HEADER TRANSFERASE/TRANSFERASE INHIBITOR 24-MAY-13 4KWP
TITLE CRYSTAL STRUCTURE OF HUMAN CK2-ALPHA IN COMPLEX WITH A BENZIMIDAZOLE
TITLE 2 INHIBITOR (K164) AT 1.25 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-336;
COMPND 5 SYNONYM: CK II ALPHA;
COMPND 6 EC: 2.7.11.1;
COMPND 7 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: CSNK2A1, CK2A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS KINASE, PHOSPHORYLATION, SMALL MOLECULE INHIBITOR, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.RANCHIO,G.LOLLI,R.BATTISTUTTA
REVDAT 3 28-FEB-24 4KWP 1 REMARK
REVDAT 2 08-OCT-14 4KWP 1 JRNL
REVDAT 1 09-APR-14 4KWP 0
JRNL AUTH G.COZZA,C.GIRARDI,A.RANCHIO,G.LOLLI,S.SARNO,A.ORZESZKO,
JRNL AUTH 2 Z.KAZIMIERCZUK,R.BATTISTUTTA,M.RUZZENE,L.A.PINNA
JRNL TITL CELL-PERMEABLE DUAL INHIBITORS OF PROTEIN KINASES CK2 AND
JRNL TITL 2 PIM-1: STRUCTURAL FEATURES AND PHARMACOLOGICAL POTENTIAL.
JRNL REF CELL.MOL.LIFE SCI. V. 71 3173 2014
JRNL REFN ISSN 1420-682X
JRNL PMID 24442476
JRNL DOI 10.1007/S00018-013-1552-5
REMARK 2
REMARK 2 RESOLUTION. 1.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
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) : 1.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 86380
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 4336
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 36.2528 - 3.8826 1.00 2852 145 0.1448 0.1518
REMARK 3 2 3.8826 - 3.0822 1.00 2761 172 0.1273 0.1463
REMARK 3 3 3.0822 - 2.6927 1.00 2778 151 0.1380 0.1685
REMARK 3 4 2.6927 - 2.4466 1.00 2766 139 0.1372 0.1756
REMARK 3 5 2.4466 - 2.2713 0.99 2739 145 0.1224 0.1514
REMARK 3 6 2.2713 - 2.1374 0.98 2681 151 0.1157 0.1553
REMARK 3 7 2.1374 - 2.0303 1.00 2743 159 0.1123 0.1248
REMARK 3 8 2.0303 - 1.9420 1.00 2723 151 0.1167 0.1443
REMARK 3 9 1.9420 - 1.8672 1.00 2700 165 0.1219 0.1739
REMARK 3 10 1.8672 - 1.8028 1.00 2762 131 0.1212 0.1607
REMARK 3 11 1.8028 - 1.7464 0.99 2746 148 0.1202 0.1835
REMARK 3 12 1.7464 - 1.6965 0.99 2705 130 0.1208 0.1630
REMARK 3 13 1.6965 - 1.6518 1.00 2757 125 0.1223 0.1834
REMARK 3 14 1.6518 - 1.6115 1.00 2752 142 0.1269 0.2164
REMARK 3 15 1.6115 - 1.5749 1.00 2731 133 0.1267 0.1634
REMARK 3 16 1.5749 - 1.5414 1.00 2751 144 0.1238 0.1792
REMARK 3 17 1.5414 - 1.5105 1.00 2703 157 0.1276 0.1672
REMARK 3 18 1.5105 - 1.4820 1.00 2719 151 0.1396 0.1940
REMARK 3 19 1.4820 - 1.4556 1.00 2732 151 0.1453 0.1707
REMARK 3 20 1.4556 - 1.4309 1.00 2707 146 0.1513 0.1935
REMARK 3 21 1.4309 - 1.4078 1.00 2761 127 0.1649 0.2045
REMARK 3 22 1.4078 - 1.3862 1.00 2730 121 0.1662 0.2433
REMARK 3 23 1.3862 - 1.3658 1.00 2737 145 0.1692 0.2301
REMARK 3 24 1.3658 - 1.3465 1.00 2702 140 0.1788 0.2496
REMARK 3 25 1.3465 - 1.3283 0.99 2732 123 0.1850 0.2449
REMARK 3 26 1.3283 - 1.3111 1.00 2729 147 0.1909 0.2511
REMARK 3 27 1.3111 - 1.2947 1.00 2692 155 0.2076 0.2321
REMARK 3 28 1.2947 - 1.2791 1.00 2713 143 0.2027 0.2838
REMARK 3 29 1.2791 - 1.2642 1.00 2736 151 0.2141 0.2449
REMARK 3 30 1.2642 - 1.2500 1.00 2704 148 0.2176 0.2750
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.090
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.92
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 2977
REMARK 3 ANGLE : 1.154 4034
REMARK 3 CHIRALITY : 0.073 416
REMARK 3 PLANARITY : 0.006 511
REMARK 3 DIHEDRAL : 14.097 1136
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 4KWP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079889.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 0.1.27, AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86589
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.250
REMARK 200 RESOLUTION RANGE LOW (A) : 59.211
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 0.2 M LITHIUM
REMARK 280 SULPHATE, 32% W/V PEG 4000, PH 8.5, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 293K
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 22.91050
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 GLN A 331
REMARK 465 ALA A 332
REMARK 465 ARG A 333
REMARK 465 MET A 334
REMARK 465 GLY A 335
REMARK 465 SER A 336
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 ASP A 330 CG OD1 OD2
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 OD2 ASP A 205 O HOH A 951 2646 1.89
REMARK 500 O HOH A 913 O HOH A 937 2546 2.05
REMARK 500 O HOH A 880 O HOH A 953 2646 2.14
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 156 43.71 -151.29
REMARK 500 ASP A 175 71.52 59.27
REMARK 500 ALA A 193 177.06 60.06
REMARK 500 MET A 208 54.77 -91.46
REMARK 500 HIS A 234 69.29 -104.09
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 SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EXX A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 411
DBREF 4KWP A 1 336 UNP P68400 CSK21_HUMAN 1 336
SEQRES 1 A 336 MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR
SEQRES 2 A 336 ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR
SEQRES 3 A 336 GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR
SEQRES 4 A 336 GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU
SEQRES 5 A 336 VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL
SEQRES 6 A 336 VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE
SEQRES 7 A 336 LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY
SEQRES 8 A 336 PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO
SEQRES 9 A 336 VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN
SEQRES 10 A 336 ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP
SEQRES 11 A 336 TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA
SEQRES 12 A 336 LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP
SEQRES 13 A 336 VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG
SEQRES 14 A 336 LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR
SEQRES 15 A 336 HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG
SEQRES 16 A 336 TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET
SEQRES 17 A 336 TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET
SEQRES 18 A 336 LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS
SEQRES 19 A 336 GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS
SEQRES 20 A 336 VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS
SEQRES 21 A 336 TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU
SEQRES 22 A 336 GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS
SEQRES 23 A 336 SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP
SEQRES 24 A 336 PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG
SEQRES 25 A 336 LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR
SEQRES 26 A 336 THR VAL VAL LYS ASP GLN ALA ARG MET GLY SER
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET EDO A 405 10
HET EDO A 406 10
HET EDO A 407 10
HET EXX A 408 21
HET PGE A 409 10
HET PEG A 410 7
HET DMS A 411 10
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM EXX 4,5,6,7-TETRABROMO-1-(2-DEOXY-BETA-D-ERYTHRO-
HETNAM 2 EXX PENTOFURANOSYL)-1H-BENZIMIDAZOLE
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN EDO ETHYLENE GLYCOL
HETSYN EXX TETRABROMO-DEOXYRIBOFURANOSYL-BENZIMIDAZOLE
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 6 EDO 3(C2 H6 O2)
FORMUL 9 EXX C12 H10 BR4 N2 O3
FORMUL 10 PGE C6 H14 O4
FORMUL 11 PEG C4 H10 O3
FORMUL 12 DMS C2 H6 O S
FORMUL 13 HOH *464(H2 O)
HELIX 1 1 PRO A 20 ASP A 25 1 6
HELIX 2 2 TYR A 26 HIS A 29 5 4
HELIX 3 3 ASN A 35 ASP A 37 5 3
HELIX 4 4 LYS A 74 ARG A 89 1 16
HELIX 5 5 ASP A 120 GLN A 126 1 7
HELIX 6 6 THR A 129 MET A 150 1 22
HELIX 7 7 LYS A 158 HIS A 160 5 3
HELIX 8 8 SER A 194 LYS A 198 5 5
HELIX 9 9 GLY A 199 VAL A 204 1 6
HELIX 10 10 TYR A 211 PHE A 227 1 17
HELIX 11 11 ASP A 237 GLY A 250 1 14
HELIX 12 12 GLY A 250 TYR A 261 1 12
HELIX 13 13 ASP A 266 ILE A 272 5 7
HELIX 14 14 ARG A 280 VAL A 285 5 6
HELIX 15 15 ASN A 289 VAL A 293 5 5
HELIX 16 16 SER A 294 LEU A 305 1 12
HELIX 17 17 ASP A 308 ARG A 312 5 5
HELIX 18 18 THR A 314 GLU A 320 1 7
HELIX 19 19 HIS A 321 TYR A 325 5 5
SHEET 1 A 5 TYR A 39 ARG A 47 0
SHEET 2 A 5 SER A 51 ASN A 58 -1 O VAL A 53 N GLY A 46
SHEET 3 A 5 LYS A 64 LEU A 70 -1 O ILE A 69 N GLU A 52
SHEET 4 A 5 THR A 108 GLU A 114 -1 O PHE A 113 N VAL A 66
SHEET 5 A 5 LEU A 97 ASP A 103 -1 N VAL A 101 O ALA A 110
SHEET 1 B 2 ILE A 152 MET A 153 0
SHEET 2 B 2 GLU A 180 PHE A 181 -1 O GLU A 180 N MET A 153
SHEET 1 C 2 VAL A 162 ASP A 165 0
SHEET 2 C 2 LYS A 170 LEU A 173 -1 O LYS A 170 N ASP A 165
CISPEP 1 GLU A 230 PRO A 231 0 -2.58
SITE 1 AC1 8 ASP A 253 ARG A 278 ARG A 306 TYR A 307
SITE 2 AC1 8 ASP A 308 HOH A 536 HOH A 558 HOH A 573
SITE 1 AC2 4 ARG A 80 ARG A 155 ASN A 189 HOH A 533
SITE 1 AC3 6 ASN A 93 LYS A 170 ARG A 172 HOH A 605
SITE 2 AC3 6 HOH A 612 HOH A 699
SITE 1 AC4 2 LYS A 74 LYS A 76
SITE 1 AC5 4 GLN A 36 TYR A 39 LEU A 41 ASP A 103
SITE 1 AC6 7 LYS A 229 PHE A 232 HOH A 543 HOH A 688
SITE 2 AC6 7 HOH A 805 HOH A 869 HOH A 870
SITE 1 AC7 6 VAL A 248 ARG A 278 LYS A 279 TRP A 281
SITE 2 AC7 6 ASP A 302 HOH A 643
SITE 1 AC8 11 LEU A 45 VAL A 66 LYS A 68 PHE A 113
SITE 2 AC8 11 GLU A 114 VAL A 116 ASN A 118 MET A 163
SITE 3 AC8 11 ASP A 175 HOH A 744 HOH A 954
SITE 1 AC9 8 ARG A 191 SER A 194 ARG A 195 LYS A 198
SITE 2 AC9 8 ASN A 238 HOH A 583 HOH A 630 HOH A 926
SITE 1 BC1 6 VAL A 105 SER A 277 ARG A 278 LYS A 279
SITE 2 BC1 6 ARG A 280 ARG A 283
SITE 1 BC2 6 HIS A 160 TYR A 196 PHE A 197 GLU A 230
SITE 2 BC2 6 HOH A 849 HOH A 925
CRYST1 58.448 45.821 63.486 90.00 111.15 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 0.017109 0.000000 0.006618 0.00000
SCALE2 0.000000 0.021824 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016889 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
