HEADER HYDROLASE 10-MAY-12 4ATX
TITLE RIGOR KINESIN MOTOR DOMAIN WITH AN ORDERED NECK-LINKER, DOCKED ON
TITLE 2 TUBULIN DIMER, MODELLED INTO THE 8A CRYO-EM MAP OF DOUBLECORTIN-
TITLE 3 MICROTUBULES DECORATED WITH KINESIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUBULIN BETA-2B CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.6.5.6;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: TUBULIN ALPHA-1D CHAIN;
COMPND 7 CHAIN: B;
COMPND 8 EC: 3.6.5.6;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: KINESIN-1 HEAVY CHAIN;
COMPND 11 CHAIN: C;
COMPND 12 FRAGMENT: MOTOR DOMAIN, RESIDUES 1-340;
COMPND 13 SYNONYM: CONVENTIONAL KINESIN HEAVY CHAIN, UBIQUITOUS KINESIN HEAVY
COMPND 14 CHAIN, UKHC;
COMPND 15 EC: 3.6.4.4;
COMPND 16 ENGINEERED: YES;
COMPND 17 MUTATION: 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: RATTUS NORVEGICUS;
SOURCE 13 ORGANISM_COMMON: NORWAY RAT;
SOURCE 14 ORGANISM_TAXID: 10116;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, MICROTUBULE, NECK-LINKER
EXPDTA ELECTRON MICROSCOPY
AUTHOR J.S.LIU,C.R.SCHUBERT,X.FU,F.J.FOURNIOL,J.K.JAISWAL,A.HOUDUSSE,
AUTHOR 2 C.M.STULTZ,C.A.MOORES,C.A.WALSH
REVDAT 2 23-AUG-17 4ATX 1 REMARK
REVDAT 1 26-SEP-12 4ATX 0
JRNL AUTH J.S.LIU,C.R.SCHUBERT,X.FU,F.J.FOURNIOL,J.K.JAISWAL,
JRNL AUTH 2 A.HOUDUSSE,C.M.STULTZ,C.A.MOORES,C.A.WALSH
JRNL TITL MOLECULAR BASIS FOR SPECIFIC REGULATION OF NEURONAL KINESIN-
JRNL TITL 2 3 MOTORS BY DOUBLECORTIN FAMILY PROTEINS.
JRNL REF MOL.CELL V. 47 707 2012
JRNL REFN ISSN 1097-2765
JRNL PMID 22857951
JRNL DOI 10.1016/J.MOLCEL.2012.06.025
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.J.FOURNIOL,C.V.SINDELAR,B.AMIGUES,D.K.CLARE,G.THOMAS,
REMARK 1 AUTH 2 M.PERDERISET,F.FRANCIS,A.HOUDUSSE,C.A.MOORES
REMARK 1 TITL TEMPLATE-FREE 13-PROTOFILAMENT MICROTUBULE-MAP ASSEMBLY
REMARK 1 TITL 2 VISUALIZED AT 8 A RESOLUTION.
REMARK 1 REF J.CELL BIOL. V. 191 463 2010
REMARK 1 REFN ISSN 0021-9525
REMARK 1 PMID 20974813
REMARK 1 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 : 2XRP
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
REMARK 3 REFINEMENT TARGET : CROSS-CORRELATION COEFFICIENT
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : METHOD--RIGID BODY
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: A HOMOLOGY MODEL OF RAT KINESIN MOTOR DOMAIN MUTANT
REMARK 3 T93N WAS GENERATED USING MODELLER, BASED ON THE STRUCTURE OF
REMARK 3 HUMAN KINESIN 1BG2. 2) KINESIN LOOP11 (AA 237-254) WAS OMITTED
REMARK 3 IN THIS MODEL AS NO CRYSTAL STRUCTURE REFLECTED THE CONFORMATION
REMARK 3 OF LOOP11 VISUALISED IN THE EM MAP SUBMISSION BASED ON
REMARK 3 EXPERIMENTAL DATA FROM EMDB EMD-2098. (DEPOSITION ID: 10790).
REMARK 4
REMARK 4 4ATX 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_1290052446.
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 : DOUBLECORTIN-STABILISED
REMARK 245 MICROTUBULES DECORATED WITH
REMARK 245 KINESIN MOTOR DOMAINS
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : HOLEY CARBON
REMARK 245 SAMPLE VITRIFICATION DETAILS : CRYOGEN- ETHANE, HUMIDITY- 100,
REMARK 245 INSTRUMENT- FEI VITROBOT
REMARK 245 SAMPLE BUFFER : 20MM 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 : 01-SEP-09
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 2
REMARK 465 LYS C 237
REMARK 465 VAL C 238
REMARK 465 SER C 239
REMARK 465 LYS C 240
REMARK 465 THR C 241
REMARK 465 GLY C 242
REMARK 465 ALA C 243
REMARK 465 GLU C 244
REMARK 465 GLY C 245
REMARK 465 ALA C 246
REMARK 465 VAL C 247
REMARK 465 LEU C 248
REMARK 465 ASP C 249
REMARK 465 GLU C 250
REMARK 465 ALA C 251
REMARK 465 LYS C 252
REMARK 465 ASN C 253
REMARK 465 ILE C 254
REMARK 465 VAL C 331
REMARK 465 ASN C 332
REMARK 465 VAL C 333
REMARK 465 GLU C 334
REMARK 465 LEU C 335
REMARK 465 THR C 336
REMARK 465 ALA C 337
REMARK 465 GLU C 338
REMARK 465 GLN C 339
REMARK 465 TRP C 340
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 CYS C 330 CA C O CB SG
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 NH1 ARG A 264 NE ARG C 278 1.89
REMARK 500 O GLN A 281 N TYR A 283 2.00
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 O ARG B 264 N HIS B 266 2.09
REMARK 500 CE1 PHE B 296 CD1 ILE B 341 2.11
REMARK 500 OD2 ASP A 427 OH TYR C 274 2.13
REMARK 500 O LEU B 70 O GLY B 95 2.17
REMARK 500 ND1 HIS A 192 OD1 ASN A 424 2.18
REMARK 500 CD1 LEU B 70 OG1 THR B 145 2.18
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. = 9.8 DEGREES
REMARK 500 PRO A 263 C - N - CA ANGL. DEV. = 13.1 DEGREES
REMARK 500 PRO A 263 C - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 ASP B 69 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 PRO B 173 C - N - CA ANGL. DEV. = 13.9 DEGREES
REMARK 500 TYR C 29 CA - CB - CG ANGL. DEV. = -11.8 DEGREES
REMARK 500 TYR C 29 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 SER C 204 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 TYR C 307 CA - CB - CG ANGL. DEV. = -21.5 DEGREES
REMARK 500 TYR C 307 CB - CG - CD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 23 -87.54 -58.93
REMARK 500 ILE A 24 -46.25 -20.31
REMARK 500 HIS A 28 16.96 -161.50
REMARK 500 PRO A 32 -84.17 -13.74
REMARK 500 SER A 35 -137.14 -111.31
REMARK 500 SER A 40 -160.30 -114.20
REMARK 500 GLN A 43 24.06 -76.80
REMARK 500 LEU A 44 -33.47 -136.09
REMARK 500 ASN A 50 -46.61 -18.53
REMARK 500 VAL A 51 -29.10 -37.90
REMARK 500 ALA A 56 -74.01 -130.25
REMARK 500 ALA A 57 -83.80 -73.15
REMARK 500 ASN A 59 -4.85 -143.62
REMARK 500 ASP A 69 140.37 -170.30
REMARK 500 THR A 74 -76.89 -58.82
REMARK 500 PRO A 82 -114.11 -61.61
REMARK 500 PHE A 83 -0.32 -54.04
REMARK 500 GLN A 85 36.93 -99.16
REMARK 500 GLN A 96 -4.01 -52.79
REMARK 500 SER A 97 -167.83 -54.83
REMARK 500 ALA A 99 38.42 -65.66
REMARK 500 ASN A 101 27.48 -73.95
REMARK 500 VAL A 118 -63.17 -102.26
REMARK 500 SER A 128 -87.87 -54.02
REMARK 500 ASP A 130 -137.84 41.32
REMARK 500 HIS A 139 175.21 172.95
REMARK 500 THR A 145 -13.18 -48.72
REMARK 500 ARG A 158 9.39 -67.40
REMARK 500 TYR A 161 65.47 -152.04
REMARK 500 PRO A 162 13.39 -61.55
REMARK 500 VAL A 171 67.82 -100.62
REMARK 500 PRO A 175 -98.49 -68.16
REMARK 500 LYS A 176 -63.50 -6.99
REMARK 500 GLU A 183 -65.46 -1.42
REMARK 500 ALA A 187 -70.77 -77.34
REMARK 500 VAL A 195 -2.71 -53.93
REMARK 500 ASN A 197 -76.09 -150.68
REMARK 500 GLU A 200 113.27 -163.61
REMARK 500 ASP A 211 -71.65 -38.90
REMARK 500 LYS A 218 6.45 -48.77
REMARK 500 ASP A 226 -71.14 -62.88
REMARK 500 VAL A 238 -88.67 -62.03
REMARK 500 THR A 239 -111.20 -59.15
REMARK 500 THR A 240 -53.91 -11.79
REMARK 500 LEU A 252 -58.32 -1.51
REMARK 500 PRO A 263 -16.71 -17.98
REMARK 500 LEU A 265 -38.12 128.18
REMARK 500 HIS A 266 145.42 54.16
REMARK 500 PHE A 268 -169.76 -109.30
REMARK 500 ALA A 273 -89.34 -87.80
REMARK 500
REMARK 500 THIS ENTRY HAS 185 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 ASP C 27 LYS C 28 -137.60
REMARK 500 LYS C 28 TYR C 29 -149.92
REMARK 500 VAL C 30 ALA C 31 -143.25
REMARK 500 SER C 305 SER C 306 -142.06
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 ARG C 16 0.12 SIDE CHAIN
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 900
REMARK 900 RELATED ENTRIES
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: 1SA0 RELATED DB: PDB
REMARK 900 TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX
REMARK 900 RELATED ID: 1SA1 RELATED DB: PDB
REMARK 900 TUBULIN-PODOPHYLLOTOXIN: STATHMIN-LIKE DOMAIN COMPLEX
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: 1Z2B RELATED DB: PDB
REMARK 900 TUBULIN-COLCHICINE-VINBLASTINE: STATHMIN-LIKE DOMAIN COMPLEX
REMARK 900 RELATED ID: 2WBE RELATED DB: PDB
REMARK 900 KINESIN-5-TUBULIN COMPLEX WITH AMPPNP
REMARK 900 RELATED ID: 2XRP RELATED DB: PDB
REMARK 900 HUMAN DOUBLECORTIN N-DC REPEAT (1MJD) AND MAMMALIAN TUBULIN (1JFF
REMARK 900 AND 3HKE) DOCKED INTO THE 8-ANGSTROM CRYO-EM MAP OF DOUBLECORTIN-
REMARK 900 STABILISED MICROTUBULES
REMARK 900 RELATED ID: 4AQV RELATED DB: PDB
REMARK 900 MODEL OF HUMAN KINESIN-5 MOTOR DOMAIN (3HQD) AND MAMMALIAN TUBULIN
REMARK 900 HETERODIMER (1JFF) DOCKED INTO THE 9. 7-ANGSTROM CRYO-EM MAP OF
REMARK 900 MICROTUBULE-BOUND KINESIN- 5 MOTOR DOMAIN IN THE AMPPPNP STATE.
REMARK 900 RELATED ID: 4AQW RELATED DB: PDB
REMARK 900 MODEL OF HUMAN KINESIN-5 MOTOR DOMAIN (1II6, 3HQD) AND MAMMALIAN
REMARK 900 TUBULIN HETERODIMER (1JFF) DOCKED INTO THE 9.5-ANGSTROM CRYO-EM MAP
REMARK 900 OF MICROTUBULE-BOUND KINESIN-5 MOTOR DOMAIN IN THE RIGOR STATE.
REMARK 900 RELATED ID: 4ATU RELATED DB: PDB
REMARK 900 HUMAN DOUBLECORTIN N-DC REPEAT PLUS LINKER, AND TUBULIN (2XRP)
REMARK 900 DOCKED INTO AN 8A CRYO-EM MAP OF DOUBLECORTIN-STABILISED
REMARK 900 MICROTUBULES RECONSTRUCTED IN ABSENCE OF KINESIN
REMARK 900 RELATED ID: EMD-2098 RELATED DB: EMDB
REMARK 900 CRYO-ELECTRON MICROSCOPY RECONSTRUCTION OF DOUBLECORTIN -STABILISED
REMARK 900 MICROTUBULES IN PRESENCE OF KINESIN
DBREF 4ATX A 1 455 UNP Q6B856 TBB2B_BOVIN 1 445
DBREF 4ATX B 1 452 UNP Q2HJ86 TBA1D_BOVIN 1 452
DBREF 4ATX C 1 340 UNP Q2PQA9 KINH_RAT 1 340
SEQADV 4ATX ALA A 57 UNP Q6B856 THR 55 CONFLICT
SEQADV 4ATX VAL A 172 UNP Q6B856 MET 170 CONFLICT
SEQADV 4ATX ALA A 298 UNP Q6B856 SER 296 CONFLICT
SEQADV 4ATX VAL A 318 UNP Q6B856 ILE 316 CONFLICT
SEQADV 4ATX ILE B 7 UNP Q2HJ86 VAL 7 CONFLICT
SEQADV 4ATX ILE B 114 UNP Q2HJ86 LEU 114 CONFLICT
SEQADV 4ATX SER B 136 UNP Q2HJ86 LEU 136 CONFLICT
SEQADV 4ATX VAL B 137 UNP Q2HJ86 ILE 137 CONFLICT
SEQADV 4ATX GLY B 265 UNP Q2HJ86 ILE 265 CONFLICT
SEQADV 4ATX GLU B 358 UNP Q2HJ86 GLN 358 CONFLICT
SEQADV 4ATX VAL B 437 UNP Q2HJ86 MET 437 CONFLICT
SEQADV 4ATX GLU B 450 UNP Q2HJ86 ASP 450 CONFLICT
SEQADV 4ATX ASN C 92 UNP Q2PQA9 THR 92 ENGINEERED MUTATION
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 340 MET ALA ASP PRO ALA GLU CYS ASN ILE LYS VAL MET CYS
SEQRES 2 C 340 ARG PHE ARG PRO LEU ASN GLU SER GLU VAL ASN ARG GLY
SEQRES 3 C 340 ASP LYS TYR VAL ALA LYS PHE GLN GLY GLU ASP THR VAL
SEQRES 4 C 340 MET ILE ALA SER LYS PRO TYR ALA PHE ASP ARG VAL PHE
SEQRES 5 C 340 GLN SER SER THR SER GLN GLU GLN VAL TYR ASN ASP CYS
SEQRES 6 C 340 ALA LYS LYS ILE VAL LYS ASP VAL LEU GLU GLY TYR ASN
SEQRES 7 C 340 GLY THR ILE PHE ALA TYR GLY GLN THR SER SER GLY LYS
SEQRES 8 C 340 ASN HIS THR MET GLU GLY LYS LEU HIS ASP PRO GLU GLY
SEQRES 9 C 340 MET GLY ILE ILE PRO ARG ILE VAL GLN ASP ILE PHE ASN
SEQRES 10 C 340 TYR ILE TYR SER MET ASP GLU ASN LEU GLU PHE HIS ILE
SEQRES 11 C 340 LYS VAL SER TYR PHE GLU ILE TYR LEU ASP LYS ILE ARG
SEQRES 12 C 340 ASP LEU LEU ASP VAL SER LYS THR ASN LEU SER VAL HIS
SEQRES 13 C 340 GLU ASP LYS ASN ARG VAL PRO TYR VAL LYS GLY CYS THR
SEQRES 14 C 340 GLU ARG PHE VAL CYS SER PRO ASP GLU VAL MET ASP THR
SEQRES 15 C 340 ILE ASP GLU GLY LYS SER ASN ARG HIS VAL ALA VAL THR
SEQRES 16 C 340 ASN MET ASN GLU HIS SER SER ARG SER HIS SER ILE PHE
SEQRES 17 C 340 LEU ILE ASN VAL LYS GLN GLU ASN THR GLN THR GLU GLN
SEQRES 18 C 340 LYS LEU SER GLY LYS LEU TYR LEU VAL ASP LEU ALA GLY
SEQRES 19 C 340 SER GLU LYS VAL SER LYS THR GLY ALA GLU GLY ALA VAL
SEQRES 20 C 340 LEU ASP GLU ALA LYS ASN ILE ASN LYS SER LEU SER ALA
SEQRES 21 C 340 LEU GLY ASN VAL ILE SER ALA LEU ALA GLU GLY SER THR
SEQRES 22 C 340 TYR VAL PRO TYR ARG ASP SER LYS MET THR ARG ILE LEU
SEQRES 23 C 340 GLN ASP SER LEU GLY GLY ASN CYS ARG THR THR ILE VAL
SEQRES 24 C 340 ILE CYS CYS SER PRO SER SER TYR ASN GLU SER GLU THR
SEQRES 25 C 340 LYS SER THR LEU LEU PHE GLY GLN ARG ALA LYS THR ILE
SEQRES 26 C 340 LYS ASN THR VAL CYS VAL ASN VAL GLU LEU THR ALA GLU
SEQRES 27 C 340 GLN TRP
HET GDP A 600 28
HET GTP B 500 32
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
FORMUL 4 GDP C10 H15 N5 O11 P2
FORMUL 5 GTP 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 ASN C 19 GLY C 26 1 8
HELIX 38 38 SER C 57 ALA C 66 1 10
HELIX 39 39 ALA C 66 GLY C 76 1 11
HELIX 40 40 GLY C 90 GLU C 96 1 7
HELIX 41 41 GLY C 106 ASP C 123 1 18
HELIX 42 42 SER C 175 VAL C 192 1 18
HELIX 43 43 ASN C 196 SER C 204 1 9
HELIX 44 44 ASN C 255 GLY C 271 1 17
HELIX 45 45 PRO C 276 ASP C 279 5 4
HELIX 46 46 SER C 280 GLN C 287 1 8
HELIX 47 47 GLU C 309 ARG C 321 1 13
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 CA 8 ARG C 50 PHE C 52 0
SHEET 2 CA 8 ASN C 8 PHE C 15 1 O CYS C 13 N PHE C 52
SHEET 3 CA 8 ARG C 295 CYS C 302 1 O THR C 296 N LYS C 10
SHEET 4 CA 8 GLY C 79 TYR C 84 1 O THR C 80 N THR C 297
SHEET 5 CA 8 LYS C 222 ASP C 231 1 O LYS C 226 N GLY C 79
SHEET 6 CA 8 HIS C 205 ASN C 216 -1 O SER C 206 N ASP C 231
SHEET 7 CA 8 LEU C 126 TYR C 138 -1 O GLU C 127 N GLU C 215
SHEET 8 CA 8 LYS C 141 ASP C 144 -1 O LYS C 141 N TYR C 138
SHEET 1 CB 8 ARG C 50 PHE C 52 0
SHEET 2 CB 8 ASN C 8 PHE C 15 1 O CYS C 13 N PHE C 52
SHEET 3 CB 8 ARG C 295 CYS C 302 1 O THR C 296 N LYS C 10
SHEET 4 CB 8 GLY C 79 TYR C 84 1 O THR C 80 N THR C 297
SHEET 5 CB 8 LYS C 222 ASP C 231 1 O LYS C 226 N GLY C 79
SHEET 6 CB 8 HIS C 205 ASN C 216 -1 O SER C 206 N ASP C 231
SHEET 7 CB 8 LEU C 126 TYR C 138 -1 O GLU C 127 N GLU C 215
SHEET 8 CB 8 ARG C 171 PHE C 172 -1 O ARG C 171 N VAL C 132
SHEET 1 CC 2 LYS C 141 ASP C 144 0
SHEET 2 CC 2 LEU C 126 TYR C 138 -1 O GLU C 136 N ARG C 143
SHEET 1 CD 3 LYS C 32 GLN C 34 0
SHEET 2 CD 3 THR C 38 ILE C 41 -1 O THR C 38 N GLN C 34
SHEET 3 CD 3 LYS C 44 ALA C 47 -1 O LYS C 44 N ILE C 41
SHEET 1 CE 2 VAL C 155 GLU C 157 0
SHEET 2 CE 2 PRO C 163 VAL C 165 -1 O TYR C 164 N HIS C 156
CISPEP 1 GLY B 57 ALA B 58 0 -0.13
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
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
