HEADER STRUCTURAL PROTEIN 19-FEB-14 3J6G
TITLE MINIMIZED AVERAGE STRUCTURE OF MICROTUBULES STABILIZED BY TAXOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUBULIN ALPHA-1A CHAIN;
COMPND 3 CHAIN: A, C, E, G, I, K, M, O, Q;
COMPND 4 SYNONYM: ALPHA-TUBULIN 1, TUBULIN ALPHA-1 CHAIN;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: TUBULIN BETA CHAIN;
COMPND 7 CHAIN: B, D, F, H, J, L, N, P, R;
COMPND 8 SYNONYM: BETA-TUBULIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 7 ORGANISM_COMMON: PIG;
SOURCE 8 ORGANISM_TAXID: 9823
KEYWDS MICROTUBULE, TAXOL, STRUCTURAL PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR G.M.ALUSHIN,G.C.LANDER,E.H.KELLOGG,R.ZHANG,D.BAKER,E.NOGALES
REVDAT 3 21-FEB-24 3J6G 1 REMARK SEQADV LINK
REVDAT 2 18-JUL-18 3J6G 1 REMARK
REVDAT 1 04-JUN-14 3J6G 0
JRNL AUTH G.M.ALUSHIN,G.C.LANDER,E.H.KELLOGG,R.ZHANG,D.BAKER,E.NOGALES
JRNL TITL HIGH-RESOLUTION MICROTUBULE STRUCTURES REVEAL THE STRUCTURAL
JRNL TITL 2 TRANSITIONS IN ALPHA BETA-TUBULIN UPON GTP HYDROLYSIS.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 157 1117 2014
JRNL REFN ISSN 0092-8674
JRNL PMID 24855948
JRNL DOI 10.1016/J.CELL.2014.03.053
REMARK 2
REMARK 2 RESOLUTION. 5.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : ROSETTA, EMAN, FREALIGN, SPARX
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 1JFF
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : REFINEMENT PROTOCOL--FLEXIBLE FITTING DETAILS-
REMARK 3 -STRUCTURE REPRESENTS THE MINIMIZED AVERAGE STRUCTURE OF THE 1%
REMARK 3 LOWEST ENERGY STRUCTURES FROM THE REFINEMENT RUN.
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 1.740
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 5.500
REMARK 3 NUMBER OF PARTICLES : 24357
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 3J6G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000160310.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : VITREOUS ICE (CRYO EM)
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : FILAMENT
REMARK 245 PARTICLE TYPE : HELICAL
REMARK 245 NAME OF SAMPLE : MICROTUBULE STABILIZED BY TAXOL
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.25
REMARK 245 SAMPLE SUPPORT DETAILS : 400 MESH C-FLAT 1.2/1.3, GLOW
REMARK 245 DISCHARGED IN EDWARDS CARBON
REMARK 245 EVAPORATOR
REMARK 245 SAMPLE VITRIFICATION DETAILS : THE GRID WAS BLOTTED FOR 2
REMARK 245 SECONDS BEFORE PLUNGING INTO
REMARK 245 LIQUID ETHANE (FEI VITROBOT
REMARK 245 MARK II).
REMARK 245 SAMPLE BUFFER : 80 MM PIPES, 1 MM EGTA, 1 MM
REMARK 245 MGCL2, 1 MM DTT, 0.05% NONIDET
REMARK 245 P-40
REMARK 245 PH : 6.80
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 29-MAY-12
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : KODAK SO-163 FILM
REMARK 245 MINIMUM DEFOCUS (NM) : 1400.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : 0.00
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : 0.00
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 2500.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 72000
REMARK 245 CALIBRATED MAGNIFICATION : 72000
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE 3 X 3 LATTICE REPRESENTED IN THIS ENTRY IS A SEGMENT OF
REMARK 300 A MICROTUBULE.
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: OCTADECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R
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 ASP A 39
REMARK 465 LYS A 40
REMARK 465 THR A 41
REMARK 465 ILE A 42
REMARK 465 GLY A 43
REMARK 465 GLY A 44
REMARK 465 GLY A 45
REMARK 465 ASP A 46
REMARK 465 ASP A 47
REMARK 465 SER A 48
REMARK 465 MET B 1
REMARK 465 MET C 1
REMARK 465 ASP C 39
REMARK 465 LYS C 40
REMARK 465 THR C 41
REMARK 465 ILE C 42
REMARK 465 GLY C 43
REMARK 465 GLY C 44
REMARK 465 GLY C 45
REMARK 465 ASP C 46
REMARK 465 ASP C 47
REMARK 465 SER C 48
REMARK 465 MET D 1
REMARK 465 MET E 1
REMARK 465 ASP E 39
REMARK 465 LYS E 40
REMARK 465 THR E 41
REMARK 465 ILE E 42
REMARK 465 GLY E 43
REMARK 465 GLY E 44
REMARK 465 GLY E 45
REMARK 465 ASP E 46
REMARK 465 ASP E 47
REMARK 465 SER E 48
REMARK 465 MET F 1
REMARK 465 MET G 1
REMARK 465 ASP G 39
REMARK 465 LYS G 40
REMARK 465 THR G 41
REMARK 465 ILE G 42
REMARK 465 GLY G 43
REMARK 465 GLY G 44
REMARK 465 GLY G 45
REMARK 465 ASP G 46
REMARK 465 ASP G 47
REMARK 465 SER G 48
REMARK 465 MET H 1
REMARK 465 MET I 1
REMARK 465 ASP I 39
REMARK 465 LYS I 40
REMARK 465 THR I 41
REMARK 465 ILE I 42
REMARK 465 GLY I 43
REMARK 465 GLY I 44
REMARK 465 GLY I 45
REMARK 465 ASP I 46
REMARK 465 ASP I 47
REMARK 465 SER I 48
REMARK 465 MET J 1
REMARK 465 MET K 1
REMARK 465 ASP K 39
REMARK 465 LYS K 40
REMARK 465 THR K 41
REMARK 465 ILE K 42
REMARK 465 GLY K 43
REMARK 465 GLY K 44
REMARK 465 GLY K 45
REMARK 465 ASP K 46
REMARK 465 ASP K 47
REMARK 465 SER K 48
REMARK 465 MET L 1
REMARK 465 MET M 1
REMARK 465 ASP M 39
REMARK 465 LYS M 40
REMARK 465 THR M 41
REMARK 465 ILE M 42
REMARK 465 GLY M 43
REMARK 465 GLY M 44
REMARK 465 GLY M 45
REMARK 465 ASP M 46
REMARK 465 ASP M 47
REMARK 465 SER M 48
REMARK 465 MET N 1
REMARK 465 MET O 1
REMARK 465 ASP O 39
REMARK 465 LYS O 40
REMARK 465 THR O 41
REMARK 465 ILE O 42
REMARK 465 GLY O 43
REMARK 465 GLY O 44
REMARK 465 GLY O 45
REMARK 465 ASP O 46
REMARK 465 ASP O 47
REMARK 465 SER O 48
REMARK 465 MET P 1
REMARK 465 MET Q 1
REMARK 465 ASP Q 39
REMARK 465 LYS Q 40
REMARK 465 THR Q 41
REMARK 465 ILE Q 42
REMARK 465 GLY Q 43
REMARK 465 GLY Q 44
REMARK 465 GLY Q 45
REMARK 465 ASP Q 46
REMARK 465 ASP Q 47
REMARK 465 SER Q 48
REMARK 465 MET R 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CD ARG F 401 NE1 TRP K 346 2.07
REMARK 500 CD ARG D 401 NE1 TRP G 346 2.08
REMARK 500 NE1 TRP C 346 CD ARG N 401 2.09
REMARK 500 NE1 TRP E 346 CD ARG R 401 2.13
REMARK 500 NE1 TRP A 346 CD ARG P 401 2.16
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 MET A 36 CA MET A 36 C -0.240
REMARK 500 SER A 38 N SER A 38 CA -0.167
REMARK 500 ARG A 264 CA ARG A 264 C -0.176
REMARK 500 HIS A 266 N HIS A 266 CA -0.242
REMARK 500 ALA A 281 N ALA A 281 CA -0.126
REMARK 500 ALA A 281 CA ALA A 281 C -0.192
REMARK 500 TYR A 282 N TYR A 282 CA -0.158
REMARK 500 TYR A 282 CA TYR A 282 C -0.176
REMARK 500 HIS A 283 N HIS A 283 CA -0.146
REMARK 500 HIS A 283 CA HIS A 283 C -0.215
REMARK 500 GLU A 284 N GLU A 284 CA -0.164
REMARK 500 GLU A 284 CA GLU A 284 C -0.167
REMARK 500 GLN A 285 N GLN A 285 CA -0.140
REMARK 500 ARG A 339 CA ARG A 339 C -0.156
REMARK 500 THR A 340 N THR A 340 CA -0.150
REMARK 500 PRO A 348 N PRO A 348 CA -0.103
REMARK 500 PRO A 348 CA PRO A 348 C -0.172
REMARK 500 THR A 349 N THR A 349 CA -0.121
REMARK 500 THR A 349 CA THR A 349 C -0.166
REMARK 500 GLY A 350 N GLY A 350 CA -0.132
REMARK 500 GLY A 436 CA GLY A 436 C -0.150
REMARK 500 VAL A 437 N VAL A 437 CA -0.122
REMARK 500 GLU B 3 N GLU B 3 CA -0.251
REMARK 500 GLY B 34 CA GLY B 34 C -0.099
REMARK 500 GLY B 58 CA GLY B 58 C -0.107
REMARK 500 ALA B 99 CA ALA B 99 C -0.175
REMARK 500 GLY B 100 N GLY B 100 CA -0.125
REMARK 500 ASN B 249 CA ASN B 249 C -0.317
REMARK 500 GLN B 436 CA GLN B 436 C -0.178
REMARK 500 ASP B 437 N ASP B 437 CA -0.145
REMARK 500 MET C 36 CA MET C 36 C -0.240
REMARK 500 SER C 38 N SER C 38 CA -0.167
REMARK 500 ARG C 264 CA ARG C 264 C -0.176
REMARK 500 HIS C 266 N HIS C 266 CA -0.242
REMARK 500 ALA C 281 N ALA C 281 CA -0.126
REMARK 500 ALA C 281 CA ALA C 281 C -0.192
REMARK 500 TYR C 282 N TYR C 282 CA -0.157
REMARK 500 TYR C 282 CA TYR C 282 C -0.177
REMARK 500 HIS C 283 N HIS C 283 CA -0.146
REMARK 500 HIS C 283 CA HIS C 283 C -0.215
REMARK 500 GLU C 284 N GLU C 284 CA -0.164
REMARK 500 GLU C 284 CA GLU C 284 C -0.167
REMARK 500 GLN C 285 N GLN C 285 CA -0.140
REMARK 500 ARG C 339 CA ARG C 339 C -0.156
REMARK 500 THR C 340 N THR C 340 CA -0.150
REMARK 500 PRO C 348 N PRO C 348 CA -0.103
REMARK 500 PRO C 348 CA PRO C 348 C -0.171
REMARK 500 THR C 349 N THR C 349 CA -0.121
REMARK 500 THR C 349 CA THR C 349 C -0.166
REMARK 500 GLY C 350 N GLY C 350 CA -0.133
REMARK 500
REMARK 500 THIS ENTRY HAS 268 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TRP A 21 CA - CB - CG ANGL. DEV. = -13.1 DEGREES
REMARK 500 ARG A 64 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 PHE A 67 CD1 - CE1 - CZ ANGL. DEV. = -11.0 DEGREES
REMARK 500 PHE A 67 CE1 - CZ - CE2 ANGL. DEV. = 18.3 DEGREES
REMARK 500 PHE A 67 CZ - CE2 - CD2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 GLU A 97 CA - C - N ANGL. DEV. = -14.2 DEGREES
REMARK 500 ASP A 98 C - N - CA ANGL. DEV. = 19.4 DEGREES
REMARK 500 ASP A 98 N - CA - CB ANGL. DEV. = -16.0 DEGREES
REMARK 500 ASP A 98 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ASP A 98 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP A 98 N - CA - C ANGL. DEV. = 16.7 DEGREES
REMARK 500 ASP A 98 CA - C - N ANGL. DEV. = -13.9 DEGREES
REMARK 500 ARG A 105 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG A 121 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 123 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 GLY A 143 C - N - CA ANGL. DEV. = -12.7 DEGREES
REMARK 500 TYR A 161 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP A 205 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 205 CB - CG - OD2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 TYR A 210 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 214 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 221 NE - CZ - NH2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG A 243 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 PHE A 244 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 TYR A 262 CB - CG - CD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 TYR A 262 CB - CG - CD1 ANGL. DEV. = -10.5 DEGREES
REMARK 500 PRO A 274 C - N - CA ANGL. DEV. = -22.3 DEGREES
REMARK 500 PRO A 274 C - N - CD ANGL. DEV. = -18.6 DEGREES
REMARK 500 PRO A 274 CA - N - CD ANGL. DEV. = -15.3 DEGREES
REMARK 500 PRO A 274 N - CA - CB ANGL. DEV. = 7.4 DEGREES
REMARK 500 PRO A 274 N - CD - CG ANGL. DEV. = 11.7 DEGREES
REMARK 500 TYR A 282 C - N - CA ANGL. DEV. = -19.6 DEGREES
REMARK 500 HIS A 283 C - N - CA ANGL. DEV. = -15.8 DEGREES
REMARK 500 HIS A 283 CA - C - N ANGL. DEV. = -15.7 DEGREES
REMARK 500 HIS A 283 O - C - N ANGL. DEV. = 9.9 DEGREES
REMARK 500 GLU A 284 C - N - CA ANGL. DEV. = -18.1 DEGREES
REMARK 500 GLU A 284 CA - C - N ANGL. DEV. = -14.8 DEGREES
REMARK 500 GLN A 301 N - CA - C ANGL. DEV. = 17.2 DEGREES
REMARK 500 ARG A 308 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 308 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 339 CA - C - N ANGL. DEV. = -19.8 DEGREES
REMARK 500 PHE A 343 CB - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 PHE A 343 CB - CG - CD1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 TRP A 346 CD2 - CE3 - CZ3 ANGL. DEV. = -12.8 DEGREES
REMARK 500 TRP A 346 CE3 - CZ3 - CH2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO A 348 C - N - CA ANGL. DEV. = -10.6 DEGREES
REMARK 500 PRO A 348 CA - N - CD ANGL. DEV. = 11.6 DEGREES
REMARK 500 THR A 349 CA - C - N ANGL. DEV. = -14.0 DEGREES
REMARK 500 GLY A 350 C - N - CA ANGL. DEV. = -15.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 781 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 MET A 36 106.46 -173.80
REMARK 500 TYR A 83 -1.57 72.45
REMARK 500 LYS A 96 -41.11 -133.04
REMARK 500 ASP A 98 132.51 -11.57
REMARK 500 TYR A 108 -77.52 -113.83
REMARK 500 TYR A 161 66.87 -118.80
REMARK 500 ARG A 264 72.10 -104.80
REMARK 500 ALA A 273 40.38 -141.69
REMARK 500 VAL A 275 76.82 -116.84
REMARK 500 MET A 302 -17.35 85.11
REMARK 500 GLN A 342 68.70 3.68
REMARK 500 THR A 349 57.57 -152.74
REMARK 500 ARG A 402 39.04 70.58
REMARK 500 PHE A 404 -0.82 68.75
REMARK 500 ASN B 50 -53.99 5.79
REMARK 500 PHE B 83 -4.28 70.52
REMARK 500 THR B 109 -86.21 -108.79
REMARK 500 LYS B 402 46.03 31.92
REMARK 500 PHE B 404 -5.79 68.48
REMARK 500 MET C 36 106.44 -173.87
REMARK 500 TYR C 83 -1.53 72.47
REMARK 500 LYS C 96 -41.17 -133.03
REMARK 500 ASP C 98 132.47 -11.53
REMARK 500 TYR C 108 -77.49 -113.81
REMARK 500 TYR C 161 66.86 -118.82
REMARK 500 ARG C 264 72.07 -104.77
REMARK 500 ALA C 273 40.40 -141.70
REMARK 500 VAL C 275 76.85 -116.80
REMARK 500 MET C 302 -17.34 85.15
REMARK 500 GLN C 342 68.62 3.74
REMARK 500 THR C 349 57.56 -152.70
REMARK 500 ARG C 402 39.01 70.60
REMARK 500 PHE C 404 -0.84 68.78
REMARK 500 ASN D 50 -54.00 5.80
REMARK 500 PHE D 83 -4.33 70.58
REMARK 500 THR D 109 -86.23 -108.80
REMARK 500 LYS D 402 46.12 31.86
REMARK 500 PHE D 404 -5.79 68.55
REMARK 500 MET E 36 106.51 -173.76
REMARK 500 TYR E 83 -1.65 72.52
REMARK 500 LYS E 96 -41.12 -133.05
REMARK 500 ASP E 98 132.51 -11.55
REMARK 500 TYR E 108 -77.51 -113.84
REMARK 500 TYR E 161 66.89 -118.84
REMARK 500 ARG E 264 72.14 -104.84
REMARK 500 ALA E 273 40.37 -141.69
REMARK 500 VAL E 275 76.80 -116.79
REMARK 500 MET E 302 -17.36 85.16
REMARK 500 GLN E 342 68.75 3.63
REMARK 500 THR E 349 57.57 -152.78
REMARK 500
REMARK 500 THIS ENTRY HAS 171 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 37 SER A 38 106.62
REMARK 500 ARG A 264 GLY A 265 -149.13
REMARK 500 GLY A 265 HIS A 266 -102.65
REMARK 500 ALA A 273 PRO A 274 134.12
REMARK 500 PRO C 37 SER C 38 106.61
REMARK 500 ARG C 264 GLY C 265 -149.09
REMARK 500 GLY C 265 HIS C 266 -102.66
REMARK 500 ALA C 273 PRO C 274 134.12
REMARK 500 PRO E 37 SER E 38 106.70
REMARK 500 ARG E 264 GLY E 265 -149.11
REMARK 500 GLY E 265 HIS E 266 -102.67
REMARK 500 ALA E 273 PRO E 274 134.14
REMARK 500 PRO G 37 SER G 38 106.63
REMARK 500 ARG G 264 GLY G 265 -149.14
REMARK 500 GLY G 265 HIS G 266 -102.62
REMARK 500 ALA G 273 PRO G 274 134.17
REMARK 500 PRO I 37 SER I 38 106.71
REMARK 500 ARG I 264 GLY I 265 -149.15
REMARK 500 GLY I 265 HIS I 266 -102.68
REMARK 500 ALA I 273 PRO I 274 134.13
REMARK 500 PRO K 37 SER K 38 106.67
REMARK 500 ARG K 264 GLY K 265 -149.11
REMARK 500 GLY K 265 HIS K 266 -102.61
REMARK 500 ALA K 273 PRO K 274 134.14
REMARK 500 PRO M 37 SER M 38 106.61
REMARK 500 ARG M 264 GLY M 265 -149.10
REMARK 500 GLY M 265 HIS M 266 -102.68
REMARK 500 ALA M 273 PRO M 274 134.15
REMARK 500 PRO O 37 SER O 38 106.61
REMARK 500 ARG O 264 GLY O 265 -149.13
REMARK 500 GLY O 265 HIS O 266 -102.62
REMARK 500 ALA O 273 PRO O 274 134.12
REMARK 500 PRO Q 37 SER Q 38 106.67
REMARK 500 ARG Q 264 GLY Q 265 -149.20
REMARK 500 GLY Q 265 HIS Q 266 -102.69
REMARK 500 ALA Q 273 PRO Q 274 134.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 PHE A 244 0.08 SIDE CHAIN
REMARK 500 PHE C 244 0.08 SIDE CHAIN
REMARK 500 PHE E 244 0.08 SIDE CHAIN
REMARK 500 PHE G 244 0.08 SIDE CHAIN
REMARK 500 PHE I 244 0.08 SIDE CHAIN
REMARK 500 PHE K 244 0.08 SIDE CHAIN
REMARK 500 PHE M 244 0.08 SIDE CHAIN
REMARK 500 PHE O 244 0.08 SIDE CHAIN
REMARK 500 PHE Q 244 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA A 273 28.16
REMARK 500 ALA C 273 28.13
REMARK 500 ALA E 273 28.18
REMARK 500 ALA G 273 28.19
REMARK 500 ALA I 273 28.19
REMARK 500 ALA K 273 28.17
REMARK 500 ALA M 273 28.21
REMARK 500 ALA O 273 28.19
REMARK 500 ALA Q 273 28.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP A 501 O1G
REMARK 620 2 HOH A 601 O 98.6
REMARK 620 3 HOH A 602 O 89.0 166.6
REMARK 620 4 HOH A 603 O 95.7 85.3 83.0
REMARK 620 5 HOH A 604 O 166.4 92.8 78.3 78.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP C 501 O1G
REMARK 620 2 HOH C 601 O 98.6
REMARK 620 3 HOH C 602 O 89.0 166.6
REMARK 620 4 HOH C 603 O 95.7 85.4 83.0
REMARK 620 5 HOH C 604 O 166.5 92.8 78.4 78.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP E 501 O1G
REMARK 620 2 HOH E 601 O 98.6
REMARK 620 3 HOH E 602 O 89.1 166.6
REMARK 620 4 HOH E 603 O 95.7 85.3 83.0
REMARK 620 5 HOH E 604 O 166.5 92.8 78.4 78.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP G 501 O1G
REMARK 620 2 HOH G 601 O 98.6
REMARK 620 3 HOH G 602 O 89.1 166.6
REMARK 620 4 HOH G 603 O 95.7 85.3 83.0
REMARK 620 5 HOH G 604 O 166.5 92.8 78.4 78.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP I 501 O1G
REMARK 620 2 HOH I 601 O 98.6
REMARK 620 3 HOH I 602 O 89.1 166.6
REMARK 620 4 HOH I 603 O 95.7 85.4 83.0
REMARK 620 5 HOH I 604 O 166.5 92.8 78.4 78.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP K 501 O1G
REMARK 620 2 HOH K 601 O 98.6
REMARK 620 3 HOH K 602 O 89.0 166.6
REMARK 620 4 HOH K 603 O 95.7 85.4 83.0
REMARK 620 5 HOH K 604 O 166.4 92.8 78.4 78.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG M 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP M 501 O1G
REMARK 620 2 HOH M 601 O 98.6
REMARK 620 3 HOH M 602 O 89.1 166.6
REMARK 620 4 HOH M 603 O 95.7 85.3 83.0
REMARK 620 5 HOH M 604 O 166.5 92.8 78.4 78.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG O 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP O 501 O1G
REMARK 620 2 HOH O 601 O 98.6
REMARK 620 3 HOH O 602 O 89.1 166.6
REMARK 620 4 HOH O 603 O 95.7 85.3 83.0
REMARK 620 5 HOH O 604 O 166.5 92.8 78.4 78.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Q 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP Q 501 O1G
REMARK 620 2 HOH Q 601 O 98.6
REMARK 620 3 HOH Q 602 O 89.1 166.6
REMARK 620 4 HOH Q 603 O 95.7 85.4 83.0
REMARK 620 5 HOH Q 604 O 166.5 92.8 78.4 78.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 F 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP G 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP H 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 H 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP I 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP J 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 J 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP K 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP L 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 L 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP M 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG M 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP N 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 N 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP O 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG O 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP P 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 P 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP Q 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP R 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 R 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-5895 RELATED DB: EMDB
REMARK 900 MICROTUBULES STABILIZED BY GMPCPP
REMARK 900 RELATED ID: EMD-5896 RELATED DB: EMDB
REMARK 900 GDP-BOUND DYNAMIC MICROTUBULES
REMARK 900 RELATED ID: EMD-5897 RELATED DB: EMDB
REMARK 900 MICROTUBULES STABILIZED BY TAXOL
REMARK 900 RELATED ID: EMD-5898 RELATED DB: EMDB
REMARK 900 MICROTUBULES STABILIZED BY GMPCPP, WITHOUT KINESIN
REMARK 900 RELATED ID: EMD-5899 RELATED DB: EMDB
REMARK 900 MICROTUBULES BOUND TO GDP, NO KINESIN
REMARK 900 RELATED ID: 3J6E RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE OF MICROTUBULES STABILIZED BY GMPCPP
REMARK 900 RELATED ID: 3J6F RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE OF GDP-BOUND DYNAMIC MICROTUBULES
DBREF 3J6G A 1 439 UNP P02550 TBA1A_PIG 1 439
DBREF 3J6G B 1 437 UNP P02554 TBB_PIG 1 427
DBREF 3J6G C 1 439 UNP P02550 TBA1A_PIG 1 439
DBREF 3J6G D 1 437 UNP P02554 TBB_PIG 1 427
DBREF 3J6G E 1 439 UNP P02550 TBA1A_PIG 1 439
DBREF 3J6G F 1 437 UNP P02554 TBB_PIG 1 427
DBREF 3J6G G 1 439 UNP P02550 TBA1A_PIG 1 439
DBREF 3J6G H 1 437 UNP P02554 TBB_PIG 1 427
DBREF 3J6G I 1 439 UNP P02550 TBA1A_PIG 1 439
DBREF 3J6G J 1 437 UNP P02554 TBB_PIG 1 427
DBREF 3J6G K 1 439 UNP P02550 TBA1A_PIG 1 439
DBREF 3J6G L 1 437 UNP P02554 TBB_PIG 1 427
DBREF 3J6G M 1 439 UNP P02550 TBA1A_PIG 1 439
DBREF 3J6G N 1 437 UNP P02554 TBB_PIG 1 427
DBREF 3J6G O 1 439 UNP P02550 TBA1A_PIG 1 439
DBREF 3J6G P 1 437 UNP P02554 TBB_PIG 1 427
DBREF 3J6G Q 1 439 UNP P02550 TBA1A_PIG 1 439
DBREF 3J6G R 1 437 UNP P02554 TBB_PIG 1 427
SEQADV 3J6G GLY A 265 UNP P02550 ALA 265 CONFLICT
SEQADV 3J6G GLY C 265 UNP P02550 ALA 265 CONFLICT
SEQADV 3J6G GLY E 265 UNP P02550 ALA 265 CONFLICT
SEQADV 3J6G GLY G 265 UNP P02550 ALA 265 CONFLICT
SEQADV 3J6G GLY I 265 UNP P02550 ALA 265 CONFLICT
SEQADV 3J6G GLY K 265 UNP P02550 ALA 265 CONFLICT
SEQADV 3J6G GLY M 265 UNP P02550 ALA 265 CONFLICT
SEQADV 3J6G GLY O 265 UNP P02550 ALA 265 CONFLICT
SEQADV 3J6G GLY Q 265 UNP P02550 ALA 265 CONFLICT
SEQRES 1 A 439 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 A 439 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 A 439 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 A 439 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 A 439 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 A 439 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 A 439 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 A 439 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 A 439 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 A 439 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 A 439 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 A 439 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 A 439 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 A 439 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 A 439 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 A 439 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 A 439 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 A 439 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 A 439 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 A 439 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 A 439 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 A 439 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 A 439 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 A 439 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 A 439 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 A 439 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 A 439 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 A 439 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 A 439 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 A 439 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 A 439 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 A 439 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 A 439 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 A 439 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER
SEQRES 1 B 427 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 B 427 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 B 427 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 B 427 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 B 427 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 B 427 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 B 427 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 B 427 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 B 427 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 B 427 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 B 427 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 B 427 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 B 427 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 B 427 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 B 427 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 B 427 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 B 427 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 B 427 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 B 427 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 B 427 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 B 427 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 B 427 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 B 427 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 B 427 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 B 427 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 B 427 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 B 427 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 B 427 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 B 427 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 B 427 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 B 427 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 B 427 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 B 427 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP
SEQRES 1 C 439 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 C 439 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 C 439 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 C 439 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 C 439 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 C 439 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 C 439 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 C 439 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 C 439 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 C 439 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 C 439 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 C 439 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 C 439 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 C 439 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 C 439 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 C 439 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 C 439 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 C 439 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 C 439 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 C 439 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 C 439 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 C 439 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 C 439 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 C 439 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 C 439 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 C 439 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 C 439 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 C 439 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 C 439 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 C 439 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 C 439 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 C 439 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 C 439 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 C 439 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER
SEQRES 1 D 427 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 D 427 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 D 427 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 D 427 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 D 427 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 D 427 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 D 427 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 D 427 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 D 427 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 D 427 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 D 427 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 D 427 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 D 427 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 D 427 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 D 427 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 D 427 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 D 427 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 D 427 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 D 427 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 D 427 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 D 427 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 D 427 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 D 427 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 D 427 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 D 427 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 D 427 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 D 427 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 D 427 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 D 427 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 D 427 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 D 427 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 D 427 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 D 427 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP
SEQRES 1 E 439 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 E 439 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 E 439 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 E 439 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 E 439 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 E 439 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 E 439 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 E 439 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 E 439 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 E 439 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 E 439 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 E 439 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 E 439 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 E 439 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 E 439 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 E 439 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 E 439 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 E 439 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 E 439 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 E 439 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 E 439 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 E 439 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 E 439 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 E 439 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 E 439 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 E 439 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 E 439 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 E 439 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 E 439 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 E 439 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 E 439 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 E 439 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 E 439 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 E 439 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER
SEQRES 1 F 427 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 F 427 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 F 427 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 F 427 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 F 427 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 F 427 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 F 427 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 F 427 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 F 427 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 F 427 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 F 427 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 F 427 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 F 427 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 F 427 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 F 427 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 F 427 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 F 427 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 F 427 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 F 427 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 F 427 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 F 427 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 F 427 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 F 427 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 F 427 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 F 427 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 F 427 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 F 427 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 F 427 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 F 427 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 F 427 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 F 427 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 F 427 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 F 427 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP
SEQRES 1 G 439 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 G 439 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 G 439 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 G 439 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 G 439 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 G 439 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 G 439 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 G 439 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 G 439 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 G 439 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 G 439 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 G 439 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 G 439 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 G 439 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 G 439 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 G 439 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 G 439 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 G 439 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 G 439 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 G 439 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 G 439 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 G 439 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 G 439 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 G 439 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 G 439 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 G 439 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 G 439 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 G 439 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 G 439 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 G 439 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 G 439 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 G 439 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 G 439 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 G 439 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER
SEQRES 1 H 427 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 H 427 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 H 427 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 H 427 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 H 427 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 H 427 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 H 427 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 H 427 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 H 427 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 H 427 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 H 427 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 H 427 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 H 427 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 H 427 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 H 427 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 H 427 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 H 427 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 H 427 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 H 427 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 H 427 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 H 427 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 H 427 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 H 427 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 H 427 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 H 427 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 H 427 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 H 427 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 H 427 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 H 427 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 H 427 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 H 427 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 H 427 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 H 427 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP
SEQRES 1 I 439 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 I 439 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 I 439 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 I 439 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 I 439 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 I 439 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 I 439 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 I 439 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 I 439 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 I 439 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 I 439 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 I 439 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 I 439 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 I 439 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 I 439 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 I 439 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 I 439 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 I 439 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 I 439 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 I 439 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 I 439 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 I 439 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 I 439 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 I 439 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 I 439 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 I 439 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 I 439 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 I 439 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 I 439 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 I 439 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 I 439 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 I 439 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 I 439 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 I 439 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER
SEQRES 1 J 427 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 J 427 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 J 427 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 J 427 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 J 427 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 J 427 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 J 427 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 J 427 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 J 427 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 J 427 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 J 427 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 J 427 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 J 427 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 J 427 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 J 427 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 J 427 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 J 427 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 J 427 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 J 427 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 J 427 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 J 427 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 J 427 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 J 427 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 J 427 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 J 427 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 J 427 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 J 427 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 J 427 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 J 427 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 J 427 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 J 427 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 J 427 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 J 427 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP
SEQRES 1 K 439 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 K 439 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 K 439 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 K 439 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 K 439 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 K 439 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 K 439 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 K 439 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 K 439 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 K 439 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 K 439 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 K 439 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 K 439 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 K 439 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 K 439 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 K 439 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 K 439 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 K 439 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 K 439 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 K 439 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 K 439 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 K 439 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 K 439 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 K 439 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 K 439 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 K 439 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 K 439 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 K 439 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 K 439 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 K 439 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 K 439 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 K 439 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 K 439 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 K 439 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER
SEQRES 1 L 427 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 L 427 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 L 427 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 L 427 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 L 427 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 L 427 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 L 427 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 L 427 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 L 427 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 L 427 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 L 427 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 L 427 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 L 427 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 L 427 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 L 427 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 L 427 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 L 427 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 L 427 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 L 427 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 L 427 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 L 427 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 L 427 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 L 427 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 L 427 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 L 427 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 L 427 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 L 427 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 L 427 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 L 427 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 L 427 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 L 427 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 L 427 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 L 427 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP
SEQRES 1 M 439 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 M 439 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 M 439 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 M 439 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 M 439 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 M 439 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 M 439 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 M 439 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 M 439 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 M 439 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 M 439 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 M 439 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 M 439 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 M 439 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 M 439 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 M 439 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 M 439 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 M 439 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 M 439 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 M 439 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 M 439 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 M 439 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 M 439 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 M 439 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 M 439 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 M 439 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 M 439 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 M 439 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 M 439 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 M 439 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 M 439 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 M 439 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 M 439 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 M 439 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER
SEQRES 1 N 427 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 N 427 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 N 427 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 N 427 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 N 427 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 N 427 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 N 427 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 N 427 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 N 427 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 N 427 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 N 427 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 N 427 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 N 427 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 N 427 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 N 427 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 N 427 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 N 427 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 N 427 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 N 427 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 N 427 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 N 427 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 N 427 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 N 427 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 N 427 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 N 427 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 N 427 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 N 427 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 N 427 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 N 427 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 N 427 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 N 427 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 N 427 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 N 427 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP
SEQRES 1 O 439 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 O 439 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 O 439 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 O 439 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 O 439 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 O 439 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 O 439 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 O 439 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 O 439 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 O 439 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 O 439 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 O 439 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 O 439 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 O 439 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 O 439 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 O 439 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 O 439 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 O 439 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 O 439 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 O 439 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 O 439 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 O 439 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 O 439 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 O 439 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 O 439 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 O 439 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 O 439 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 O 439 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 O 439 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 O 439 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 O 439 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 O 439 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 O 439 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 O 439 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER
SEQRES 1 P 427 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 P 427 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 P 427 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 P 427 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 P 427 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 P 427 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 P 427 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 P 427 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 P 427 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 P 427 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 P 427 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 P 427 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 P 427 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 P 427 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 P 427 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 P 427 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 P 427 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 P 427 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 P 427 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 P 427 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 P 427 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 P 427 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 P 427 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 P 427 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 P 427 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 P 427 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 P 427 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 P 427 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 P 427 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 P 427 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 P 427 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 P 427 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 P 427 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP
SEQRES 1 Q 439 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 Q 439 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 Q 439 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 Q 439 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 Q 439 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 Q 439 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 Q 439 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 Q 439 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 Q 439 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 Q 439 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 Q 439 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 Q 439 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 Q 439 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 Q 439 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 Q 439 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 Q 439 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 Q 439 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 Q 439 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 Q 439 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 Q 439 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 Q 439 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 Q 439 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 Q 439 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 Q 439 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 Q 439 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 Q 439 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 Q 439 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 Q 439 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 Q 439 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 Q 439 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 Q 439 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 Q 439 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 Q 439 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 Q 439 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER
SEQRES 1 R 427 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 R 427 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 R 427 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 R 427 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 R 427 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 R 427 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 R 427 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 R 427 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 R 427 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 R 427 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 R 427 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 R 427 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 R 427 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 R 427 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 R 427 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 R 427 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 R 427 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 R 427 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 R 427 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 R 427 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 R 427 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 R 427 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 R 427 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 R 427 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 R 427 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 R 427 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 R 427 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 R 427 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 R 427 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 R 427 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 R 427 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 R 427 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 R 427 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP
HET GTP A 501 32
HET MG A 502 1
HET GDP B 501 28
HET TA1 B 502 62
HET GTP C 501 32
HET MG C 502 1
HET GDP D 501 28
HET TA1 D 502 62
HET GTP E 501 32
HET MG E 502 1
HET GDP F 501 28
HET TA1 F 502 62
HET GTP G 501 32
HET MG G 502 1
HET GDP H 501 28
HET TA1 H 502 62
HET GTP I 501 32
HET MG I 502 1
HET GDP J 501 28
HET TA1 J 502 62
HET GTP K 501 32
HET MG K 502 1
HET GDP L 501 28
HET TA1 L 502 62
HET GTP M 501 32
HET MG M 502 1
HET GDP N 501 28
HET TA1 N 502 62
HET GTP O 501 32
HET MG O 502 1
HET GDP P 501 28
HET TA1 P 502 62
HET GTP Q 501 32
HET MG Q 502 1
HET GDP R 501 28
HET TA1 R 502 62
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM TA1 TAXOL
FORMUL 19 GTP 9(C10 H16 N5 O14 P3)
FORMUL 20 MG 9(MG 2+)
FORMUL 21 GDP 9(C10 H15 N5 O11 P2)
FORMUL 22 TA1 9(C47 H51 N O14)
FORMUL 55 HOH *36(H2 O)
HELIX 1 1 GLY A 10 GLY A 29 1 20
HELIX 2 2 PRO A 72 THR A 80 1 9
HELIX 3 3 ASN A 102 TYR A 108 1 7
HELIX 4 4 ILE A 110 GLN A 128 1 19
HELIX 5 5 SER A 147 TYR A 161 1 15
HELIX 6 6 VAL A 182 SER A 198 1 17
HELIX 7 7 ASN A 206 ASN A 216 1 11
HELIX 8 8 THR A 223 PHE A 244 1 22
HELIX 9 9 ASP A 251 VAL A 260 1 10
HELIX 10 10 GLU A 279 HIS A 283 5 5
HELIX 11 11 SER A 287 PHE A 296 1 10
HELIX 12 12 GLU A 297 GLN A 301 5 5
HELIX 13 13 ASP A 306 GLY A 310 5 5
HELIX 14 14 VAL A 324 LYS A 338 1 15
HELIX 15 15 ALA A 383 ARG A 402 1 20
HELIX 16 16 VAL A 405 GLY A 410 1 6
HELIX 17 17 GLU A 414 ASP A 438 1 25
HELIX 18 18 GLY B 10 HIS B 28 1 19
HELIX 19 19 SER B 40 ARG B 48 1 7
HELIX 20 20 ILE B 49 VAL B 51 5 3
HELIX 21 21 PRO B 72 GLY B 81 1 10
HELIX 22 22 PHE B 83 PHE B 87 5 5
HELIX 23 23 ARG B 88 ASP B 90 5 3
HELIX 24 24 ASN B 102 TYR B 108 1 7
HELIX 25 25 THR B 109 CYS B 129 1 21
HELIX 26 26 SER B 147 TYR B 161 1 15
HELIX 27 27 VAL B 182 THR B 198 1 17
HELIX 28 28 ASP B 205 THR B 216 1 12
HELIX 29 29 THR B 223 PHE B 244 1 22
HELIX 30 30 ASP B 251 VAL B 260 1 10
HELIX 31 31 GLY B 279 TYR B 283 5 5
HELIX 32 32 THR B 287 ASP B 297 1 11
HELIX 33 33 ALA B 298 MET B 301 5 4
HELIX 34 34 SER B 324 ASN B 339 1 16
HELIX 35 35 SER B 340 PHE B 343 5 4
HELIX 36 36 ILE B 384 ARG B 401 1 18
HELIX 37 37 PHE B 404 GLY B 412 1 9
HELIX 38 38 ASP B 414 ASP B 437 1 24
HELIX 39 39 GLY C 10 GLY C 29 1 20
HELIX 40 40 PRO C 72 THR C 80 1 9
HELIX 41 41 ASN C 102 TYR C 108 1 7
HELIX 42 42 ILE C 110 GLN C 128 1 19
HELIX 43 43 SER C 147 TYR C 161 1 15
HELIX 44 44 VAL C 182 SER C 198 1 17
HELIX 45 45 ASN C 206 ASN C 216 1 11
HELIX 46 46 THR C 223 PHE C 244 1 22
HELIX 47 47 ASP C 251 VAL C 260 1 10
HELIX 48 48 GLU C 279 HIS C 283 5 5
HELIX 49 49 SER C 287 PHE C 296 1 10
HELIX 50 50 GLU C 297 GLN C 301 5 5
HELIX 51 51 ASP C 306 GLY C 310 5 5
HELIX 52 52 VAL C 324 LYS C 338 1 15
HELIX 53 53 ALA C 383 ARG C 402 1 20
HELIX 54 54 VAL C 405 GLY C 410 1 6
HELIX 55 55 GLU C 414 ASP C 438 1 25
HELIX 56 56 GLY D 10 HIS D 28 1 19
HELIX 57 57 SER D 40 ARG D 48 1 7
HELIX 58 58 ILE D 49 VAL D 51 5 3
HELIX 59 59 PRO D 72 GLY D 81 1 10
HELIX 60 60 PHE D 83 PHE D 87 5 5
HELIX 61 61 ARG D 88 ASP D 90 5 3
HELIX 62 62 ASN D 102 TYR D 108 1 7
HELIX 63 63 THR D 109 CYS D 129 1 21
HELIX 64 64 SER D 147 TYR D 161 1 15
HELIX 65 65 VAL D 182 THR D 198 1 17
HELIX 66 66 ASP D 205 THR D 216 1 12
HELIX 67 67 THR D 223 PHE D 244 1 22
HELIX 68 68 ASP D 251 VAL D 260 1 10
HELIX 69 69 GLY D 279 TYR D 283 5 5
HELIX 70 70 THR D 287 ASP D 297 1 11
HELIX 71 71 ALA D 298 MET D 301 5 4
HELIX 72 72 SER D 324 ASN D 339 1 16
HELIX 73 73 SER D 340 PHE D 343 5 4
HELIX 74 74 ILE D 384 ARG D 401 1 18
HELIX 75 75 PHE D 404 GLY D 412 1 9
HELIX 76 76 ASP D 414 ASP D 437 1 24
HELIX 77 77 GLY E 10 GLY E 29 1 20
HELIX 78 78 PRO E 72 THR E 80 1 9
HELIX 79 79 ASN E 102 TYR E 108 1 7
HELIX 80 80 ILE E 110 GLN E 128 1 19
HELIX 81 81 SER E 147 TYR E 161 1 15
HELIX 82 82 VAL E 182 SER E 198 1 17
HELIX 83 83 ASN E 206 ASN E 216 1 11
HELIX 84 84 THR E 223 PHE E 244 1 22
HELIX 85 85 ASP E 251 VAL E 260 1 10
HELIX 86 86 GLU E 279 HIS E 283 5 5
HELIX 87 87 SER E 287 PHE E 296 1 10
HELIX 88 88 GLU E 297 GLN E 301 5 5
HELIX 89 89 ASP E 306 GLY E 310 5 5
HELIX 90 90 VAL E 324 LYS E 338 1 15
HELIX 91 91 ALA E 383 ARG E 402 1 20
HELIX 92 92 VAL E 405 GLY E 410 1 6
HELIX 93 93 GLU E 414 ASP E 438 1 25
HELIX 94 94 GLY F 10 HIS F 28 1 19
HELIX 95 95 SER F 40 ARG F 48 1 7
HELIX 96 96 ILE F 49 VAL F 51 5 3
HELIX 97 97 PRO F 72 GLY F 81 1 10
HELIX 98 98 PHE F 83 PHE F 87 5 5
HELIX 99 99 ARG F 88 ASP F 90 5 3
HELIX 100 100 ASN F 102 TYR F 108 1 7
HELIX 101 101 THR F 109 CYS F 129 1 21
HELIX 102 102 SER F 147 TYR F 161 1 15
HELIX 103 103 VAL F 182 THR F 198 1 17
HELIX 104 104 ASP F 205 THR F 216 1 12
HELIX 105 105 THR F 223 PHE F 244 1 22
HELIX 106 106 ASP F 251 VAL F 260 1 10
HELIX 107 107 GLY F 279 TYR F 283 5 5
HELIX 108 108 THR F 287 ASP F 297 1 11
HELIX 109 109 ALA F 298 MET F 301 5 4
HELIX 110 110 SER F 324 SER F 340 1 17
HELIX 111 111 SER F 341 PHE F 343 5 3
HELIX 112 112 ILE F 384 ARG F 401 1 18
HELIX 113 113 PHE F 404 GLY F 412 1 9
HELIX 114 114 ASP F 414 ASP F 437 1 24
HELIX 115 115 GLY G 10 GLY G 29 1 20
HELIX 116 116 PRO G 72 THR G 80 1 9
HELIX 117 117 ASN G 102 TYR G 108 1 7
HELIX 118 118 ILE G 110 GLN G 128 1 19
HELIX 119 119 SER G 147 TYR G 161 1 15
HELIX 120 120 VAL G 182 SER G 198 1 17
HELIX 121 121 ASN G 206 ASN G 216 1 11
HELIX 122 122 THR G 223 PHE G 244 1 22
HELIX 123 123 ASP G 251 VAL G 260 1 10
HELIX 124 124 GLU G 279 HIS G 283 5 5
HELIX 125 125 SER G 287 PHE G 296 1 10
HELIX 126 126 GLU G 297 GLN G 301 5 5
HELIX 127 127 ASP G 306 GLY G 310 5 5
HELIX 128 128 VAL G 324 LYS G 338 1 15
HELIX 129 129 ALA G 383 ARG G 402 1 20
HELIX 130 130 VAL G 405 GLY G 410 1 6
HELIX 131 131 GLU G 414 ASP G 438 1 25
HELIX 132 132 GLY H 10 HIS H 28 1 19
HELIX 133 133 SER H 40 ARG H 48 1 7
HELIX 134 134 ILE H 49 VAL H 51 5 3
HELIX 135 135 PRO H 72 GLY H 81 1 10
HELIX 136 136 PHE H 83 PHE H 87 5 5
HELIX 137 137 ARG H 88 ASP H 90 5 3
HELIX 138 138 ASN H 102 TYR H 108 1 7
HELIX 139 139 THR H 109 CYS H 129 1 21
HELIX 140 140 SER H 147 TYR H 161 1 15
HELIX 141 141 VAL H 182 THR H 198 1 17
HELIX 142 142 ASP H 205 THR H 216 1 12
HELIX 143 143 THR H 223 PHE H 244 1 22
HELIX 144 144 ASP H 251 VAL H 260 1 10
HELIX 145 145 GLY H 279 TYR H 283 5 5
HELIX 146 146 THR H 287 ASP H 297 1 11
HELIX 147 147 ALA H 298 MET H 301 5 4
HELIX 148 148 SER H 324 ASN H 339 1 16
HELIX 149 149 SER H 340 PHE H 343 5 4
HELIX 150 150 ILE H 384 ARG H 401 1 18
HELIX 151 151 PHE H 404 GLY H 412 1 9
HELIX 152 152 ASP H 414 ASP H 437 1 24
HELIX 153 153 GLY I 10 GLY I 29 1 20
HELIX 154 154 PRO I 72 THR I 80 1 9
HELIX 155 155 ASN I 102 TYR I 108 1 7
HELIX 156 156 ILE I 110 GLN I 128 1 19
HELIX 157 157 SER I 147 TYR I 161 1 15
HELIX 158 158 VAL I 182 SER I 198 1 17
HELIX 159 159 ASN I 206 ASN I 216 1 11
HELIX 160 160 THR I 223 PHE I 244 1 22
HELIX 161 161 ASP I 251 VAL I 260 1 10
HELIX 162 162 GLU I 279 HIS I 283 5 5
HELIX 163 163 SER I 287 PHE I 296 1 10
HELIX 164 164 GLU I 297 GLN I 301 5 5
HELIX 165 165 ASP I 306 GLY I 310 5 5
HELIX 166 166 VAL I 324 LYS I 338 1 15
HELIX 167 167 ALA I 383 ARG I 402 1 20
HELIX 168 168 VAL I 405 GLY I 410 1 6
HELIX 169 169 GLU I 414 ASP I 438 1 25
HELIX 170 170 GLY J 10 HIS J 28 1 19
HELIX 171 171 SER J 40 ARG J 48 1 7
HELIX 172 172 ILE J 49 VAL J 51 5 3
HELIX 173 173 PRO J 72 GLY J 81 1 10
HELIX 174 174 PHE J 83 PHE J 87 5 5
HELIX 175 175 ARG J 88 ASP J 90 5 3
HELIX 176 176 ASN J 102 TYR J 108 1 7
HELIX 177 177 THR J 109 CYS J 129 1 21
HELIX 178 178 SER J 147 TYR J 161 1 15
HELIX 179 179 VAL J 182 THR J 198 1 17
HELIX 180 180 ASP J 205 THR J 216 1 12
HELIX 181 181 THR J 223 PHE J 244 1 22
HELIX 182 182 ASP J 251 VAL J 260 1 10
HELIX 183 183 GLY J 279 TYR J 283 5 5
HELIX 184 184 THR J 287 ASP J 297 1 11
HELIX 185 185 ALA J 298 MET J 301 5 4
HELIX 186 186 SER J 324 SER J 340 1 17
HELIX 187 187 SER J 341 PHE J 343 5 3
HELIX 188 188 ILE J 384 ARG J 401 1 18
HELIX 189 189 PHE J 404 GLY J 412 1 9
HELIX 190 190 ASP J 414 ASP J 437 1 24
HELIX 191 191 GLY K 10 GLY K 29 1 20
HELIX 192 192 PRO K 72 THR K 80 1 9
HELIX 193 193 ASN K 102 TYR K 108 1 7
HELIX 194 194 ILE K 110 GLN K 128 1 19
HELIX 195 195 SER K 147 TYR K 161 1 15
HELIX 196 196 VAL K 182 SER K 198 1 17
HELIX 197 197 ASN K 206 ASN K 216 1 11
HELIX 198 198 THR K 223 PHE K 244 1 22
HELIX 199 199 ASP K 251 VAL K 260 1 10
HELIX 200 200 GLU K 279 HIS K 283 5 5
HELIX 201 201 SER K 287 PHE K 296 1 10
HELIX 202 202 GLU K 297 GLN K 301 5 5
HELIX 203 203 ASP K 306 GLY K 310 5 5
HELIX 204 204 VAL K 324 LYS K 338 1 15
HELIX 205 205 ALA K 383 ARG K 402 1 20
HELIX 206 206 VAL K 405 GLY K 410 1 6
HELIX 207 207 GLU K 414 ASP K 438 1 25
HELIX 208 208 GLY L 10 HIS L 28 1 19
HELIX 209 209 SER L 40 ARG L 48 1 7
HELIX 210 210 ILE L 49 VAL L 51 5 3
HELIX 211 211 PRO L 72 GLY L 81 1 10
HELIX 212 212 PHE L 83 PHE L 87 5 5
HELIX 213 213 ARG L 88 ASP L 90 5 3
HELIX 214 214 ASN L 102 TYR L 108 1 7
HELIX 215 215 THR L 109 CYS L 129 1 21
HELIX 216 216 SER L 147 TYR L 161 1 15
HELIX 217 217 VAL L 182 THR L 198 1 17
HELIX 218 218 ASP L 205 THR L 216 1 12
HELIX 219 219 THR L 223 PHE L 244 1 22
HELIX 220 220 ASP L 251 VAL L 260 1 10
HELIX 221 221 GLY L 279 TYR L 283 5 5
HELIX 222 222 THR L 287 ASP L 297 1 11
HELIX 223 223 ALA L 298 MET L 301 5 4
HELIX 224 224 SER L 324 ASN L 339 1 16
HELIX 225 225 SER L 340 PHE L 343 5 4
HELIX 226 226 ILE L 384 ARG L 401 1 18
HELIX 227 227 PHE L 404 GLY L 412 1 9
HELIX 228 228 ASP L 414 ASP L 437 1 24
HELIX 229 229 GLY M 10 GLY M 29 1 20
HELIX 230 230 PRO M 72 THR M 80 1 9
HELIX 231 231 ASN M 102 TYR M 108 1 7
HELIX 232 232 ILE M 110 GLN M 128 1 19
HELIX 233 233 SER M 147 TYR M 161 1 15
HELIX 234 234 VAL M 182 SER M 198 1 17
HELIX 235 235 ASN M 206 ASN M 216 1 11
HELIX 236 236 THR M 223 PHE M 244 1 22
HELIX 237 237 ASP M 251 VAL M 260 1 10
HELIX 238 238 GLU M 279 HIS M 283 5 5
HELIX 239 239 SER M 287 PHE M 296 1 10
HELIX 240 240 GLU M 297 GLN M 301 5 5
HELIX 241 241 ASP M 306 GLY M 310 5 5
HELIX 242 242 VAL M 324 LYS M 338 1 15
HELIX 243 243 ALA M 383 ARG M 402 1 20
HELIX 244 244 VAL M 405 GLY M 410 1 6
HELIX 245 245 GLU M 414 ASP M 438 1 25
HELIX 246 246 GLY N 10 HIS N 28 1 19
HELIX 247 247 SER N 40 ARG N 48 1 7
HELIX 248 248 ILE N 49 VAL N 51 5 3
HELIX 249 249 PRO N 72 GLY N 81 1 10
HELIX 250 250 PHE N 83 PHE N 87 5 5
HELIX 251 251 ARG N 88 ASP N 90 5 3
HELIX 252 252 ASN N 102 TYR N 108 1 7
HELIX 253 253 THR N 109 CYS N 129 1 21
HELIX 254 254 SER N 147 TYR N 161 1 15
HELIX 255 255 VAL N 182 THR N 198 1 17
HELIX 256 256 ASP N 205 THR N 216 1 12
HELIX 257 257 THR N 223 PHE N 244 1 22
HELIX 258 258 ASP N 251 VAL N 260 1 10
HELIX 259 259 GLY N 279 TYR N 283 5 5
HELIX 260 260 THR N 287 ASP N 297 1 11
HELIX 261 261 ALA N 298 MET N 301 5 4
HELIX 262 262 SER N 324 ASN N 339 1 16
HELIX 263 263 SER N 340 PHE N 343 5 4
HELIX 264 264 ILE N 384 ARG N 401 1 18
HELIX 265 265 PHE N 404 GLY N 412 1 9
HELIX 266 266 ASP N 414 ASP N 437 1 24
HELIX 267 267 GLY O 10 GLY O 29 1 20
HELIX 268 268 PRO O 72 THR O 80 1 9
HELIX 269 269 ASN O 102 TYR O 108 1 7
HELIX 270 270 ILE O 110 GLN O 128 1 19
HELIX 271 271 SER O 147 TYR O 161 1 15
HELIX 272 272 VAL O 182 SER O 198 1 17
HELIX 273 273 ASN O 206 ASN O 216 1 11
HELIX 274 274 THR O 223 PHE O 244 1 22
HELIX 275 275 ASP O 251 VAL O 260 1 10
HELIX 276 276 GLU O 279 HIS O 283 5 5
HELIX 277 277 SER O 287 PHE O 296 1 10
HELIX 278 278 GLU O 297 GLN O 301 5 5
HELIX 279 279 ASP O 306 GLY O 310 5 5
HELIX 280 280 VAL O 324 LYS O 338 1 15
HELIX 281 281 ALA O 383 ARG O 402 1 20
HELIX 282 282 VAL O 405 GLY O 410 1 6
HELIX 283 283 GLU O 414 ASP O 438 1 25
HELIX 284 284 GLY P 10 HIS P 28 1 19
HELIX 285 285 SER P 40 ARG P 48 1 7
HELIX 286 286 ILE P 49 VAL P 51 5 3
HELIX 287 287 PRO P 72 GLY P 81 1 10
HELIX 288 288 PHE P 83 PHE P 87 5 5
HELIX 289 289 ARG P 88 ASP P 90 5 3
HELIX 290 290 ASN P 102 TYR P 108 1 7
HELIX 291 291 THR P 109 CYS P 129 1 21
HELIX 292 292 SER P 147 TYR P 161 1 15
HELIX 293 293 VAL P 182 THR P 198 1 17
HELIX 294 294 ASP P 205 THR P 216 1 12
HELIX 295 295 THR P 223 PHE P 244 1 22
HELIX 296 296 ASP P 251 VAL P 260 1 10
HELIX 297 297 GLY P 279 TYR P 283 5 5
HELIX 298 298 THR P 287 ASP P 297 1 11
HELIX 299 299 ALA P 298 MET P 301 5 4
HELIX 300 300 SER P 324 ASN P 339 1 16
HELIX 301 301 SER P 340 PHE P 343 5 4
HELIX 302 302 ILE P 384 ARG P 401 1 18
HELIX 303 303 PHE P 404 GLY P 412 1 9
HELIX 304 304 ASP P 414 ASP P 437 1 24
HELIX 305 305 GLY Q 10 GLY Q 29 1 20
HELIX 306 306 PRO Q 72 THR Q 80 1 9
HELIX 307 307 ASN Q 102 TYR Q 108 1 7
HELIX 308 308 ILE Q 110 GLN Q 128 1 19
HELIX 309 309 SER Q 147 TYR Q 161 1 15
HELIX 310 310 VAL Q 182 SER Q 198 1 17
HELIX 311 311 ASN Q 206 ASN Q 216 1 11
HELIX 312 312 THR Q 223 PHE Q 244 1 22
HELIX 313 313 ASP Q 251 VAL Q 260 1 10
HELIX 314 314 GLU Q 279 HIS Q 283 5 5
HELIX 315 315 SER Q 287 PHE Q 296 1 10
HELIX 316 316 GLU Q 297 GLN Q 301 5 5
HELIX 317 317 ASP Q 306 GLY Q 310 5 5
HELIX 318 318 VAL Q 324 LYS Q 338 1 15
HELIX 319 319 ALA Q 383 ARG Q 402 1 20
HELIX 320 320 VAL Q 405 GLY Q 410 1 6
HELIX 321 321 GLU Q 414 ASP Q 438 1 25
HELIX 322 322 GLY R 10 HIS R 28 1 19
HELIX 323 323 SER R 40 ARG R 48 1 7
HELIX 324 324 ILE R 49 VAL R 51 5 3
HELIX 325 325 PRO R 72 GLY R 81 1 10
HELIX 326 326 PHE R 83 PHE R 87 5 5
HELIX 327 327 ARG R 88 ASP R 90 5 3
HELIX 328 328 ASN R 102 TYR R 108 1 7
HELIX 329 329 THR R 109 CYS R 129 1 21
HELIX 330 330 SER R 147 TYR R 161 1 15
HELIX 331 331 VAL R 182 THR R 198 1 17
HELIX 332 332 ASP R 205 THR R 216 1 12
HELIX 333 333 THR R 223 PHE R 244 1 22
HELIX 334 334 ASP R 251 VAL R 260 1 10
HELIX 335 335 GLY R 279 TYR R 283 5 5
HELIX 336 336 THR R 287 ASP R 297 1 11
HELIX 337 337 ALA R 298 MET R 301 5 4
HELIX 338 338 SER R 324 SER R 340 1 17
HELIX 339 339 SER R 341 PHE R 343 5 3
HELIX 340 340 ILE R 384 ARG R 401 1 18
HELIX 341 341 PHE R 404 GLY R 412 1 9
HELIX 342 342 ASP R 414 ASP R 437 1 24
SHEET 1 A 6 LEU A 92 THR A 94 0
SHEET 2 A 6 ALA A 65 ASP A 69 1 N ASP A 69 O ILE A 93
SHEET 3 A 6 GLU A 3 VAL A 9 1 N HIS A 8 O VAL A 66
SHEET 4 A 6 LEU A 132 SER A 140 1 O SER A 136 N ILE A 7
SHEET 5 A 6 SER A 165 TYR A 172 1 O PHE A 169 N VAL A 137
SHEET 6 A 6 CYS A 200 ASP A 205 1 O CYS A 200 N GLU A 168
SHEET 1 B 2 PHE A 53 GLU A 55 0
SHEET 2 B 2 HIS A 61 PRO A 63 -1 O VAL A 62 N SER A 54
SHEET 1 C 4 LEU A 269 TYR A 272 0
SHEET 2 C 4 ARG A 373 THR A 381 -1 O SER A 379 N LEU A 269
SHEET 3 C 4 TYR A 312 GLY A 321 -1 N CYS A 316 O LEU A 378
SHEET 4 C 4 VAL A 353 ASN A 356 1 O GLY A 354 N TYR A 319
SHEET 1 D10 PHE B 92 PHE B 94 0
SHEET 2 D10 ALA B 65 ASP B 69 1 N LEU B 67 O VAL B 93
SHEET 3 D10 GLU B 3 ALA B 9 1 N GLN B 8 O VAL B 68
SHEET 4 D10 LEU B 132 SER B 140 1 O GLN B 136 N ILE B 7
SHEET 5 D10 ILE B 165 VAL B 171 1 O PHE B 169 N LEU B 137
SHEET 6 D10 GLU B 200 ILE B 204 1 O TYR B 202 N SER B 170
SHEET 7 D10 PHE B 267 PHE B 272 1 O PHE B 268 N CYS B 203
SHEET 8 D10 SER B 374 SER B 381 -1 O PHE B 377 N GLY B 271
SHEET 9 D10 TYR B 312 ARG B 320 -1 N LEU B 313 O ASN B 380
SHEET 10 D10 VAL B 351 CYS B 356 1 O LYS B 352 N VAL B 315
SHEET 1 E 2 TYR B 53 ALA B 56 0
SHEET 2 E 2 LYS B 60 PRO B 63 -1 O LYS B 60 N ALA B 56
SHEET 1 F 6 LEU C 92 THR C 94 0
SHEET 2 F 6 ALA C 65 ASP C 69 1 N ASP C 69 O ILE C 93
SHEET 3 F 6 GLU C 3 VAL C 9 1 N HIS C 8 O VAL C 66
SHEET 4 F 6 LEU C 132 SER C 140 1 O SER C 136 N ILE C 7
SHEET 5 F 6 SER C 165 TYR C 172 1 O PHE C 169 N VAL C 137
SHEET 6 F 6 CYS C 200 ASP C 205 1 O CYS C 200 N GLU C 168
SHEET 1 G 2 PHE C 53 GLU C 55 0
SHEET 2 G 2 HIS C 61 PRO C 63 -1 O VAL C 62 N SER C 54
SHEET 1 H 4 LEU C 269 TYR C 272 0
SHEET 2 H 4 ARG C 373 THR C 381 -1 O SER C 379 N LEU C 269
SHEET 3 H 4 TYR C 312 GLY C 321 -1 N CYS C 316 O LEU C 378
SHEET 4 H 4 VAL C 353 ASN C 356 1 O GLY C 354 N TYR C 319
SHEET 1 I10 PHE D 92 PHE D 94 0
SHEET 2 I10 ALA D 65 ASP D 69 1 N LEU D 67 O VAL D 93
SHEET 3 I10 GLU D 3 ALA D 9 1 N GLN D 8 O VAL D 68
SHEET 4 I10 LEU D 132 SER D 140 1 O GLN D 136 N ILE D 7
SHEET 5 I10 ILE D 165 VAL D 171 1 O PHE D 169 N LEU D 137
SHEET 6 I10 GLU D 200 ILE D 204 1 O TYR D 202 N SER D 170
SHEET 7 I10 PHE D 267 PHE D 272 1 O PHE D 268 N CYS D 203
SHEET 8 I10 SER D 374 SER D 381 -1 O PHE D 377 N GLY D 271
SHEET 9 I10 TYR D 312 ARG D 320 -1 N LEU D 313 O ASN D 380
SHEET 10 I10 VAL D 351 CYS D 356 1 O LYS D 352 N VAL D 315
SHEET 1 J 2 TYR D 53 ALA D 56 0
SHEET 2 J 2 LYS D 60 PRO D 63 -1 O LYS D 60 N ALA D 56
SHEET 1 K 6 LEU E 92 THR E 94 0
SHEET 2 K 6 ALA E 65 ASP E 69 1 N ASP E 69 O ILE E 93
SHEET 3 K 6 GLU E 3 VAL E 9 1 N HIS E 8 O VAL E 66
SHEET 4 K 6 LEU E 132 SER E 140 1 O SER E 136 N ILE E 7
SHEET 5 K 6 SER E 165 TYR E 172 1 O PHE E 169 N VAL E 137
SHEET 6 K 6 CYS E 200 ASP E 205 1 O CYS E 200 N GLU E 168
SHEET 1 L 2 PHE E 53 GLU E 55 0
SHEET 2 L 2 HIS E 61 PRO E 63 -1 O VAL E 62 N SER E 54
SHEET 1 M 4 LEU E 269 TYR E 272 0
SHEET 2 M 4 ARG E 373 THR E 381 -1 O SER E 379 N LEU E 269
SHEET 3 M 4 TYR E 312 GLY E 321 -1 N CYS E 316 O LEU E 378
SHEET 4 M 4 VAL E 353 ASN E 356 1 O GLY E 354 N TYR E 319
SHEET 1 N10 PHE F 92 PHE F 94 0
SHEET 2 N10 ALA F 65 ASP F 69 1 N LEU F 67 O VAL F 93
SHEET 3 N10 GLU F 3 ALA F 9 1 N GLN F 8 O VAL F 68
SHEET 4 N10 LEU F 132 SER F 140 1 O GLN F 136 N ILE F 7
SHEET 5 N10 ILE F 165 VAL F 171 1 O PHE F 169 N LEU F 137
SHEET 6 N10 GLU F 200 ILE F 204 1 O TYR F 202 N SER F 170
SHEET 7 N10 PHE F 267 PHE F 272 1 O PHE F 268 N CYS F 203
SHEET 8 N10 SER F 374 SER F 381 -1 O PHE F 377 N GLY F 271
SHEET 9 N10 TYR F 312 ARG F 320 -1 N LEU F 313 O ASN F 380
SHEET 10 N10 VAL F 351 CYS F 356 1 O LYS F 352 N VAL F 315
SHEET 1 O 2 TYR F 53 ALA F 56 0
SHEET 2 O 2 LYS F 60 PRO F 63 -1 O LYS F 60 N ALA F 56
SHEET 1 P 6 LEU G 92 THR G 94 0
SHEET 2 P 6 ALA G 65 ASP G 69 1 N ASP G 69 O ILE G 93
SHEET 3 P 6 GLU G 3 VAL G 9 1 N HIS G 8 O VAL G 66
SHEET 4 P 6 LEU G 132 SER G 140 1 O SER G 136 N ILE G 7
SHEET 5 P 6 SER G 165 TYR G 172 1 O PHE G 169 N VAL G 137
SHEET 6 P 6 CYS G 200 ASP G 205 1 O CYS G 200 N GLU G 168
SHEET 1 Q 2 PHE G 53 GLU G 55 0
SHEET 2 Q 2 HIS G 61 PRO G 63 -1 O VAL G 62 N SER G 54
SHEET 1 R 4 LEU G 269 TYR G 272 0
SHEET 2 R 4 ARG G 373 THR G 381 -1 O SER G 379 N LEU G 269
SHEET 3 R 4 TYR G 312 GLY G 321 -1 N CYS G 316 O LEU G 378
SHEET 4 R 4 VAL G 353 ASN G 356 1 O GLY G 354 N TYR G 319
SHEET 1 S10 PHE H 92 PHE H 94 0
SHEET 2 S10 ALA H 65 ASP H 69 1 N LEU H 67 O VAL H 93
SHEET 3 S10 GLU H 3 ALA H 9 1 N GLN H 8 O VAL H 68
SHEET 4 S10 LEU H 132 SER H 140 1 O GLN H 136 N ILE H 7
SHEET 5 S10 ILE H 165 VAL H 171 1 O PHE H 169 N LEU H 137
SHEET 6 S10 GLU H 200 ILE H 204 1 O TYR H 202 N SER H 170
SHEET 7 S10 PHE H 267 PHE H 272 1 O PHE H 268 N CYS H 203
SHEET 8 S10 SER H 374 SER H 381 -1 O PHE H 377 N GLY H 271
SHEET 9 S10 TYR H 312 ARG H 320 -1 N LEU H 313 O ASN H 380
SHEET 10 S10 VAL H 351 CYS H 356 1 O LYS H 352 N VAL H 315
SHEET 1 T 2 TYR H 53 ALA H 56 0
SHEET 2 T 2 LYS H 60 PRO H 63 -1 O LYS H 60 N ALA H 56
SHEET 1 U 6 LEU I 92 THR I 94 0
SHEET 2 U 6 ALA I 65 ASP I 69 1 N ASP I 69 O ILE I 93
SHEET 3 U 6 GLU I 3 VAL I 9 1 N HIS I 8 O VAL I 66
SHEET 4 U 6 LEU I 132 SER I 140 1 O SER I 136 N ILE I 7
SHEET 5 U 6 SER I 165 TYR I 172 1 O PHE I 169 N VAL I 137
SHEET 6 U 6 CYS I 200 ASP I 205 1 O CYS I 200 N GLU I 168
SHEET 1 V 2 PHE I 53 GLU I 55 0
SHEET 2 V 2 HIS I 61 PRO I 63 -1 O VAL I 62 N SER I 54
SHEET 1 W 4 LEU I 269 TYR I 272 0
SHEET 2 W 4 ARG I 373 THR I 381 -1 O SER I 379 N LEU I 269
SHEET 3 W 4 TYR I 312 GLY I 321 -1 N CYS I 316 O LEU I 378
SHEET 4 W 4 VAL I 353 ASN I 356 1 O GLY I 354 N TYR I 319
SHEET 1 X10 PHE J 92 PHE J 94 0
SHEET 2 X10 ALA J 65 ASP J 69 1 N LEU J 67 O VAL J 93
SHEET 3 X10 GLU J 3 ALA J 9 1 N GLN J 8 O VAL J 68
SHEET 4 X10 LEU J 132 SER J 140 1 O GLN J 136 N ILE J 7
SHEET 5 X10 ILE J 165 VAL J 171 1 O PHE J 169 N LEU J 137
SHEET 6 X10 GLU J 200 ILE J 204 1 O TYR J 202 N SER J 170
SHEET 7 X10 PHE J 267 PHE J 272 1 O PHE J 268 N CYS J 203
SHEET 8 X10 SER J 374 SER J 381 -1 O PHE J 377 N GLY J 271
SHEET 9 X10 TYR J 312 ARG J 320 -1 N LEU J 313 O ASN J 380
SHEET 10 X10 VAL J 351 CYS J 356 1 O LYS J 352 N VAL J 315
SHEET 1 Y 2 TYR J 53 ALA J 56 0
SHEET 2 Y 2 LYS J 60 PRO J 63 -1 O LYS J 60 N ALA J 56
SHEET 1 Z 6 LEU K 92 THR K 94 0
SHEET 2 Z 6 ALA K 65 ASP K 69 1 N ASP K 69 O ILE K 93
SHEET 3 Z 6 GLU K 3 VAL K 9 1 N HIS K 8 O VAL K 66
SHEET 4 Z 6 LEU K 132 SER K 140 1 O SER K 136 N ILE K 7
SHEET 5 Z 6 SER K 165 TYR K 172 1 O PHE K 169 N VAL K 137
SHEET 6 Z 6 CYS K 200 ASP K 205 1 O CYS K 200 N GLU K 168
SHEET 1 AA 2 PHE K 53 GLU K 55 0
SHEET 2 AA 2 HIS K 61 PRO K 63 -1 O VAL K 62 N SER K 54
SHEET 1 AB 4 LEU K 269 TYR K 272 0
SHEET 2 AB 4 ARG K 373 THR K 381 -1 O SER K 379 N LEU K 269
SHEET 3 AB 4 TYR K 312 GLY K 321 -1 N CYS K 316 O LEU K 378
SHEET 4 AB 4 VAL K 353 ASN K 356 1 O GLY K 354 N TYR K 319
SHEET 1 AC10 PHE L 92 PHE L 94 0
SHEET 2 AC10 ALA L 65 ASP L 69 1 N LEU L 67 O VAL L 93
SHEET 3 AC10 GLU L 3 ALA L 9 1 N GLN L 8 O VAL L 68
SHEET 4 AC10 LEU L 132 SER L 140 1 O GLN L 136 N ILE L 7
SHEET 5 AC10 ILE L 165 VAL L 171 1 O PHE L 169 N LEU L 137
SHEET 6 AC10 GLU L 200 ILE L 204 1 O TYR L 202 N SER L 170
SHEET 7 AC10 PHE L 267 PHE L 272 1 O PHE L 268 N CYS L 203
SHEET 8 AC10 SER L 374 SER L 381 -1 O PHE L 377 N GLY L 271
SHEET 9 AC10 TYR L 312 ARG L 320 -1 N LEU L 313 O ASN L 380
SHEET 10 AC10 VAL L 351 CYS L 356 1 O LYS L 352 N VAL L 315
SHEET 1 AD 2 TYR L 53 ALA L 56 0
SHEET 2 AD 2 LYS L 60 PRO L 63 -1 O LYS L 60 N ALA L 56
SHEET 1 AE 6 LEU M 92 THR M 94 0
SHEET 2 AE 6 ALA M 65 ASP M 69 1 N ASP M 69 O ILE M 93
SHEET 3 AE 6 GLU M 3 VAL M 9 1 N HIS M 8 O VAL M 66
SHEET 4 AE 6 LEU M 132 SER M 140 1 O SER M 136 N ILE M 7
SHEET 5 AE 6 SER M 165 TYR M 172 1 O PHE M 169 N VAL M 137
SHEET 6 AE 6 CYS M 200 ASP M 205 1 O CYS M 200 N GLU M 168
SHEET 1 AF 2 PHE M 53 GLU M 55 0
SHEET 2 AF 2 HIS M 61 PRO M 63 -1 O VAL M 62 N SER M 54
SHEET 1 AG 4 LEU M 269 TYR M 272 0
SHEET 2 AG 4 ARG M 373 THR M 381 -1 O SER M 379 N LEU M 269
SHEET 3 AG 4 TYR M 312 GLY M 321 -1 N CYS M 316 O LEU M 378
SHEET 4 AG 4 VAL M 353 ASN M 356 1 O GLY M 354 N TYR M 319
SHEET 1 AH10 PHE N 92 PHE N 94 0
SHEET 2 AH10 ALA N 65 ASP N 69 1 N LEU N 67 O VAL N 93
SHEET 3 AH10 GLU N 3 ALA N 9 1 N GLN N 8 O VAL N 68
SHEET 4 AH10 LEU N 132 SER N 140 1 O GLN N 136 N ILE N 7
SHEET 5 AH10 ILE N 165 VAL N 171 1 O PHE N 169 N LEU N 137
SHEET 6 AH10 GLU N 200 ILE N 204 1 O TYR N 202 N SER N 170
SHEET 7 AH10 PHE N 267 PHE N 272 1 O PHE N 268 N CYS N 203
SHEET 8 AH10 SER N 374 SER N 381 -1 O PHE N 377 N GLY N 271
SHEET 9 AH10 TYR N 312 ARG N 320 -1 N LEU N 313 O ASN N 380
SHEET 10 AH10 VAL N 351 CYS N 356 1 O LYS N 352 N VAL N 315
SHEET 1 AI 2 TYR N 53 ALA N 56 0
SHEET 2 AI 2 LYS N 60 PRO N 63 -1 O LYS N 60 N ALA N 56
SHEET 1 AJ 6 LEU O 92 THR O 94 0
SHEET 2 AJ 6 ALA O 65 ASP O 69 1 N ASP O 69 O ILE O 93
SHEET 3 AJ 6 GLU O 3 VAL O 9 1 N HIS O 8 O VAL O 66
SHEET 4 AJ 6 LEU O 132 SER O 140 1 O SER O 136 N ILE O 7
SHEET 5 AJ 6 SER O 165 TYR O 172 1 O PHE O 169 N VAL O 137
SHEET 6 AJ 6 CYS O 200 ASP O 205 1 O CYS O 200 N GLU O 168
SHEET 1 AK 2 PHE O 53 GLU O 55 0
SHEET 2 AK 2 HIS O 61 PRO O 63 -1 O VAL O 62 N SER O 54
SHEET 1 AL 4 LEU O 269 TYR O 272 0
SHEET 2 AL 4 ARG O 373 THR O 381 -1 O SER O 379 N LEU O 269
SHEET 3 AL 4 TYR O 312 GLY O 321 -1 N CYS O 316 O LEU O 378
SHEET 4 AL 4 VAL O 353 ASN O 356 1 O GLY O 354 N TYR O 319
SHEET 1 AM10 PHE P 92 PHE P 94 0
SHEET 2 AM10 ALA P 65 ASP P 69 1 N LEU P 67 O VAL P 93
SHEET 3 AM10 GLU P 3 ALA P 9 1 N GLN P 8 O VAL P 68
SHEET 4 AM10 LEU P 132 SER P 140 1 O GLN P 136 N ILE P 7
SHEET 5 AM10 ILE P 165 VAL P 171 1 O PHE P 169 N LEU P 137
SHEET 6 AM10 GLU P 200 ILE P 204 1 O TYR P 202 N SER P 170
SHEET 7 AM10 PHE P 267 PHE P 272 1 O PHE P 268 N CYS P 203
SHEET 8 AM10 SER P 374 SER P 381 -1 O PHE P 377 N GLY P 271
SHEET 9 AM10 TYR P 312 ARG P 320 -1 N LEU P 313 O ASN P 380
SHEET 10 AM10 VAL P 351 CYS P 356 1 O LYS P 352 N VAL P 315
SHEET 1 AN 2 TYR P 53 ALA P 56 0
SHEET 2 AN 2 LYS P 60 PRO P 63 -1 O LYS P 60 N ALA P 56
SHEET 1 AO 6 LEU Q 92 THR Q 94 0
SHEET 2 AO 6 ALA Q 65 ASP Q 69 1 N ASP Q 69 O ILE Q 93
SHEET 3 AO 6 GLU Q 3 VAL Q 9 1 N HIS Q 8 O VAL Q 66
SHEET 4 AO 6 LEU Q 132 SER Q 140 1 O SER Q 136 N ILE Q 7
SHEET 5 AO 6 SER Q 165 TYR Q 172 1 O PHE Q 169 N VAL Q 137
SHEET 6 AO 6 CYS Q 200 ASP Q 205 1 O CYS Q 200 N GLU Q 168
SHEET 1 AP 2 PHE Q 53 GLU Q 55 0
SHEET 2 AP 2 HIS Q 61 PRO Q 63 -1 O VAL Q 62 N SER Q 54
SHEET 1 AQ 4 LEU Q 269 TYR Q 272 0
SHEET 2 AQ 4 ARG Q 373 THR Q 381 -1 O SER Q 379 N LEU Q 269
SHEET 3 AQ 4 TYR Q 312 GLY Q 321 -1 N CYS Q 316 O LEU Q 378
SHEET 4 AQ 4 VAL Q 353 ASN Q 356 1 O GLY Q 354 N TYR Q 319
SHEET 1 AR10 PHE R 92 PHE R 94 0
SHEET 2 AR10 ALA R 65 ASP R 69 1 N LEU R 67 O VAL R 93
SHEET 3 AR10 GLU R 3 ALA R 9 1 N GLN R 8 O VAL R 68
SHEET 4 AR10 LEU R 132 SER R 140 1 O GLN R 136 N ILE R 7
SHEET 5 AR10 ILE R 165 VAL R 171 1 O PHE R 169 N LEU R 137
SHEET 6 AR10 GLU R 200 ILE R 204 1 O TYR R 202 N SER R 170
SHEET 7 AR10 PHE R 267 PHE R 272 1 O PHE R 268 N CYS R 203
SHEET 8 AR10 SER R 374 SER R 381 -1 O PHE R 377 N GLY R 271
SHEET 9 AR10 TYR R 312 ARG R 320 -1 N LEU R 313 O ASN R 380
SHEET 10 AR10 VAL R 351 CYS R 356 1 O LYS R 352 N VAL R 315
SHEET 1 AS 2 TYR R 53 ALA R 56 0
SHEET 2 AS 2 LYS R 60 PRO R 63 -1 O LYS R 60 N ALA R 56
LINK O1G GTP A 501 MG MG A 502 1555 1555 2.45
LINK MG MG A 502 O HOH A 601 1555 1555 2.07
LINK MG MG A 502 O HOH A 602 1555 1555 2.31
LINK MG MG A 502 O HOH A 603 1555 1555 2.44
LINK MG MG A 502 O HOH A 604 1555 1555 2.29
LINK O1G GTP C 501 MG MG C 502 1555 1555 2.45
LINK MG MG C 502 O HOH C 601 1555 1555 2.07
LINK MG MG C 502 O HOH C 602 1555 1555 2.31
LINK MG MG C 502 O HOH C 603 1555 1555 2.44
LINK MG MG C 502 O HOH C 604 1555 1555 2.29
LINK O1G GTP E 501 MG MG E 502 1555 1555 2.45
LINK MG MG E 502 O HOH E 601 1555 1555 2.07
LINK MG MG E 502 O HOH E 602 1555 1555 2.31
LINK MG MG E 502 O HOH E 603 1555 1555 2.43
LINK MG MG E 502 O HOH E 604 1555 1555 2.29
LINK O1G GTP G 501 MG MG G 502 1555 1555 2.45
LINK MG MG G 502 O HOH G 601 1555 1555 2.07
LINK MG MG G 502 O HOH G 602 1555 1555 2.31
LINK MG MG G 502 O HOH G 603 1555 1555 2.44
LINK MG MG G 502 O HOH G 604 1555 1555 2.29
LINK O1G GTP I 501 MG MG I 502 1555 1555 2.45
LINK MG MG I 502 O HOH I 601 1555 1555 2.07
LINK MG MG I 502 O HOH I 602 1555 1555 2.31
LINK MG MG I 502 O HOH I 603 1555 1555 2.44
LINK MG MG I 502 O HOH I 604 1555 1555 2.29
LINK O1G GTP K 501 MG MG K 502 1555 1555 2.45
LINK MG MG K 502 O HOH K 601 1555 1555 2.07
LINK MG MG K 502 O HOH K 602 1555 1555 2.31
LINK MG MG K 502 O HOH K 603 1555 1555 2.43
LINK MG MG K 502 O HOH K 604 1555 1555 2.29
LINK O1G GTP M 501 MG MG M 502 1555 1555 2.45
LINK MG MG M 502 O HOH M 601 1555 1555 2.07
LINK MG MG M 502 O HOH M 602 1555 1555 2.31
LINK MG MG M 502 O HOH M 603 1555 1555 2.44
LINK MG MG M 502 O HOH M 604 1555 1555 2.29
LINK O1G GTP O 501 MG MG O 502 1555 1555 2.45
LINK MG MG O 502 O HOH O 601 1555 1555 2.07
LINK MG MG O 502 O HOH O 602 1555 1555 2.31
LINK MG MG O 502 O HOH O 603 1555 1555 2.44
LINK MG MG O 502 O HOH O 604 1555 1555 2.29
LINK O1G GTP Q 501 MG MG Q 502 1555 1555 2.45
LINK MG MG Q 502 O HOH Q 601 1555 1555 2.07
LINK MG MG Q 502 O HOH Q 602 1555 1555 2.31
LINK MG MG Q 502 O HOH Q 603 1555 1555 2.43
LINK MG MG Q 502 O HOH Q 604 1555 1555 2.29
CISPEP 1 GLN B 96 SER B 97 0 -0.85
CISPEP 2 GLN D 96 SER D 97 0 -0.85
CISPEP 3 GLN F 96 SER F 97 0 -0.87
CISPEP 4 GLN H 96 SER H 97 0 -0.78
CISPEP 5 GLN J 96 SER J 97 0 -0.84
CISPEP 6 GLN L 96 SER L 97 0 -0.81
CISPEP 7 GLN N 96 SER N 97 0 -0.81
CISPEP 8 GLN P 96 SER P 97 0 -0.82
CISPEP 9 GLN R 96 SER R 97 0 -0.84
SITE 1 AC1 17 GLN A 11 ALA A 12 GLN A 15 ASN A 101
SITE 2 AC1 17 SER A 140 GLY A 143 GLY A 144 THR A 145
SITE 3 AC1 17 GLY A 146 ILE A 171 GLU A 183 ASN A 206
SITE 4 AC1 17 TYR A 224 ASN A 228 MG A 502 HOH A 601
SITE 5 AC1 17 LYS B 254
SITE 1 AC2 5 GTP A 501 HOH A 601 HOH A 602 HOH A 603
SITE 2 AC2 5 HOH A 604
SITE 1 AC3 13 GLN B 11 CYS B 12 GLN B 15 ASN B 101
SITE 2 AC3 13 SER B 140 GLY B 143 GLY B 144 THR B 145
SITE 3 AC3 13 GLY B 146 GLU B 183 ASN B 206 TYR B 224
SITE 4 AC3 13 ASN B 228
SITE 1 AC4 13 VAL B 23 ASP B 26 ASP B 226 HIS B 229
SITE 2 AC4 13 LEU B 230 ALA B 233 SER B 236 PHE B 272
SITE 3 AC4 13 PRO B 274 THR B 276 GLN B 281 ARG B 369
SITE 4 AC4 13 LEU B 371
SITE 1 AC5 17 GLN C 11 ALA C 12 GLN C 15 ASN C 101
SITE 2 AC5 17 SER C 140 GLY C 143 GLY C 144 THR C 145
SITE 3 AC5 17 GLY C 146 ILE C 171 GLU C 183 ASN C 206
SITE 4 AC5 17 TYR C 224 ASN C 228 MG C 502 HOH C 601
SITE 5 AC5 17 LYS D 254
SITE 1 AC6 5 GTP C 501 HOH C 601 HOH C 602 HOH C 603
SITE 2 AC6 5 HOH C 604
SITE 1 AC7 13 GLN D 11 CYS D 12 GLN D 15 ASN D 101
SITE 2 AC7 13 SER D 140 GLY D 143 GLY D 144 THR D 145
SITE 3 AC7 13 GLY D 146 GLU D 183 ASN D 206 TYR D 224
SITE 4 AC7 13 ASN D 228
SITE 1 AC8 13 VAL D 23 ASP D 26 ASP D 226 HIS D 229
SITE 2 AC8 13 LEU D 230 ALA D 233 SER D 236 PHE D 272
SITE 3 AC8 13 PRO D 274 THR D 276 GLN D 281 ARG D 369
SITE 4 AC8 13 LEU D 371
SITE 1 AC9 17 GLN E 11 ALA E 12 GLN E 15 ASN E 101
SITE 2 AC9 17 SER E 140 GLY E 143 GLY E 144 THR E 145
SITE 3 AC9 17 GLY E 146 ILE E 171 GLU E 183 ASN E 206
SITE 4 AC9 17 TYR E 224 ASN E 228 MG E 502 HOH E 601
SITE 5 AC9 17 LYS F 254
SITE 1 BC1 5 GTP E 501 HOH E 601 HOH E 602 HOH E 603
SITE 2 BC1 5 HOH E 604
SITE 1 BC2 13 GLN F 11 CYS F 12 GLN F 15 ASN F 101
SITE 2 BC2 13 SER F 140 GLY F 143 GLY F 144 THR F 145
SITE 3 BC2 13 GLY F 146 GLU F 183 ASN F 206 TYR F 224
SITE 4 BC2 13 ASN F 228
SITE 1 BC3 13 VAL F 23 ASP F 26 ASP F 226 HIS F 229
SITE 2 BC3 13 LEU F 230 ALA F 233 SER F 236 PHE F 272
SITE 3 BC3 13 PRO F 274 THR F 276 GLN F 281 ARG F 369
SITE 4 BC3 13 LEU F 371
SITE 1 BC4 17 GLN G 11 ALA G 12 GLN G 15 ASN G 101
SITE 2 BC4 17 SER G 140 GLY G 143 GLY G 144 THR G 145
SITE 3 BC4 17 GLY G 146 ILE G 171 GLU G 183 ASN G 206
SITE 4 BC4 17 TYR G 224 ASN G 228 MG G 502 HOH G 601
SITE 5 BC4 17 LYS H 254
SITE 1 BC5 5 GTP G 501 HOH G 601 HOH G 602 HOH G 603
SITE 2 BC5 5 HOH G 604
SITE 1 BC6 13 GLN H 11 CYS H 12 GLN H 15 ASN H 101
SITE 2 BC6 13 SER H 140 GLY H 143 GLY H 144 THR H 145
SITE 3 BC6 13 GLY H 146 GLU H 183 ASN H 206 TYR H 224
SITE 4 BC6 13 ASN H 228
SITE 1 BC7 13 VAL H 23 ASP H 26 ASP H 226 HIS H 229
SITE 2 BC7 13 LEU H 230 ALA H 233 SER H 236 PHE H 272
SITE 3 BC7 13 PRO H 274 THR H 276 GLN H 281 ARG H 369
SITE 4 BC7 13 LEU H 371
SITE 1 BC8 17 GLN I 11 ALA I 12 GLN I 15 ASN I 101
SITE 2 BC8 17 SER I 140 GLY I 143 GLY I 144 THR I 145
SITE 3 BC8 17 GLY I 146 ILE I 171 GLU I 183 ASN I 206
SITE 4 BC8 17 TYR I 224 ASN I 228 MG I 502 HOH I 601
SITE 5 BC8 17 LYS J 254
SITE 1 BC9 5 GTP I 501 HOH I 601 HOH I 602 HOH I 603
SITE 2 BC9 5 HOH I 604
SITE 1 CC1 13 GLN J 11 CYS J 12 GLN J 15 ASN J 101
SITE 2 CC1 13 SER J 140 GLY J 143 GLY J 144 THR J 145
SITE 3 CC1 13 GLY J 146 GLU J 183 ASN J 206 TYR J 224
SITE 4 CC1 13 ASN J 228
SITE 1 CC2 13 VAL J 23 ASP J 26 ASP J 226 HIS J 229
SITE 2 CC2 13 LEU J 230 ALA J 233 SER J 236 PHE J 272
SITE 3 CC2 13 PRO J 274 THR J 276 GLN J 281 ARG J 369
SITE 4 CC2 13 LEU J 371
SITE 1 CC3 17 GLN K 11 ALA K 12 GLN K 15 ASN K 101
SITE 2 CC3 17 SER K 140 GLY K 143 GLY K 144 THR K 145
SITE 3 CC3 17 GLY K 146 ILE K 171 GLU K 183 ASN K 206
SITE 4 CC3 17 TYR K 224 ASN K 228 MG K 502 HOH K 601
SITE 5 CC3 17 LYS L 254
SITE 1 CC4 5 GTP K 501 HOH K 601 HOH K 602 HOH K 603
SITE 2 CC4 5 HOH K 604
SITE 1 CC5 13 GLN L 11 CYS L 12 GLN L 15 ASN L 101
SITE 2 CC5 13 SER L 140 GLY L 143 GLY L 144 THR L 145
SITE 3 CC5 13 GLY L 146 GLU L 183 ASN L 206 TYR L 224
SITE 4 CC5 13 ASN L 228
SITE 1 CC6 13 VAL L 23 ASP L 26 ASP L 226 HIS L 229
SITE 2 CC6 13 LEU L 230 ALA L 233 SER L 236 PHE L 272
SITE 3 CC6 13 PRO L 274 THR L 276 GLN L 281 ARG L 369
SITE 4 CC6 13 LEU L 371
SITE 1 CC7 17 GLN M 11 ALA M 12 GLN M 15 ASN M 101
SITE 2 CC7 17 SER M 140 GLY M 143 GLY M 144 THR M 145
SITE 3 CC7 17 GLY M 146 ILE M 171 GLU M 183 ASN M 206
SITE 4 CC7 17 TYR M 224 ASN M 228 MG M 502 HOH M 601
SITE 5 CC7 17 LYS N 254
SITE 1 CC8 5 GTP M 501 HOH M 601 HOH M 602 HOH M 603
SITE 2 CC8 5 HOH M 604
SITE 1 CC9 13 GLN N 11 CYS N 12 GLN N 15 ASN N 101
SITE 2 CC9 13 SER N 140 GLY N 143 GLY N 144 THR N 145
SITE 3 CC9 13 GLY N 146 GLU N 183 ASN N 206 TYR N 224
SITE 4 CC9 13 ASN N 228
SITE 1 DC1 13 VAL N 23 ASP N 26 ASP N 226 HIS N 229
SITE 2 DC1 13 LEU N 230 ALA N 233 SER N 236 PHE N 272
SITE 3 DC1 13 PRO N 274 THR N 276 GLN N 281 ARG N 369
SITE 4 DC1 13 LEU N 371
SITE 1 DC2 17 GLN O 11 ALA O 12 GLN O 15 ASN O 101
SITE 2 DC2 17 SER O 140 GLY O 143 GLY O 144 THR O 145
SITE 3 DC2 17 GLY O 146 ILE O 171 GLU O 183 ASN O 206
SITE 4 DC2 17 TYR O 224 ASN O 228 MG O 502 HOH O 601
SITE 5 DC2 17 LYS P 254
SITE 1 DC3 5 GTP O 501 HOH O 601 HOH O 602 HOH O 603
SITE 2 DC3 5 HOH O 604
SITE 1 DC4 13 GLN P 11 CYS P 12 GLN P 15 ASN P 101
SITE 2 DC4 13 SER P 140 GLY P 143 GLY P 144 THR P 145
SITE 3 DC4 13 GLY P 146 GLU P 183 ASN P 206 TYR P 224
SITE 4 DC4 13 ASN P 228
SITE 1 DC5 13 VAL P 23 ASP P 26 ASP P 226 HIS P 229
SITE 2 DC5 13 LEU P 230 ALA P 233 SER P 236 PHE P 272
SITE 3 DC5 13 PRO P 274 THR P 276 GLN P 281 ARG P 369
SITE 4 DC5 13 LEU P 371
SITE 1 DC6 17 GLN Q 11 ALA Q 12 GLN Q 15 ASN Q 101
SITE 2 DC6 17 SER Q 140 GLY Q 143 GLY Q 144 THR Q 145
SITE 3 DC6 17 GLY Q 146 ILE Q 171 GLU Q 183 ASN Q 206
SITE 4 DC6 17 TYR Q 224 ASN Q 228 MG Q 502 HOH Q 601
SITE 5 DC6 17 LYS R 254
SITE 1 DC7 5 GTP Q 501 HOH Q 601 HOH Q 602 HOH Q 603
SITE 2 DC7 5 HOH Q 604
SITE 1 DC8 13 GLN R 11 CYS R 12 GLN R 15 ASN R 101
SITE 2 DC8 13 SER R 140 GLY R 143 GLY R 144 THR R 145
SITE 3 DC8 13 GLY R 146 GLU R 183 ASN R 206 TYR R 224
SITE 4 DC8 13 ASN R 228
SITE 1 DC9 13 VAL R 23 ASP R 26 ASP R 226 HIS R 229
SITE 2 DC9 13 LEU R 230 ALA R 233 SER R 236 PHE R 272
SITE 3 DC9 13 PRO R 274 THR R 276 GLN R 281 ARG R 369
SITE 4 DC9 13 LEU R 371
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
