HEADER TRANSPORT PROTEIN 12-MAR-07 2P4N
TITLE HUMAN MONOMERIC KINESIN (1BG2) AND BOVINE TUBULIN (1JFF) DOCKED INTO
TITLE 2 THE 9-ANGSTROM CRYO-EM MAP OF NUCLEOTIDE-FREE KINESIN COMPLEXED TO
TITLE 3 THE MICROTUBULE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KINESIN HEAVY CHAIN;
COMPND 3 CHAIN: K;
COMPND 4 FRAGMENT: K349 CONSTRUCT OF HUMAN KINESIN;
COMPND 5 SYNONYM: UBIQUITOUS KINESIN HEAVY CHAIN, UKHC;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TUBULIN ALPHA CHAIN;
COMPND 8 CHAIN: A;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: TUBULIN BETA CHAIN;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: BETA TUBULIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 OTHER_DETAILS: THE ACTUAL CONSTRUCT USED IN THE EM STUDIES IS A
SOURCE 5 MUTANT PROTEIN (CALLED CYS-LITE);
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 8 ORGANISM_COMMON: BOVINE;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 11 ORGANISM_COMMON: BOVINE
KEYWDS MOTOR PROTEIN, ATPASE, TRANSPORT PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR C.V.SINDELAR,K.H.DOWNING
REVDAT 5 21-FEB-24 2P4N 1 REMARK LINK
REVDAT 4 18-JUL-18 2P4N 1 REMARK
REVDAT 3 14-APR-09 2P4N 1 REMARK
REVDAT 2 24-FEB-09 2P4N 1 VERSN
REVDAT 1 08-JUL-08 2P4N 0
JRNL AUTH C.V.SINDELAR,K.H.DOWNING
JRNL TITL THE BEGINNING OF KINESIN'S FORCE-GENERATING CYCLE VISUALIZED
JRNL TITL 2 AT 9-A RESOLUTION.
JRNL REF J.CELL BIOL. V. 177 377 2007
JRNL REFN ISSN 0021-9525
JRNL PMID 17470637
JRNL DOI 10.1083/JCB.200612090
REMARK 2
REMARK 2 RESOLUTION. 9.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : SITUS, 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 : RECIPROCAL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 1.000
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 9.000
REMARK 3 NUMBER OF PARTICLES : 150000
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: THE MAGNIFICATION WAS
REMARK 3 CALIBRATED BY ASSUMING A MICROTUBULE DIMER SPACING OF 80.0
REMARK 3 ANGSTROMS.
REMARK 3
REMARK 3 OTHER DETAILS: SINGLE-PARTICLE ANALYSIS WAS EMPLOYED.
REMARK 4
REMARK 4 2P4N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000041960.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : FILAMENT
REMARK 245 PARTICLE TYPE : HELICAL
REMARK 245 NAME OF SAMPLE : NUCLEOTIDE-FREE KINESIN BOUND
REMARK 245 TO A 13-PROTOFILAMENT
REMARK 245 MICROTUBULE; KINESIN HEAVY
REMARK 245 CHAIN; TUBULIN ALPHA CHAIN;
REMARK 245 TUBULIN BETA CHAIN
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : 300 MESH COPPER GRID
REMARK 245 SAMPLE VITRIFICATION DETAILS : ETHANE
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 6.80
REMARK 245 SAMPLE DETAILS : MICROTUBULE ASSOCIATED COMPLEX;
REMARK 245 MICROTUBULE; MICROTUBULE
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : 103.15
REMARK 245 MICROSCOPE MODEL : JEOL 4000
REMARK 245 DETECTOR TYPE : KODAK SO-163 FILM
REMARK 245 MINIMUM DEFOCUS (NM) : 700.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 1500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : 0.00
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : 0.00
REMARK 245 NOMINAL CS : 4.10
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 1600.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 60000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : LAB6
REMARK 245 ACCELERATION VOLTAGE (KV) : 400
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 APPLY THE FOLLOWING TO CHAINS: K, A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 K 1
REMARK 465 ALA K 2
REMARK 465 MET A 1
REMARK 465 GLN A 35
REMARK 465 MET A 36
REMARK 465 PRO A 37
REMARK 465 SER A 38
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 PHE A 49
REMARK 465 ASN A 50
REMARK 465 THR A 51
REMARK 465 PHE A 52
REMARK 465 PHE A 53
REMARK 465 SER A 54
REMARK 465 GLU A 55
REMARK 465 THR A 56
REMARK 465 GLY A 57
REMARK 465 ALA A 58
REMARK 465 GLY A 59
REMARK 465 LYS A 60
REMARK 465 VAL A 440
REMARK 465 GLU A 441
REMARK 465 GLY A 442
REMARK 465 GLU A 443
REMARK 465 GLY A 444
REMARK 465 GLU A 445
REMARK 465 GLU A 446
REMARK 465 GLU A 447
REMARK 465 GLY A 448
REMARK 465 GLU A 449
REMARK 465 GLU A 450
REMARK 465 TYR A 451
REMARK 465 MET B 1
REMARK 465 ALA B 438
REMARK 465 THR B 439
REMARK 465 ALA B 440
REMARK 465 ASP B 441
REMARK 465 GLU B 442
REMARK 465 GLN B 443
REMARK 465 GLY B 444
REMARK 465 GLU B 445
REMARK 465 PHE B 446
REMARK 465 GLU B 447
REMARK 465 GLU B 448
REMARK 465 GLU B 449
REMARK 465 GLY B 450
REMARK 465 GLU B 451
REMARK 465 GLU B 452
REMARK 465 ASP B 453
REMARK 465 GLU B 454
REMARK 465 ALA B 455
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 ALA A 265 CB
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 N ASP K 249 CD LYS A 112 0.24
REMARK 500 O LYS K 252 CA GLY A 412 0.35
REMARK 500 CD2 LEU K 248 CB ILE A 115 0.39
REMARK 500 NZ LYS K 237 C MET A 413 0.43
REMARK 500 OD1 ASN K 253 N GLU A 411 0.62
REMARK 500 ND2 ASN K 253 O GLY A 410 0.63
REMARK 500 CG ASN K 253 C GLY A 410 0.66
REMARK 500 OE2 GLU K 250 O TYR A 108 0.81
REMARK 500 O GLU K 250 CB TYR A 108 0.85
REMARK 500 CA ASP K 249 CG LYS A 112 0.87
REMARK 500 CG1 VAL K 247 OD1 ASP A 116 0.95
REMARK 500 CB ALA K 251 CA THR A 109 1.10
REMARK 500 C LEU K 248 CD LYS A 112 1.12
REMARK 500 OD1 ASN K 253 CA GLU A 411 1.12
REMARK 500 CE LYS K 237 C MET A 413 1.15
REMARK 500 ND2 ASN K 253 C GLY A 410 1.18
REMARK 500 CE LYS K 237 O MET A 413 1.21
REMARK 500 NZ LYS K 237 O MET A 413 1.24
REMARK 500 CD GLU K 250 O HIS A 107 1.28
REMARK 500 CG ASN K 253 N GLU A 411 1.35
REMARK 500 OD1 ASN K 253 C GLY A 410 1.36
REMARK 500 O LYS K 252 N GLY A 412 1.36
REMARK 500 C LYS K 252 CA GLY A 412 1.37
REMARK 500 CB LEU K 248 CG2 ILE A 115 1.38
REMARK 500 CG ASN K 253 O GLY A 410 1.39
REMARK 500 CD2 LEU K 248 CG2 ILE A 115 1.41
REMARK 500 C LYS K 252 N GLY A 412 1.41
REMARK 500 CA ASN K 253 O VAL A 409 1.42
REMARK 500 N ASP K 249 CG LYS A 112 1.42
REMARK 500 OE2 GLU K 250 C TYR A 108 1.43
REMARK 500 N ASP K 249 CE LYS A 112 1.44
REMARK 500 NZ LYS K 237 CA MET A 413 1.45
REMARK 500 CG LEU K 248 CB ILE A 115 1.46
REMARK 500 CD2 LEU K 248 CG1 ILE A 115 1.47
REMARK 500 OE1 GLU K 250 O HIS A 107 1.49
REMARK 500 CG LEU K 248 CG2 ILE A 115 1.49
REMARK 500 CD LYS K 237 O MET A 413 1.51
REMARK 500 NZ LYS K 237 N GLU A 414 1.55
REMARK 500 CG GLU K 250 CA TYR A 108 1.55
REMARK 500 O LYS K 252 C GLY A 412 1.63
REMARK 500 CA ASP K 249 CD LYS A 112 1.64
REMARK 500 CB ILE K 254 CG1 VAL A 409 1.64
REMARK 500 CG GLU K 250 N TYR A 108 1.66
REMARK 500 CG2 VAL K 247 NH1 ARG A 156 1.67
REMARK 500 CB LEU K 248 O LYS A 112 1.68
REMARK 500 C ASP K 249 CG LYS A 112 1.69
REMARK 500 CA ALA K 251 N THR A 109 1.71
REMARK 500 CG1 VAL K 247 CG ASP A 116 1.72
REMARK 500 CB ASN K 253 O VAL A 409 1.72
REMARK 500 CB VAL K 247 OD1 ASP A 116 1.77
REMARK 500
REMARK 500 THIS ENTRY HAS 100 CLOSE CONTACTS
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 PRO A 173 C - N - CA ANGL. DEV. = 13.9 DEGREES
REMARK 500 MET B 235 CG - SD - CE ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO B 263 C - N - CA ANGL. DEV. = 13.0 DEGREES
REMARK 500 PRO B 263 C - N - CD ANGL. DEV. = -13.7 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 ALA K 5 -9.60 -140.21
REMARK 500 GLU K 6 112.03 67.33
REMARK 500 CYS K 7 76.10 68.73
REMARK 500 ASN K 8 55.33 -95.23
REMARK 500 SER K 43 -19.32 73.13
REMARK 500 ARG K 50 148.98 -171.82
REMARK 500 SER K 88 6.98 80.79
REMARK 500 MET K 122 -79.39 -92.60
REMARK 500 ASP K 123 11.61 34.58
REMARK 500 GLU K 124 -84.90 -92.41
REMARK 500 ASN K 160 42.67 -106.88
REMARK 500 ARG K 161 -22.31 64.59
REMARK 500 GLU K 220 -14.03 77.99
REMARK 500 SER K 239 30.12 71.61
REMARK 500 GLU K 244 -152.45 177.35
REMARK 500 ALA K 246 -77.08 -36.77
REMARK 500 VAL K 247 33.14 -96.29
REMARK 500 LEU K 248 82.77 -161.71
REMARK 500 GLU K 250 23.18 178.83
REMARK 500 LYS K 252 133.52 -178.50
REMARK 500 ALA K 322 72.52 -101.53
REMARK 500 LEU A 23 -38.38 -38.56
REMARK 500 TYR A 24 -79.83 -51.90
REMARK 500 GLN A 31 -179.94 -53.26
REMARK 500 PRO A 32 -59.24 -29.52
REMARK 500 PRO A 63 -153.11 -59.34
REMARK 500 ARG A 64 44.43 -166.16
REMARK 500 PRO A 89 3.89 -52.67
REMARK 500 LYS A 96 -26.98 -27.23
REMARK 500 GLU A 97 -131.64 -51.28
REMARK 500 ALA A 100 112.24 74.01
REMARK 500 ASN A 101 43.75 -73.63
REMARK 500 TYR A 103 -79.69 -38.57
REMARK 500 ALA A 104 -70.06 -21.27
REMARK 500 TYR A 108 -116.94 -70.82
REMARK 500 THR A 109 -94.34 -11.61
REMARK 500 ILE A 110 -70.70 -67.58
REMARK 500 GLU A 113 -38.93 -39.68
REMARK 500 ASP A 116 -73.01 -40.05
REMARK 500 CYS A 129 -164.35 -67.44
REMARK 500 SER A 140 65.53 -112.33
REMARK 500 PHE A 141 -67.80 11.54
REMARK 500 SER A 147 -70.39 -81.90
REMARK 500 PHE A 149 -74.66 -26.93
REMARK 500 SER A 158 -18.45 -48.59
REMARK 500 TYR A 161 43.91 -147.05
REMARK 500 LYS A 163 44.22 -81.92
REMARK 500 PRO A 173 119.98 -23.29
REMARK 500 GLN A 176 -21.17 -144.27
REMARK 500 VAL A 177 57.62 -103.87
REMARK 500
REMARK 500 THIS ENTRY HAS 198 RAMACHANDRAN OUTLIERS.
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 K 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR K 92 OG1
REMARK 620 2 ADP K 401 O1B 74.9
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP K 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TA1 B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BG2 RELATED DB: PDB
REMARK 900 MONOMERIC HUMAN KINESIN
REMARK 900 RELATED ID: 1JFF RELATED DB: PDB
REMARK 900 REFINED STRUCTURE OF ALPHA-BETA TUBULIN FROM ZINC-INDUCED SHEETS
REMARK 900 STABILIZED WITH TAXOL
REMARK 900 RELATED ID: EMD-1340 RELATED DB: EMDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF KINESIN (CHAIN K) IN THE SAMPLE INCLUDED
REMARK 999 MUTATIONS.THE CONSTRUCT IS KNOWN AS CYS-LITE. MODEL CRYSTAL
REMARK 999 STRUCTURE FOR FITTING THE MAP WAS THE NATIVE SEQUENCE. IN THE CASE
REMARK 999 OF TUBULIN A AND B (CHAINS A AND B), THE SEQUENCE IN THE SAMPLE WAS
REMARK 999 DERIVED FROM COW, WHILE THE MODEL USED FOR FITTING THE MAP WAS A
REMARK 999 PIG PROTEIN.
DBREF 2P4N K 1 325 PDB 2P4N 2P4N 1 325
DBREF 2P4N A 1 451 PDB 2P4N 2P4N 1 451
DBREF 2P4N B 1 455 PDB 2P4N 2P4N 1 455
SEQRES 1 K 325 MET ALA ASP LEU ALA GLU CYS ASN ILE LYS VAL MET CYS
SEQRES 2 K 325 ARG PHE ARG PRO LEU ASN GLU SER GLU VAL ASN ARG GLY
SEQRES 3 K 325 ASP LYS TYR ILE ALA LYS PHE GLN GLY GLU ASP THR VAL
SEQRES 4 K 325 VAL ILE ALA SER LYS PRO TYR ALA PHE ASP ARG VAL PHE
SEQRES 5 K 325 GLN SER SER THR SER GLN GLU GLN VAL TYR ASN ASP CYS
SEQRES 6 K 325 ALA LYS LYS ILE VAL LYS ASP VAL LEU GLU GLY TYR ASN
SEQRES 7 K 325 GLY THR ILE PHE ALA TYR GLY GLN THR SER SER GLY LYS
SEQRES 8 K 325 THR HIS THR MET GLU GLY LYS LEU HIS ASP PRO GLU GLY
SEQRES 9 K 325 MET GLY ILE ILE PRO ARG ILE VAL GLN ASP ILE PHE ASN
SEQRES 10 K 325 TYR ILE TYR SER MET ASP GLU ASN LEU GLU PHE HIS ILE
SEQRES 11 K 325 LYS VAL SER TYR PHE GLU ILE TYR LEU ASP LYS ILE ARG
SEQRES 12 K 325 ASP LEU LEU ASP VAL SER LYS THR ASN LEU SER VAL HIS
SEQRES 13 K 325 GLU ASP LYS ASN ARG VAL PRO TYR VAL LYS GLY CYS THR
SEQRES 14 K 325 GLU ARG PHE VAL CYS SER PRO ASP GLU VAL MET ASP THR
SEQRES 15 K 325 ILE ASP GLU GLY LYS SER ASN ARG HIS VAL ALA VAL THR
SEQRES 16 K 325 ASN MET ASN GLU HIS SER SER ARG SER HIS SER ILE PHE
SEQRES 17 K 325 LEU ILE ASN VAL LYS GLN GLU ASN THR GLN THR GLU GLN
SEQRES 18 K 325 LYS LEU SER GLY LYS LEU TYR LEU VAL ASP LEU ALA GLY
SEQRES 19 K 325 SER GLU LYS VAL SER LYS THR GLY ALA GLU GLY ALA VAL
SEQRES 20 K 325 LEU ASP GLU ALA LYS ASN ILE ASN LYS SER LEU SER ALA
SEQRES 21 K 325 LEU GLY ASN VAL ILE SER ALA LEU ALA GLU GLY SER THR
SEQRES 22 K 325 TYR VAL PRO TYR ARG ASP SER LYS MET THR ARG ILE LEU
SEQRES 23 K 325 GLN ASP SER LEU GLY GLY ASN CYS ARG THR THR ILE VAL
SEQRES 24 K 325 ILE CYS CYS SER PRO SER SER TYR ASN GLU SER GLU THR
SEQRES 25 K 325 LYS SER THR LEU LEU PHE GLY GLN ARG ALA LYS THR ILE
SEQRES 1 A 451 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 A 451 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 A 451 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 A 451 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 A 451 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 A 451 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 A 451 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 A 451 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 A 451 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 A 451 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 A 451 GLY LEU GLN GLY PHE SER VAL PHE HIS SER PHE GLY GLY
SEQRES 12 A 451 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 A 451 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 A 451 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 A 451 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 A 451 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 A 451 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 A 451 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 A 451 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 A 451 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 A 451 PRO TYR PRO ARG ALA HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 A 451 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 A 451 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 A 451 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 A 451 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 A 451 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 A 451 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 A 451 LYS VAL GLY ILE ASN TYR GLU PRO PRO THR VAL VAL PRO
SEQRES 29 A 451 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 A 451 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 A 451 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 A 451 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 A 451 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 A 451 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 A 451 GLU GLY GLU GLU GLU GLY GLU GLU TYR
SEQRES 1 B 445 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 B 445 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 B 445 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 B 445 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 B 445 GLU ALA ALA GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 B 445 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 B 445 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 B 445 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 B 445 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 B 445 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 B 445 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 B 445 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 B 445 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 B 445 VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 B 445 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 B 445 THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 B 445 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 B 445 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 B 445 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 B 445 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 B 445 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 B 445 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 B 445 PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET
SEQRES 24 B 445 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 B 445 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 B 445 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 B 445 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 B 445 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 B 445 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 B 445 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 B 445 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 B 445 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 B 445 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR
SEQRES 34 B 445 ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLY GLU GLU
SEQRES 35 B 445 ASP GLU ALA
HET MG K 402 1
HET ADP K 401 27
HET ZN A 900 1
HET MG A 501 1
HET GTP B 500 32
HET GDP B 600 28
HET TA1 B 601 62
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM ZN ZINC ION
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM TA1 TAXOL
FORMUL 4 MG 2(MG 2+)
FORMUL 5 ADP C10 H15 N5 O10 P2
FORMUL 6 ZN ZN 2+
FORMUL 8 GTP C10 H16 N5 O14 P3
FORMUL 9 GDP C10 H15 N5 O11 P2
FORMUL 10 TA1 C47 H51 N O14
HELIX 1 1 ASN K 19 GLY K 26 1 8
HELIX 2 2 SER K 57 ALA K 66 1 10
HELIX 3 3 ALA K 66 GLU K 75 1 10
HELIX 4 4 GLY K 90 GLU K 96 1 7
HELIX 5 5 GLY K 106 ASP K 123 1 18
HELIX 6 6 SER K 175 ARG K 190 1 16
HELIX 7 7 ASN K 196 SER K 204 1 9
HELIX 8 8 ASN K 255 GLU K 270 1 16
HELIX 9 9 PRO K 276 ASP K 279 5 4
HELIX 10 10 SER K 280 LEU K 286 1 7
HELIX 11 11 GLN K 287 SER K 289 5 3
HELIX 12 12 SER K 305 TYR K 307 5 3
HELIX 13 13 ASN K 308 ARG K 321 1 14
HELIX 14 14 GLY A 10 GLU A 27 1 18
HELIX 15 15 GLU A 71 GLY A 81 1 11
HELIX 16 16 ASN A 102 TYR A 108 1 7
HELIX 17 17 TYR A 108 CYS A 129 1 22
HELIX 18 18 SER A 147 TYR A 161 1 15
HELIX 19 19 GLU A 183 LEU A 195 1 13
HELIX 20 20 ASP A 205 ASN A 216 1 12
HELIX 21 21 THR A 223 ARG A 243 1 21
HELIX 22 22 ASP A 251 VAL A 260 1 10
HELIX 23 23 SER A 287 THR A 292 1 6
HELIX 24 24 THR A 292 GLU A 297 1 6
HELIX 25 25 VAL A 324 THR A 337 1 14
HELIX 26 26 ILE A 384 ALA A 400 1 17
HELIX 27 27 LYS A 401 PHE A 404 5 4
HELIX 28 28 VAL A 405 GLY A 410 1 6
HELIX 29 29 GLU A 414 LYS A 430 1 17
HELIX 30 30 LYS A 430 VAL A 435 1 6
HELIX 31 31 GLN B 11 GLU B 27 1 17
HELIX 32 32 ARG B 48 TYR B 53 5 6
HELIX 33 33 GLU B 71 ARG B 79 1 9
HELIX 34 34 PRO B 82 ILE B 86 5 5
HELIX 35 35 ARG B 88 ASP B 90 5 3
HELIX 36 36 GLU B 110 GLU B 127 1 18
HELIX 37 37 GLY B 143 TYR B 161 1 19
HELIX 38 38 GLU B 183 VAL B 195 1 13
HELIX 39 39 ASP B 205 ARG B 215 1 11
HELIX 40 40 THR B 223 ARG B 243 1 21
HELIX 41 41 ASP B 251 VAL B 260 1 10
HELIX 42 42 VAL B 288 PHE B 296 1 9
HELIX 43 43 ASP B 306 GLY B 310 5 5
HELIX 44 44 SER B 324 ASN B 339 1 16
HELIX 45 45 ILE B 384 ARG B 400 1 17
HELIX 46 46 LYS B 402 PHE B 404 5 3
HELIX 47 47 LEU B 405 GLY B 410 1 6
HELIX 48 48 ASP B 414 ASP B 437 1 24
SHEET 1 A 8 ARG K 50 PHE K 52 0
SHEET 2 A 8 ASN K 8 PHE K 15 1 N CYS K 13 O PHE K 52
SHEET 3 A 8 ARG K 295 CYS K 302 1 O THR K 296 N LYS K 10
SHEET 4 A 8 GLY K 79 TYR K 84 1 N TYR K 84 O CYS K 301
SHEET 5 A 8 LYS K 222 ASP K 231 1 O VAL K 230 N ILE K 81
SHEET 6 A 8 HIS K 205 ASN K 216 -1 N PHE K 208 O LEU K 229
SHEET 7 A 8 LEU K 126 TYR K 138 -1 N LYS K 131 O ASN K 211
SHEET 8 A 8 LYS K 141 ASP K 144 -1 O ARG K 143 N GLU K 136
SHEET 1 B 8 ARG K 50 PHE K 52 0
SHEET 2 B 8 ASN K 8 PHE K 15 1 N CYS K 13 O PHE K 52
SHEET 3 B 8 ARG K 295 CYS K 302 1 O THR K 296 N LYS K 10
SHEET 4 B 8 GLY K 79 TYR K 84 1 N TYR K 84 O CYS K 301
SHEET 5 B 8 LYS K 222 ASP K 231 1 O VAL K 230 N ILE K 81
SHEET 6 B 8 HIS K 205 ASN K 216 -1 N PHE K 208 O LEU K 229
SHEET 7 B 8 LEU K 126 TYR K 138 -1 N LYS K 131 O ASN K 211
SHEET 8 B 8 ARG K 171 VAL K 173 -1 O ARG K 171 N VAL K 132
SHEET 1 C 3 LYS K 32 GLN K 34 0
SHEET 2 C 3 THR K 38 ILE K 41 -1 O VAL K 40 N LYS K 32
SHEET 3 C 3 LYS K 44 ALA K 47 -1 O TYR K 46 N VAL K 39
SHEET 1 D 2 VAL K 155 GLU K 157 0
SHEET 2 D 2 PRO K 163 VAL K 165 -1 O TYR K 164 N HIS K 156
SHEET 1 E 6 LEU A 92 THR A 94 0
SHEET 2 E 6 ALA A 65 ASP A 69 1 N PHE A 67 O ILE A 93
SHEET 3 E 6 CYS A 4 VAL A 9 1 N SER A 6 O VAL A 66
SHEET 4 E 6 GLY A 134 HIS A 139 1 O SER A 136 N ILE A 5
SHEET 5 E 6 LEU A 167 SER A 170 1 O PHE A 169 N VAL A 137
SHEET 6 E 6 CYS A 200 MET A 203 1 O PHE A 202 N SER A 170
SHEET 1 F 4 LEU A 269 THR A 271 0
SHEET 2 F 4 ARG A 373 THR A 381 -1 O SER A 379 N LEU A 269
SHEET 3 F 4 TYR A 312 GLY A 321 -1 N CYS A 316 O LEU A 378
SHEET 4 F 4 PHE A 351 ILE A 355 1 O GLY A 354 N TYR A 319
SHEET 1 G10 PHE B 92 PHE B 94 0
SHEET 2 G10 ALA B 65 ASP B 69 1 N LEU B 67 O VAL B 93
SHEET 3 G10 HIS B 6 ALA B 9 1 N GLN B 8 O ILE B 66
SHEET 4 G10 GLY B 134 HIS B 139 1 O THR B 138 N ILE B 7
SHEET 5 G10 ILE B 165 SER B 170 1 O PHE B 169 N LEU B 137
SHEET 6 G10 GLU B 200 TYR B 202 1 O TYR B 202 N THR B 168
SHEET 7 G10 PHE B 267 GLY B 271 1 O PHE B 268 N THR B 201
SHEET 8 G10 ALA B 375 SER B 381 -1 O PHE B 377 N GLY B 271
SHEET 9 G10 TYR B 312 ARG B 320 -1 N VAL B 318 O THR B 376
SHEET 10 G10 VAL B 351 CYS B 356 1 O CYS B 356 N PHE B 319
LINK OG1 THR K 92 MG MG K 402 1555 1555 2.29
LINK O1B ADP K 401 MG MG K 402 1555 1555 2.42
LINK MG MG A 501 O1G GTP B 500 1555 1555 2.45
SITE 1 AC1 2 THR K 92 ADP K 401
SITE 1 AC2 1 HIS A 283
SITE 1 AC3 3 GLN A 11 GLU A 71 GTP B 500
SITE 1 AC4 12 ARG K 14 ARG K 16 PRO K 17 GLN K 86
SITE 2 AC4 12 THR K 87 SER K 88 SER K 89 GLY K 90
SITE 3 AC4 12 LYS K 91 THR K 92 HIS K 93 MG K 402
SITE 1 AC5 20 GLY A 10 GLN A 11 ALA A 12 GLN A 15
SITE 2 AC5 20 ALA A 99 ALA A 100 ASN A 101 SER A 140
SITE 3 AC5 20 GLY A 143 GLY A 144 THR A 145 GLY A 146
SITE 4 AC5 20 ILE A 171 GLU A 183 ASN A 206 TYR A 224
SITE 5 AC5 20 ASN A 228 MG A 501 LEU B 248 LYS B 254
SITE 1 AC6 13 GLY B 10 GLN B 11 CYS B 12 GLN B 15
SITE 2 AC6 13 SER B 140 GLY B 142 GLY B 144 THR B 145
SITE 3 AC6 13 GLY B 146 ASP B 179 ASN B 206 TYR B 224
SITE 4 AC6 13 ASN B 228
SITE 1 AC7 15 VAL B 23 ASP B 26 GLU B 27 HIS B 229
SITE 2 AC7 15 LEU B 230 ALA B 233 SER B 236 PHE B 272
SITE 3 AC7 15 PRO B 274 LEU B 275 THR B 276 ARG B 278
SITE 4 AC7 15 PRO B 360 ARG B 369 GLY B 370
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
