HEADER TRANSFERASE 08-JUN-16 5L8K
TITLE AURORA-A KINASE DOMAIN IN COMPLEX WITH VNAR-D01 (CRYSTAL FORM 2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AURORA KINASE A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AURORA 2,AURORA/IPL1-RELATED KINASE 1,HARK1,BREAST TUMOR-
COMPND 5 AMPLIFIED KINASE,SERINE/THREONINE-PROTEIN KINASE 15,SERINE/THREONINE-
COMPND 6 PROTEIN KINASE 6,SERINE/THREONINE-PROTEIN KINASE AURORA-A;
COMPND 7 EC: 2.7.11.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: NEW ANTIGEN RECEPTOR VARIABLE DOMAIN;
COMPND 12 CHAIN: B;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AURKA, AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET30TEV;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ORECTOLOBUS MACULATUS;
SOURCE 13 ORGANISM_COMMON: SPOTTED WOBBEGONG;
SOURCE 14 ORGANISM_TAXID: 168098;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_VARIANT: RIL;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PET26B(+)
KEYWDS KINASE, VNAR, INHIBITOR, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.G.BURGESS,R.BAYLISS
REVDAT 3 10-JAN-24 5L8K 1 ATOM
REVDAT 2 27-JUL-16 5L8K 1 JRNL
REVDAT 1 20-JUL-16 5L8K 0
JRNL AUTH S.G.BURGESS,A.OLEKSY,T.CAVAZZA,M.W.RICHARDS,I.VERNOS,
JRNL AUTH 2 D.MATTHEWS,R.BAYLISS
JRNL TITL ALLOSTERIC INHIBITION OF AURORA-A KINASE BY A SYNTHETIC VNAR
JRNL TITL 2 DOMAIN.
JRNL REF OPEN BIOLOGY V. 6 2016
JRNL REFN ESSN 2046-2441
JRNL PMID 27411893
JRNL DOI 10.1098/RSOB.160089
REMARK 2
REMARK 2 RESOLUTION. 1.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 41890
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870
REMARK 3 FREE R VALUE TEST SET COUNT : 2042
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 46.6730 - 4.4134 0.98 2881 132 0.1814 0.2306
REMARK 3 2 4.4134 - 3.5034 1.00 2772 136 0.1462 0.1918
REMARK 3 3 3.5034 - 3.0607 0.97 2672 126 0.1799 0.2087
REMARK 3 4 3.0607 - 2.7809 1.00 2728 150 0.1924 0.2294
REMARK 3 5 2.7809 - 2.5816 1.00 2705 153 0.1983 0.2777
REMARK 3 6 2.5816 - 2.4294 1.00 2699 125 0.2010 0.2158
REMARK 3 7 2.4294 - 2.3077 1.00 2693 148 0.1969 0.2343
REMARK 3 8 2.3077 - 2.2073 0.97 2605 138 0.1919 0.2576
REMARK 3 9 2.2073 - 2.1223 0.99 2679 136 0.2016 0.2393
REMARK 3 10 2.1223 - 2.0491 0.99 2689 137 0.2086 0.2531
REMARK 3 11 2.0491 - 1.9850 0.99 2646 133 0.2186 0.2707
REMARK 3 12 1.9850 - 1.9282 0.98 2623 143 0.2465 0.2959
REMARK 3 13 1.9282 - 1.8775 0.94 2519 126 0.2850 0.3424
REMARK 3 14 1.8775 - 1.8317 0.93 2482 129 0.3282 0.3561
REMARK 3 15 1.8317 - 1.7900 0.91 2455 130 0.3786 0.4009
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.007 3021
REMARK 3 ANGLE : 1.227 4094
REMARK 3 CHIRALITY : 0.050 463
REMARK 3 PLANARITY : 0.004 514
REMARK 3 DIHEDRAL : 13.864 1083
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 5L8K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000310.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91741
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41932
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 46.660
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4CEG, 2COQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M BIS-TRIS
REMARK 280 PH 5.5, 25 % PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 44.35000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.86000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.35000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.86000
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 757 LIES ON A SPECIAL POSITION.
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 GLY A 119
REMARK 465 ALA A 120
REMARK 465 MET A 121
REMARK 465 GLU A 122
REMARK 465 SER A 123
REMARK 465 LYS A 124
REMARK 465 LYS A 125
REMARK 465 ALA A 393
REMARK 465 GLN A 394
REMARK 465 ASN A 395
REMARK 465 LYS A 396
REMARK 465 GLU A 397
REMARK 465 SER A 398
REMARK 465 ALA A 399
REMARK 465 SER A 400
REMARK 465 LYS A 401
REMARK 465 GLN A 402
REMARK 465 SER A 403
REMARK 465 GLY B 106
REMARK 465 ALA B 107
REMARK 465 ALA B 108
REMARK 465 ALA B 109
REMARK 465 LEU B 110
REMARK 465 GLU B 111
REMARK 465 HIS B 112
REMARK 465 HIS B 113
REMARK 465 HIS B 114
REMARK 465 HIS B 115
REMARK 465 HIS B 116
REMARK 465 HIS B 117
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 ARG A 126 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 141 CG CD CE NZ
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 GLN A 177 CG CD OE1 NE2
REMARK 470 ARG A 180 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 220 NE CZ NH1 NH2
REMARK 470 LYS A 224 CG CD CE NZ
REMARK 470 HIS A 280 CG ND1 CD2 CE1 NE2
REMARK 470 PRO A 282 CG CD
REMARK 470 SER A 284 OG
REMARK 470 ARG A 285 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 286 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 304 NE CZ NH1 NH2
REMARK 470 MET A 305 CG SD CE
REMARK 470 GLU A 308 CD OE1 OE2
REMARK 470 LYS A 326 CG CD CE NZ
REMARK 470 GLN A 335 CG CD OE1 NE2
REMARK 470 GLU A 336 CG CD OE1 OE2
REMARK 470 GLU A 354 CG CD OE1 OE2
REMARK 470 ARG A 375 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 389 CE NZ
REMARK 470 ASN A 392 CG OD1 ND2
REMARK 470 MET B 1 CG SD CE
REMARK 470 LYS B 46 CG CD CE NZ
REMARK 470 GLU B 62 CG CD OE1 OE2
REMARK 470 ARG B 72 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 73 CG OD1 OD2
REMARK 470 ARG B 75 CZ NH1 NH2
REMARK 470 LYS B 104 CG CD CE NZ
REMARK 470 GLY B 105 C O
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 O2P TPO A 288 O HOH A 601 1.45
REMARK 500 O HOH A 799 O HOH A 807 1.98
REMARK 500 O HOH A 710 O HOH A 765 2.04
REMARK 500 O THR A 292 O HOH A 602 2.09
REMARK 500 OE2 GLU A 269 O HOH A 603 2.14
REMARK 500 OG SER A 266 O HOH A 604 2.15
REMARK 500 O HOH A 676 O HOH A 733 2.17
REMARK 500 O HOH A 678 O HOH B 325 2.17
REMARK 500 O HOH A 727 O HOH A 793 2.19
REMARK 500 O4 SO4 A 502 O HOH A 605 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 359 O HOH B 359 2555 1.76
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 ASP A 202 -159.44 -127.74
REMARK 500 SER A 226 -47.68 70.75
REMARK 500 VAL A 279 -47.86 130.96
REMARK 500 ASP A 307 -155.48 -146.65
REMARK 500 LEU A 364 47.45 -94.10
REMARK 500 SER A 391 -178.25 -64.15
REMARK 500 SER B 34 61.40 -157.26
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 A 806 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A 807 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH A 808 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A 809 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH A 810 DISTANCE = 7.50 ANGSTROMS
REMARK 525 HOH A 811 DISTANCE = 11.04 ANGSTROMS
REMARK 525 HOH B 368 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH B 369 DISTANCE = 7.83 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5L8L RELATED DB: PDB
REMARK 900 DIFFERENT SPACE GROUP OF THE SAME PROTEIN-PROTEIN COMPLEX
DBREF 5L8K A 122 403 UNP O14965 AURKA_HUMAN 122 403
DBREF 5L8K B 2 104 UNP Q8JJ25 Q8JJ25_9CHON 1 108
SEQADV 5L8K GLY A 119 UNP O14965 EXPRESSION TAG
SEQADV 5L8K ALA A 120 UNP O14965 EXPRESSION TAG
SEQADV 5L8K MET A 121 UNP O14965 EXPRESSION TAG
SEQADV 5L8K ALA A 290 UNP O14965 CYS 290 ENGINEERED MUTATION
SEQADV 5L8K ALA A 393 UNP O14965 CYS 393 ENGINEERED MUTATION
SEQADV 5L8K MET B 1 UNP Q8JJ25 INITIATING METHIONINE
SEQADV 5L8K ILE B 87 UNP Q8JJ25 TYR 86 CONFLICT
SEQADV 5L8K ASP B 88 UNP Q8JJ25 ARG 87 CONFLICT
SEQADV 5L8K SER B 89 UNP Q8JJ25 ARG 88 ENGINEERED MUTATION
SEQADV 5L8K B UNP Q8JJ25 ALA 90 DELETION
SEQADV 5L8K B UNP Q8JJ25 PHE 91 DELETION
SEQADV 5L8K B UNP Q8JJ25 ASN 92 DELETION
SEQADV 5L8K B UNP Q8JJ25 THR 93 DELETION
SEQADV 5L8K B UNP Q8JJ25 GLY 94 DELETION
SEQADV 5L8K TRP B 91 UNP Q8JJ25 VAL 95 CONFLICT
SEQADV 5L8K LEU B 92 UNP Q8JJ25 GLY 96 CONFLICT
SEQADV 5L8K SER B 93 UNP Q8JJ25 TYR 97 CONFLICT
SEQADV 5L8K ARG B 94 UNP Q8JJ25 LYS 98 CONFLICT
SEQADV 5L8K GLY B 105 UNP Q8JJ25 EXPRESSION TAG
SEQADV 5L8K GLY B 106 UNP Q8JJ25 EXPRESSION TAG
SEQADV 5L8K ALA B 107 UNP Q8JJ25 EXPRESSION TAG
SEQADV 5L8K ALA B 108 UNP Q8JJ25 EXPRESSION TAG
SEQADV 5L8K ALA B 109 UNP Q8JJ25 EXPRESSION TAG
SEQADV 5L8K LEU B 110 UNP Q8JJ25 EXPRESSION TAG
SEQADV 5L8K GLU B 111 UNP Q8JJ25 EXPRESSION TAG
SEQADV 5L8K HIS B 112 UNP Q8JJ25 EXPRESSION TAG
SEQADV 5L8K HIS B 113 UNP Q8JJ25 EXPRESSION TAG
SEQADV 5L8K HIS B 114 UNP Q8JJ25 EXPRESSION TAG
SEQADV 5L8K HIS B 115 UNP Q8JJ25 EXPRESSION TAG
SEQADV 5L8K HIS B 116 UNP Q8JJ25 EXPRESSION TAG
SEQADV 5L8K HIS B 117 UNP Q8JJ25 EXPRESSION TAG
SEQRES 1 A 285 GLY ALA MET GLU SER LYS LYS ARG GLN TRP ALA LEU GLU
SEQRES 2 A 285 ASP PHE GLU ILE GLY ARG PRO LEU GLY LYS GLY LYS PHE
SEQRES 3 A 285 GLY ASN VAL TYR LEU ALA ARG GLU LYS GLN SER LYS PHE
SEQRES 4 A 285 ILE LEU ALA LEU LYS VAL LEU PHE LYS ALA GLN LEU GLU
SEQRES 5 A 285 LYS ALA GLY VAL GLU HIS GLN LEU ARG ARG GLU VAL GLU
SEQRES 6 A 285 ILE GLN SER HIS LEU ARG HIS PRO ASN ILE LEU ARG LEU
SEQRES 7 A 285 TYR GLY TYR PHE HIS ASP ALA THR ARG VAL TYR LEU ILE
SEQRES 8 A 285 LEU GLU TYR ALA PRO LEU GLY THR VAL TYR ARG GLU LEU
SEQRES 9 A 285 GLN LYS LEU SER LYS PHE ASP GLU GLN ARG THR ALA THR
SEQRES 10 A 285 TYR ILE THR GLU LEU ALA ASN ALA LEU SER TYR CYS HIS
SEQRES 11 A 285 SER LYS ARG VAL ILE HIS ARG ASP ILE LYS PRO GLU ASN
SEQRES 12 A 285 LEU LEU LEU GLY SER ALA GLY GLU LEU LYS ILE ALA ASP
SEQRES 13 A 285 PHE GLY TRP SER VAL HIS ALA PRO SER SER ARG ARG THR
SEQRES 14 A 285 TPO LEU ALA GLY THR LEU ASP TYR LEU PRO PRO GLU MET
SEQRES 15 A 285 ILE GLU GLY ARG MET HIS ASP GLU LYS VAL ASP LEU TRP
SEQRES 16 A 285 SER LEU GLY VAL LEU CYS TYR GLU PHE LEU VAL GLY LYS
SEQRES 17 A 285 PRO PRO PHE GLU ALA ASN THR TYR GLN GLU THR TYR LYS
SEQRES 18 A 285 ARG ILE SER ARG VAL GLU PHE THR PHE PRO ASP PHE VAL
SEQRES 19 A 285 THR GLU GLY ALA ARG ASP LEU ILE SER ARG LEU LEU LYS
SEQRES 20 A 285 HIS ASN PRO SER GLN ARG PRO MET LEU ARG GLU VAL LEU
SEQRES 21 A 285 GLU HIS PRO TRP ILE THR ALA ASN SER SER LYS PRO SER
SEQRES 22 A 285 ASN ALA GLN ASN LYS GLU SER ALA SER LYS GLN SER
SEQRES 1 B 117 MET ALA ARG VAL ASP GLN THR PRO ARG ILE ALA THR LYS
SEQRES 2 B 117 GLU THR GLY GLU SER LEU THR ILE ASN CYS VAL LEU ARG
SEQRES 3 B 117 ASP THR ALA CYS ALA LEU ASP SER THR ASN TRP TYR ARG
SEQRES 4 B 117 THR LYS LEU GLY SER THR LYS GLU GLN THR ILE SER ILE
SEQRES 5 B 117 GLY GLY ARG TYR SER GLU THR VAL ASP GLU GLY SER ASN
SEQRES 6 B 117 SER ALA SER LEU THR ILE ARG ASP LEU ARG VAL GLU ASP
SEQRES 7 B 117 SER GLY THR TYR LYS CYS LYS ALA ILE ASP SER CYS TRP
SEQRES 8 B 117 LEU SER ARG GLU GLY ALA GLY THR VAL LEU THR VAL LYS
SEQRES 9 B 117 GLY GLY ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 5L8K TPO A 288 THR MODIFIED RESIDUE
HET TPO A 288 11
HET ADP A 501 27
HET SO4 A 502 5
HET EDO A 503 4
HET EDO A 504 4
HET EDO A 505 4
HET EDO A 506 4
HET EDO A 507 4
HET EDO A 508 4
HET EDO A 509 4
HET EDO A 510 4
HET EDO A 511 4
HET EDO A 512 4
HET SO4 B 201 5
HETNAM TPO PHOSPHOTHREONINE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN TPO PHOSPHONOTHREONINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 5 EDO 10(C2 H6 O2)
FORMUL 16 HOH *280(H2 O)
HELIX 1 AA1 ALA A 129 GLU A 131 5 3
HELIX 2 AA2 LYS A 166 ALA A 172 1 7
HELIX 3 AA3 VAL A 174 SER A 186 1 13
HELIX 4 AA4 THR A 217 SER A 226 1 10
HELIX 5 AA5 ASP A 229 SER A 249 1 21
HELIX 6 AA6 LYS A 258 GLU A 260 5 3
HELIX 7 AA7 PRO A 297 GLU A 302 1 6
HELIX 8 AA8 LYS A 309 GLY A 325 1 17
HELIX 9 AA9 THR A 333 ARG A 343 1 11
HELIX 10 AB1 THR A 353 LEU A 364 1 12
HELIX 11 AB2 ASN A 367 ARG A 371 5 5
HELIX 12 AB3 MET A 373 GLU A 379 1 7
HELIX 13 AB4 HIS A 380 SER A 387 1 8
HELIX 14 AB5 GLU B 62 SER B 64 5 3
HELIX 15 AB6 ARG B 75 ASP B 78 5 4
SHEET 1 AA1 5 PHE A 133 GLY A 142 0
SHEET 2 AA1 5 GLY A 145 GLU A 152 -1 O VAL A 147 N LEU A 139
SHEET 3 AA1 5 ILE A 158 PHE A 165 -1 O LEU A 161 N TYR A 148
SHEET 4 AA1 5 ARG A 205 LEU A 210 -1 O LEU A 210 N ALA A 160
SHEET 5 AA1 5 LEU A 196 HIS A 201 -1 N GLY A 198 O ILE A 209
SHEET 1 AA2 2 ILE A 253 HIS A 254 0
SHEET 2 AA2 2 TRP A 277 SER A 278 -1 O SER A 278 N ILE A 253
SHEET 1 AA3 2 LEU A 262 LEU A 264 0
SHEET 2 AA3 2 LEU A 270 ILE A 272 -1 O LYS A 271 N LEU A 263
SHEET 1 AA4 4 ARG B 3 THR B 7 0
SHEET 2 AA4 4 LEU B 19 ARG B 26 -1 O ASN B 22 N THR B 7
SHEET 3 AA4 4 SER B 66 ILE B 71 -1 O LEU B 69 N ILE B 21
SHEET 4 AA4 4 TYR B 56 ASP B 61 -1 N SER B 57 O THR B 70
SHEET 1 AA5 5 ILE B 10 GLU B 14 0
SHEET 2 AA5 5 THR B 99 LYS B 104 1 O VAL B 100 N ALA B 11
SHEET 3 AA5 5 GLY B 80 ILE B 87 -1 N GLY B 80 O LEU B 101
SHEET 4 AA5 5 ASN B 36 LYS B 41 -1 N ASN B 36 O LYS B 85
SHEET 5 AA5 5 GLU B 47 THR B 49 -1 O GLN B 48 N ARG B 39
SHEET 1 AA6 4 ILE B 10 GLU B 14 0
SHEET 2 AA6 4 THR B 99 LYS B 104 1 O VAL B 100 N ALA B 11
SHEET 3 AA6 4 GLY B 80 ILE B 87 -1 N GLY B 80 O LEU B 101
SHEET 4 AA6 4 SER B 93 GLU B 95 -1 O ARG B 94 N ALA B 86
SSBOND 1 CYS B 23 CYS B 84 1555 1555 2.04
SSBOND 2 CYS B 30 CYS B 90 1555 1555 2.05
LINK C THR A 287 N TPO A 288 1555 1555 1.33
LINK C TPO A 288 N LEU A 289 1555 1555 1.33
CISPEP 1 SER A 278 VAL A 279 0 -5.95
CISPEP 2 ALA A 281 PRO A 282 0 -7.46
CISPEP 3 THR B 7 PRO B 8 0 -2.72
SITE 1 AC1 16 GLY A 140 GLY A 142 LYS A 143 VAL A 147
SITE 2 AC1 16 ALA A 160 LYS A 162 LEU A 194 GLU A 211
SITE 3 AC1 16 ALA A 213 LEU A 263 HOH A 624 HOH A 632
SITE 4 AC1 16 HOH A 651 HOH A 687 HOH A 719 HOH A 722
SITE 1 AC2 5 HIS A 248 MET A 373 LEU A 374 HOH A 605
SITE 2 AC2 5 HOH A 629
SITE 1 AC3 6 LYS A 153 PRO A 349 ASP A 350 PHE A 351
SITE 2 AC3 6 HOH A 627 HOH A 640
SITE 1 AC4 3 TYR A 246 LYS A 250 HOH B 333
SITE 1 AC5 4 SER A 266 LYS A 339 ARG A 343 HOH A 608
SITE 1 AC6 2 GLN A 127 HOH A 634
SITE 1 AC7 1 VAL A 163
SITE 1 AC8 3 HIS A 187 GLU B 47 LYS B 85
SITE 1 AC9 3 ARG A 251 ARG B 55 TYR B 56
SITE 1 AD1 3 ARG A 232 THR A 235 SER A 388
SITE 1 AD2 5 ARG A 255 SER A 278 VAL A 279 SER A 283
SITE 2 AD2 5 HIS A 306
SITE 1 AD3 3 ARG A 126 GLN A 127 HOH A 615
SITE 1 AD4 4 MET B 1 ALA B 2 HOH B 307 HOH B 328
CRYST1 88.700 109.720 45.760 90.00 90.00 90.00 P 21 21 2 4
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 0.011274 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009114 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021853 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
