T.YAMAGUCHI,T.INOUE
JRNL TITL OXIDATION OF ARCHAEAL PEROXIREDOXIN INVOLVES A HYPERVALENT
JRNL TITL 2 SULFUR INTERMEDIATE
JRNL REF PROC.NATL.ACAD.SCI.USA V. 105 6238 2008
JRNL REFN ISSN 0027-8424
JRNL PMID 18436649
JRNL DOI 10.1073/PNAS.0709822105
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.8
REMARK 3 NUMBER OF REFLECTIONS : 95723
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 + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5036
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.45
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5274
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 65.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.1820
REMARK 3 BIN FREE R VALUE SET COUNT : 292
REMARK 3 BIN FREE R VALUE : 0.2840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19336
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 542
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : -0.01000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.433
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.267
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.173
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.413
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19877 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 27023 ; 2.140 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2362 ; 7.007 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 941 ;35.995 ;22.019
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3302 ;20.887 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 220 ;22.261 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2932 ; 0.134 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15304 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 9630 ; 0.239 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 13461 ; 0.322 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 941 ; 0.179 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 79 ; 0.359 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.123 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 12271 ; 1.233 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 19386 ; 1.971 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8825 ; 3.262 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7637 ; 5.175 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2E2G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000026140.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115754
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.2
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1X0R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M ACETATE BUFFER PH4.8, 0.2M
REMARK 280 CALCIUM CHLORIDE, 10%(V/V)ISOPROPANOL, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 46050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 79320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -305.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 PRO A 2
REMARK 465 GLY A 3
REMARK 465 HIS A 117
REMARK 465 ALA A 118
REMARK 465 GLU A 119
REMARK 465 SER A 120
REMARK 465 ARG A 246
REMARK 465 THR A 247
REMARK 465 HIS A 248
REMARK 465 LEU A 249
REMARK 465 HIS A 250
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 GLY B 3
REMARK 465 ALA B 118
REMARK 465 GLU B 119
REMARK 465 SER B 120
REMARK 465 ARG B 246
REMARK 465 THR B 247
REMARK 465 HIS B 248
REMARK 465 LEU B 249
REMARK 465 HIS B 250
REMARK 465 MET C 1
REMARK 465 PRO C 2
REMARK 465 GLY C 3
REMARK 465 HIS C 117
REMARK 465 ALA C 118
REMARK 465 GLU C 119
REMARK 465 ARG C 246
REMARK 465 THR C 247
REMARK 465 HIS C 248
REMARK 465 LEU C 249
REMARK 465 HIS C 250
REMARK 465 MET D 1
REMARK 465 PRO D 2
REMARK 465 GLY D 3
REMARK 465 HIS D 117
REMARK 465 ALA D 118
REMARK 465 GLU D 119
REMARK 465 SER D 120
REMARK 465 ARG D 246
REMARK 465 THR D 247
REMARK 465 HIS D 248
REMARK 465 LEU D 249
REMARK 465 HIS D 250
REMARK 465 MET E 1
REMARK 465 PRO E 2
REMARK 465 GLY E 3
REMARK 465 HIS E 117
REMARK 465 ALA E 118
REMARK 465 GLU E 119
REMARK 465 SER E 120
REMARK 465 ARG E 246
REMARK 465 THR E 247
REMARK 465 HIS E 248
REMARK 465 LEU E 249
REMARK 465 HIS E 250
REMARK 465 MET F 1
REMARK 465 PRO F 2
REMARK 465 GLY F 3
REMARK 465 HIS F 117
REMARK 465 ALA F 118
REMARK 465 GLU F 119
REMARK 465 SER F 120
REMARK 465 ARG F 246
REMARK 465 THR F 247
REMARK 465 HIS F 248
REMARK 465 LEU F 249
REMARK 465 HIS F 250
REMARK 465 MET G 1
REMARK 465 PRO G 2
REMARK 465 GLY G 3
REMARK 465 HIS G 117
REMARK 465 ALA G 118
REMARK 465 GLU G 119
REMARK 465 SER G 120
REMARK 465 ARG G 246
REMARK 465 THR G 247
REMARK 465 HIS G 248
REMARK 465 LEU G 249
REMARK 465 HIS G 250
REMARK 465 MET H 1
REMARK 465 PRO H 2
REMARK 465 GLY H 3
REMARK 465 HIS H 117
REMARK 465 ALA H 118
REMARK 465 GLU H 119
REMARK 465 SER H 120
REMARK 465 ARG H 246
REMARK 465 THR H 247
REMARK 465 HIS H 248
REMARK 465 LEU H 249
REMARK 465 HIS H 250
REMARK 465 MET I 1
REMARK 465 PRO I 2
REMARK 465 GLY I 3
REMARK 465 HIS I 117
REMARK 465 ALA I 118
REMARK 465 GLU I 119
REMARK 465 SER I 120
REMARK 465 ARG I 246
REMARK 465 THR I 247
REMARK 465 HIS I 248
REMARK 465 LEU I 249
REMARK 465 HIS I 250
REMARK 465 MET J 1
REMARK 465 PRO J 2
REMARK 465 GLY J 3
REMARK 465 HIS J 117
REMARK 465 ALA J 118
REMARK 465 GLU J 119
REMARK 465 SER J 120
REMARK 465 ARG J 246
REMARK 465 THR J 247
REMARK 465 HIS J 248
REMARK 465 LEU J 249
REMARK 465 HIS J 250
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 O GLN H 106 NH2 ARG H 111 2.05
REMARK 500 NE ARG C 228 O HOH C 287 2.08
REMARK 500 NH1 ARG F 11 OE2 GLU F 14 2.12
REMARK 500 OD1 ASP H 194 NH2 ARG H 197 2.18
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 NH1 ARG F 228 CB ARG H 228 1544 2.19
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 B 90 CG GLU B 90 CD 0.104
REMARK 500 ARG B 149 CZ ARG B 149 NH1 0.095
REMARK 500 GLU B 179 CD GLU B 179 OE2 0.068
REMARK 500 GLU C 62 CG GLU C 62 CD 0.097
REMARK 500 GLU C 183 CD GLU C 183 OE2 0.083
REMARK 500 GLU C 235 CB GLU C 235 CG 0.136
REMARK 500 GLU C 235 CG GLU C 235 CD 0.099
REMARK 500 PHE D 37 CZ PHE D 37 CE2 0.115
REMARK 500 GLU D 224 CG GLU D 224 CD 0.113
REMARK 500 GLU E 183 CD GLU E 183 OE2 0.071
REMARK 500 GLU E 225 CB GLU E 225 CG 0.141
REMARK 500 GLU E 225 CG GLU E 225 CD 0.114
REMARK 500 ARG E 228 CG ARG E 228 CD 0.185
REMARK 500 GLU F 62 CG GLU F 62 CD 0.123
REMARK 500 GLU F 183 CD GLU F 183 OE2 0.112
REMARK 500 GLU F 225 CG GLU F 225 CD 0.118
REMARK 500 GLU G 243 CG GLU G 243 CD 0.100
REMARK 500 ARG H 197 CG ARG H 197 CD 0.155
REMARK 500 GLU H 225 CG GLU H 225 CD 0.129
REMARK 500 ARG H 228 CG ARG H 228 CD 0.179
REMARK 500 GLU J 62 CG GLU J 62 CD 0.099
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 LEU A 74 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 149 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 199 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 199 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 LEU B 74 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 GLY B 127 C - N - CA ANGL. DEV. = -15.7 DEGREES
REMARK 500 ARG B 134 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 134 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 149 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 149 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG B 206 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 209 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 LEU C 74 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 ARG C 111 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG C 126 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG C 206 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG C 231 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 231 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 LEU D 74 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 ARG D 149 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ASP D 174 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 LEU E 74 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG E 138 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG E 138 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG E 197 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG E 206 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG E 228 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG E 228 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 PRO F 43 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG F 126 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG F 149 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG H 126 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG H 126 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LEU H 147 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 LEU H 208 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG H 227 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 LEU I 7 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ASP I 77 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG I 126 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG I 156 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG I 199 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG I 206 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU J 74 CA - CB - CG ANGL. DEV. = 14.0 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 ASP A 20 10.29 -62.16
REMARK 500 ALA A 44 143.09 -172.97
REMARK 500 GLN A 106 -23.64 78.15
REMARK 500 THR A 122 -20.95 47.43
REMARK 500 LYS A 239 114.18 86.50
REMARK 500 GLN B 106 -23.18 79.79
REMARK 500 THR B 122 -20.41 60.30
REMARK 500 ASN B 177 50.49 -114.45
REMARK 500 ASP B 209 162.36 174.53
REMARK 500 LYS B 239 112.58 75.95
REMARK 500 ASP C 104 56.97 -113.69
REMARK 500 GLN C 106 -18.06 84.74
REMARK 500 ALA C 121 -121.39 -65.97
REMARK 500 THR C 122 -45.48 82.11
REMARK 500 LYS C 239 92.65 63.61
REMARK 500 ILE D 8 130.26 -34.42
REMARK 500 MET D 15 148.68 -171.86
REMARK 500 ASP D 20 4.54 -64.99
REMARK 500 GLN D 106 -6.21 68.22
REMARK 500 THR D 122 -35.87 88.17
REMARK 500 THR D 139 143.97 -174.60
REMARK 500 ASP D 209 156.84 175.12
REMARK 500 LYS D 239 98.44 86.52
REMARK 500 GLU D 243 -71.03 -63.21
REMARK 500 PRO E 6 164.78 -47.91
REMARK 500 PRO E 13 114.29 -39.19
REMARK 500 GLN E 106 -5.22 73.26
REMARK 500 THR E 122 -28.03 87.08
REMARK 500 LYS E 239 99.46 76.26
REMARK 500 GLU E 244 1.37 -66.20
REMARK 500 SER F 32 -3.09 -49.49
REMARK 500 ALA F 44 165.26 178.38
REMARK 500 GLN F 106 -20.33 78.23
REMARK 500 THR F 122 -36.53 98.41
REMARK 500 THR F 124 3.68 -69.57
REMARK 500 LYS F 239 89.84 77.38
REMARK 500 MET G 15 145.22 -178.63
REMARK 500 ASP G 20 1.52 -63.20
REMARK 500 ASP G 28 -56.85 -25.52
REMARK 500 GLN G 106 -26.57 88.34
REMARK 500 THR G 122 -30.22 88.09
REMARK 500 THR G 124 -9.30 -57.67
REMARK 500 THR G 139 143.65 -173.56
REMARK 500 LYS G 239 114.64 71.16
REMARK 500 GLU G 243 -74.94 -50.37
REMARK 500 GLN H 106 -34.83 91.18
REMARK 500 THR H 122 -30.53 98.69
REMARK 500 ASN H 177 44.41 -109.31
REMARK 500 THR H 216 77.94 -117.37
REMARK 500 LYS H 239 95.95 63.36
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NVL RELATED DB: PDB
REMARK 900 THE SAME PROTEIN(SULFONIC ACID FORM)
REMARK 900 RELATED ID: 2E2M RELATED DB: PDB
REMARK 900 THE SAME PROTEIN(SULFINIC ACID FORM)
DBREF 2E2G A 1 250 UNP Q9Y9L0 TDXH_AERPE 1 250
DBREF 2E2G B 1 250 UNP Q9Y9L0 TDXH_AERPE 1 250
DBREF 2E2G C 1 250 UNP Q9Y9L0 TDXH_AERPE 1 250
DBREF 2E2G D 1 250 UNP Q9Y9L0 TDXH_AERPE 1 250
DBREF 2E2G E 1 250 UNP Q9Y9L0 TDXH_AERPE 1 250
DBREF 2E2G F 1 250 UNP Q9Y9L0 TDXH_AERPE 1 250
DBREF 2E2G G 1 250 UNP Q9Y9L0 TDXH_AERPE 1 250
DBREF 2E2G H 1 250 UNP Q9Y9L0 TDXH_AERPE 1 250
DBREF 2E2G I 1 250 UNP Q9Y9L0 TDXH_AERPE 1 250
DBREF 2E2G J 1 250 UNP Q9Y9L0 TDXH_AERPE 1 250
SEQADV 2E2G SER A 207 UNP Q9Y9L0 CYS 207 ENGINEERED MUTATION
SEQADV 2E2G SER B 207 UNP Q9Y9L0 CYS 207 ENGINEERED MUTATION
SEQADV 2E2G SER C 207 UNP Q9Y9L0 CYS 207 ENGINEERED MUTATION
SEQADV 2E2G SER D 207 UNP Q9Y9L0 CYS 207 ENGINEERED MUTATION
SEQADV 2E2G SER E 207 UNP Q9Y9L0 CYS 207 ENGINEERED MUTATION
SEQADV 2E2G SER F 207 UNP Q9Y9L0 CYS 207 ENGINEERED MUTATION
SEQADV 2E2G SER G 207 UNP Q9Y9L0 CYS 207 ENGINEERED MUTATION
SEQADV 2E2G SER H 207 UNP Q9Y9L0 CYS 207 ENGINEERED MUTATION
SEQADV 2E2G SER I 207 UNP Q9Y9L0 CYS 207 ENGINEERED MUTATION
SEQADV 2E2G SER J 207 UNP Q9Y9L0 CYS 207 ENGINEERED MUTATION
SEQRES 1 A 250 MET PRO GLY SER ILE PRO LEU ILE GLY GLU ARG PHE PRO
SEQRES 2 A 250 GLU MET GLU VAL THR THR ASP HIS GLY VAL ILE LYS LEU
SEQRES 3 A 250 PRO ASP HIS TYR VAL SER GLN GLY LYS TRP PHE VAL LEU
SEQRES 4 A 250 PHE SER HIS PRO ALA ASP PHE THR PRO VAL CYS THR THR
SEQRES 5 A 250 GLU PHE VAL SER PHE ALA ARG ARG TYR GLU ASP PHE GLN
SEQRES 6 A 250 ARG LEU GLY VAL ASP LEU ILE GLY LEU SER VAL ASP SER
SEQRES 7 A 250 VAL PHE SER HIS ILE LYS TRP LYS GLU TRP ILE GLU ARG
SEQRES 8 A 250 HIS ILE GLY VAL ARG ILE PRO PHE PRO ILE ILE ALA ASP
SEQRES 9 A 250 PRO GLN GLY THR VAL ALA ARG ARG LEU GLY LEU LEU HIS
SEQRES 10 A 250 ALA GLU SER ALA THR HIS THR VAL ARG GLY VAL PHE ILE
SEQRES 11 A 250 VAL ASP ALA ARG GLY VAL ILE ARG THR MET LEU TYR TYR
SEQRES 12 A 250 PRO MET GLU LEU GLY ARG LEU VAL ASP GLU ILE LEU ARG
SEQRES 13 A 250 ILE VAL LYS ALA LEU LYS LEU GLY ASP SER LEU LYS ARG
SEQRES 14 A 250 ALA VAL PRO ALA ASP TRP PRO ASN ASN GLU ILE ILE GLY
SEQRES 15 A 250 GLU GLY LEU ILE VAL PRO PRO PRO THR THR GLU ASP GLN
SEQRES 16 A 250 ALA ARG ALA ARG MET GLU SER GLY GLN TYR ARG SER LEU
SEQRES 17 A 250 ASP TRP TRP PHE CYS TRP ASP THR PRO ALA SER ARG ASP
SEQRES 18 A 250 ASP VAL GLU GLU ALA ARG ARG TYR LEU ARG ARG ALA ALA
SEQRES 19 A 250 GLU LYS PRO ALA LYS LEU LEU TYR GLU GLU ALA ARG THR
SEQRES 20 A 250 HIS LEU HIS
SEQRES 1 B 250 MET PRO GLY SER ILE PRO LEU ILE GLY GLU ARG PHE PRO
SEQRES 2 B 250 GLU MET GLU VAL THR THR ASP HIS GLY VAL ILE LYS LEU
SEQRES 3 B 250 PRO ASP HIS TYR VAL SER GLN GLY LYS TRP PHE VAL LEU
SEQRES 4 B 250 PHE SER HIS PRO ALA ASP PHE THR PRO VAL CYS THR THR
SEQRES 5 B 250 GLU PHE VAL SER PHE ALA ARG ARG TYR GLU ASP PHE GLN
SEQRES 6 B 250 ARG LEU GLY VAL ASP LEU ILE GLY LEU SER VAL ASP SER
SEQRES 7 B 250 VAL PHE SER HIS ILE LYS TRP LYS GLU TRP ILE GLU ARG
SEQRES 8 B 250 HIS ILE GLY VAL ARG ILE PRO PHE PRO ILE ILE ALA ASP
SEQRES 9 B 250 PRO GLN GLY THR VAL ALA ARG ARG LEU GLY LEU LEU HIS
SEQRES 10 B 250 ALA GLU SER ALA THR HIS THR VAL ARG GLY VAL PHE ILE
SEQRES 11 B 250 VAL ASP ALA ARG GLY VAL ILE ARG THR MET LEU TYR TYR
SEQRES 12 B 250 PRO MET GLU LEU GLY ARG LEU VAL ASP GLU ILE LEU ARG
SEQRES 13 B 250 ILE VAL LYS ALA LEU LYS LEU GLY ASP SER LEU LYS ARG
SEQRES 14 B 250 ALA VAL PRO ALA ASP TRP PRO ASN ASN GLU ILE ILE GLY
SEQRES 15 B 250 GLU GLY LEU ILE VAL PRO PRO PRO THR THR GLU ASP GLN
SEQRES 16 B 250 ALA ARG ALA ARG MET GLU SER GLY GLN TYR ARG SER LEU
SEQRES 17 B 250 ASP TRP TRP PHE CYS TRP ASP THR PRO ALA SER ARG ASP
SEQRES 18 B 250 ASP VAL GLU GLU ALA ARG ARG TYR LEU ARG ARG ALA ALA
SEQRES 19 B 250 GLU LYS PRO ALA LYS LEU LEU TYR GLU GLU ALA ARG THR
SEQRES 20 B 250 HIS LEU HIS
SEQRES 1 C 250 MET PRO GLY SER ILE PRO LEU ILE GLY GLU ARG PHE PRO
SEQRES 2 C 250 GLU MET GLU VAL THR THR ASP HIS GLY VAL ILE LYS LEU
SEQRES 3 C 250 PRO ASP HIS TYR VAL SER GLN GLY LYS TRP PHE VAL LEU
SEQRES 4 C 250 PHE SER HIS PRO ALA ASP PHE THR PRO VAL CYS THR THR
SEQRES 5 C 250 GLU PHE VAL SER PHE ALA ARG ARG TYR GLU ASP PHE GLN
SEQRES 6 C 250 ARG LEU GLY VAL ASP LEU ILE GLY LEU SER VAL ASP SER
SEQRES 7 C 250 VAL PHE SER HIS ILE LYS TRP LYS GLU TRP ILE GLU ARG
SEQRES 8 C 250 HIS ILE GLY VAL ARG ILE PRO PHE PRO ILE ILE ALA ASP
SEQRES 9 C 250 PRO GLN GLY THR VAL ALA ARG ARG LEU GLY LEU LEU HIS
SEQRES 10 C 250 ALA GLU SER ALA THR HIS THR VAL ARG GLY VAL PHE ILE
SEQRES 11 C 250 VAL ASP ALA ARG GLY VAL ILE ARG THR MET LEU TYR TYR
SEQRES 12 C 250 PRO MET GLU LEU GLY ARG LEU VAL ASP GLU ILE LEU ARG
SEQRES 13 C 250 ILE VAL LYS ALA LEU LYS LEU GLY ASP SER LEU LYS ARG
SEQRES 14 C 250 ALA VAL PRO ALA ASP TRP PRO ASN ASN GLU ILE ILE GLY
SEQRES 15 C 250 GLU GLY LEU ILE VAL PRO PRO PRO THR THR GLU ASP GLN
SEQRES 16 C 250 ALA ARG ALA ARG MET GLU SER GLY GLN TYR ARG SER LEU
SEQRES 17 C 250 ASP TRP TRP PHE CYS TRP ASP THR PRO ALA SER ARG ASP
SEQRES 18 C 250 ASP VAL GLU GLU ALA ARG ARG TYR LEU ARG ARG ALA ALA
SEQRES 19 C 250 GLU LYS PRO ALA LYS LEU LEU TYR GLU GLU ALA ARG THR
SEQRES 20 C 250 HIS LEU HIS
SEQRES 1 D 250 MET PRO GLY SER ILE PRO LEU ILE GLY GLU ARG PHE PRO
SEQRES 2 D 250 GLU MET GLU VAL THR THR ASP HIS GLY VAL ILE LYS LEU
SEQRES 3 D 250 PRO ASP HIS TYR VAL SER GLN GLY LYS TRP PHE VAL LEU
SEQRES 4 D 250 PHE SER HIS PRO ALA ASP PHE THR PRO VAL CYS THR THR
SEQRES 5 D 250 GLU PHE VAL SER PHE ALA ARG ARG TYR GLU ASP PHE GLN
SEQRES 6 D 250 ARG LEU GLY VAL ASP LEU ILE GLY LEU SER VAL ASP SER
SEQRES 7 D 250 VAL PHE SER HIS ILE LYS TRP LYS GLU TRP ILE GLU ARG
SEQRES 8 D 250 HIS ILE GLY VAL ARG ILE PRO PHE PRO ILE ILE ALA ASP
SEQRES 9 D 250 PRO GLN GLY THR VAL ALA ARG ARG LEU GLY LEU LEU HIS
SEQRES 10 D 250 ALA GLU SER ALA THR HIS THR VAL ARG GLY VAL PHE ILE
SEQRES 11 D 250 VAL ASP ALA ARG GLY VAL ILE ARG THR MET LEU TYR TYR
SEQRES 12 D 250 PRO MET GLU LEU GLY ARG LEU VAL ASP GLU ILE LEU ARG
SEQRES 13 D 250 ILE VAL LYS ALA LEU LYS LEU GLY ASP SER LEU LYS ARG
SEQRES 14 D 250 ALA VAL PRO ALA ASP TRP PRO ASN ASN GLU ILE ILE GLY
SEQRES 15 D 250 GLU GLY LEU ILE VAL PRO PRO PRO THR THR GLU ASP GLN
SEQRES 16 D 250 ALA ARG ALA ARG MET GLU SER GLY GLN TYR ARG SER LEU
SEQRES 17 D 250 ASP TRP TRP PHE CYS TRP ASP THR PRO ALA SER ARG ASP
SEQRES 18 D 250 ASP VAL GLU GLU ALA ARG ARG TYR LEU ARG ARG ALA ALA
SEQRES 19 D 250 GLU LYS PRO ALA LYS LEU LEU TYR GLU GLU ALA ARG THR
SEQRES 20 D 250 HIS LEU HIS
SEQRES 1 E 250 MET PRO GLY SER ILE PRO LEU ILE GLY GLU ARG PHE PRO
SEQRES 2 E 250 GLU MET GLU VAL THR THR ASP HIS GLY VAL ILE LYS LEU
SEQRES 3 E 250 PRO ASP HIS TYR VAL SER GLN GLY LYS TRP PHE VAL LEU
SEQRES 4 E 250 PHE SER HIS PRO ALA ASP PHE THR PRO VAL CYS THR THR
SEQRES 5 E 250 GLU PHE VAL SER PHE ALA ARG ARG TYR GLU ASP PHE GLN
SEQRES 6 E 250 ARG LEU GLY VAL ASP LEU ILE GLY LEU SER VAL ASP SER
SEQRES 7 E 250 VAL PHE SER HIS ILE LYS TRP LYS GLU TRP ILE GLU ARG
SEQRES 8 E 250 HIS ILE GLY VAL ARG ILE PRO PHE PRO ILE ILE ALA ASP
SEQRES 9 E 250 PRO GLN GLY THR VAL ALA ARG ARG LEU GLY LEU LEU HIS
SEQRES 10 E 250 ALA GLU SER ALA THR HIS THR VAL ARG GLY VAL PHE ILE
SEQRES 11 E 250 VAL ASP ALA ARG GLY VAL ILE ARG THR MET LEU TYR TYR
SEQRES 12 E 250 PRO MET GLU LEU GLY ARG LEU VAL ASP GLU ILE LEU ARG
SEQRES 13 E 250 ILE VAL LYS ALA LEU LYS LEU GLY ASP SER LEU LYS ARG
SEQRES 14 E 250 ALA VAL PRO ALA ASP TRP PRO ASN ASN GLU ILE ILE GLY
SEQRES 15 E 250 GLU GLY LEU ILE VAL PRO PRO PRO THR THR GLU ASP GLN
SEQRES 16 E 250 ALA ARG ALA ARG MET GLU SER GLY GLN TYR ARG SER LEU
SEQRES 17 E 250 ASP TRP TRP PHE CYS TRP ASP THR PRO ALA SER ARG ASP
SEQRES 18 E 250 ASP VAL GLU GLU ALA ARG ARG TYR LEU ARG ARG ALA ALA
SEQRES 19 E 250 GLU LYS PRO ALA LYS LEU LEU TYR GLU GLU ALA ARG THR
SEQRES 20 E 250 HIS LEU HIS
SEQRES 1 F 250 MET PRO GLY SER ILE PRO LEU ILE GLY GLU ARG PHE PRO
SEQRES 2 F 250 GLU MET GLU VAL THR THR ASP HIS GLY VAL ILE LYS LEU
SEQRES 3 F 250 PRO ASP HIS TYR VAL SER GLN GLY LYS TRP PHE VAL LEU
SEQRES 4 F 250 PHE SER HIS PRO ALA ASP PHE THR PRO VAL CYS THR THR
SEQRES 5 F 250 GLU PHE VAL SER PHE ALA ARG ARG TYR GLU ASP PHE GLN
SEQRES 6 F 250 ARG LEU GLY VAL ASP LEU ILE GLY LEU SER VAL ASP SER
SEQRES 7 F 250 VAL PHE SER HIS ILE LYS TRP LYS GLU TRP ILE GLU ARG
SEQRES 8 F 250 HIS ILE GLY VAL ARG ILE PRO PHE PRO ILE ILE ALA ASP
SEQRES 9 F 250 PRO GLN GLY THR VAL ALA ARG ARG LEU GLY LEU LEU HIS
SEQRES 10 F 250 ALA GLU SER ALA THR HIS THR VAL ARG GLY VAL PHE ILE
SEQRES 11 F 250 VAL ASP ALA ARG GLY VAL ILE ARG THR MET LEU TYR TYR
SEQRES 12 F 250 PRO MET GLU LEU GLY ARG LEU VAL ASP GLU ILE LEU ARG
SEQRES 13 F 250 ILE VAL LYS ALA LEU LYS LEU GLY ASP SER LEU LYS ARG
SEQRES 14 F 250 ALA VAL PRO ALA ASP TRP PRO ASN ASN GLU ILE ILE GLY
SEQRES 15 F 250 GLU GLY LEU ILE VAL PRO PRO PRO THR THR GLU ASP GLN
SEQRES 16 F 250 ALA ARG ALA ARG MET GLU SER GLY GLN TYR ARG SER LEU
SEQRES 17 F 250 ASP TRP TRP PHE CYS TRP ASP THR PRO ALA SER ARG ASP
SEQRES 18 F 250 ASP VAL GLU GLU ALA ARG ARG TYR LEU ARG ARG ALA ALA
SEQRES 19 F 250 GLU LYS PRO ALA LYS LEU LEU TYR GLU GLU ALA ARG THR
SEQRES 20 F 250 HIS LEU HIS
SEQRES 1 G 250 MET PRO GLY SER ILE PRO LEU ILE GLY GLU ARG PHE PRO
SEQRES 2 G 250 GLU MET GLU VAL THR THR ASP HIS GLY VAL ILE LYS LEU
SEQRES 3 G 250 PRO ASP HIS TYR VAL SER GLN GLY LYS TRP PHE VAL LEU
SEQRES 4 G 250 PHE SER HIS PRO ALA ASP PHE THR PRO VAL CYS THR THR
SEQRES 5 G 250 GLU PHE VAL SER PHE ALA ARG ARG TYR GLU ASP PHE GLN
SEQRES 6 G 250 ARG LEU GLY VAL ASP LEU ILE GLY LEU SER VAL ASP SER
SEQRES 7 G 250 VAL PHE SER HIS ILE LYS TRP LYS GLU TRP ILE GLU ARG
SEQRES 8 G 250 HIS ILE GLY VAL ARG ILE PRO PHE PRO ILE ILE ALA ASP
SEQRES 9 G 250 PRO GLN GLY THR VAL ALA ARG ARG LEU GLY LEU LEU HIS
SEQRES 10 G 250 ALA GLU SER ALA THR HIS THR VAL ARG GLY VAL PHE ILE
SEQRES 11 G 250 VAL ASP ALA ARG GLY VAL ILE ARG THR MET LEU TYR TYR
SEQRES 12 G 250 PRO MET GLU LEU GLY ARG LEU VAL ASP GLU ILE LEU ARG
SEQRES 13 G 250 ILE VAL LYS ALA LEU LYS LEU GLY ASP SER LEU LYS ARG
SEQRES 14 G 250 ALA VAL PRO ALA ASP TRP PRO ASN ASN GLU ILE ILE GLY
SEQRES 15 G 250 GLU GLY LEU ILE VAL PRO PRO PRO THR THR GLU ASP GLN
SEQRES 16 G 250 ALA ARG ALA ARG MET GLU SER GLY GLN TYR ARG SER LEU
SEQRES 17 G 250 ASP TRP TRP PHE CYS TRP ASP THR PRO ALA SER ARG ASP
SEQRES 18 G 250 ASP VAL GLU GLU ALA ARG ARG TYR LEU ARG ARG ALA ALA
SEQRES 19 G 250 GLU LYS PRO ALA LYS LEU LEU TYR GLU GLU ALA ARG THR
SEQRES 20 G 250 HIS LEU HIS
SEQRES 1 H 250 MET PRO GLY SER ILE PRO LEU ILE GLY GLU ARG PHE PRO
SEQRES 2 H 250 GLU MET GLU VAL THR THR ASP HIS GLY VAL ILE LYS LEU
SEQRES 3 H 250 PRO ASP HIS TYR VAL SER GLN GLY LYS TRP PHE VAL LEU
SEQRES 4 H 250 PHE SER HIS PRO ALA ASP PHE THR PRO VAL CYS THR THR
SEQRES 5 H 250 GLU PHE VAL SER PHE ALA ARG ARG TYR GLU ASP PHE GLN
SEQRES 6 H 250 ARG LEU GLY VAL ASP LEU ILE GLY LEU SER VAL ASP SER
SEQRES 7 H 250 VAL PHE SER HIS ILE LYS TRP LYS GLU TRP ILE GLU ARG
SEQRES 8 H 250 HIS ILE GLY VAL ARG ILE PRO PHE PRO ILE ILE ALA ASP
SEQRES 9 H 250 PRO GLN GLY THR VAL ALA ARG ARG LEU GLY LEU LEU HIS
SEQRES 10 H 250 ALA GLU SER ALA THR HIS THR VAL ARG GLY VAL PHE ILE
SEQRES 11 H 250 VAL ASP ALA ARG GLY VAL ILE ARG THR MET LEU TYR TYR
SEQRES 12 H 250 PRO MET GLU LEU GLY ARG LEU VAL ASP GLU ILE LEU ARG
SEQRES 13 H 250 ILE VAL LYS ALA LEU LYS LEU GLY ASP SER LEU LYS ARG
SEQRES 14 H 250 ALA VAL PRO ALA ASP TRP PRO ASN ASN GLU ILE ILE GLY
SEQRES 15 H 250 GLU GLY LEU ILE VAL PRO PRO PRO THR THR GLU ASP GLN
SEQRES 16 H 250 ALA ARG ALA ARG MET GLU SER GLY GLN TYR ARG SER LEU
SEQRES 17 H 250 ASP TRP TRP PHE CYS TRP ASP THR PRO ALA SER ARG ASP
SEQRES 18 H 250 ASP VAL GLU GLU ALA ARG ARG TYR LEU ARG ARG ALA ALA
SEQRES 19 H 250 GLU LYS PRO ALA LYS LEU LEU TYR GLU GLU ALA ARG THR
SEQRES 20 H 250 HIS LEU HIS
SEQRES 1 I 250 MET PRO GLY SER ILE PRO LEU ILE GLY GLU ARG PHE PRO
SEQRES 2 I 250 GLU MET GLU VAL THR THR ASP HIS GLY VAL ILE LYS LEU
SEQRES 3 I 250 PRO ASP HIS TYR VAL SER GLN GLY LYS TRP PHE VAL LEU
SEQRES 4 I 250 PHE SER HIS PRO ALA ASP PHE THR PRO VAL CYS THR THR
SEQRES 5 I 250 GLU PHE VAL SER PHE ALA ARG ARG TYR GLU ASP PHE GLN
SEQRES 6 I 250 ARG LEU GLY VAL ASP LEU ILE GLY LEU SER VAL ASP SER
SEQRES 7 I 250 VAL PHE SER HIS ILE LYS TRP LYS GLU TRP ILE GLU ARG
SEQRES 8 I 250 HIS ILE GLY VAL ARG ILE PRO PHE PRO ILE ILE ALA ASP
SEQRES 9 I 250 PRO GLN GLY THR VAL ALA ARG ARG LEU GLY LEU LEU HIS
SEQRES 10 I 250 ALA GLU SER ALA THR HIS THR VAL ARG GLY VAL PHE ILE
SEQRES 11 I 250 VAL ASP ALA ARG GLY VAL ILE ARG THR MET LEU TYR TYR
SEQRES 12 I 250 PRO MET GLU LEU GLY ARG LEU VAL ASP GLU ILE LEU ARG
SEQRES 13 I 250 ILE VAL LYS ALA LEU LYS LEU GLY ASP SER LEU LYS ARG
SEQRES 14 I 250 ALA VAL PRO ALA ASP TRP PRO ASN ASN GLU ILE ILE GLY
SEQRES 15 I 250 GLU GLY LEU ILE VAL PRO PRO PRO THR THR GLU ASP GLN
SEQRES 16 I 250 ALA ARG ALA ARG MET GLU SER GLY GLN TYR ARG SER LEU
SEQRES 17 I 250 ASP TRP TRP PHE CYS TRP ASP THR PRO ALA SER ARG ASP
SEQRES 18 I 250 ASP VAL GLU GLU ALA ARG ARG TYR LEU ARG ARG ALA ALA
SEQRES 19 I 250 GLU LYS PRO ALA LYS LEU LEU TYR GLU GLU ALA ARG THR
SEQRES 20 I 250 HIS LEU HIS
SEQRES 1 J 250 MET PRO GLY SER ILE PRO LEU ILE GLY GLU ARG PHE PRO
SEQRES 2 J 250 GLU MET GLU VAL THR THR ASP HIS GLY VAL ILE LYS LEU
SEQRES 3 J 250 PRO ASP HIS TYR VAL SER GLN GLY LYS TRP PHE VAL LEU
SEQRES 4 J 250 PHE SER HIS PRO ALA ASP PHE THR PRO VAL CYS THR THR
SEQRES 5 J 250 GLU PHE VAL SER PHE ALA ARG ARG TYR GLU ASP PHE GLN
SEQRES 6 J 250 ARG LEU GLY VAL ASP LEU ILE GLY LEU SER VAL ASP SER
SEQRES 7 J 250 VAL PHE SER HIS ILE LYS TRP LYS GLU TRP ILE GLU ARG
SEQRES 8 J 250 HIS ILE GLY VAL ARG ILE PRO PHE PRO ILE ILE ALA ASP
SEQRES 9 J 250 PRO GLN GLY THR VAL ALA ARG ARG LEU GLY LEU LEU HIS
SEQRES 10 J 250 ALA GLU SER ALA THR HIS THR VAL ARG GLY VAL PHE ILE
SEQRES 11 J 250 VAL ASP ALA ARG GLY VAL ILE ARG THR MET LEU TYR TYR
SEQRES 12 J 250 PRO MET GLU LEU GLY ARG LEU VAL ASP GLU ILE LEU ARG
SEQRES 13 J 250 ILE VAL LYS ALA LEU LYS LEU GLY ASP SER LEU LYS ARG
SEQRES 14 J 250 ALA VAL PRO ALA ASP TRP PRO ASN ASN GLU ILE ILE GLY
SEQRES 15 J 250 GLU GLY LEU ILE VAL PRO PRO PRO THR THR GLU ASP GLN
SEQRES 16 J 250 ALA ARG ALA ARG MET GLU SER GLY GLN TYR ARG SER LEU
SEQRES 17 J 250 ASP TRP TRP PHE CYS TRP ASP THR PRO ALA SER ARG ASP
SEQRES 18 J 250 ASP VAL GLU GLU ALA ARG ARG TYR LEU ARG ARG ALA ALA
SEQRES 19 J 250 GLU LYS PRO ALA LYS LEU LEU TYR GLU GLU ALA ARG THR
SEQRES 20 J 250 HIS LEU HIS
FORMUL 11 HOH *542(H2 O)
HELIX 1 1 PRO A 27 SER A 32 1 6
HELIX 2 2 THR A 47 ARG A 60 1 14
HELIX 3 3 ARG A 60 LEU A 67 1 8
HELIX 4 4 SER A 78 ILE A 93 1 16
HELIX 5 5 GLY A 107 LEU A 113 1 7
HELIX 6 6 LEU A 150 LYS A 168 1 19
HELIX 7 7 THR A 192 GLY A 203 1 12
HELIX 8 8 SER A 219 GLU A 235 1 17
HELIX 9 9 PRO B 27 SER B 32 1 6
HELIX 10 10 THR B 47 ARG B 60 1 14
HELIX 11 11 ARG B 60 LEU B 67 1 8
HELIX 12 12 SER B 78 ILE B 93 1 16
HELIX 13 13 GLY B 107 LEU B 113 1 7
HELIX 14 14 LEU B 150 LYS B 168 1 19
HELIX 15 15 THR B 192 GLY B 203 1 12
HELIX 16 16 SER B 219 GLU B 235 1 17
HELIX 17 17 LEU B 240 ALA B 245 1 6
HELIX 18 18 PRO C 27 SER C 32 1 6
HELIX 19 19 THR C 47 ARG C 60 1 14
HELIX 20 20 ARG C 60 LEU C 67 1 8
HELIX 21 21 SER C 78 GLY C 94 1 17
HELIX 22 22 GLY C 107 LEU C 113 1 7
HELIX 23 23 LEU C 150 LYS C 168 1 19
HELIX 24 24 THR C 192 GLY C 203 1 12
HELIX 25 25 SER C 219 GLU C 235 1 17
HELIX 26 26 LEU C 240 ALA C 245 1 6
HELIX 27 27 PRO D 27 SER D 32 1 6
HELIX 28 28 THR D 47 ARG D 60 1 14
HELIX 29 29 ARG D 60 LEU D 67 1 8
HELIX 30 30 SER D 78 ILE D 93 1 16
HELIX 31 31 GLY D 107 LEU D 113 1 7
HELIX 32 32 LEU D 150 LYS D 168 1 19
HELIX 33 33 THR D 192 SER D 202 1 11
HELIX 34 34 SER D 219 GLU D 235 1 17
HELIX 35 35 PRO E 27 SER E 32 1 6
HELIX 36 36 THR E 47 ARG E 60 1 14
HELIX 37 37 ARG E 60 ARG E 66 1 7
HELIX 38 38 SER E 78 ILE E 93 1 16
HELIX 39 39 GLY E 107 LEU E 113 1 7
HELIX 40 40 LEU E 150 LEU E 167 1 18
HELIX 41 41 THR E 192 GLY E 203 1 12
HELIX 42 42 SER E 219 GLU E 235 1 17
HELIX 43 43 LEU E 240 ALA E 245 1 6
HELIX 44 44 PRO F 27 SER F 32 1 6
HELIX 45 45 THR F 47 ARG F 60 1 14
HELIX 46 46 ARG F 60 LEU F 67 1 8
HELIX 47 47 SER F 78 GLY F 94 1 17
HELIX 48 48 GLY F 107 LEU F 113 1 7
HELIX 49 49 LEU F 150 LYS F 168 1 19
HELIX 50 50 THR F 192 GLY F 203 1 12
HELIX 51 51 SER F 219 GLU F 235 1 17
HELIX 52 52 LEU F 240 ALA F 245 1 6
HELIX 53 53 PRO G 27 SER G 32 1 6
HELIX 54 54 THR G 47 ARG G 60 1 14
HELIX 55 55 ARG G 60 LEU G 67 1 8
HELIX 56 56 SER G 78 ILE G 93 1 16
HELIX 57 57 GLY G 107 LEU G 113 1 7
HELIX 58 58 LEU G 150 LYS G 168 1 19
HELIX 59 59 THR G 192 GLY G 203 1 12
HELIX 60 60 SER G 219 GLU G 235 1 17
HELIX 61 61 LEU G 240 ALA G 245 1 6
HELIX 62 62 PRO H 27 SER H 32 1 6
HELIX 63 63 THR H 47 ARG H 59 1 13
HELIX 64 64 ARG H 60 LEU H 67 1 8
HELIX 65 65 SER H 78 ILE H 93 1 16
HELIX 66 66 GLY H 107 LEU H 113 1 7
HELIX 67 67 LEU H 150 LYS H 168 1 19
HELIX 68 68 THR H 192 GLY H 203 1 12
HELIX 69 69 SER H 219 GLU H 235 1 17
HELIX 70 70 LEU H 240 ALA H 245 1 6
HELIX 71 71 PRO I 27 SER I 32 1 6
HELIX 72 72 THR I 47 ARG I 60 1 14
HELIX 73 73 ARG I 60 LEU I 67 1 8
HELIX 74 74 SER I 78 GLY I 94 1 17
HELIX 75 75 GLY I 107 GLY I 114 1 8
HELIX 76 76 LEU I 150 LEU I 167 1 18
HELIX 77 77 THR I 192 SER I 202 1 11
HELIX 78 78 SER I 219 GLU I 235 1 17
HELIX 79 79 PRO J 27 SER J 32 1 6
HELIX 80 80 THR J 47 ARG J 60 1 14
HELIX 81 81 ARG J 60 LEU J 67 1 8
HELIX 82 82 SER J 78 GLY J 94 1 17
HELIX 83 83 GLY J 107 LEU J 113 1 7
HELIX 84 84 LEU J 150 LYS J 168 1 19
HELIX 85 85 THR J 192 SER J 202 1 11
HELIX 86 86 SER J 219 GLU J 235 1 17
HELIX 87 87 LEU J 240 ALA J 245 1 6
SHEET 1 A 2 MET A 15 THR A 19 0
SHEET 2 A 2 GLY A 22 LEU A 26 -1 O LEU A 26 N MET A 15
SHEET 1 B10 ILE A 101 ALA A 103 0
SHEET 2 B10 VAL A 69 SER A 75 1 N GLY A 73 O ILE A 102
SHEET 3 B10 TRP A 36 HIS A 42 1 N VAL A 38 O ASP A 70
SHEET 4 B10 VAL A 128 VAL A 131 -1 O VAL A 131 N PHE A 37
SHEET 5 B10 ILE A 137 TYR A 142 -1 O ARG A 138 N ILE A 130
SHEET 6 B10 ILE F 137 TYR F 142 -1 O MET F 140 N TYR A 142
SHEET 7 B10 VAL F 128 VAL F 131 -1 N ILE F 130 O ARG F 138
SHEET 8 B10 TRP F 36 HIS F 42 -1 N LEU F 39 O PHE F 129
SHEET 9 B10 VAL F 69 SER F 75 1 O ASP F 70 N TRP F 36
SHEET 10 B10 ILE F 101 ALA F 103 1 O ILE F 102 N GLY F 73
SHEET 1 C 3 LEU A 185 ILE A 186 0
SHEET 2 C 3 PHE A 212 ASP A 215 -1 O ASP A 215 N LEU A 185
SHEET 3 C 3 ARG A 206 ASP A 209 -1 N ASP A 209 O PHE A 212
SHEET 1 D 2 MET B 15 THR B 19 0
SHEET 2 D 2 GLY B 22 LEU B 26 -1 O ILE B 24 N VAL B 17
SHEET 1 E10 ILE B 101 ALA B 103 0
SHEET 2 E10 VAL B 69 SER B 75 1 N GLY B 73 O ILE B 102
SHEET 3 E10 TRP B 36 HIS B 42 1 N TRP B 36 O ASP B 70
SHEET 4 E10 VAL B 128 VAL B 131 -1 O VAL B 131 N PHE B 37
SHEET 5 E10 ILE B 137 TYR B 142 -1 O ARG B 138 N ILE B 130
SHEET 6 E10 ILE E 137 TYR E 142 -1 O TYR E 142 N MET B 140
SHEET 7 E10 GLY E 127 VAL E 131 -1 N ILE E 130 O ARG E 138
SHEET 8 E10 TRP E 36 HIS E 42 -1 N PHE E 37 O VAL E 131
SHEET 9 E10 VAL E 69 SER E 75 1 O ASP E 70 N TRP E 36
SHEET 10 E10 ILE E 101 ALA E 103 1 O ILE E 102 N GLY E 73
SHEET 1 F 3 LEU B 185 VAL B 187 0
SHEET 2 F 3 PHE B 212 ASP B 215 -1 O CYS B 213 N VAL B 187
SHEET 3 F 3 ARG B 206 ASP B 209 -1 N LEU B 208 O PHE B 212
SHEET 1 G 2 MET C 15 THR C 19 0
SHEET 2 G 2 GLY C 22 LEU C 26 -1 O LEU C 26 N MET C 15
SHEET 1 H10 ILE C 101 ALA C 103 0
SHEET 2 H10 VAL C 69 SER C 75 1 N GLY C 73 O ILE C 102
SHEET 3 H10 TRP C 36 HIS C 42 1 N TRP C 36 O ASP C 70
SHEET 4 H10 VAL C 128 VAL C 131 -1 O VAL C 131 N PHE C 37
SHEET 5 H10 ILE C 137 TYR C 142 -1 O ARG C 138 N ILE C 130
SHEET 6 H10 ILE D 137 TYR D 142 -1 O MET D 140 N TYR C 142
SHEET 7 H10 VAL D 128 VAL D 131 -1 N ILE D 130 O ARG D 138
SHEET 8 H10 TRP D 36 HIS D 42 -1 N LEU D 39 O PHE D 129
SHEET 9 H10 VAL D 69 SER D 75 1 O ASP D 70 N VAL D 38
SHEET 10 H10 ILE D 101 ALA D 103 1 O ILE D 102 N GLY D 73
SHEET 1 I 3 LEU C 185 ILE C 186 0
SHEET 2 I 3 PHE C 212 ASP C 215 -1 O ASP C 215 N LEU C 185
SHEET 3 I 3 ARG C 206 ASP C 209 -1 N LEU C 208 O PHE C 212
SHEET 1 J 2 MET D 15 THR D 19 0
SHEET 2 J 2 GLY D 22 LEU D 26 -1 O LEU D 26 N MET D 15
SHEET 1 K 3 LEU D 185 ILE D 186 0
SHEET 2 K 3 PHE D 212 ASP D 215 -1 O ASP D 215 N LEU D 185
SHEET 3 K 3 ARG D 206 ASP D 209 -1 N LEU D 208 O PHE D 212
SHEET 1 L 2 MET E 15 THR E 19 0
SHEET 2 L 2 GLY E 22 LEU E 26 -1 O LEU E 26 N MET E 15
SHEET 1 M 3 LEU E 185 VAL E 187 0
SHEET 2 M 3 PHE E 212 ASP E 215 -1 O CYS E 213 N VAL E 187
SHEET 3 M 3 ARG E 206 ASP E 209 -1 N LEU E 208 O PHE E 212
SHEET 1 N 2 MET F 15 THR F 19 0
SHEET 2 N 2 GLY F 22 LEU F 26 -1 O LEU F 26 N MET F 15
SHEET 1 O 3 LEU F 185 VAL F 187 0
SHEET 2 O 3 PHE F 212 ASP F 215 -1 O ASP F 215 N LEU F 185
SHEET 3 O 3 ARG F 206 ASP F 209 -1 N LEU F 208 O PHE F 212
SHEET 1 P 2 MET G 15 THR G 19 0
SHEET 2 P 2 GLY G 22 LEU G 26 -1 O LEU G 26 N MET G 15
SHEET 1 Q12 ILE G 101 ALA G 103 0
SHEET 2 Q12 VAL G 69 SER G 75 1 N GLY G 73 O ILE G 102
SHEET 3 Q12 TRP G 36 HIS G 42 1 N TRP G 36 O ASP G 70
SHEET 4 Q12 GLY G 127 VAL G 131 -1 O VAL G 131 N PHE G 37
SHEET 5 Q12 ILE G 137 TYR G 142 -1 O ARG G 138 N ILE G 130
SHEET 6 Q12 ILE H 137 TYR H 142 -1 O TYR H 142 N MET G 140
SHEET 7 Q12 VAL H 128 VAL H 131 -1 N ILE H 130 O ARG H 138
SHEET 8 Q12 TRP H 36 HIS H 42 -1 N PHE H 37 O VAL H 131
SHEET 9 Q12 VAL H 69 SER H 75 1 O ASP H 70 N TRP H 36
SHEET 10 Q12 ILE H 101 ALA H 103 1 O ILE H 102 N GLY H 73
SHEET 11 Q12 MET H 15 THR H 19 -1 N THR H 18 O ALA H 103
SHEET 12 Q12 GLY H 22 LEU H 26 -1 O LEU H 26 N MET H 15
SHEET 1 R 3 LEU G 185 ILE G 186 0
SHEET 2 R 3 PHE G 212 ASP G 215 -1 O ASP G 215 N LEU G 185
SHEET 3 R 3 ARG G 206 ASP G 209 -1 N LEU G 208 O PHE G 212
SHEET 1 S 3 LEU H 185 VAL H 187 0
SHEET 2 S 3 PHE H 212 ASP H 215 -1 O ASP H 215 N LEU H 185
SHEET 3 S 3 ARG H 206 ASP H 209 -1 N ARG H 206 O TRP H 214
SHEET 1 T 2 MET I 15 THR I 19 0
SHEET 2 T 2 GLY I 22 LEU I 26 -1 O LEU I 26 N MET I 15
SHEET 1 U10 ILE I 101 ALA I 103 0
SHEET 2 U10 VAL I 69 SER I 75 1 N GLY I 73 O ILE I 102
SHEET 3 U10 TRP I 36 HIS I 42 1 N TRP I 36 O ASP I 70
SHEET 4 U10 VAL I 128 VAL I 131 -1 O PHE I 129 N LEU I 39
SHEET 5 U10 ILE I 137 TYR I 142 -1 O ARG I 138 N ILE I 130
SHEET 6 U10 ILE J 137 TYR J 142 -1 O TYR J 142 N MET I 140
SHEET 7 U10 VAL J 128 VAL J 131 -1 N ILE J 130 O ARG J 138
SHEET 8 U10 TRP J 36 HIS J 42 -1 N LEU J 39 O PHE J 129
SHEET 9 U10 VAL J 69 SER J 75 1 O ASP J 70 N TRP J 36
SHEET 10 U10 ILE J 101 ALA J 103 1 O ILE J 102 N GLY J 73
SHEET 1 V 3 LEU I 185 ILE I 186 0
SHEET 2 V 3 PHE I 212 ASP I 215 -1 O ASP I 215 N LEU I 185
SHEET 3 V 3 ARG I 206 ASP I 209 -1 N LEU I 208 O PHE I 212
SHEET 1 W 2 MET J 15 THR J 19 0
SHEET 2 W 2 GLY J 22 LEU J 26 -1 O LEU J 26 N MET J 15
SHEET 1 X 3 LEU J 185 ILE J 186 0
SHEET 2 X 3 PHE J 212 ASP J 215 -1 O ASP J 215 N LEU J 185
SHEET 3 X 3 ARG J 206 ASP J 209 -1 N LEU J 208 O PHE J 212
CISPEP 1 LEU A 26 PRO A 27 0 -2.74
CISPEP 2 TRP A 175 PRO A 176 0 9.89
CISPEP 3 LEU B 26 PRO B 27 0 1.58
CISPEP 4 TRP B 175 PRO B 176 0 18.95
CISPEP 5 LEU C 26 PRO C 27 0 2.57
CISPEP 6 TRP C 175 PRO C 176 0 9.84
CISPEP 7 LEU D 26 PRO D 27 0 -5.52
CISPEP 8 TRP D 175 PRO D 176 0 12.61
CISPEP 9 LEU E 26 PRO E 27 0 -5.02
CISPEP 10 TRP E 175 PRO E 176 0 4.07
CISPEP 11 LEU F 26 PRO F 27 0 4.20
CISPEP 12 TRP F 175 PRO F 176 0 5.67
CISPEP 13 LEU G 26 PRO G 27 0 1.41
CISPEP 14 TRP G 175 PRO G 176 0 9.04
CISPEP 15 LEU H 26 PRO H 27 0 -6.32
CISPEP 16 TRP H 175 PRO H 176 0 2.03
CISPEP 17 LEU I 26 PRO I 27 0 1.65
CISPEP 18 TRP I 175 PRO I 176 0 10.73
CISPEP 19 LEU J 26 PRO J 27 0 -4.17
CISPEP 20 TRP J 175 PRO J 176 0 13.93
CRYST1 76.204 103.353 104.632 105.79 105.19 92.68 P 1 10
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 0.013123 0.000614 0.003919 0.00000
SCALE2 0.000000 0.009686 0.002991 0.00000
SCALE3 0.000000 0.000000 0.010365 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
