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HEADER HYDROLASE 16-SEP-25 9WTK
TITLE CRYSTAL STRUCTURE OF MONOALKYL PHTHALATE HYDROLASE IN COMPLEX WITH MBP
TITLE 2 FROM RHODOCOCCUS SP. EG-5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO-ETHYLHEXYLPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP. EG-5;
SOURCE 3 ORGANISM_TAXID: 1747801;
SOURCE 4 GENE: MEHPH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS MONO-BUTYL PHTHALATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.AGGARWAL,K.JANGID,S.SINGH,A.K.SHARMA,P.KUMAR
REVDAT 1 27-MAY-26 9WTK 0
JRNL AUTH S.AGGARWAL,K.JANGID,S.SINGH,A.K.SHARMA,P.KUMAR
JRNL TITL CRYSTAL STRUCTURE OF MONOALKYL PHTHALATE HYDROLASE IN
JRNL TITL 2 COMPLEX WITH MBP FROM RHODOCOCCUS SP. EG-5
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.21.2_5419: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 101732
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.258
REMARK 3 R VALUE (WORKING SET) : 0.257
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4987
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 24.2900 - 8.5800 0.98 3359 173 0.1835 0.1785
REMARK 3 2 8.5700 - 6.8600 1.00 3314 153 0.2030 0.2144
REMARK 3 3 6.8600 - 6.0100 1.00 3311 149 0.2371 0.2399
REMARK 3 4 6.0000 - 5.4600 1.00 3249 186 0.2360 0.2821
REMARK 3 5 5.4600 - 5.0800 1.00 3269 153 0.2270 0.2365
REMARK 3 6 5.0700 - 4.7800 1.00 3214 181 0.2225 0.2435
REMARK 3 7 4.7800 - 4.5400 1.00 3249 162 0.2310 0.2549
REMARK 3 8 4.5400 - 4.3400 1.00 3216 190 0.2335 0.2470
REMARK 3 9 4.3400 - 4.1800 1.00 3253 148 0.2394 0.2613
REMARK 3 10 4.1800 - 4.0300 1.00 3222 174 0.2400 0.2557
REMARK 3 11 4.0300 - 3.9100 1.00 3215 178 0.2471 0.2677
REMARK 3 12 3.9100 - 3.8000 1.00 3208 162 0.2590 0.2724
REMARK 3 13 3.8000 - 3.7000 1.00 3184 179 0.2530 0.2708
REMARK 3 14 3.7000 - 3.6100 1.00 3226 183 0.2611 0.2975
REMARK 3 15 3.6100 - 3.5300 1.00 3203 170 0.2662 0.2980
REMARK 3 16 3.5300 - 3.4500 1.00 3227 154 0.2724 0.3176
REMARK 3 17 3.4500 - 3.3800 1.00 3221 148 0.2649 0.3305
REMARK 3 18 3.3800 - 3.3200 1.00 3213 160 0.2841 0.3193
REMARK 3 19 3.3200 - 3.2600 1.00 3178 182 0.2875 0.3338
REMARK 3 20 3.2600 - 3.2000 1.00 3198 159 0.2804 0.2960
REMARK 3 21 3.2000 - 3.1500 1.00 3205 183 0.2827 0.3321
REMARK 3 22 3.1500 - 3.1000 1.00 3223 166 0.2960 0.3404
REMARK 3 23 3.1000 - 3.0600 1.00 3188 159 0.3036 0.3476
REMARK 3 24 3.0600 - 3.0200 1.00 3207 151 0.3084 0.4163
REMARK 3 25 3.0200 - 2.9800 1.00 3219 168 0.3020 0.3338
REMARK 3 26 2.9800 - 2.9400 1.00 3194 172 0.2896 0.3037
REMARK 3 27 2.9400 - 2.9000 1.00 3207 154 0.2897 0.2880
REMARK 3 28 2.9000 - 2.8700 1.00 3176 169 0.3042 0.3504
REMARK 3 29 2.8700 - 2.8300 1.00 3240 150 0.3034 0.3959
REMARK 3 30 2.8300 - 2.8000 1.00 3157 171 0.3000 0.3655
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 23333
REMARK 3 ANGLE : 0.562 31407
REMARK 3 CHIRALITY : 0.044 3463
REMARK 3 PLANARITY : 0.005 4042
REMARK 3 DIHEDRAL : 14.017 8418
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -75.8523 -34.9219 29.7239
REMARK 3 T TENSOR
REMARK 3 T11: 0.1428 T22: 0.1322
REMARK 3 T33: 0.1182 T12: -0.0021
REMARK 3 T13: -0.0298 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.0611 L22: 0.0224
REMARK 3 L33: 0.0553 L12: 0.0047
REMARK 3 L13: -0.0785 L23: 0.0042
REMARK 3 S TENSOR
REMARK 3 S11: 0.0036 S12: -0.0175 S13: -0.0095
REMARK 3 S21: -0.0119 S22: -0.0129 S23: -0.0024
REMARK 3 S31: -0.0789 S32: -0.0129 S33: 0.0032
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9WTK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-SEP-25.
REMARK 100 THE DEPOSITION ID IS D_1300063493.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUN-25
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : RIGAKU HYPIX-6000HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101798
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 24.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM SULFATE HEPTAHYDRATE,
REMARK 280 20% W/V PEG 3350, PH 6.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 88.15650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 122.44500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 88.15650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 122.44500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 88.15650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 122.44500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 88.15650
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 122.44500
REMARK 290 SMTRY3 8 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, 7, 8, 9, 10
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 LYS A 142
REMARK 465 PHE A 143
REMARK 465 ARG A 144
REMARK 465 ASP A 145
REMARK 465 VAL A 146
REMARK 465 SER A 298
REMARK 465 TYR A 299
REMARK 465 ALA A 300
REMARK 465 THR A 301
REMARK 465 ARG A 302
REMARK 465 ARG A 303
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 THR B 3
REMARK 465 ASP B 4
REMARK 465 ASP B 140
REMARK 465 ALA B 141
REMARK 465 LYS B 142
REMARK 465 PHE B 143
REMARK 465 ARG B 144
REMARK 465 ALA B 300
REMARK 465 THR B 301
REMARK 465 ARG B 302
REMARK 465 ARG B 303
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 THR C 139
REMARK 465 ASP C 140
REMARK 465 ALA C 141
REMARK 465 LYS C 142
REMARK 465 PHE C 143
REMARK 465 ARG C 144
REMARK 465 ASP C 145
REMARK 465 TYR C 299
REMARK 465 ALA C 300
REMARK 465 THR C 301
REMARK 465 ARG C 302
REMARK 465 ARG C 303
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 THR D 3
REMARK 465 ASP D 4
REMARK 465 ALA D 141
REMARK 465 LYS D 142
REMARK 465 TYR D 299
REMARK 465 ALA D 300
REMARK 465 THR D 301
REMARK 465 ARG D 302
REMARK 465 ARG D 303
REMARK 465 MET E 1
REMARK 465 ASN E 2
REMARK 465 ALA E 141
REMARK 465 LYS E 142
REMARK 465 PHE E 143
REMARK 465 ARG E 144
REMARK 465 ASP E 145
REMARK 465 TYR E 299
REMARK 465 ALA E 300
REMARK 465 THR E 301
REMARK 465 ARG E 302
REMARK 465 ARG E 303
REMARK 465 MET F 1
REMARK 465 ASN F 2
REMARK 465 THR F 3
REMARK 465 ASP F 4
REMARK 465 THR F 139
REMARK 465 ASP F 140
REMARK 465 ALA F 141
REMARK 465 LYS F 142
REMARK 465 PHE F 143
REMARK 465 TYR F 299
REMARK 465 ALA F 300
REMARK 465 THR F 301
REMARK 465 ARG F 302
REMARK 465 ARG F 303
REMARK 465 MET G 1
REMARK 465 ASN G 2
REMARK 465 ARG G 144
REMARK 465 ASP G 145
REMARK 465 VAL G 146
REMARK 465 GLU G 147
REMARK 465 PHE G 148
REMARK 465 TYR G 149
REMARK 465 ASP G 150
REMARK 465 ALA G 151
REMARK 465 ILE G 152
REMARK 465 THR G 153
REMARK 465 ARG G 154
REMARK 465 TYR G 299
REMARK 465 ALA G 300
REMARK 465 THR G 301
REMARK 465 ARG G 302
REMARK 465 ARG G 303
REMARK 465 MET H 1
REMARK 465 ASN H 2
REMARK 465 THR H 3
REMARK 465 ALA H 141
REMARK 465 LYS H 142
REMARK 465 PHE H 143
REMARK 465 ARG H 144
REMARK 465 THR H 301
REMARK 465 ARG H 302
REMARK 465 ARG H 303
REMARK 465 MET I 1
REMARK 465 ASN I 2
REMARK 465 THR I 3
REMARK 465 ASP I 4
REMARK 465 LYS I 142
REMARK 465 TYR I 299
REMARK 465 ALA I 300
REMARK 465 THR I 301
REMARK 465 ARG I 302
REMARK 465 ARG I 303
REMARK 465 MET J 1
REMARK 465 ASN J 2
REMARK 465 LYS J 142
REMARK 465 PHE J 143
REMARK 465 ARG J 144
REMARK 465 ASP J 145
REMARK 465 VAL J 146
REMARK 465 ALA J 300
REMARK 465 THR J 301
REMARK 465 ARG J 302
REMARK 465 ARG J 303
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 5 -92.36 -58.99
REMARK 500 SER A 6 58.42 -93.14
REMARK 500 SER A 108 -122.89 60.61
REMARK 500 TYR A 209 -50.33 -120.77
REMARK 500 SER B 6 36.52 -80.67
REMARK 500 GLU B 24 -6.84 -149.68
REMARK 500 SER B 108 -122.72 62.63
REMARK 500 ALA B 158 -5.75 -37.85
REMARK 500 TYR B 209 -50.26 -122.64
REMARK 500 ALA B 297 -73.48 -43.40
REMARK 500 SER B 298 -31.32 74.56
REMARK 500 ASP C 4 -101.87 72.40
REMARK 500 LEU C 5 91.28 71.27
REMARK 500 SER C 108 -125.50 63.65
REMARK 500 TYR C 209 -50.38 -120.72
REMARK 500 ALA C 297 174.42 -44.67
REMARK 500 SER D 6 37.44 -86.83
REMARK 500 GLU D 24 88.81 -154.10
REMARK 500 SER D 108 -125.66 64.53
REMARK 500 TYR D 209 -51.12 -122.56
REMARK 500 ASP E 4 -105.08 -163.65
REMARK 500 LEU E 5 86.70 78.74
REMARK 500 GLU E 24 89.40 -153.80
REMARK 500 SER E 108 -124.24 63.59
REMARK 500 THR E 139 -169.68 -113.00
REMARK 500 TYR E 209 -51.38 -121.49
REMARK 500 SER F 6 48.38 -89.53
REMARK 500 SER F 108 -124.39 63.87
REMARK 500 ASP F 145 -75.23 68.08
REMARK 500 TYR F 209 -50.68 -121.82
REMARK 500 ALA F 297 -75.79 -42.70
REMARK 500 GLU G 24 86.61 -151.64
REMARK 500 SER G 108 -124.64 63.77
REMARK 500 ALA G 141 4.61 -69.40
REMARK 500 ALA G 158 -8.02 -37.58
REMARK 500 LEU H 5 75.97 -161.41
REMARK 500 SER H 6 49.82 -80.85
REMARK 500 SER H 108 -123.62 63.16
REMARK 500 ALA H 158 -7.69 67.82
REMARK 500 TYR H 209 -51.10 -121.21
REMARK 500 ALA H 297 -72.48 -41.25
REMARK 500 VAL I 7 116.31 29.66
REMARK 500 GLU I 24 88.26 -154.34
REMARK 500 SER I 108 -125.09 64.40
REMARK 500 ASP I 140 109.31 -57.76
REMARK 500 ALA I 158 -7.71 66.87
REMARK 500 TYR I 209 -50.61 -121.33
REMARK 500 ALA I 297 74.97 53.78
REMARK 500 ASP J 4 -163.62 -122.69
REMARK 500 GLU J 24 89.95 -153.32
REMARK 500
REMARK 500 THIS ENTRY HAS 53 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9WTK A 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 9WTK A A0A0U5ADH4 1 303
DBREF1 9WTK B 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 9WTK B A0A0U5ADH4 1 303
DBREF1 9WTK C 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 9WTK C A0A0U5ADH4 1 303
DBREF1 9WTK D 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 9WTK D A0A0U5ADH4 1 303
DBREF1 9WTK E 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 9WTK E A0A0U5ADH4 1 303
DBREF1 9WTK F 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 9WTK F A0A0U5ADH4 1 303
DBREF1 9WTK G 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 9WTK G A0A0U5ADH4 1 303
DBREF1 9WTK H 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 9WTK H A0A0U5ADH4 1 303
DBREF1 9WTK I 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 9WTK I A0A0U5ADH4 1 303
DBREF1 9WTK J 1 303 UNP A0A0U5ADH4_9NOCA
DBREF2 9WTK J A0A0U5ADH4 1 303
SEQRES 1 A 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 A 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 A 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 A 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 A 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 A 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 A 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 A 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 A 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 A 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 A 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 A 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 A 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 A 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 A 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 A 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 A 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 A 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 A 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 A 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 A 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 A 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 A 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 A 303 ALA THR ARG ARG
SEQRES 1 B 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 B 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 B 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 B 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 B 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 B 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 B 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 B 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 B 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 B 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 B 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 B 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 B 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 B 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 B 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 B 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 B 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 B 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 B 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 B 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 B 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 B 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 B 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 B 303 ALA THR ARG ARG
SEQRES 1 C 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 C 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 C 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 C 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 C 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 C 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 C 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 C 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 C 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 C 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 C 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 C 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 C 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 C 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 C 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 C 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 C 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 C 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 C 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 C 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 C 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 C 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 C 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 C 303 ALA THR ARG ARG
SEQRES 1 D 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 D 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 D 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 D 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 D 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 D 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 D 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 D 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 D 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 D 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 D 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 D 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 D 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 D 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 D 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 D 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 D 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 D 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 D 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 D 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 D 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 D 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 D 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 D 303 ALA THR ARG ARG
SEQRES 1 E 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 E 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 E 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 E 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 E 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 E 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 E 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 E 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 E 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 E 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 E 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 E 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 E 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 E 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 E 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 E 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 E 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 E 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 E 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 E 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 E 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 E 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 E 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 E 303 ALA THR ARG ARG
SEQRES 1 F 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 F 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 F 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 F 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 F 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 F 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 F 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 F 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 F 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 F 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 F 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 F 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 F 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 F 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 F 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 F 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 F 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 F 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 F 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 F 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 F 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 F 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 F 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 F 303 ALA THR ARG ARG
SEQRES 1 G 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 G 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 G 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 G 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 G 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 G 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 G 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 G 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 G 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 G 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 G 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 G 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 G 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 G 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 G 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 G 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 G 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 G 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 G 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 G 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 G 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 G 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 G 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 G 303 ALA THR ARG ARG
SEQRES 1 H 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 H 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 H 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 H 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 H 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 H 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 H 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 H 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 H 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 H 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 H 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 H 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 H 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 H 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 H 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 H 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 H 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 H 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 H 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 H 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 H 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 H 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 H 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 H 303 ALA THR ARG ARG
SEQRES 1 I 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 I 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 I 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 I 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 I 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 I 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 I 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 I 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 I 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 I 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 I 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 I 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 I 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 I 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 I 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 I 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 I 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 I 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 I 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 I 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 I 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 I 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 I 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 I 303 ALA THR ARG ARG
SEQRES 1 J 303 MET ASN THR ASP LEU SER VAL ASN TYR ILE SER VAL GLY
SEQRES 2 J 303 GLY ILE ARG THR ARG TYR ILE ASP GLN GLY GLU GLY PRO
SEQRES 3 J 303 VAL ILE LEU LEU ILE HIS GLY GLY HIS SER GLY MET SER
SEQRES 4 J 303 MET PRO VAL GLY GLY ASP GLY TRP ALA PRO VAL ILE ALA
SEQRES 5 J 303 PRO LEU VAL ASP LYS GLY PHE ARG VAL VAL THR PHE ASP
SEQRES 6 J 303 LYS LEU GLY GLN GLY GLU THR ASP LEU ALA PRO THR HIS
SEQRES 7 J 303 ALA GLU TRP THR PHE ASP ALA VAL VAL LYS HIS ALA ARG
SEQRES 8 J 303 GLY PHE ILE ASP ALA LEU GLY LEU GLU ASP MET ILE LEU
SEQRES 9 J 303 VAL GLY HIS SER ARG GLY GLY LEU LEU ALA SER LYS LEU
SEQRES 10 J 303 ALA LEU ASP MET PRO GLU SER THR LYS GLY LEU PHE ILE
SEQRES 11 J 303 VAL SER SER ALA THR LEU ALA GLY THR ASP ALA LYS PHE
SEQRES 12 J 303 ARG ASP VAL GLU PHE TYR ASP ALA ILE THR ARG SER LEU
SEQRES 13 J 303 PRO ALA ASP ALA SER PRO GLU GLU ILE CYS GLY ALA TYR
SEQRES 14 J 303 PHE ARG ALA LEU TYR VAL THR PRO VAL PRO GLN GLU GLN
SEQRES 15 J 303 ILE ASN ALA ALA ALA ALA LYS TYR VAL LYS GLU ASN HIS
SEQRES 16 J 303 GLN ASN ALA LEU LYS THR TYR PRO MET VAL GLU LYS LYS
SEQRES 17 J 303 TYR TRP GLU PRO SER LEU GLN ALA ALA LYS ASP ASP ILE
SEQRES 18 J 303 ARG ALA ARG LEU PHE ALA GLY GLU VAL ASN ILE PRO VAL
SEQRES 19 J 303 GLU VAL VAL TRP GLY ARG ASP ASP ARG SER ALA PRO VAL
SEQRES 20 J 303 ASP LEU GLY ILE ALA PHE TYR GLN LYS LEU ALA LEU VAL
SEQRES 21 J 303 SER GLU THR THR SER LEU HIS ILE LEU GLY THR ALA GLY
SEQRES 22 J 303 HIS ASN VAL PHE ALA GLU ARG THR GLU ASP PHE VAL ARG
SEQRES 23 J 303 ILE LEU ALA ASP TYR ALA GLY ARG ARG SER ALA SER TYR
SEQRES 24 J 303 ALA THR ARG ARG
HET PEG A 401 7
HET PEG A 402 7
HET EDO A 403 4
HET EDO A 404 4
HET PHT A 405 12
HET 1BO A 406 5
HET EDO A 407 4
HET PEG A 408 7
HET PEG A 409 7
HET PEG A 410 7
HET PEG A 411 7
HET EDO A 412 4
HET EDO B 401 4
HET EDO B 402 4
HET PEG B 403 7
HET PHT B 404 12
HET 1BO B 405 5
HET EDO B 406 4
HET EDO B 407 4
HET EDO B 408 4
HET EDO B 409 4
HET PEG B 410 7
HET EDO B 411 4
HET EDO B 412 4
HET EDO B 413 4
HET EDO B 414 4
HET EDO B 415 4
HET EDO B 416 4
HET EDO B 417 4
HET EDO C 401 4
HET PEG C 402 7
HET PHT C 403 12
HET EDO C 404 4
HET PEG C 405 7
HET PEG C 406 7
HET EDO C 407 4
HET EDO C 408 4
HET EDO C 409 4
HET PEG D 401 7
HET PEG D 402 7
HET EDO D 403 4
HET PEG D 404 7
HET EDO D 405 4
HET PHT D 406 12
HET 1BO D 407 5
HET EDO D 408 4
HET EDO D 409 4
HET EDO D 410 4
HET PEG D 411 7
HET PEG D 412 7
HET PEG D 413 7
HET PEG D 414 7
HET EDO D 415 4
HET EDO E 401 4
HET PEG E 402 7
HET PEG E 403 7
HET PHT E 404 12
HET PEG E 405 7
HET PEG E 406 7
HET PEG E 407 7
HET PEG E 408 7
HET PEG E 409 7
HET EDO E 410 4
HET EDO E 411 4
HET EDO E 412 4
HET EDO F 401 4
HET PHT F 402 12
HET EDO F 403 4
HET EDO F 404 4
HET MLI F 405 7
HET PEG F 406 7
HET PEG F 407 7
HET PEG F 408 7
HET PEG F 409 7
HET PEG F 410 7
HET EDO F 411 4
HET EDO F 412 4
HET EDO F 413 4
HET EDO F 414 4
HET PEG G 401 7
HET EDO G 402 4
HET EDO G 403 4
HET EDO G 404 4
HET EDO G 405 4
HET PEG G 406 7
HET PHT G 407 12
HET EDO G 408 4
HET PEG G 409 7
HET PEG G 410 7
HET EDO G 411 4
HET EDO G 412 4
HET EDO G 413 4
HET EDO H 401 4
HET EDO H 402 4
HET EDO H 403 4
HET PEG H 404 7
HET PHT H 405 12
HET EDO H 406 4
HET EDO H 407 4
HET EDO I 401 4
HET PEG I 402 7
HET PEG I 403 7
HET EDO I 404 4
HET PHT I 405 12
HET PEG I 406 7
HET PEG I 407 7
HET EDO I 408 4
HET EDO I 409 4
HET PEG J 401 7
HET PEG J 402 7
HET PEG J 403 7
HET PHT J 404 12
HET EDO J 405 4
HET MLI J 406 7
HET PEG J 407 7
HET PEG J 408 7
HET EDO J 409 4
HET EDO J 410 4
HET EDO J 411 4
HET EDO J 412 4
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PHT PHTHALIC ACID
HETNAM 1BO 1-BUTANOL
HETNAM MLI MALONATE ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN 1BO BUTAN-1-OL
FORMUL 11 PEG 44(C4 H10 O3)
FORMUL 13 EDO 61(C2 H6 O2)
FORMUL 15 PHT 10(C8 H6 O4)
FORMUL 16 1BO 3(C4 H10 O)
FORMUL 80 MLI 2(C3 H2 O4 2-)
FORMUL 31 HOH *4(H2 O)
HELIX 1 AA1 GLY A 43 GLY A 46 5 4
HELIX 2 AA2 TRP A 47 LYS A 57 1 11
HELIX 3 AA3 THR A 77 TRP A 81 5 5
HELIX 4 AA4 THR A 82 GLY A 98 1 17
HELIX 5 AA5 SER A 108 MET A 121 1 14
HELIX 6 AA6 SER A 133 GLY A 138 1 6
HELIX 7 AA7 PHE A 148 SER A 155 1 8
HELIX 8 AA8 SER A 161 TYR A 174 1 14
HELIX 9 AA9 PRO A 179 VAL A 191 1 13
HELIX 10 AB1 LYS A 192 GLU A 206 1 15
HELIX 11 AB2 TYR A 209 PHE A 226 1 18
HELIX 12 AB3 PRO A 246 LEU A 259 1 14
HELIX 13 AB4 ASN A 275 ARG A 280 1 6
HELIX 14 AB5 ARG A 280 ALA A 297 1 18
HELIX 15 AB6 GLY B 43 GLY B 46 5 4
HELIX 16 AB7 TRP B 47 LYS B 57 1 11
HELIX 17 AB8 THR B 77 TRP B 81 5 5
HELIX 18 AB9 THR B 82 GLY B 98 1 17
HELIX 19 AC1 SER B 108 MET B 121 1 14
HELIX 20 AC2 SER B 133 GLY B 138 1 6
HELIX 21 AC3 VAL B 146 SER B 155 1 10
HELIX 22 AC4 SER B 161 TYR B 174 1 14
HELIX 23 AC5 PRO B 179 VAL B 191 1 13
HELIX 24 AC6 LYS B 192 LYS B 207 1 16
HELIX 25 AC7 TYR B 209 PHE B 226 1 18
HELIX 26 AC8 PRO B 246 LEU B 259 1 14
HELIX 27 AC9 ASN B 275 ARG B 280 1 6
HELIX 28 AD1 ARG B 280 SER B 298 1 19
HELIX 29 AD2 GLY C 43 GLY C 46 5 4
HELIX 30 AD3 TRP C 47 LYS C 57 1 11
HELIX 31 AD4 THR C 77 TRP C 81 5 5
HELIX 32 AD5 THR C 82 GLY C 98 1 17
HELIX 33 AD6 SER C 108 MET C 121 1 14
HELIX 34 AD7 SER C 133 GLY C 138 1 6
HELIX 35 AD8 GLU C 147 SER C 155 1 9
HELIX 36 AD9 SER C 161 TYR C 174 1 14
HELIX 37 AE1 PRO C 179 VAL C 191 1 13
HELIX 38 AE2 LYS C 192 GLU C 206 1 15
HELIX 39 AE3 TYR C 209 PHE C 226 1 18
HELIX 40 AE4 PRO C 246 LEU C 259 1 14
HELIX 41 AE5 ASN C 275 ARG C 280 1 6
HELIX 42 AE6 ARG C 280 ALA C 297 1 18
HELIX 43 AE7 GLY D 43 GLY D 46 5 4
HELIX 44 AE8 TRP D 47 LYS D 57 1 11
HELIX 45 AE9 THR D 77 TRP D 81 5 5
HELIX 46 AF1 THR D 82 GLY D 98 1 17
HELIX 47 AF2 ARG D 109 MET D 121 1 13
HELIX 48 AF3 SER D 133 GLY D 138 1 6
HELIX 49 AF4 VAL D 146 SER D 155 1 10
HELIX 50 AF5 SER D 161 TYR D 174 1 14
HELIX 51 AF6 PRO D 179 VAL D 191 1 13
HELIX 52 AF7 LYS D 192 LYS D 207 1 16
HELIX 53 AF8 TYR D 209 PHE D 226 1 18
HELIX 54 AF9 PRO D 246 LEU D 259 1 14
HELIX 55 AG1 ASN D 275 ARG D 280 1 6
HELIX 56 AG2 ARG D 280 SER D 298 1 19
HELIX 57 AG3 GLY E 43 GLY E 46 5 4
HELIX 58 AG4 TRP E 47 LYS E 57 1 11
HELIX 59 AG5 THR E 77 TRP E 81 5 5
HELIX 60 AG6 THR E 82 GLY E 98 1 17
HELIX 61 AG7 SER E 108 MET E 121 1 14
HELIX 62 AG8 SER E 133 GLY E 138 1 6
HELIX 63 AG9 GLU E 147 SER E 155 1 9
HELIX 64 AH1 SER E 161 TYR E 174 1 14
HELIX 65 AH2 PRO E 179 VAL E 191 1 13
HELIX 66 AH3 LYS E 192 GLU E 206 1 15
HELIX 67 AH4 TYR E 209 PHE E 226 1 18
HELIX 68 AH5 PRO E 246 LEU E 259 1 14
HELIX 69 AH6 ASN E 275 ARG E 280 1 6
HELIX 70 AH7 ARG E 280 SER E 298 1 19
HELIX 71 AH8 GLY F 43 GLY F 46 5 4
HELIX 72 AH9 TRP F 47 LYS F 57 1 11
HELIX 73 AI1 THR F 77 TRP F 81 5 5
HELIX 74 AI2 THR F 82 GLY F 98 1 17
HELIX 75 AI3 SER F 108 MET F 121 1 14
HELIX 76 AI4 VAL F 146 SER F 155 1 10
HELIX 77 AI5 SER F 161 TYR F 174 1 14
HELIX 78 AI6 PRO F 179 VAL F 191 1 13
HELIX 79 AI7 LYS F 192 GLU F 206 1 15
HELIX 80 AI8 TYR F 209 PHE F 226 1 18
HELIX 81 AI9 PRO F 246 LEU F 259 1 14
HELIX 82 AJ1 ASN F 275 ARG F 280 1 6
HELIX 83 AJ2 ARG F 280 SER F 298 1 19
HELIX 84 AJ3 GLY G 43 GLY G 46 5 4
HELIX 85 AJ4 TRP G 47 LYS G 57 1 11
HELIX 86 AJ5 THR G 77 TRP G 81 5 5
HELIX 87 AJ6 THR G 82 GLY G 98 1 17
HELIX 88 AJ7 SER G 108 MET G 121 1 14
HELIX 89 AJ8 SER G 133 GLY G 138 1 6
HELIX 90 AJ9 SER G 161 TYR G 174 1 14
HELIX 91 AK1 PRO G 179 VAL G 191 1 13
HELIX 92 AK2 LYS G 192 GLU G 206 1 15
HELIX 93 AK3 TYR G 209 PHE G 226 1 18
HELIX 94 AK4 PRO G 246 LEU G 259 1 14
HELIX 95 AK5 ASN G 275 ARG G 280 1 6
HELIX 96 AK6 ARG G 280 SER G 298 1 19
HELIX 97 AK7 GLY H 43 GLY H 46 5 4
HELIX 98 AK8 TRP H 47 LYS H 57 1 11
HELIX 99 AK9 THR H 77 TRP H 81 5 5
HELIX 100 AL1 THR H 82 GLY H 98 1 17
HELIX 101 AL2 SER H 108 MET H 121 1 14
HELIX 102 AL3 SER H 133 GLY H 138 1 6
HELIX 103 AL4 VAL H 146 SER H 155 1 10
HELIX 104 AL5 SER H 161 TYR H 174 1 14
HELIX 105 AL6 PRO H 179 VAL H 191 1 13
HELIX 106 AL7 LYS H 192 GLU H 206 1 15
HELIX 107 AL8 TYR H 209 PHE H 226 1 18
HELIX 108 AL9 PRO H 246 LEU H 259 1 14
HELIX 109 AM1 ASN H 275 ARG H 280 1 6
HELIX 110 AM2 ARG H 280 SER H 298 1 19
HELIX 111 AM3 GLY I 43 GLY I 46 5 4
HELIX 112 AM4 TRP I 47 LYS I 57 1 11
HELIX 113 AM5 THR I 77 TRP I 81 5 5
HELIX 114 AM6 THR I 82 GLY I 98 1 17
HELIX 115 AM7 SER I 108 MET I 121 1 14
HELIX 116 AM8 SER I 133 GLY I 138 1 6
HELIX 117 AM9 VAL I 146 SER I 155 1 10
HELIX 118 AN1 SER I 161 TYR I 174 1 14
HELIX 119 AN2 PRO I 179 VAL I 191 1 13
HELIX 120 AN3 LYS I 192 GLU I 206 1 15
HELIX 121 AN4 TYR I 209 PHE I 226 1 18
HELIX 122 AN5 PRO I 246 LEU I 259 1 14
HELIX 123 AN6 ASN I 275 ARG I 280 1 6
HELIX 124 AN7 ARG I 280 ALA I 297 1 18
HELIX 125 AN8 GLY J 43 GLY J 46 5 4
HELIX 126 AN9 TRP J 47 LYS J 57 1 11
HELIX 127 AO1 THR J 77 TRP J 81 5 5
HELIX 128 AO2 THR J 82 GLY J 98 1 17
HELIX 129 AO3 SER J 108 MET J 121 1 14
HELIX 130 AO4 SER J 133 GLY J 138 1 6
HELIX 131 AO5 PHE J 148 ARG J 154 1 7
HELIX 132 AO6 SER J 161 TYR J 174 1 14
HELIX 133 AO7 PRO J 179 VAL J 191 1 13
HELIX 134 AO8 LYS J 192 GLU J 206 1 15
HELIX 135 AO9 TYR J 209 PHE J 226 1 18
HELIX 136 AP1 PRO J 246 LEU J 259 1 14
HELIX 137 AP2 ASN J 275 ARG J 280 1 6
HELIX 138 AP3 ARG J 280 TYR J 299 1 20
SHEET 1 AA116 VAL A 7 VAL A 12 0
SHEET 2 AA116 ILE A 15 GLN A 22 -1 O TYR A 19 N ASN A 8
SHEET 3 AA116 ARG A 60 PHE A 64 -1 O THR A 63 N ILE A 20
SHEET 4 AA116 VAL A 27 ILE A 31 1 N ILE A 28 O ARG A 60
SHEET 5 AA116 MET A 102 HIS A 107 1 O VAL A 105 N ILE A 31
SHEET 6 AA116 THR A 125 VAL A 131 1 O GLY A 127 N LEU A 104
SHEET 7 AA116 VAL A 234 GLY A 239 1 O VAL A 237 N ILE A 130
SHEET 8 AA116 THR A 263 LEU A 269 1 O SER A 265 N VAL A 236
SHEET 9 AA116 THR B 263 LEU B 269 -1 O THR B 264 N ILE A 268
SHEET 10 AA116 VAL B 234 GLY B 239 1 N VAL B 236 O SER B 265
SHEET 11 AA116 THR B 125 VAL B 131 1 N ILE B 130 O VAL B 237
SHEET 12 AA116 MET B 102 HIS B 107 1 N LEU B 104 O PHE B 129
SHEET 13 AA116 VAL B 27 ILE B 31 1 N ILE B 31 O VAL B 105
SHEET 14 AA116 ARG B 60 PHE B 64 1 O ARG B 60 N ILE B 28
SHEET 15 AA116 ILE B 15 GLN B 22 -1 N ILE B 20 O THR B 63
SHEET 16 AA116 VAL B 7 VAL B 12 -1 N ASN B 8 O TYR B 19
SHEET 1 AA216 VAL C 7 VAL C 12 0
SHEET 2 AA216 ILE C 15 GLN C 22 -1 O TYR C 19 N ASN C 8
SHEET 3 AA216 ARG C 60 PHE C 64 -1 O THR C 63 N ILE C 20
SHEET 4 AA216 VAL C 27 ILE C 31 1 N ILE C 28 O ARG C 60
SHEET 5 AA216 MET C 102 HIS C 107 1 O VAL C 105 N ILE C 31
SHEET 6 AA216 THR C 125 VAL C 131 1 O GLY C 127 N LEU C 104
SHEET 7 AA216 VAL C 234 GLY C 239 1 O VAL C 237 N ILE C 130
SHEET 8 AA216 THR C 263 LEU C 269 1 O SER C 265 N VAL C 236
SHEET 9 AA216 THR D 263 LEU D 269 -1 O LEU D 266 N LEU C 266
SHEET 10 AA216 VAL D 234 GLY D 239 1 N TRP D 238 O HIS D 267
SHEET 11 AA216 THR D 125 VAL D 131 1 N ILE D 130 O VAL D 237
SHEET 12 AA216 MET D 102 HIS D 107 1 N LEU D 104 O GLY D 127
SHEET 13 AA216 VAL D 27 ILE D 31 1 N ILE D 31 O VAL D 105
SHEET 14 AA216 ARG D 60 PHE D 64 1 O ARG D 60 N ILE D 28
SHEET 15 AA216 ILE D 15 GLN D 22 -1 N ILE D 20 O THR D 63
SHEET 16 AA216 VAL D 7 VAL D 12 -1 N ASN D 8 O TYR D 19
SHEET 1 AA316 VAL E 7 VAL E 12 0
SHEET 2 AA316 ILE E 15 GLN E 22 -1 O THR E 17 N ILE E 10
SHEET 3 AA316 ARG E 60 PHE E 64 -1 O THR E 63 N ILE E 20
SHEET 4 AA316 VAL E 27 ILE E 31 1 N LEU E 30 O VAL E 62
SHEET 5 AA316 MET E 102 HIS E 107 1 O VAL E 105 N ILE E 31
SHEET 6 AA316 THR E 125 VAL E 131 1 O GLY E 127 N LEU E 104
SHEET 7 AA316 VAL E 234 GLY E 239 1 O VAL E 237 N ILE E 130
SHEET 8 AA316 THR E 263 LEU E 269 1 O SER E 265 N VAL E 236
SHEET 9 AA316 THR H 263 LEU H 269 -1 O THR H 264 N ILE E 268
SHEET 10 AA316 VAL H 234 GLY H 239 1 N VAL H 236 O SER H 265
SHEET 11 AA316 THR H 125 VAL H 131 1 N ILE H 130 O VAL H 237
SHEET 12 AA316 MET H 102 HIS H 107 1 N GLY H 106 O PHE H 129
SHEET 13 AA316 VAL H 27 ILE H 31 1 N ILE H 31 O VAL H 105
SHEET 14 AA316 ARG H 60 PHE H 64 1 O ARG H 60 N ILE H 28
SHEET 15 AA316 ILE H 15 GLN H 22 -1 N ILE H 20 O THR H 63
SHEET 16 AA316 VAL H 7 VAL H 12 -1 N ILE H 10 O THR H 17
SHEET 1 AA416 VAL F 7 VAL F 12 0
SHEET 2 AA416 ILE F 15 GLN F 22 -1 O THR F 17 N ILE F 10
SHEET 3 AA416 ARG F 60 PHE F 64 -1 O THR F 63 N ILE F 20
SHEET 4 AA416 VAL F 27 ILE F 31 1 N ILE F 28 O ARG F 60
SHEET 5 AA416 MET F 102 HIS F 107 1 O ILE F 103 N VAL F 27
SHEET 6 AA416 THR F 125 VAL F 131 1 O GLY F 127 N LEU F 104
SHEET 7 AA416 VAL F 234 GLY F 239 1 O VAL F 237 N ILE F 130
SHEET 8 AA416 THR F 263 LEU F 269 1 O HIS F 267 N VAL F 236
SHEET 9 AA416 THR G 263 LEU G 269 -1 O LEU G 266 N LEU F 266
SHEET 10 AA416 VAL G 234 GLY G 239 1 N VAL G 236 O HIS G 267
SHEET 11 AA416 THR G 125 VAL G 131 1 N ILE G 130 O VAL G 237
SHEET 12 AA416 MET G 102 HIS G 107 1 N LEU G 104 O PHE G 129
SHEET 13 AA416 VAL G 27 ILE G 31 1 N ILE G 31 O VAL G 105
SHEET 14 AA416 ARG G 60 PHE G 64 1 O ARG G 60 N ILE G 28
SHEET 15 AA416 ILE G 15 GLN G 22 -1 N ILE G 20 O THR G 63
SHEET 16 AA416 VAL G 7 VAL G 12 -1 N ILE G 10 O THR G 17
SHEET 1 AA516 ASN I 8 VAL I 12 0
SHEET 2 AA516 ILE I 15 GLN I 22 -1 O TYR I 19 N ASN I 8
SHEET 3 AA516 ARG I 60 PHE I 64 -1 O THR I 63 N ILE I 20
SHEET 4 AA516 VAL I 27 ILE I 31 1 N ILE I 28 O ARG I 60
SHEET 5 AA516 MET I 102 HIS I 107 1 O VAL I 105 N ILE I 31
SHEET 6 AA516 THR I 125 VAL I 131 1 O PHE I 129 N GLY I 106
SHEET 7 AA516 VAL I 234 GLY I 239 1 O VAL I 237 N ILE I 130
SHEET 8 AA516 THR I 263 LEU I 269 1 O SER I 265 N VAL I 236
SHEET 9 AA516 THR J 263 LEU J 269 -1 O LEU J 266 N LEU I 266
SHEET 10 AA516 VAL J 234 GLY J 239 1 N TRP J 238 O HIS J 267
SHEET 11 AA516 THR J 125 VAL J 131 1 N ILE J 130 O VAL J 237
SHEET 12 AA516 MET J 102 HIS J 107 1 N LEU J 104 O GLY J 127
SHEET 13 AA516 VAL J 27 ILE J 31 1 N ILE J 31 O VAL J 105
SHEET 14 AA516 ARG J 60 PHE J 64 1 O VAL J 62 N LEU J 30
SHEET 15 AA516 ILE J 15 GLN J 22 -1 N ILE J 20 O THR J 63
SHEET 16 AA516 VAL J 7 VAL J 12 -1 N ASN J 8 O TYR J 19
CRYST1 176.313 244.890 192.097 90.00 90.00 90.00 C 2 2 2 80
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 0.005672 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005206 0.00000
TER 2225 ALA A 297
TER 4447 TYR B 299
TER 6657 SER C 298
TER 8897 SER D 298
TER 11122 SER E 298
TER 13336 SER F 298
TER 15508 SER G 298
TER 17751 ALA H 300
TER 19996 SER I 298
TER 22231 TYR J 299
MASTER 512 0 120 138 80 0 0 622926 10 701 240
END |