HEADER TRANSFERASE 17-SEP-18 6HNW
TITLE HUMAN PROTEIN KINASE CK2 ALPHA IN COMPLEX WITH COUMESTROL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN (RESIDUES 1-337);
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: 562
KEYWDS KINASE DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BATTISTUTTA,G.LOLLI
REVDAT 2 24-JAN-24 6HNW 1 REMARK
REVDAT 1 07-AUG-19 6HNW 0
JRNL AUTH R.BATTISTUTTA,G.LOLLI
JRNL TITL INHIBITORY PROPERTIES OF ATP-COMPETITIVE COUMESTROL AND
JRNL TITL 2 BOLDINE ARE CORRELATED TO DIFFERENT MODULATIONS OF CK2
JRNL TITL 3 FLEXIBILITY.
JRNL REF J.NAT.PROD. V. 82 1014 2019
JRNL REFN ESSN 1520-6025
JRNL PMID 30840451
JRNL DOI 10.1021/ACS.JNATPROD.8B00889
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 21061
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.290
REMARK 3 FREE R VALUE TEST SET COUNT : 1115
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 36.3706 - 3.9985 0.99 2583 165 0.1465 0.1909
REMARK 3 2 3.9985 - 3.1743 0.97 2487 131 0.1580 0.1793
REMARK 3 3 3.1743 - 2.7732 1.00 2510 155 0.2020 0.2509
REMARK 3 4 2.7732 - 2.5197 0.99 2515 131 0.2247 0.2441
REMARK 3 5 2.5197 - 2.3392 1.00 2482 156 0.2151 0.2713
REMARK 3 6 2.3392 - 2.2013 0.96 2442 124 0.2367 0.3050
REMARK 3 7 2.2013 - 2.0910 1.00 2525 137 0.2310 0.2523
REMARK 3 8 2.0910 - 2.0000 0.95 2402 116 0.2783 0.3049
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.72
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 : 0.003 2883
REMARK 3 ANGLE : 0.708 3906
REMARK 3 CHIRALITY : 0.028 401
REMARK 3 PLANARITY : 0.003 498
REMARK 3 DIHEDRAL : 14.206 1080
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1039 -2.2614 -11.0239
REMARK 3 T TENSOR
REMARK 3 T11: 0.2490 T22: 0.2468
REMARK 3 T33: 0.3466 T12: 0.0004
REMARK 3 T13: 0.0331 T23: 0.1249
REMARK 3 L TENSOR
REMARK 3 L11: 0.2322 L22: 0.0234
REMARK 3 L33: 0.3762 L12: -0.0014
REMARK 3 L13: 0.1312 L23: 0.0127
REMARK 3 S TENSOR
REMARK 3 S11: -0.1630 S12: -0.2904 S13: -0.3224
REMARK 3 S21: -0.0035 S22: 0.1918 S23: 0.1739
REMARK 3 S31: 0.0753 S32: -0.0582 S33: -0.0072
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 45 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.4627 8.4876 -12.8799
REMARK 3 T TENSOR
REMARK 3 T11: 0.1880 T22: 0.2801
REMARK 3 T33: 0.2529 T12: 0.0149
REMARK 3 T13: -0.0268 T23: 0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 0.4847 L22: 0.1639
REMARK 3 L33: 0.0543 L12: -0.2002
REMARK 3 L13: 0.1201 L23: -0.1250
REMARK 3 S TENSOR
REMARK 3 S11: 0.0395 S12: -0.0635 S13: -0.0727
REMARK 3 S21: -0.0295 S22: -0.0078 S23: 0.1178
REMARK 3 S31: 0.1359 S32: -0.0509 S33: -0.0009
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 104 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9987 18.2415 -13.7588
REMARK 3 T TENSOR
REMARK 3 T11: 0.2925 T22: 0.2918
REMARK 3 T33: 0.2968 T12: -0.0456
REMARK 3 T13: -0.0480 T23: 0.0590
REMARK 3 L TENSOR
REMARK 3 L11: 0.0380 L22: -0.0100
REMARK 3 L33: 0.1528 L12: -0.0134
REMARK 3 L13: -0.0404 L23: -0.0670
REMARK 3 S TENSOR
REMARK 3 S11: -0.2190 S12: 0.0396 S13: 0.0191
REMARK 3 S21: -0.2563 S22: 0.0816 S23: 0.0475
REMARK 3 S31: -0.2591 S32: 0.1051 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 130 THROUGH 280 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0899 7.9619 -19.3999
REMARK 3 T TENSOR
REMARK 3 T11: 0.1847 T22: 0.1365
REMARK 3 T33: 0.1531 T12: -0.0048
REMARK 3 T13: -0.0112 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 1.3663 L22: 0.5453
REMARK 3 L33: 0.5775 L12: 0.0606
REMARK 3 L13: -0.4530 L23: -0.1088
REMARK 3 S TENSOR
REMARK 3 S11: -0.0623 S12: -0.1388 S13: -0.0653
REMARK 3 S21: -0.1238 S22: 0.0552 S23: 0.1121
REMARK 3 S31: 0.0051 S32: 0.0464 S33: 0.0411
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 281 THROUGH 330 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5786 13.8265 -10.2044
REMARK 3 T TENSOR
REMARK 3 T11: 0.1363 T22: 0.2598
REMARK 3 T33: 0.1360 T12: -0.0216
REMARK 3 T13: 0.0016 T23: -0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 0.2602 L22: 0.2147
REMARK 3 L33: 0.3466 L12: 0.0797
REMARK 3 L13: -0.1177 L23: 0.0063
REMARK 3 S TENSOR
REMARK 3 S11: 0.0114 S12: -0.4062 S13: 0.0437
REMARK 3 S21: 0.0011 S22: 0.0029 S23: 0.0240
REMARK 3 S31: 0.0351 S32: 0.4075 S33: -0.0025
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 6HNW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1200011971.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-15
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21155
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 46.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.71400
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: 3Q04
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG4000, 0.2 M LITHIUM SULFATE, PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 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 23.13700
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 TOTAL BURIED SURFACE AREA: 410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
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 SER A 2
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 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 ASN A 61 2.84 -151.55
REMARK 500 ASP A 156 41.38 -150.61
REMARK 500 ASP A 175 79.04 50.26
REMARK 500 ALA A 193 171.51 59.54
REMARK 500 ASP A 210 -156.98 -156.07
REMARK 500 HIS A 234 70.10 -106.48
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 712 DISTANCE = 6.50 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CUE 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
DBREF 6HNW 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 CUE A 401 20
HET SO4 A 402 5
HET SO4 A 403 5
HETNAM CUE COUMESTROL
HETNAM SO4 SULFATE ION
HETSYN CUE 3,9-DIHYDROXY-6H-[1]BENZOFURO[3,2-C]CHROMEN-6-ONE
FORMUL 2 CUE C15 H8 O5
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *212(H2 O)
HELIX 1 AA1 PRO A 20 ASP A 25 1 6
HELIX 2 AA2 TYR A 26 HIS A 29 5 4
HELIX 3 AA3 ASN A 35 ASP A 37 5 3
HELIX 4 AA4 LYS A 74 ARG A 89 1 16
HELIX 5 AA5 ASP A 120 LEU A 128 1 9
HELIX 6 AA6 THR A 129 MET A 150 1 22
HELIX 7 AA7 LYS A 158 HIS A 160 5 3
HELIX 8 AA8 SER A 194 LYS A 198 5 5
HELIX 9 AA9 GLY A 199 VAL A 204 1 6
HELIX 10 AB1 TYR A 211 PHE A 227 1 17
HELIX 11 AB2 ASP A 237 GLY A 250 1 14
HELIX 12 AB3 GLY A 250 TYR A 261 1 12
HELIX 13 AB4 ASP A 266 ILE A 272 5 7
HELIX 14 AB5 ARG A 280 VAL A 285 5 6
HELIX 15 AB6 ASN A 289 VAL A 293 5 5
HELIX 16 AB7 SER A 294 LEU A 305 1 12
HELIX 17 AB8 ASP A 308 ARG A 312 5 5
HELIX 18 AB9 THR A 314 GLU A 320 1 7
HELIX 19 AC1 HIS A 321 TYR A 325 5 5
SHEET 1 AA1 5 TYR A 39 ARG A 47 0
SHEET 2 AA1 5 SER A 51 ASN A 58 -1 O VAL A 53 N GLY A 46
SHEET 3 AA1 5 LYS A 64 LEU A 70 -1 O VAL A 65 N ALA A 56
SHEET 4 AA1 5 PRO A 109 GLU A 114 -1 O PHE A 113 N VAL A 66
SHEET 5 AA1 5 LEU A 97 LYS A 102 -1 N VAL A 101 O ALA A 110
SHEET 1 AA2 2 ILE A 152 MET A 153 0
SHEET 2 AA2 2 GLU A 180 PHE A 181 -1 O GLU A 180 N MET A 153
SHEET 1 AA3 2 VAL A 162 ASP A 165 0
SHEET 2 AA3 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 -3.51
SITE 1 AC1 10 LEU A 45 VAL A 53 VAL A 66 LYS A 68
SITE 2 AC1 10 PHE A 113 VAL A 116 ASN A 118 ILE A 174
SITE 3 AC1 10 ASP A 175 HOH A 513
SITE 1 AC2 8 ASP A 253 ARG A 278 ARG A 306 TYR A 307
SITE 2 AC2 8 ASP A 308 HOH A 521 HOH A 552 HOH A 633
SITE 1 AC3 5 ARG A 80 ARG A 155 ASN A 189 VAL A 192
SITE 2 AC3 5 HOH A 600
CRYST1 58.329 46.274 63.428 90.00 112.02 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 0.017144 0.000000 0.006932 0.00000
SCALE2 0.000000 0.021610 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017006 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
