HEADER STRUCTURAL PROTEIN 18-SEP-10 2XRP
TITLE HUMAN DOUBLECORTIN N-DC REPEAT (1MJD) AND MAMMALIAN TUBULIN (1JFF AND
TITLE 2 3HKE) DOCKED INTO THE 8-ANGSTROM CRYO-EM MAP OF DOUBLECORTIN-
TITLE 3 STABILISED MICROTUBULES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUBULIN BETA-2B CHAIN;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 SYNONYM: TUBULIN BETA CHAIN;
COMPND 5 EC: 3.6.5.6;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TUBULIN ALPHA-1D CHAIN;
COMPND 8 CHAIN: B, D, F, H;
COMPND 9 SYNONYM: TUBULIN ALPHA CHAIN;
COMPND 10 EC: 3.6.5.6;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: NEURONAL MIGRATION PROTEIN DOUBLECORTIN;
COMPND 13 CHAIN: I;
COMPND 14 FRAGMENT: RESIDUES 46-140;
COMPND 15 SYNONYM: DOUBLECORTIN, LISSENCEPHALIN-X, LIS-X, DOUBLIN;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 8 ORGANISM_COMMON: CATTLE;
SOURCE 9 ORGANISM_TAXID: 9913;
SOURCE 10 ORGAN: BRAIN;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 ORGAN: BRAIN;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS STRUCTURAL PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR F.J.FOURNIOL,C.V.SINDELAR,B.AMIGUES,D.K.CLARE,G.THOMAS,M.PERDERISET,
AUTHOR 2 F.FRANCIS,A.HOUDUSSE,C.A.MOORES
REVDAT 3 23-AUG-17 2XRP 1 REMARK ATOM
REVDAT 2 21-MAR-12 2XRP 1 REMARK VERSN
REVDAT 1 24-NOV-10 2XRP 0
JRNL AUTH F.J.FOURNIOL,C.V.SINDELAR,B.AMIGUES,D.K.CLARE,G.THOMAS,
JRNL AUTH 2 M.PERDERISET,F.FRANCIS,A.HOUDUSSE,C.A.MOORES
JRNL TITL TEMPLATE-FREE 13-PROTOFILAMENT MICROTUBULE-MAP ASSEMBLY
JRNL TITL 2 VISUALIZED AT 8 A RESOLUTION.
JRNL REF J.CELL BIOL. V. 191 463 2010
JRNL REFN ISSN 0021-9525
JRNL PMID 20974813
JRNL DOI 10.1083/JCB.201007081
REMARK 2
REMARK 2 RESOLUTION. 8.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : FLEX-EM, UCSF CHIMERA, FREALIGN, SPIDER
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 1JFF
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : OTHER
REMARK 3 REFINEMENT TARGET : CROSS-CORRELATION COEFFICIENT
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : METHOD--LOCAL CORRELATION REFINEMENT PROTOCOL-
REMARK 3 -ELECTRON CRYSTALLOGRAPHY
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 2.800
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 8.200
REMARK 3 NUMBER OF PARTICLES : 168000
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: THE STRUCTURE WAS DETERMINED IN THE ABSENCE OF A
REMARK 3 STABILISING DRUG. SUBMISSION BASED ON EXPERIMENTAL DATA FROM
REMARK 3 EMDB EMD-1788. (DEPOSITION ID: 7535).
REMARK 4
REMARK 4 2XRP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.
REMARK 100 THE DEPOSITION ID IS D_1290045434.
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 : MICROTUBULES NUCLEATED AND
REMARK 245 STABILISED BY DOUBLECORTIN
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.20
REMARK 245 SAMPLE SUPPORT DETAILS : HOLEY CARBON
REMARK 245 SAMPLE VITRIFICATION DETAILS : LIQUID ETHANE
REMARK 245 SAMPLE BUFFER : 80MM PIPES, 1MM EGTA, 3MM
REMARK 245 MGCL2, 1MM TCEP, 0.5MM GTP
REMARK 245 PH : 6.80
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : 93.00
REMARK 245 MICROSCOPE MODEL : FEI TECNAI F20
REMARK 245 DETECTOR TYPE : KODAK SO-163 FILM
REMARK 245 MINIMUM DEFOCUS (NM) : 760.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2900.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.00
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 15.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 50000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
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 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: NONAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ALA A 438
REMARK 465 THR A 439
REMARK 465 ALA A 440
REMARK 465 ASP A 441
REMARK 465 GLU A 442
REMARK 465 GLN A 443
REMARK 465 GLY A 444
REMARK 465 GLU A 445
REMARK 465 PHE A 446
REMARK 465 GLU A 447
REMARK 465 GLU A 448
REMARK 465 GLU A 449
REMARK 465 GLU A 450
REMARK 465 GLY A 451
REMARK 465 GLU A 452
REMARK 465 ASP A 453
REMARK 465 GLU A 454
REMARK 465 ALA A 455
REMARK 465 MET B 1
REMARK 465 SER B 38
REMARK 465 ASP B 39
REMARK 465 LYS B 40
REMARK 465 THR B 41
REMARK 465 ILE B 42
REMARK 465 GLY B 43
REMARK 465 GLY B 44
REMARK 465 GLY B 45
REMARK 465 ASP B 46
REMARK 465 VAL B 440
REMARK 465 GLU B 441
REMARK 465 GLY B 442
REMARK 465 GLU B 443
REMARK 465 GLY B 444
REMARK 465 GLU B 445
REMARK 465 GLU B 446
REMARK 465 GLU B 447
REMARK 465 GLU B 448
REMARK 465 GLY B 449
REMARK 465 GLU B 450
REMARK 465 GLU B 451
REMARK 465 TYR B 452
REMARK 465 MET C 1
REMARK 465 ALA C 438
REMARK 465 THR C 439
REMARK 465 ALA C 440
REMARK 465 ASP C 441
REMARK 465 GLU C 442
REMARK 465 GLN C 443
REMARK 465 GLY C 444
REMARK 465 GLU C 445
REMARK 465 PHE C 446
REMARK 465 GLU C 447
REMARK 465 GLU C 448
REMARK 465 GLU C 449
REMARK 465 GLU C 450
REMARK 465 GLY C 451
REMARK 465 GLU C 452
REMARK 465 ASP C 453
REMARK 465 GLU C 454
REMARK 465 ALA C 455
REMARK 465 MET D 1
REMARK 465 SER D 38
REMARK 465 ASP D 39
REMARK 465 LYS D 40
REMARK 465 THR D 41
REMARK 465 ILE D 42
REMARK 465 GLY D 43
REMARK 465 GLY D 44
REMARK 465 GLY D 45
REMARK 465 ASP D 46
REMARK 465 VAL D 440
REMARK 465 GLU D 441
REMARK 465 GLY D 442
REMARK 465 GLU D 443
REMARK 465 GLY D 444
REMARK 465 GLU D 445
REMARK 465 GLU D 446
REMARK 465 GLU D 447
REMARK 465 GLU D 448
REMARK 465 GLY D 449
REMARK 465 GLU D 450
REMARK 465 GLU D 451
REMARK 465 TYR D 452
REMARK 465 MET E 1
REMARK 465 ALA E 438
REMARK 465 THR E 439
REMARK 465 ALA E 440
REMARK 465 ASP E 441
REMARK 465 GLU E 442
REMARK 465 GLN E 443
REMARK 465 GLY E 444
REMARK 465 GLU E 445
REMARK 465 PHE E 446
REMARK 465 GLU E 447
REMARK 465 GLU E 448
REMARK 465 GLU E 449
REMARK 465 GLU E 450
REMARK 465 GLY E 451
REMARK 465 GLU E 452
REMARK 465 ASP E 453
REMARK 465 GLU E 454
REMARK 465 ALA E 455
REMARK 465 MET F 1
REMARK 465 SER F 38
REMARK 465 ASP F 39
REMARK 465 LYS F 40
REMARK 465 THR F 41
REMARK 465 ILE F 42
REMARK 465 GLY F 43
REMARK 465 GLY F 44
REMARK 465 GLY F 45
REMARK 465 ASP F 46
REMARK 465 VAL F 440
REMARK 465 GLU F 441
REMARK 465 GLY F 442
REMARK 465 GLU F 443
REMARK 465 GLY F 444
REMARK 465 GLU F 445
REMARK 465 GLU F 446
REMARK 465 GLU F 447
REMARK 465 GLU F 448
REMARK 465 GLY F 449
REMARK 465 GLU F 450
REMARK 465 GLU F 451
REMARK 465 TYR F 452
REMARK 465 MET G 1
REMARK 465 ALA G 438
REMARK 465 THR G 439
REMARK 465 ALA G 440
REMARK 465 ASP G 441
REMARK 465 GLU G 442
REMARK 465 GLN G 443
REMARK 465 GLY G 444
REMARK 465 GLU G 445
REMARK 465 PHE G 446
REMARK 465 GLU G 447
REMARK 465 GLU G 448
REMARK 465 GLU G 449
REMARK 465 GLU G 450
REMARK 465 GLY G 451
REMARK 465 GLU G 452
REMARK 465 ASP G 453
REMARK 465 GLU G 454
REMARK 465 ALA G 455
REMARK 465 MET H 1
REMARK 465 SER H 38
REMARK 465 ASP H 39
REMARK 465 LYS H 40
REMARK 465 THR H 41
REMARK 465 ILE H 42
REMARK 465 GLY H 43
REMARK 465 GLY H 44
REMARK 465 GLY H 45
REMARK 465 ASP H 46
REMARK 465 VAL H 440
REMARK 465 GLU H 441
REMARK 465 GLY H 442
REMARK 465 GLU H 443
REMARK 465 GLY H 444
REMARK 465 GLU H 445
REMARK 465 GLU H 446
REMARK 465 GLU H 447
REMARK 465 GLU H 448
REMARK 465 GLY H 449
REMARK 465 GLU H 450
REMARK 465 GLU H 451
REMARK 465 TYR H 452
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN B 35 CG CD OE1 NE2
REMARK 470 ASP B 47 CG OD1 OD2
REMARK 470 THR B 51 OG1 CG2
REMARK 470 GLU B 55 CG CD OE1 OE2
REMARK 470 THR B 56 OG1 CG2
REMARK 470 GLU B 77 CG CD OE1 OE2
REMARK 470 GLN B 285 CG CD OE1 NE2
REMARK 470 GLN D 35 CG CD OE1 NE2
REMARK 470 ASP D 47 CG OD1 OD2
REMARK 470 THR D 51 OG1 CG2
REMARK 470 GLU D 55 CG CD OE1 OE2
REMARK 470 THR D 56 OG1 CG2
REMARK 470 GLU D 77 CG CD OE1 OE2
REMARK 470 GLN D 285 CG CD OE1 NE2
REMARK 470 GLN F 35 CG CD OE1 NE2
REMARK 470 ASP F 47 CG OD1 OD2
REMARK 470 THR F 51 OG1 CG2
REMARK 470 GLU F 55 CG CD OE1 OE2
REMARK 470 THR F 56 OG1 CG2
REMARK 470 GLU F 77 CG CD OE1 OE2
REMARK 470 GLN F 285 CG CD OE1 NE2
REMARK 470 GLN H 35 CG CD OE1 NE2
REMARK 470 ASP H 47 CG OD1 OD2
REMARK 470 THR H 51 OG1 CG2
REMARK 470 GLU H 55 CG CD OE1 OE2
REMARK 470 THR H 56 OG1 CG2
REMARK 470 GLU H 77 CG CD OE1 OE2
REMARK 470 GLN H 285 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLN A 281 N TYR A 283 2.00
REMARK 500 O GLN C 281 N TYR C 283 2.00
REMARK 500 O GLN G 281 N TYR G 283 2.00
REMARK 500 O GLN E 281 N TYR E 283 2.00
REMARK 500 CG2 VAL G 257 CB TRP H 407 2.02
REMARK 500 O GLU B 55 N GLY B 57 2.04
REMARK 500 CG1 ILE B 5 NH1 ARG B 64 2.05
REMARK 500 CG2 VAL G 257 CG TRP H 407 2.06
REMARK 500 O ARG D 264 N HIS D 266 2.09
REMARK 500 O ARG F 264 N HIS F 266 2.09
REMARK 500 O ARG B 264 N HIS B 266 2.09
REMARK 500 O ARG H 264 N HIS H 266 2.09
REMARK 500 CE2 PHE B 296 CD1 ILE B 341 2.11
REMARK 500 CE2 PHE D 296 CD1 ILE D 341 2.11
REMARK 500 CE2 PHE F 296 CD1 ILE F 341 2.11
REMARK 500 CE2 PHE H 296 CD1 ILE H 341 2.11
REMARK 500 CD ARG C 88 OH TYR G 283 2.13
REMARK 500 OD2 ASP G 179 O2' GDP G 600 2.15
REMARK 500 O GLU D 55 N GLY D 57 2.17
REMARK 500 OD1 ASN C 249 OE1 GLU D 71 2.17
REMARK 500 O LEU D 70 O GLY D 95 2.17
REMARK 500 O LEU B 70 O GLY B 95 2.17
REMARK 500 O LEU H 70 O GLY H 95 2.17
REMARK 500 O LEU F 70 O GLY F 95 2.18
REMARK 500 CB LYS F 326 CG PRO G 222 2.18
REMARK 500 ND1 HIS E 192 OD1 ASN E 424 2.18
REMARK 500 ND1 HIS A 192 OD1 ASN A 424 2.18
REMARK 500 CD PRO B 348 CE MET C 398 2.18
REMARK 500 ND1 HIS C 192 OD1 ASN C 424 2.18
REMARK 500 ND1 HIS G 192 OD1 ASN G 424 2.18
REMARK 500 CD1 LEU B 70 OG1 THR B 145 2.18
REMARK 500 CD1 LEU H 70 OG1 THR H 145 2.18
REMARK 500 CD1 LEU F 70 OG1 THR F 145 2.18
REMARK 500 CD1 LEU D 70 OG1 THR D 145 2.18
REMARK 500 CG PRO B 63 OE1 GLN B 91 2.19
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 MET A 235 CG - SD - CE ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO A 263 C - N - CA ANGL. DEV. = 13.0 DEGREES
REMARK 500 PRO A 263 C - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 ASP B 69 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 PRO B 173 C - N - CA ANGL. DEV. = 13.9 DEGREES
REMARK 500 MET C 235 CG - SD - CE ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO C 263 C - N - CA ANGL. DEV. = 13.0 DEGREES
REMARK 500 PRO C 263 C - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 ASP D 69 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 PRO D 173 C - N - CA ANGL. DEV. = 13.9 DEGREES
REMARK 500 MET E 235 CG - SD - CE ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO E 263 C - N - CA ANGL. DEV. = 13.0 DEGREES
REMARK 500 PRO E 263 C - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 ASP F 69 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 PRO F 173 C - N - CA ANGL. DEV. = 13.9 DEGREES
REMARK 500 MET G 235 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 PRO G 263 C - N - CA ANGL. DEV. = 13.0 DEGREES
REMARK 500 PRO G 263 C - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 ASP H 69 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 PRO H 173 C - N - CA ANGL. DEV. = 13.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 23 -87.57 -58.91
REMARK 500 ILE A 24 -46.23 -20.28
REMARK 500 HIS A 28 17.02 -161.50
REMARK 500 PRO A 32 -84.18 -13.72
REMARK 500 SER A 35 -137.18 -111.36
REMARK 500 SER A 40 -160.31 -114.23
REMARK 500 GLN A 43 24.06 -76.80
REMARK 500 LEU A 44 -33.52 -136.07
REMARK 500 ASN A 50 -46.60 -18.56
REMARK 500 VAL A 51 -29.08 -37.95
REMARK 500 ALA A 56 -74.02 -130.26
REMARK 500 ALA A 57 -83.87 -73.11
REMARK 500 ASN A 59 -4.88 -143.63
REMARK 500 ASP A 69 140.40 -170.30
REMARK 500 THR A 74 -76.95 -58.81
REMARK 500 PRO A 82 -114.12 -61.54
REMARK 500 PHE A 83 -0.35 -54.05
REMARK 500 GLN A 85 36.89 -99.12
REMARK 500 GLN A 96 -4.07 -52.72
REMARK 500 SER A 97 -167.82 -54.79
REMARK 500 ALA A 99 38.42 -65.59
REMARK 500 ASN A 101 27.46 -73.90
REMARK 500 VAL A 118 -63.17 -102.22
REMARK 500 SER A 128 -87.87 -53.96
REMARK 500 ASP A 130 -137.79 41.22
REMARK 500 HIS A 139 175.19 172.97
REMARK 500 THR A 145 -13.19 -48.72
REMARK 500 ARG A 158 9.34 -67.34
REMARK 500 TYR A 161 65.51 -152.09
REMARK 500 PRO A 162 13.38 -61.54
REMARK 500 VAL A 171 67.81 -100.63
REMARK 500 PRO A 175 -98.44 -68.15
REMARK 500 LYS A 176 -63.50 -7.03
REMARK 500 GLU A 183 -65.39 -1.47
REMARK 500 ALA A 187 -70.77 -77.35
REMARK 500 VAL A 195 -2.63 -53.96
REMARK 500 ASN A 197 -76.11 -150.71
REMARK 500 GLU A 200 113.28 -163.62
REMARK 500 ASP A 211 -71.61 -38.91
REMARK 500 LYS A 218 6.49 -48.79
REMARK 500 ASP A 226 -71.17 -62.91
REMARK 500 VAL A 238 -88.67 -62.05
REMARK 500 THR A 239 -111.23 -59.21
REMARK 500 THR A 240 -53.97 -11.73
REMARK 500 LEU A 252 -58.30 -1.52
REMARK 500 PRO A 263 -16.73 -17.99
REMARK 500 LEU A 265 -38.17 128.14
REMARK 500 HIS A 266 145.39 54.16
REMARK 500 PHE A 268 -169.79 -109.29
REMARK 500 ALA A 273 -89.27 -87.84
REMARK 500
REMARK 500 THIS ENTRY HAS 712 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP E 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP F 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP G 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP H 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WBE RELATED DB: PDB
REMARK 900 KINESIN-5-TUBULIN COMPLEX WITH AMPPNP
REMARK 900 RELATED ID: 1Z2B RELATED DB: PDB
REMARK 900 TUBULIN-COLCHICINE-VINBLASTINE: STATHMIN-LIKE DOMAIN COMPLEX
REMARK 900 RELATED ID: 2BQQ RELATED DB: PDB
REMARK 900 X-RAY STRUCURE OF THE N-TERMINAL DOMAIN OF HUMAN DOUBLECORTIN
REMARK 900 RELATED ID: 1SA1 RELATED DB: PDB
REMARK 900 TUBULIN-PODOPHYLLOTOXIN: STATHMIN-LIKE DOMAIN COMPLEX
REMARK 900 RELATED ID: 1MJD RELATED DB: PDB
REMARK 900 STRUCTURE OF N-TERMINAL DOMAIN OF HUMAN DOUBLECORTIN
REMARK 900 RELATED ID: 1JFF RELATED DB: PDB
REMARK 900 REFINED STRUCTURE OF ALPHA-BETA TUBULIN FROM ZINC-INDUCEDSHEETS
REMARK 900 STABILIZED WITH TAXOL
REMARK 900 RELATED ID: 1TVK RELATED DB: PDB
REMARK 900 THE BINDING MODE OF EPOTHILONE A ON A,B -TUBULIN BY
REMARK 900 ELECTRONCRYSTALLOGRAPHY
REMARK 900 RELATED ID: 1SA0 RELATED DB: PDB
REMARK 900 TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX
REMARK 900 RELATED ID: EMD-1788 RELATED DB: EMDB
REMARK 900 DOUBLECORTIN-STABILISED MICROTUBULES AT SECONDARY STRUCTURE
REMARK 900 RESOLUTION
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHIMERIC SEQUENCE OF SHEEP AND CATTLE MAIN ALPHA-TUBULIN
REMARK 999 ISOFORMS (1JFF AND 3HKE)
DBREF 2XRP A 1 455 UNP Q6B856 TBB2B_BOVIN 1 445
DBREF 2XRP B 1 449 UNP Q2HJ86 TBA1D_BOVIN 1 449
DBREF 2XRP C 1 455 UNP Q6B856 TBB2B_BOVIN 1 445
DBREF 2XRP D 1 449 UNP Q2HJ86 TBA1D_BOVIN 1 449
DBREF 2XRP E 1 455 UNP Q6B856 TBB2B_BOVIN 1 445
DBREF 2XRP F 1 449 UNP Q2HJ86 TBA1D_BOVIN 1 449
DBREF 2XRP G 1 455 UNP Q6B856 TBB2B_BOVIN 1 445
DBREF 2XRP H 1 449 UNP Q2HJ86 TBA1D_BOVIN 1 449
DBREF 2XRP I 46 140 UNP O43602 DCX_HUMAN 46 140
SEQADV 2XRP VAL A 172 UNP Q6B856 MET 170 CONFLICT
SEQADV 2XRP VAL A 318 UNP Q6B856 ILE 316 CONFLICT
SEQADV 2XRP ILE B 7 UNP Q2HJ86 VAL 7 CONFLICT
SEQADV 2XRP ILE B 114 UNP Q2HJ86 LEU 114 CONFLICT
SEQADV 2XRP SER B 136 UNP Q2HJ86 LEU 136 CONFLICT
SEQADV 2XRP GLU B 358 UNP Q2HJ86 GLN 358 CONFLICT
SEQADV 2XRP VAL B 437 UNP Q2HJ86 MET 437 CONFLICT
SEQADV 2XRP GLU B 450 UNP Q2HJ86 ASP 450 CONFLICT
SEQADV 2XRP VAL C 172 UNP Q6B856 MET 170 CONFLICT
SEQADV 2XRP VAL C 318 UNP Q6B856 ILE 316 CONFLICT
SEQADV 2XRP ILE D 7 UNP Q2HJ86 VAL 7 CONFLICT
SEQADV 2XRP ILE D 114 UNP Q2HJ86 LEU 114 CONFLICT
SEQADV 2XRP SER D 136 UNP Q2HJ86 LEU 136 CONFLICT
SEQADV 2XRP GLU D 358 UNP Q2HJ86 GLN 358 CONFLICT
SEQADV 2XRP VAL D 437 UNP Q2HJ86 MET 437 CONFLICT
SEQADV 2XRP GLU D 450 UNP Q2HJ86 ASP 450 CONFLICT
SEQADV 2XRP VAL E 172 UNP Q6B856 MET 170 CONFLICT
SEQADV 2XRP VAL E 318 UNP Q6B856 ILE 316 CONFLICT
SEQADV 2XRP ILE F 7 UNP Q2HJ86 VAL 7 CONFLICT
SEQADV 2XRP ILE F 114 UNP Q2HJ86 LEU 114 CONFLICT
SEQADV 2XRP SER F 136 UNP Q2HJ86 LEU 136 CONFLICT
SEQADV 2XRP GLU F 358 UNP Q2HJ86 GLN 358 CONFLICT
SEQADV 2XRP VAL F 437 UNP Q2HJ86 MET 437 CONFLICT
SEQADV 2XRP GLU F 450 UNP Q2HJ86 ASP 450 CONFLICT
SEQADV 2XRP VAL G 172 UNP Q6B856 MET 170 CONFLICT
SEQADV 2XRP VAL G 318 UNP Q6B856 ILE 316 CONFLICT
SEQADV 2XRP ILE H 7 UNP Q2HJ86 VAL 7 CONFLICT
SEQADV 2XRP ILE H 114 UNP Q2HJ86 LEU 114 CONFLICT
SEQADV 2XRP SER H 136 UNP Q2HJ86 LEU 136 CONFLICT
SEQADV 2XRP GLU H 358 UNP Q2HJ86 GLN 358 CONFLICT
SEQADV 2XRP VAL H 437 UNP Q2HJ86 MET 437 CONFLICT
SEQADV 2XRP GLU H 450 UNP Q2HJ86 ASP 450 CONFLICT
SEQRES 1 A 445 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 A 445 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 A 445 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 A 445 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 A 445 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 A 445 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 A 445 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 A 445 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 A 445 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 A 445 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 A 445 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 A 445 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 A 445 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 A 445 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 A 445 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 A 445 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 A 445 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 A 445 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 A 445 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 A 445 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 A 445 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 A 445 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 A 445 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 A 445 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 A 445 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 A 445 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 A 445 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 A 445 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 A 445 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 A 445 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 A 445 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 A 445 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 A 445 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR
SEQRES 34 A 445 ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLU GLY GLU
SEQRES 35 A 445 ASP GLU ALA
SEQRES 1 B 452 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 B 452 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 B 452 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 B 452 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 B 452 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 B 452 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 B 452 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 B 452 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 B 452 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 B 452 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 B 452 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 B 452 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 B 452 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 B 452 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 B 452 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 B 452 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 B 452 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 B 452 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 B 452 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 B 452 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 B 452 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 B 452 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 B 452 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 B 452 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 B 452 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 B 452 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 B 452 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 B 452 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 B 452 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 B 452 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 B 452 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 B 452 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 B 452 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 B 452 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 B 452 GLU GLY GLU GLU GLU GLU GLY GLU GLU TYR
SEQRES 1 C 445 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 C 445 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 C 445 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 C 445 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 C 445 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 C 445 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 C 445 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 C 445 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 C 445 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 C 445 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 C 445 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 C 445 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 C 445 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 C 445 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 C 445 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 C 445 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 C 445 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 C 445 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 C 445 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 C 445 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 C 445 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 C 445 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 C 445 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 C 445 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 C 445 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 C 445 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 C 445 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 C 445 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 C 445 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 C 445 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 C 445 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 C 445 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 C 445 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR
SEQRES 34 C 445 ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLU GLY GLU
SEQRES 35 C 445 ASP GLU ALA
SEQRES 1 D 452 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 D 452 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 D 452 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 D 452 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 D 452 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 D 452 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 D 452 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 D 452 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 D 452 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 D 452 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 D 452 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 D 452 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 D 452 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 D 452 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 D 452 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 D 452 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 D 452 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 D 452 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 D 452 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 D 452 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 D 452 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 D 452 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 D 452 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 D 452 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 D 452 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 D 452 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 D 452 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 D 452 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 D 452 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 D 452 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 D 452 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 D 452 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 D 452 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 D 452 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 D 452 GLU GLY GLU GLU GLU GLU GLY GLU GLU TYR
SEQRES 1 E 445 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 E 445 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 E 445 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 E 445 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 E 445 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 E 445 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 E 445 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 E 445 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 E 445 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 E 445 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 E 445 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 E 445 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 E 445 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 E 445 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 E 445 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 E 445 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 E 445 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 E 445 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 E 445 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 E 445 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 E 445 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 E 445 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 E 445 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 E 445 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 E 445 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 E 445 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 E 445 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 E 445 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 E 445 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 E 445 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 E 445 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 E 445 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 E 445 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR
SEQRES 34 E 445 ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLU GLY GLU
SEQRES 35 E 445 ASP GLU ALA
SEQRES 1 F 452 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 F 452 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 F 452 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 F 452 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 F 452 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 F 452 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 F 452 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 F 452 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 F 452 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 F 452 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 F 452 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 F 452 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 F 452 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 F 452 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 F 452 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 F 452 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 F 452 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 F 452 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 F 452 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 F 452 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 F 452 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 F 452 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 F 452 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 F 452 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 F 452 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 F 452 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 F 452 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 F 452 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 F 452 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 F 452 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 F 452 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 F 452 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 F 452 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 F 452 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 F 452 GLU GLY GLU GLU GLU GLU GLY GLU GLU TYR
SEQRES 1 G 445 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 G 445 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 G 445 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 G 445 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 G 445 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 G 445 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 G 445 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 G 445 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 G 445 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 G 445 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 G 445 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 G 445 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 G 445 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 G 445 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 G 445 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 G 445 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 G 445 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 G 445 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 G 445 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 G 445 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 G 445 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 G 445 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 G 445 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 G 445 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 G 445 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 G 445 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 G 445 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 G 445 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 G 445 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 G 445 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 G 445 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 G 445 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 G 445 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR
SEQRES 34 G 445 ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLU GLY GLU
SEQRES 35 G 445 ASP GLU ALA
SEQRES 1 H 452 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 H 452 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 H 452 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 H 452 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 H 452 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 H 452 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 H 452 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 H 452 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 H 452 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 H 452 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 H 452 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 H 452 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 H 452 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 H 452 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 H 452 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 H 452 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 H 452 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 H 452 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 H 452 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 H 452 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 H 452 PRO TYR PRO ARG GLY HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 H 452 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 H 452 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 H 452 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 H 452 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 H 452 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 H 452 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 H 452 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 H 452 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 H 452 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 H 452 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 H 452 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 H 452 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 H 452 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 H 452 GLU GLY GLU GLU GLU GLU GLY GLU GLU TYR
SEQRES 1 I 95 LEU SER ASN GLU LYS LYS ALA LYS LYS VAL ARG PHE TYR
SEQRES 2 I 95 ARG ASN GLY ASP ARG TYR PHE LYS GLY ILE VAL TYR ALA
SEQRES 3 I 95 VAL SER SER ASP ARG PHE ARG SER PHE ASP ALA LEU LEU
SEQRES 4 I 95 ALA ASP LEU THR ARG SER LEU SER ASP ASN ILE ASN LEU
SEQRES 5 I 95 PRO GLN GLY VAL ARG TYR ILE TYR THR ILE ASP GLY SER
SEQRES 6 I 95 ARG LYS ILE GLY SER MET ASP GLU LEU GLU GLU GLY GLU
SEQRES 7 I 95 SER TYR VAL CYS SER SER ASP ASN PHE PHE LYS LYS VAL
SEQRES 8 I 95 GLU TYR THR LYS
HET GDP A 600 28
HET GTP B 500 32
HET GDP C 600 28
HET GTP D 500 32
HET GDP E 600 28
HET GTP F 500 32
HET GDP G 600 28
HET GTP H 500 32
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
FORMUL 10 GDP 4(C10 H15 N5 O11 P2)
FORMUL 11 GTP 4(C10 H16 N5 O14 P3)
HELIX 1 1 GLN A 11 GLU A 27 1 17
HELIX 2 2 ARG A 48 TYR A 53 5 6
HELIX 3 3 GLU A 71 ARG A 79 1 9
HELIX 4 4 PRO A 82 ILE A 86 5 5
HELIX 5 5 ARG A 88 ASP A 90 5 3
HELIX 6 6 ALA A 104 THR A 109 1 6
HELIX 7 7 GLU A 110 GLU A 127 1 18
HELIX 8 8 GLY A 143 TYR A 161 1 19
HELIX 9 9 GLU A 183 VAL A 195 1 13
HELIX 10 10 ASP A 205 ARG A 215 1 11
HELIX 11 11 THR A 223 ARG A 243 1 21
HELIX 12 12 ASP A 251 VAL A 260 1 10
HELIX 13 13 VAL A 288 PHE A 296 1 9
HELIX 14 14 ASP A 306 GLY A 310 5 5
HELIX 15 15 SER A 324 ASN A 339 1 16
HELIX 16 16 ILE A 384 ARG A 400 1 17
HELIX 17 17 LYS A 402 PHE A 404 5 3
HELIX 18 18 LEU A 405 GLY A 410 1 6
HELIX 19 19 ASP A 414 ASP A 437 1 24
HELIX 20 20 GLY B 10 GLU B 27 1 18
HELIX 21 21 PRO B 72 ARG B 79 1 8
HELIX 22 22 ASN B 102 TYR B 108 1 7
HELIX 23 23 TYR B 108 CYS B 129 1 22
HELIX 24 24 SER B 147 TYR B 161 1 15
HELIX 25 25 GLU B 183 LEU B 195 1 13
HELIX 26 26 ASP B 205 ASN B 216 1 12
HELIX 27 27 THR B 223 ARG B 243 1 21
HELIX 28 28 ASP B 251 VAL B 260 1 10
HELIX 29 29 SER B 287 CYS B 295 1 9
HELIX 30 30 PHE B 296 GLN B 301 5 6
HELIX 31 31 VAL B 324 THR B 337 1 14
HELIX 32 32 ILE B 384 ALA B 400 1 17
HELIX 33 33 LYS B 401 PHE B 404 5 4
HELIX 34 34 VAL B 405 GLY B 410 1 6
HELIX 35 35 GLU B 414 LYS B 430 1 17
HELIX 36 36 LYS B 430 VAL B 435 1 6
HELIX 37 37 GLN C 11 GLU C 27 1 17
HELIX 38 38 ARG C 48 TYR C 53 5 6
HELIX 39 39 GLU C 71 ARG C 79 1 9
HELIX 40 40 PRO C 82 ILE C 86 5 5
HELIX 41 41 ARG C 88 ASP C 90 5 3
HELIX 42 42 ALA C 104 THR C 109 1 6
HELIX 43 43 GLU C 110 GLU C 127 1 18
HELIX 44 44 GLY C 143 TYR C 161 1 19
HELIX 45 45 GLU C 183 VAL C 195 1 13
HELIX 46 46 ASP C 205 ARG C 215 1 11
HELIX 47 47 THR C 223 ARG C 243 1 21
HELIX 48 48 ASP C 251 VAL C 260 1 10
HELIX 49 49 VAL C 288 PHE C 296 1 9
HELIX 50 50 ASP C 306 GLY C 310 5 5
HELIX 51 51 SER C 324 ASN C 339 1 16
HELIX 52 52 ILE C 384 ARG C 400 1 17
HELIX 53 53 LYS C 402 PHE C 404 5 3
HELIX 54 54 LEU C 405 GLY C 410 1 6
HELIX 55 55 ASP C 414 ASP C 437 1 24
HELIX 56 56 GLY D 10 GLU D 27 1 18
HELIX 57 57 PRO D 72 ARG D 79 1 8
HELIX 58 58 ASN D 102 TYR D 108 1 7
HELIX 59 59 TYR D 108 CYS D 129 1 22
HELIX 60 60 SER D 147 TYR D 161 1 15
HELIX 61 61 GLU D 183 LEU D 195 1 13
HELIX 62 62 ASP D 205 ASN D 216 1 12
HELIX 63 63 THR D 223 ARG D 243 1 21
HELIX 64 64 ASP D 251 VAL D 260 1 10
HELIX 65 65 SER D 287 CYS D 295 1 9
HELIX 66 66 PHE D 296 GLN D 301 5 6
HELIX 67 67 VAL D 324 THR D 337 1 14
HELIX 68 68 ILE D 384 ALA D 400 1 17
HELIX 69 69 LYS D 401 PHE D 404 5 4
HELIX 70 70 VAL D 405 GLY D 410 1 6
HELIX 71 71 GLU D 414 LYS D 430 1 17
HELIX 72 72 LYS D 430 VAL D 435 1 6
HELIX 73 73 GLN E 11 GLU E 27 1 17
HELIX 74 74 ARG E 48 TYR E 53 5 6
HELIX 75 75 GLU E 71 ARG E 79 1 9
HELIX 76 76 PRO E 82 ILE E 86 5 5
HELIX 77 77 ARG E 88 ASP E 90 5 3
HELIX 78 78 ALA E 104 THR E 109 1 6
HELIX 79 79 GLU E 110 GLU E 127 1 18
HELIX 80 80 GLY E 143 TYR E 161 1 19
HELIX 81 81 GLU E 183 VAL E 195 1 13
HELIX 82 82 ASP E 205 ARG E 215 1 11
HELIX 83 83 THR E 223 ARG E 243 1 21
HELIX 84 84 ASP E 251 VAL E 260 1 10
HELIX 85 85 VAL E 288 PHE E 296 1 9
HELIX 86 86 ASP E 306 GLY E 310 5 5
HELIX 87 87 SER E 324 ASN E 339 1 16
HELIX 88 88 ILE E 384 ARG E 400 1 17
HELIX 89 89 LYS E 402 PHE E 404 5 3
HELIX 90 90 LEU E 405 GLY E 410 1 6
HELIX 91 91 ASP E 414 ASP E 437 1 24
HELIX 92 92 GLY F 10 GLU F 27 1 18
HELIX 93 93 PRO F 72 ARG F 79 1 8
HELIX 94 94 ASN F 102 TYR F 108 1 7
HELIX 95 95 TYR F 108 CYS F 129 1 22
HELIX 96 96 SER F 147 TYR F 161 1 15
HELIX 97 97 GLU F 183 LEU F 195 1 13
HELIX 98 98 ASP F 205 ASN F 216 1 12
HELIX 99 99 THR F 223 ARG F 243 1 21
HELIX 100 100 ASP F 251 VAL F 260 1 10
HELIX 101 101 SER F 287 CYS F 295 1 9
HELIX 102 102 PHE F 296 GLN F 301 5 6
HELIX 103 103 VAL F 324 THR F 337 1 14
HELIX 104 104 ILE F 384 ALA F 400 1 17
HELIX 105 105 LYS F 401 PHE F 404 5 4
HELIX 106 106 VAL F 405 GLY F 410 1 6
HELIX 107 107 GLU F 414 LYS F 430 1 17
HELIX 108 108 LYS F 430 VAL F 435 1 6
HELIX 109 109 GLN G 11 GLU G 27 1 17
HELIX 110 110 ARG G 48 TYR G 53 5 6
HELIX 111 111 GLU G 71 ARG G 79 1 9
HELIX 112 112 PRO G 82 ILE G 86 5 5
HELIX 113 113 ARG G 88 ASP G 90 5 3
HELIX 114 114 ALA G 104 THR G 109 1 6
HELIX 115 115 GLU G 110 GLU G 127 1 18
HELIX 116 116 GLY G 143 TYR G 161 1 19
HELIX 117 117 GLU G 183 VAL G 195 1 13
HELIX 118 118 ASP G 205 ARG G 215 1 11
HELIX 119 119 THR G 223 ARG G 243 1 21
HELIX 120 120 ASP G 251 VAL G 260 1 10
HELIX 121 121 VAL G 288 PHE G 296 1 9
HELIX 122 122 ASP G 306 GLY G 310 5 5
HELIX 123 123 SER G 324 ASN G 339 1 16
HELIX 124 124 ILE G 384 ARG G 400 1 17
HELIX 125 125 LYS G 402 PHE G 404 5 3
HELIX 126 126 LEU G 405 GLY G 410 1 6
HELIX 127 127 ASP G 414 ASP G 437 1 24
HELIX 128 128 GLY H 10 GLU H 27 1 18
HELIX 129 129 PRO H 72 ARG H 79 1 8
HELIX 130 130 ASN H 102 TYR H 108 1 7
HELIX 131 131 TYR H 108 CYS H 129 1 22
HELIX 132 132 SER H 147 TYR H 161 1 15
HELIX 133 133 GLU H 183 LEU H 195 1 13
HELIX 134 134 ASP H 205 ASN H 216 1 12
HELIX 135 135 THR H 223 ARG H 243 1 21
HELIX 136 136 ASP H 251 VAL H 260 1 10
HELIX 137 137 SER H 287 CYS H 295 1 9
HELIX 138 138 PHE H 296 GLN H 301 5 6
HELIX 139 139 VAL H 324 THR H 337 1 14
HELIX 140 140 ILE H 384 ALA H 400 1 17
HELIX 141 141 LYS H 401 PHE H 404 5 4
HELIX 142 142 VAL H 405 GLY H 410 1 6
HELIX 143 143 GLU H 414 LYS H 430 1 17
HELIX 144 144 LYS H 430 VAL H 435 1 6
HELIX 145 145 SER I 79 SER I 92 1 14
HELIX 146 146 SER I 115 LEU I 119 5 5
SHEET 1 AA10 PHE A 92 PHE A 94 0
SHEET 2 AA10 ALA A 65 ASP A 69 1 O LEU A 67 N VAL A 93
SHEET 3 AA10 HIS A 6 ALA A 9 1 O HIS A 6 N ILE A 66
SHEET 4 AA10 GLY A 134 HIS A 139 1 O GLN A 136 N ILE A 7
SHEET 5 AA10 ILE A 165 SER A 170 1 O ILE A 165 N PHE A 135
SHEET 6 AA10 GLU A 200 TYR A 202 1 O GLU A 200 N THR A 168
SHEET 7 AA10 PHE A 267 GLY A 271 1 N PHE A 268 O THR A 201
SHEET 8 AA10 ALA A 375 SER A 381 -1 O PHE A 377 N GLY A 271
SHEET 9 AA10 TYR A 312 ARG A 320 -1 N LEU A 313 O ASN A 380
SHEET 10 AA10 VAL A 351 CYS A 356 1 O LYS A 352 N ALA A 317
SHEET 1 BA 6 LEU B 92 THR B 94 0
SHEET 2 BA 6 ALA B 65 ASP B 69 1 O PHE B 67 N ILE B 93
SHEET 3 BA 6 CYS B 4 VAL B 9 1 O SER B 6 N VAL B 66
SHEET 4 BA 6 GLY B 134 HIS B 139 1 O GLY B 134 N ILE B 5
SHEET 5 BA 6 LEU B 167 SER B 170 1 O LEU B 167 N VAL B 137
SHEET 6 BA 6 CYS B 200 MET B 203 1 O CYS B 200 N GLU B 168
SHEET 1 BB 4 LEU B 269 THR B 271 0
SHEET 2 BB 4 ARG B 373 THR B 381 -1 O MET B 377 N THR B 271
SHEET 3 BB 4 TYR B 312 GLY B 321 -1 N MET B 313 O ASN B 380
SHEET 4 BB 4 PHE B 351 ILE B 355 1 N LYS B 352 O CYS B 315
SHEET 1 CA10 PHE C 92 PHE C 94 0
SHEET 2 CA10 ALA C 65 ASP C 69 1 O LEU C 67 N VAL C 93
SHEET 3 CA10 HIS C 6 ALA C 9 1 O HIS C 6 N ILE C 66
SHEET 4 CA10 GLY C 134 HIS C 139 1 O GLN C 136 N ILE C 7
SHEET 5 CA10 ILE C 165 SER C 170 1 O ILE C 165 N PHE C 135
SHEET 6 CA10 GLU C 200 TYR C 202 1 O GLU C 200 N THR C 168
SHEET 7 CA10 PHE C 267 GLY C 271 1 N PHE C 268 O THR C 201
SHEET 8 CA10 ALA C 375 SER C 381 -1 O PHE C 377 N GLY C 271
SHEET 9 CA10 TYR C 312 ARG C 320 -1 N LEU C 313 O ASN C 380
SHEET 10 CA10 VAL C 351 CYS C 356 1 O LYS C 352 N ALA C 317
SHEET 1 DA 6 LEU D 92 THR D 94 0
SHEET 2 DA 6 ALA D 65 ASP D 69 1 O PHE D 67 N ILE D 93
SHEET 3 DA 6 CYS D 4 VAL D 9 1 O SER D 6 N VAL D 66
SHEET 4 DA 6 GLY D 134 HIS D 139 1 O GLY D 134 N ILE D 5
SHEET 5 DA 6 LEU D 167 SER D 170 1 O LEU D 167 N VAL D 137
SHEET 6 DA 6 CYS D 200 MET D 203 1 O CYS D 200 N GLU D 168
SHEET 1 DB 4 LEU D 269 THR D 271 0
SHEET 2 DB 4 ARG D 373 THR D 381 -1 O MET D 377 N THR D 271
SHEET 3 DB 4 TYR D 312 GLY D 321 -1 N MET D 313 O ASN D 380
SHEET 4 DB 4 PHE D 351 ILE D 355 1 N LYS D 352 O CYS D 315
SHEET 1 EA10 PHE E 92 PHE E 94 0
SHEET 2 EA10 ALA E 65 ASP E 69 1 O LEU E 67 N VAL E 93
SHEET 3 EA10 HIS E 6 ALA E 9 1 O HIS E 6 N ILE E 66
SHEET 4 EA10 GLY E 134 HIS E 139 1 O GLN E 136 N ILE E 7
SHEET 5 EA10 ILE E 165 SER E 170 1 O ILE E 165 N PHE E 135
SHEET 6 EA10 GLU E 200 TYR E 202 1 O GLU E 200 N THR E 168
SHEET 7 EA10 PHE E 267 GLY E 271 1 N PHE E 268 O THR E 201
SHEET 8 EA10 ALA E 375 SER E 381 -1 O PHE E 377 N GLY E 271
SHEET 9 EA10 TYR E 312 ARG E 320 -1 N LEU E 313 O ASN E 380
SHEET 10 EA10 VAL E 351 CYS E 356 1 O LYS E 352 N ALA E 317
SHEET 1 FA 6 LEU F 92 THR F 94 0
SHEET 2 FA 6 ALA F 65 ASP F 69 1 O PHE F 67 N ILE F 93
SHEET 3 FA 6 CYS F 4 VAL F 9 1 O SER F 6 N VAL F 66
SHEET 4 FA 6 GLY F 134 HIS F 139 1 O GLY F 134 N ILE F 5
SHEET 5 FA 6 LEU F 167 SER F 170 1 O LEU F 167 N VAL F 137
SHEET 6 FA 6 CYS F 200 MET F 203 1 O CYS F 200 N GLU F 168
SHEET 1 FB 4 LEU F 269 THR F 271 0
SHEET 2 FB 4 ARG F 373 THR F 381 -1 O MET F 377 N THR F 271
SHEET 3 FB 4 TYR F 312 GLY F 321 -1 N MET F 313 O ASN F 380
SHEET 4 FB 4 PHE F 351 ILE F 355 1 N LYS F 352 O CYS F 315
SHEET 1 GA10 PHE G 92 PHE G 94 0
SHEET 2 GA10 ALA G 65 ASP G 69 1 O LEU G 67 N VAL G 93
SHEET 3 GA10 HIS G 6 ALA G 9 1 O HIS G 6 N ILE G 66
SHEET 4 GA10 GLY G 134 HIS G 139 1 O GLN G 136 N ILE G 7
SHEET 5 GA10 ILE G 165 SER G 170 1 O ILE G 165 N PHE G 135
SHEET 6 GA10 GLU G 200 TYR G 202 1 O GLU G 200 N THR G 168
SHEET 7 GA10 PHE G 267 GLY G 271 1 N PHE G 268 O THR G 201
SHEET 8 GA10 ALA G 375 SER G 381 -1 O PHE G 377 N GLY G 271
SHEET 9 GA10 TYR G 312 ARG G 320 -1 N LEU G 313 O ASN G 380
SHEET 10 GA10 VAL G 351 CYS G 356 1 O LYS G 352 N ALA G 317
SHEET 1 HA 6 LEU H 92 THR H 94 0
SHEET 2 HA 6 ALA H 65 ASP H 69 1 O PHE H 67 N ILE H 93
SHEET 3 HA 6 CYS H 4 VAL H 9 1 O SER H 6 N VAL H 66
SHEET 4 HA 6 GLY H 134 HIS H 139 1 O GLY H 134 N ILE H 5
SHEET 5 HA 6 LEU H 167 SER H 170 1 O LEU H 167 N VAL H 137
SHEET 6 HA 6 CYS H 200 MET H 203 1 O CYS H 200 N GLU H 168
SHEET 1 HB 4 LEU H 269 THR H 271 0
SHEET 2 HB 4 ARG H 373 THR H 381 -1 O MET H 377 N THR H 271
SHEET 3 HB 4 TYR H 312 GLY H 321 -1 N MET H 313 O ASN H 380
SHEET 4 HB 4 PHE H 351 ILE H 355 1 N LYS H 352 O CYS H 315
SHEET 1 IA 5 ILE I 68 VAL I 72 0
SHEET 2 IA 5 LYS I 53 ARG I 59 -1 O LYS I 53 N VAL I 72
SHEET 3 IA 5 GLU I 123 SER I 128 1 O GLU I 123 N ARG I 56
SHEET 4 IA 5 TYR I 103 THR I 106 -1 O TYR I 103 N SER I 128
SHEET 5 IA 5 LYS I 112 ILE I 113 -1 O ILE I 113 N ILE I 104
CISPEP 1 GLY B 57 ALA B 58 0 -0.12
CISPEP 2 GLY D 57 ALA D 58 0 -0.06
SITE 1 AC1 13 GLY A 10 GLN A 11 CYS A 12 GLN A 15
SITE 2 AC1 13 SER A 140 GLY A 142 GLY A 144 THR A 145
SITE 3 AC1 13 GLY A 146 ASP A 179 ASN A 206 TYR A 224
SITE 4 AC1 13 ASN A 228
SITE 1 AC2 19 LEU A 248 LYS A 254 GLY B 10 GLN B 11
SITE 2 AC2 19 ALA B 12 GLN B 15 ALA B 99 ALA B 100
SITE 3 AC2 19 ASN B 101 SER B 140 GLY B 143 GLY B 144
SITE 4 AC2 19 THR B 145 GLY B 146 ILE B 171 GLU B 183
SITE 5 AC2 19 ASN B 206 TYR B 224 ASN B 228
SITE 1 AC3 13 GLY C 10 GLN C 11 CYS C 12 GLN C 15
SITE 2 AC3 13 SER C 140 GLY C 142 GLY C 144 THR C 145
SITE 3 AC3 13 GLY C 146 ASP C 179 ASN C 206 TYR C 224
SITE 4 AC3 13 ASN C 228
SITE 1 AC4 19 LEU C 248 LYS C 254 GLY D 10 GLN D 11
SITE 2 AC4 19 ALA D 12 GLN D 15 ALA D 99 ALA D 100
SITE 3 AC4 19 ASN D 101 SER D 140 GLY D 143 GLY D 144
SITE 4 AC4 19 THR D 145 GLY D 146 ILE D 171 GLU D 183
SITE 5 AC4 19 ASN D 206 TYR D 224 ASN D 228
SITE 1 AC5 13 GLY E 10 GLN E 11 CYS E 12 GLN E 15
SITE 2 AC5 13 SER E 140 GLY E 142 GLY E 144 THR E 145
SITE 3 AC5 13 GLY E 146 ASP E 179 ASN E 206 TYR E 224
SITE 4 AC5 13 ASN E 228
SITE 1 AC6 19 LEU E 248 LYS E 254 GLY F 10 GLN F 11
SITE 2 AC6 19 ALA F 12 GLN F 15 ALA F 99 ALA F 100
SITE 3 AC6 19 ASN F 101 SER F 140 GLY F 143 GLY F 144
SITE 4 AC6 19 THR F 145 GLY F 146 ILE F 171 GLU F 183
SITE 5 AC6 19 ASN F 206 TYR F 224 ASN F 228
SITE 1 AC7 13 GLY G 10 GLN G 11 CYS G 12 GLN G 15
SITE 2 AC7 13 SER G 140 GLY G 142 GLY G 144 THR G 145
SITE 3 AC7 13 GLY G 146 ASP G 179 ASN G 206 TYR G 224
SITE 4 AC7 13 ASN G 228
SITE 1 AC8 18 LEU G 248 GLY H 10 GLN H 11 ALA H 12
SITE 2 AC8 18 GLN H 15 ALA H 99 ALA H 100 ASN H 101
SITE 3 AC8 18 SER H 140 GLY H 143 GLY H 144 THR H 145
SITE 4 AC8 18 GLY H 146 ILE H 171 GLU H 183 ASN H 206
SITE 5 AC8 18 TYR H 224 ASN H 228
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
