HEADER CELL CYCLE 29-OCT-15 5EIB
TITLE CRYSTAL STRUCTURE OF CPAP PN2-3 C-TERMINAL LOOP-HELIX IN COMPLEX WITH
TITLE 2 DARPIN-TUBULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUBULIN ALPHA-1B CHAIN;
COMPND 3 CHAIN: C;
COMPND 4 SYNONYM: ALPHA-TUBULIN UBIQUITOUS,TUBULIN K-ALPHA-1,TUBULIN ALPHA-
COMPND 5 UBIQUITOUS CHAIN;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TUBULIN BETA-2B CHAIN;
COMPND 8 CHAIN: D;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: DESIGNED ANKYRIN REPEAT PROTEIN;
COMPND 11 CHAIN: E;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: PEPTIDE FROM CENTROMERE PROTEIN J;
COMPND 15 CHAIN: F;
COMPND 16 SYNONYM: CENP-J,CENTROSOMAL P4.1-ASSOCIATED PROTEIN,LAG-3-ASSOCIATED
COMPND 17 PROTEIN,LYST-INTERACTING PROTEIN 1;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 7 ORGANISM_COMMON: BOVINE;
SOURCE 8 ORGANISM_TAXID: 9913;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 MOL_ID: 4;
SOURCE 15 SYNTHETIC: YES;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 9606
KEYWDS PN2-3, TUBULIN COMPLEX, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,X.ZHENG
REVDAT 3 08-NOV-23 5EIB 1 LINK
REVDAT 2 04-OCT-17 5EIB 1 REMARK
REVDAT 1 26-OCT-16 5EIB 0
JRNL AUTH X.ZHENG,A.RAMANI,K.SONI,M.GOTTARDO,S.ZHENG,L.MING GOOI,W.LI,
JRNL AUTH 2 S.FENG,A.MARIAPPAN,A.WASON,P.WIDLUND,A.POZNIAKOVSKY,I.POSER,
JRNL AUTH 3 H.DENG,G.OU,M.RIPARBELLI,C.GIULIANO,A.A.HYMAN,M.SATTLER,
JRNL AUTH 4 J.GOPALAKRISHNAN,H.LI
JRNL TITL MOLECULAR BASIS FOR CPAP-TUBULIN INTERACTION IN CONTROLLING
JRNL TITL 2 CENTRIOLAR AND CILIARY LENGTH
JRNL REF NAT COMMUN V. 7 11874 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 27306797
JRNL DOI 10.1038/NCOMMS11874
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 63538
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 3127
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.3550 - 5.8707 0.99 2856 128 0.1528 0.1755
REMARK 3 2 5.8707 - 4.6618 1.00 2788 164 0.1651 0.1802
REMARK 3 3 4.6618 - 4.0731 1.00 2794 145 0.1395 0.1950
REMARK 3 4 4.0731 - 3.7010 0.99 2775 128 0.1450 0.1745
REMARK 3 5 3.7010 - 3.4358 0.99 2766 160 0.1577 0.2033
REMARK 3 6 3.4358 - 3.2334 1.00 2742 148 0.1775 0.2139
REMARK 3 7 3.2334 - 3.0715 1.00 2774 141 0.1855 0.2430
REMARK 3 8 3.0715 - 2.9378 1.00 2761 162 0.1853 0.2334
REMARK 3 9 2.9378 - 2.8248 1.00 2781 143 0.1974 0.2251
REMARK 3 10 2.8248 - 2.7273 1.00 2752 138 0.1918 0.2552
REMARK 3 11 2.7273 - 2.6420 0.99 2787 128 0.1989 0.2731
REMARK 3 12 2.6420 - 2.5665 0.99 2743 131 0.1910 0.2758
REMARK 3 13 2.5665 - 2.4990 0.99 2772 131 0.1950 0.2776
REMARK 3 14 2.4990 - 2.4380 1.00 2732 140 0.1940 0.2219
REMARK 3 15 2.4380 - 2.3826 0.99 2722 131 0.1942 0.2306
REMARK 3 16 2.3826 - 2.3319 0.98 2730 149 0.2059 0.2552
REMARK 3 17 2.3319 - 2.2852 0.99 2733 141 0.2112 0.3027
REMARK 3 18 2.2852 - 2.2421 0.98 2721 149 0.2175 0.2736
REMARK 3 19 2.2421 - 2.2021 0.99 2709 146 0.2100 0.2407
REMARK 3 20 2.2021 - 2.1648 0.98 2686 145 0.2171 0.2455
REMARK 3 21 2.1648 - 2.1298 0.98 2717 140 0.2360 0.2862
REMARK 3 22 2.1298 - 2.0971 0.93 2570 139 0.2518 0.3190
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.44
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 8257
REMARK 3 ANGLE : 1.261 11211
REMARK 3 CHIRALITY : 0.056 1245
REMARK 3 PLANARITY : 0.007 1459
REMARK 3 DIHEDRAL : 17.381 3013
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5EIB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000214884.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : ADSC QUANTUM 315R
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63572
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.12800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.89900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4DRX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM SODIUM TARTRATE, PEG 3000,
REMARK 280 PH 6.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 282K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 45.55800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 C 1
REMARK 465 ASP C 39
REMARK 465 LYS C 40
REMARK 465 THR C 41
REMARK 465 ILE C 42
REMARK 465 GLY C 43
REMARK 465 GLY C 44
REMARK 465 GLY C 45
REMARK 465 ASP C 46
REMARK 465 SER C 439
REMARK 465 VAL C 440
REMARK 465 GLU C 441
REMARK 465 GLY C 442
REMARK 465 GLU C 443
REMARK 465 GLY C 444
REMARK 465 GLU C 445
REMARK 465 GLU C 446
REMARK 465 GLU C 447
REMARK 465 GLY C 448
REMARK 465 GLU C 449
REMARK 465 GLU C 450
REMARK 465 TYR C 451
REMARK 465 MET D 1
REMARK 465 GLU D 442
REMARK 465 GLN D 443
REMARK 465 GLY D 444
REMARK 465 GLU D 445
REMARK 465 PHE D 446
REMARK 465 GLU D 447
REMARK 465 GLU D 448
REMARK 465 GLU D 449
REMARK 465 GLU D 450
REMARK 465 GLY D 451
REMARK 465 GLU D 452
REMARK 465 ASP D 453
REMARK 465 GLU D 454
REMARK 465 ALA D 455
REMARK 465 MET E 1
REMARK 465 GLY E 2
REMARK 465 SER E 3
REMARK 465 SER E 4
REMARK 465 HIS E 5
REMARK 465 HIS E 6
REMARK 465 HIS E 7
REMARK 465 HIS E 8
REMARK 465 HIS E 9
REMARK 465 HIS E 10
REMARK 465 GLY E 11
REMARK 465 SER E 12
REMARK 465 ASN E 169
REMARK 465 ASN F 387
REMARK 465 ALA F 388
REMARK 465 LYS F 389
REMARK 465 SER F 390
REMARK 465 LYS F 391
REMARK 465 PHE F 392
REMARK 465 GLN F 393
REMARK 465 LYS F 394
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 D 281 CG CD OE1 NE2
REMARK 470 TYR D 283 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU E 168 CG CD1 CD2
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 OE2 GLU C 297 NH2 ARG C 339 1.74
REMARK 500 CG2 VAL E 139 O HOH E 284 1.78
REMARK 500 NH2 ARG D 308 O HOH D 601 1.82
REMARK 500 OE1 GLU E 29 O HOH E 201 1.84
REMARK 500 O HOH D 782 O HOH D 783 1.92
REMARK 500 OG1 THR D 396 O HOH D 602 1.92
REMARK 500 NH1 ARG D 88 O HOH D 603 1.94
REMARK 500 O PRO C 263 O HOH C 601 1.94
REMARK 500 OD2 ASP D 437 O HOH D 604 1.94
REMARK 500 O SER C 340 O HOH C 602 1.94
REMARK 500 NZ LYS D 372 O HOH D 605 1.95
REMARK 500 NH1 ARG D 278 O HOH D 606 1.98
REMARK 500 NE1 TRP C 346 O HOH C 603 2.03
REMARK 500 O HOH C 826 O HOH D 639 2.03
REMARK 500 O HOH C 692 O HOH C 853 2.05
REMARK 500 NH1 ARG C 229 O HOH C 604 2.08
REMARK 500 O HOH C 648 O HOH C 859 2.08
REMARK 500 O ASP D 39 O HOH D 607 2.10
REMARK 500 O HOH E 273 O HOH E 321 2.11
REMARK 500 NH2 ARG E 23 O HOH E 202 2.12
REMARK 500 O HOH C 673 O HOH C 820 2.12
REMARK 500 O HOH C 771 O HOH C 843 2.13
REMARK 500 NH1 ARG C 156 O HOH C 605 2.14
REMARK 500 O HOH E 294 O HOH E 310 2.14
REMARK 500 O HOH C 606 O HOH C 804 2.16
REMARK 500 O HOH C 608 O HOH C 811 2.17
REMARK 500 OD2 ASP E 138 O HOH E 203 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 PRO C 263 C - N - CA ANGL. DEV. = 10.4 DEGREES
REMARK 500 HIS D 107 N - CA - C ANGL. DEV. = -16.4 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 THR C 109 -82.56 -101.39
REMARK 500 TYR C 161 58.90 -141.66
REMARK 500 LYS C 280 54.69 -102.63
REMARK 500 PHE C 404 -0.90 68.60
REMARK 500 HIS D 37 31.22 -145.23
REMARK 500 SER D 97 -81.68 -104.21
REMARK 500 HIS D 107 -73.71 -76.95
REMARK 500 CYS D 131 89.24 -152.67
REMARK 500 GLN D 282 -120.88 62.33
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 GLY D 98 ALA D 99 -128.07
REMARK 500 TYR D 108 THR D 109 -147.70
REMARK 500 GLY D 279 SER D 280 146.59
REMARK 500 SER D 280 GLN D 281 -53.68
REMARK 500 GLN D 281 GLN D 282 145.30
REMARK 500 GLN D 282 TYR D 283 -119.78
REMARK 500 TYR D 283 ARG D 284 36.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY D 106 -17.00
REMARK 500 TYR D 108 -14.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 782 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH D 783 DISTANCE = 7.13 ANGSTROMS
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 C 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP C 501 O2G
REMARK 620 2 GTP C 501 O1B 87.1
REMARK 620 3 HOH C 661 O 94.5 87.0
REMARK 620 4 HOH C 666 O 173.9 91.0 79.6
REMARK 620 5 HOH C 733 O 103.0 169.7 90.2 78.8
REMARK 620 6 HOH C 777 O 102.0 86.8 162.0 83.7 92.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP D 501 O2G
REMARK 620 2 GTP D 501 O1B 84.9
REMARK 620 3 HOH D 610 O 98.0 154.0
REMARK 620 4 HOH D 615 O 151.4 82.6 82.8
REMARK 620 5 HOH D 625 O 86.7 75.2 79.1 65.3
REMARK 620 6 HOH D 628 O 90.1 97.6 108.2 116.9 172.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GTP C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GTP D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 502
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE C201S IS BASED ON REFERENCE 1 OF DATABASE Q6B856 (TBB2B_
REMARK 999 BOVIN).
DBREF 5EIB C 1 451 UNP P81947 TBA1B_BOVIN 1 451
DBREF 5EIB D 1 455 UNP Q6B856 TBB2B_BOVIN 1 445
DBREF 5EIB E 1 169 PDB 5EIB 5EIB 1 169
DBREF 5EIB F 372 394 UNP Q9HC77 CENPJ_HUMAN 372 394
SEQADV 5EIB SER D 203 UNP Q6B856 CYS 201 SEE SEQUENCE DETAILS
SEQRES 1 C 451 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 C 451 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 C 451 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 C 451 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 C 451 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 C 451 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 C 451 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 C 451 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 C 451 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 C 451 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 C 451 GLY LEU GLN GLY PHE LEU VAL PHE HIS SER PHE GLY GLY
SEQRES 12 C 451 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 C 451 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 C 451 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 C 451 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 C 451 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 C 451 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 C 451 PRO THR TYR THR ASN LEU ASN ARG LEU ILE SER GLN ILE
SEQRES 19 C 451 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 C 451 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 C 451 PRO TYR PRO ARG ILE HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 C 451 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 C 451 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 C 451 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 C 451 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 C 451 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 C 451 ARG SER ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 C 451 LYS VAL GLY ILE ASN TYR GLN PRO PRO THR VAL VAL PRO
SEQRES 29 C 451 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 C 451 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 C 451 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 C 451 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 C 451 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 C 451 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 C 451 GLU GLY GLU GLU GLU GLY GLU GLU TYR
SEQRES 1 D 445 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 D 445 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 D 445 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 D 445 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 D 445 GLU ALA THR GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 D 445 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 D 445 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 D 445 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 D 445 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 D 445 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 D 445 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 D 445 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 D 445 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 D 445 MET PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 D 445 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 D 445 THR ASP GLU THR TYR SER ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 D 445 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 D 445 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 D 445 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 D 445 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 D 445 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 D 445 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 D 445 PRO GLU LEU THR GLN GLN MET PHE ASP SER LYS ASN MET
SEQRES 24 D 445 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 D 445 VAL ALA ALA ILE PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 D 445 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 D 445 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 D 445 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 D 445 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 D 445 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 D 445 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 D 445 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 D 445 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR
SEQRES 34 D 445 ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLU GLY GLU
SEQRES 35 D 445 ASP GLU ALA
SEQRES 1 E 169 MET GLY SER SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 E 169 LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN
SEQRES 3 E 169 ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP
SEQRES 4 E 169 VAL ASN ALA THR ASP ALA SER GLY LEU THR PRO LEU HIS
SEQRES 5 E 169 LEU ALA ALA THR TYR GLY HIS LEU GLU ILE VAL GLU VAL
SEQRES 6 E 169 LEU LEU LYS HIS GLY ALA ASP VAL ASN ALA ILE ASP ILE
SEQRES 7 E 169 MET GLY SER THR PRO LEU HIS LEU ALA ALA LEU ILE GLY
SEQRES 8 E 169 HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS HIS GLY ALA
SEQRES 9 E 169 ASP VAL ASN ALA VAL ASP THR TRP GLY ASP THR PRO LEU
SEQRES 10 E 169 HIS LEU ALA ALA ILE MET GLY HIS LEU GLU ILE VAL GLU
SEQRES 11 E 169 VAL LEU LEU LYS HIS GLY ALA ASP VAL ASN ALA GLN ASP
SEQRES 12 E 169 LYS PHE GLY LYS THR ALA PHE ASP ILE SER ILE ASP ASN
SEQRES 13 E 169 GLY ASN GLU ASP LEU ALA GLU ILE LEU GLN LYS LEU ASN
SEQRES 1 F 23 LYS GLN PRO PHE LEU LYS ARG GLY GLU GLY LEU ALA ARG
SEQRES 2 F 23 PHE THR ASN ALA LYS SER LYS PHE GLN LYS
HET GTP C 501 32
HET MG C 502 1
HET GTP D 501 32
HET MG D 502 1
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 5 GTP 2(C10 H16 N5 O14 P3)
FORMUL 6 MG 2(MG 2+)
FORMUL 9 HOH *597(H2 O)
HELIX 1 AA1 GLY C 10 GLY C 29 1 20
HELIX 2 AA2 ASP C 47 THR C 51 5 5
HELIX 3 AA3 PRO C 72 GLY C 81 1 10
HELIX 4 AA4 HIS C 88 GLU C 90 5 3
HELIX 5 AA5 ASN C 102 TYR C 108 1 7
HELIX 6 AA6 THR C 109 GLU C 113 5 5
HELIX 7 AA7 ILE C 114 GLN C 128 1 15
HELIX 8 AA8 GLY C 143 TYR C 161 1 19
HELIX 9 AA9 VAL C 182 LEU C 195 1 14
HELIX 10 AB1 ASN C 206 LEU C 217 1 12
HELIX 11 AB2 THR C 223 PHE C 244 1 22
HELIX 12 AB3 ASP C 251 VAL C 260 1 10
HELIX 13 AB4 SER C 277 ALA C 281 5 5
HELIX 14 AB5 SER C 287 ALA C 294 1 8
HELIX 15 AB6 CYS C 295 GLN C 301 5 7
HELIX 16 AB7 ASP C 306 GLY C 310 5 5
HELIX 17 AB8 VAL C 324 THR C 337 1 14
HELIX 18 AB9 ILE C 384 LYS C 401 1 18
HELIX 19 AC1 PHE C 404 GLY C 410 1 7
HELIX 20 AC2 GLU C 415 GLY C 436 1 22
HELIX 21 AC3 GLY D 10 GLY D 29 1 20
HELIX 22 AC4 SER D 40 LEU D 46 5 5
HELIX 23 AC5 ARG D 48 VAL D 51 5 4
HELIX 24 AC6 PRO D 72 GLY D 81 1 10
HELIX 25 AC7 PHE D 83 PHE D 87 5 5
HELIX 26 AC8 ARG D 88 ASP D 90 5 3
HELIX 27 AC9 ASN D 102 HIS D 107 1 6
HELIX 28 AD1 TYR D 108 SER D 128 1 21
HELIX 29 AD2 GLY D 144 TYR D 161 1 18
HELIX 30 AD3 VAL D 182 THR D 198 1 17
HELIX 31 AD4 ASN D 206 THR D 216 1 11
HELIX 32 AD5 THR D 223 THR D 239 1 17
HELIX 33 AD6 THR D 239 PHE D 244 1 6
HELIX 34 AD7 ASP D 251 VAL D 260 1 10
HELIX 35 AD8 THR D 287 PHE D 296 1 10
HELIX 36 AD9 ASP D 297 MET D 301 5 5
HELIX 37 AE1 ASP D 306 GLY D 310 5 5
HELIX 38 AE2 SER D 324 ASN D 339 1 16
HELIX 39 AE3 SER D 340 PHE D 343 5 4
HELIX 40 AE4 ILE D 384 ARG D 401 1 18
HELIX 41 AE5 LEU D 405 GLY D 410 1 6
HELIX 42 AE6 GLU D 415 ASP D 437 1 23
HELIX 43 AE7 LEU E 14 GLY E 25 1 12
HELIX 44 AE8 GLN E 26 ASN E 36 1 11
HELIX 45 AE9 THR E 49 TYR E 57 1 9
HELIX 46 AF1 HIS E 59 HIS E 69 1 11
HELIX 47 AF2 THR E 82 GLY E 91 1 10
HELIX 48 AF3 HIS E 92 HIS E 102 1 11
HELIX 49 AF4 THR E 115 MET E 123 1 9
HELIX 50 AF5 HIS E 125 HIS E 135 1 11
HELIX 51 AF6 THR E 148 GLY E 157 1 10
HELIX 52 AF7 ASN E 158 LYS E 167 1 10
HELIX 53 AF8 GLY F 379 THR F 386 5 8
SHEET 1 AA1 6 LEU C 92 THR C 94 0
SHEET 2 AA1 6 ALA C 65 ASP C 69 1 N PHE C 67 O ILE C 93
SHEET 3 AA1 6 CYS C 4 VAL C 9 1 N HIS C 8 O VAL C 68
SHEET 4 AA1 6 GLY C 134 SER C 140 1 O LEU C 136 N ILE C 7
SHEET 5 AA1 6 SER C 165 TYR C 172 1 O LEU C 167 N VAL C 137
SHEET 6 AA1 6 CYS C 200 ASP C 205 1 O PHE C 202 N GLU C 168
SHEET 1 AA2 2 PHE C 53 GLU C 55 0
SHEET 2 AA2 2 HIS C 61 PRO C 63 -1 O VAL C 62 N SER C 54
SHEET 1 AA3 4 LEU C 269 ALA C 273 0
SHEET 2 AA3 4 ARG C 373 THR C 381 -1 O SER C 379 N LEU C 269
SHEET 3 AA3 4 TYR C 312 GLY C 321 -1 N MET C 313 O ASN C 380
SHEET 4 AA3 4 LYS C 352 ASN C 356 1 O ASN C 356 N GLY C 321
SHEET 1 AA410 PHE D 92 PHE D 94 0
SHEET 2 AA410 ALA D 65 ASP D 69 1 N LEU D 67 O VAL D 93
SHEET 3 AA410 GLU D 3 ALA D 9 1 N HIS D 6 O ILE D 66
SHEET 4 AA410 LEU D 132 SER D 140 1 O GLN D 136 N ILE D 7
SHEET 5 AA410 ILE D 165 MET D 172 1 O PHE D 169 N LEU D 137
SHEET 6 AA410 GLU D 200 ASP D 205 1 O TYR D 202 N THR D 168
SHEET 7 AA410 PHE D 267 ALA D 273 1 O PHE D 268 N THR D 201
SHEET 8 AA410 MET D 373 SER D 381 -1 O PHE D 377 N GLY D 271
SHEET 9 AA410 TYR D 312 GLY D 321 -1 N ARG D 320 O SER D 374
SHEET 10 AA410 VAL D 351 CYS D 356 1 O ALA D 354 N PHE D 319
SHEET 1 AA5 2 TYR D 53 ALA D 56 0
SHEET 2 AA5 2 LYS D 60 PRO D 63 -1 O VAL D 62 N ASN D 54
LINK O2G GTP C 501 MG MG C 502 1555 1555 1.73
LINK O1B GTP C 501 MG MG C 502 1555 1555 2.30
LINK MG MG C 502 O HOH C 661 1555 1555 2.36
LINK MG MG C 502 O HOH C 666 1555 1555 2.73
LINK MG MG C 502 O HOH C 733 1555 1555 2.19
LINK MG MG C 502 O HOH C 777 1555 1555 2.04
LINK O2G GTP D 501 MG MG D 502 1555 1555 2.19
LINK O1B GTP D 501 MG MG D 502 1555 1555 2.39
LINK MG MG D 502 O HOH D 610 1555 1555 2.30
LINK MG MG D 502 O HOH D 615 1555 1555 2.22
LINK MG MG D 502 O HOH D 625 1555 1555 2.59
LINK MG MG D 502 O HOH D 628 1555 1555 2.26
CISPEP 1 ALA C 273 PRO C 274 0 -3.61
CISPEP 2 THR D 57 GLY D 58 0 -5.79
CISPEP 3 GLY D 58 ASN D 59 0 -7.52
CISPEP 4 ALA D 273 PRO D 274 0 -1.05
SITE 1 AC1 27 GLY C 10 GLN C 11 ALA C 12 GLN C 15
SITE 2 AC1 27 ASP C 98 ALA C 99 ASN C 101 SER C 140
SITE 3 AC1 27 GLY C 143 GLY C 144 THR C 145 GLY C 146
SITE 4 AC1 27 VAL C 177 GLU C 183 ASN C 206 TYR C 224
SITE 5 AC1 27 ASN C 228 ILE C 231 MG C 502 HOH C 654
SITE 6 AC1 27 HOH C 661 HOH C 687 HOH C 709 HOH C 733
SITE 7 AC1 27 HOH C 750 HOH C 777 LYS D 254
SITE 1 AC2 6 GTP C 501 HOH C 661 HOH C 666 HOH C 733
SITE 2 AC2 6 HOH C 777 LYS D 254
SITE 1 AC3 27 GLY D 10 GLN D 11 CYS D 12 GLN D 15
SITE 2 AC3 27 ALA D 99 GLY D 100 ASN D 101 SER D 140
SITE 3 AC3 27 GLY D 142 GLY D 143 GLY D 144 THR D 145
SITE 4 AC3 27 GLY D 146 VAL D 177 SER D 178 GLU D 183
SITE 5 AC3 27 ASN D 206 TYR D 224 ASN D 228 MG D 502
SITE 6 AC3 27 HOH D 615 HOH D 625 HOH D 626 HOH D 628
SITE 7 AC3 27 HOH D 640 HOH D 657 HOH D 683
SITE 1 AC4 5 GTP D 501 HOH D 610 HOH D 615 HOH D 625
SITE 2 AC4 5 HOH D 628
CRYST1 73.856 91.116 83.310 90.00 96.97 90.00 P 1 21 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013540 0.000000 0.001656 0.00000
SCALE2 0.000000 0.010975 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012093 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
