HEADER DNA BINDING PROTEIN, HYDROLASE 20-SEP-18 6MJ5
TITLE CRYSTAL STRUCTURE OF TDP1 CATALYTIC DOMAIN IN COMPLEX WITH COMPOUND
TITLE 2 XZ519
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSYL-DNA PHOSPHODIESTERASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TYR-DNA PHOSPHODIESTERASE 1;
COMPND 5 EC: 3.1.4.-;
COMPND 6 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: TDP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDN2454
KEYWDS FRAGMENT BASED DRUG DESIGN, ANTI-CANCER DRUG DESIGN, DNA BINDING
KEYWDS 2 PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.T.LOUNTOS,X.Z.ZHAO,E.KISELEV,J.E.TROPEA,D.NEEDLE,T.R.BURKE JR.,
AUTHOR 2 Y.POMMIER,D.S.WAUGH
REVDAT 3 11-OCT-23 6MJ5 1 REMARK
REVDAT 2 13-NOV-19 6MJ5 1 JRNL
REVDAT 1 03-JUL-19 6MJ5 0
JRNL AUTH G.T.LOUNTOS,X.Z.ZHAO,E.KISELEV,J.E.TROPEA,D.NEEDLE,
JRNL AUTH 2 Y.POMMIER,T.R.BURKE,D.S.WAUGH
JRNL TITL IDENTIFICATION OF A LIGAND BINDING HOT SPOT AND STRUCTURAL
JRNL TITL 2 MOTIFS REPLICATING ASPECTS OF TYROSYL-DNA PHOSPHODIESTERASE
JRNL TITL 3 I (TDP1) PHOSPHORYL RECOGNITION BY CRYSTALLOGRAPHIC FRAGMENT
JRNL TITL 4 COCKTAIL SCREENING.
JRNL REF NUCLEIC ACIDS RES. V. 47 10134 2019
JRNL REFN ESSN 1362-4962
JRNL PMID 31199869
JRNL DOI 10.1093/NAR/GKZ515
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 83777
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.390
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 36.4274 - 4.4631 0.98 6417 157 0.1578 0.1811
REMARK 3 2 4.4631 - 3.5435 1.00 6255 153 0.1398 0.1595
REMARK 3 3 3.5435 - 3.0958 1.00 6218 152 0.1710 0.2193
REMARK 3 4 3.0958 - 2.8129 0.99 6144 150 0.1931 0.2625
REMARK 3 5 2.8129 - 2.6113 0.97 6018 147 0.1928 0.1950
REMARK 3 6 2.6113 - 2.4574 0.95 5882 144 0.1874 0.2443
REMARK 3 7 2.4574 - 2.3344 0.94 5764 141 0.1871 0.2594
REMARK 3 8 2.3344 - 2.2328 0.93 5680 140 0.1873 0.2475
REMARK 3 9 2.2328 - 2.1468 0.92 5645 137 0.1929 0.2474
REMARK 3 10 2.1468 - 2.0727 0.92 5644 139 0.1968 0.2560
REMARK 3 11 2.0727 - 2.0079 0.92 5620 137 0.2068 0.2505
REMARK 3 12 2.0079 - 1.9505 0.91 5589 137 0.2140 0.2692
REMARK 3 13 1.9505 - 1.8992 0.91 5588 136 0.2304 0.2966
REMARK 3 14 1.8992 - 1.8529 0.88 5313 130 0.2402 0.2941
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.610
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 : 0.006 7531
REMARK 3 ANGLE : 0.830 10274
REMARK 3 CHIRALITY : 0.056 1066
REMARK 3 PLANARITY : 0.006 1313
REMARK 3 DIHEDRAL : 5.378 6041
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 6MJ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1000237010.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83875
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
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 (%) : 95.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.80100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: 1JY1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 22 MG/ML 0.1M MOPS/HEPES-NA PH
REMARK 280 7.5 10% W/V PEG 8000 20% V/V ETHYLENE GLYCOL 0.03M SODIUM
REMARK 280 FLUORIDE 0.03M SODIUM BROMIDE 0.03M SODIUM IODIDE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 25.07800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.99200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.84300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 96.99200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.07800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.84300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 GLY A 149
REMARK 465 GLU A 150
REMARK 465 GLY A 151
REMARK 465 GLN A 152
REMARK 465 ASP A 153
REMARK 465 ILE A 154
REMARK 465 TRP A 155
REMARK 465 ASP A 156
REMARK 465 MET A 157
REMARK 465 LEU A 158
REMARK 465 ASP A 159
REMARK 465 LYS A 160
REMARK 465 GLY A 161
REMARK 465 LYS A 428
REMARK 465 THR A 429
REMARK 465 PRO A 430
REMARK 465 GLY A 431
REMARK 465 LYS A 432
REMARK 465 SER A 563
REMARK 465 GLN A 564
REMARK 465 GLU A 565
REMARK 465 SER A 608
REMARK 465 GLY B 149
REMARK 465 GLU B 150
REMARK 465 GLY B 151
REMARK 465 GLN B 152
REMARK 465 ASP B 153
REMARK 465 ILE B 154
REMARK 465 TRP B 155
REMARK 465 ASP B 156
REMARK 465 MET B 157
REMARK 465 LEU B 158
REMARK 465 ASP B 159
REMARK 465 LYS B 160
REMARK 465 GLY B 161
REMARK 465 LYS B 428
REMARK 465 THR B 429
REMARK 465 PRO B 430
REMARK 465 GLY B 431
REMARK 465 LYS B 432
REMARK 465 GLY B 562
REMARK 465 SER B 563
REMARK 465 GLN B 564
REMARK 465 GLU B 565
REMARK 465 SER B 608
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 GLU A 246 CG CD OE1 OE2
REMARK 470 MET A 567 CG SD CE
REMARK 470 GLU B 246 CG CD OE1 OE2
REMARK 470 GLU B 526 CG CD OE1 OE2
REMARK 470 MET B 567 CG SD CE
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 O HOH B 877 O HOH B 994 2.19
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 ARG A 232 -127.19 54.88
REMARK 500 HIS A 290 -65.92 -98.29
REMARK 500 TRP A 411 -46.02 -153.05
REMARK 500 GLN A 470 48.34 -146.35
REMARK 500 ALA A 482 43.93 -148.45
REMARK 500 MET A 567 2.20 -66.71
REMARK 500 ARG B 232 -129.07 61.33
REMARK 500 HIS B 290 -68.38 -97.27
REMARK 500 TRP B 411 -45.17 -160.17
REMARK 500 GLN B 470 50.22 -147.75
REMARK 500 ALA B 482 45.07 -147.33
REMARK 500 MET B 567 8.58 -55.98
REMARK 500 ALA B 568 30.79 -86.03
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 A1149 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH B1031 DISTANCE = 6.63 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue JTA A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue JTA B 703
DBREF 6MJ5 A 149 608 UNP Q9NUW8 TYDP1_HUMAN 149 608
DBREF 6MJ5 B 149 608 UNP Q9NUW8 TYDP1_HUMAN 149 608
SEQRES 1 A 460 GLY GLU GLY GLN ASP ILE TRP ASP MET LEU ASP LYS GLY
SEQRES 2 A 460 ASN PRO PHE GLN PHE TYR LEU THR ARG VAL SER GLY VAL
SEQRES 3 A 460 LYS PRO LYS TYR ASN SER GLY ALA LEU HIS ILE LYS ASP
SEQRES 4 A 460 ILE LEU SER PRO LEU PHE GLY THR LEU VAL SER SER ALA
SEQRES 5 A 460 GLN PHE ASN TYR CYS PHE ASP VAL ASP TRP LEU VAL LYS
SEQRES 6 A 460 GLN TYR PRO PRO GLU PHE ARG LYS LYS PRO ILE LEU LEU
SEQRES 7 A 460 VAL HIS GLY ASP LYS ARG GLU ALA LYS ALA HIS LEU HIS
SEQRES 8 A 460 ALA GLN ALA LYS PRO TYR GLU ASN ILE SER LEU CYS GLN
SEQRES 9 A 460 ALA LYS LEU ASP ILE ALA PHE GLY THR HIS HIS THR LYS
SEQRES 10 A 460 MET MET LEU LEU LEU TYR GLU GLU GLY LEU ARG VAL VAL
SEQRES 11 A 460 ILE HIS THR SER ASN LEU ILE HIS ALA ASP TRP HIS GLN
SEQRES 12 A 460 LYS THR GLN GLY ILE TRP LEU SER PRO LEU TYR PRO ARG
SEQRES 13 A 460 ILE ALA ASP GLY THR HIS LYS SER GLY GLU SER PRO THR
SEQRES 14 A 460 HIS PHE LYS ALA ASP LEU ILE SER TYR LEU MET ALA TYR
SEQRES 15 A 460 ASN ALA PRO SER LEU LYS GLU TRP ILE ASP VAL ILE HIS
SEQRES 16 A 460 LYS HIS ASP LEU SER GLU THR ASN VAL TYR LEU ILE GLY
SEQRES 17 A 460 SER THR PRO GLY ARG PHE GLN GLY SER GLN LYS ASP ASN
SEQRES 18 A 460 TRP GLY HIS PHE ARG LEU LYS LYS LEU LEU LYS ASP HIS
SEQRES 19 A 460 ALA SER SER MET PRO ASN ALA GLU SER TRP PRO VAL VAL
SEQRES 20 A 460 GLY GLN PHE SER SER VAL GLY SER LEU GLY ALA ASP GLU
SEQRES 21 A 460 SER LYS TRP LEU CYS SER GLU PHE LYS GLU SER MET LEU
SEQRES 22 A 460 THR LEU GLY LYS GLU SER LYS THR PRO GLY LYS SER SER
SEQRES 23 A 460 VAL PRO LEU TYR LEU ILE TYR PRO SER VAL GLU ASN VAL
SEQRES 24 A 460 ARG THR SER LEU GLU GLY TYR PRO ALA GLY GLY SER LEU
SEQRES 25 A 460 PRO TYR SER ILE GLN THR ALA GLU LYS GLN ASN TRP LEU
SEQRES 26 A 460 HIS SER TYR PHE HIS LYS TRP SER ALA GLU THR SER GLY
SEQRES 27 A 460 ARG SER ASN ALA MET PRO HIS ILE LYS THR TYR MET ARG
SEQRES 28 A 460 PRO SER PRO ASP PHE SER LYS ILE ALA TRP PHE LEU VAL
SEQRES 29 A 460 THR SER ALA ASN LEU SER LYS ALA ALA TRP GLY ALA LEU
SEQRES 30 A 460 GLU LYS ASN GLY THR GLN LEU MET ILE ARG SER TYR GLU
SEQRES 31 A 460 LEU GLY VAL LEU PHE LEU PRO SER ALA PHE GLY LEU ASP
SEQRES 32 A 460 SER PHE LYS VAL LYS GLN LYS PHE PHE ALA GLY SER GLN
SEQRES 33 A 460 GLU PRO MET ALA THR PHE PRO VAL PRO TYR ASP LEU PRO
SEQRES 34 A 460 PRO GLU LEU TYR GLY SER LYS ASP ARG PRO TRP ILE TRP
SEQRES 35 A 460 ASN ILE PRO TYR VAL LYS ALA PRO ASP THR HIS GLY ASN
SEQRES 36 A 460 MET TRP VAL PRO SER
SEQRES 1 B 460 GLY GLU GLY GLN ASP ILE TRP ASP MET LEU ASP LYS GLY
SEQRES 2 B 460 ASN PRO PHE GLN PHE TYR LEU THR ARG VAL SER GLY VAL
SEQRES 3 B 460 LYS PRO LYS TYR ASN SER GLY ALA LEU HIS ILE LYS ASP
SEQRES 4 B 460 ILE LEU SER PRO LEU PHE GLY THR LEU VAL SER SER ALA
SEQRES 5 B 460 GLN PHE ASN TYR CYS PHE ASP VAL ASP TRP LEU VAL LYS
SEQRES 6 B 460 GLN TYR PRO PRO GLU PHE ARG LYS LYS PRO ILE LEU LEU
SEQRES 7 B 460 VAL HIS GLY ASP LYS ARG GLU ALA LYS ALA HIS LEU HIS
SEQRES 8 B 460 ALA GLN ALA LYS PRO TYR GLU ASN ILE SER LEU CYS GLN
SEQRES 9 B 460 ALA LYS LEU ASP ILE ALA PHE GLY THR HIS HIS THR LYS
SEQRES 10 B 460 MET MET LEU LEU LEU TYR GLU GLU GLY LEU ARG VAL VAL
SEQRES 11 B 460 ILE HIS THR SER ASN LEU ILE HIS ALA ASP TRP HIS GLN
SEQRES 12 B 460 LYS THR GLN GLY ILE TRP LEU SER PRO LEU TYR PRO ARG
SEQRES 13 B 460 ILE ALA ASP GLY THR HIS LYS SER GLY GLU SER PRO THR
SEQRES 14 B 460 HIS PHE LYS ALA ASP LEU ILE SER TYR LEU MET ALA TYR
SEQRES 15 B 460 ASN ALA PRO SER LEU LYS GLU TRP ILE ASP VAL ILE HIS
SEQRES 16 B 460 LYS HIS ASP LEU SER GLU THR ASN VAL TYR LEU ILE GLY
SEQRES 17 B 460 SER THR PRO GLY ARG PHE GLN GLY SER GLN LYS ASP ASN
SEQRES 18 B 460 TRP GLY HIS PHE ARG LEU LYS LYS LEU LEU LYS ASP HIS
SEQRES 19 B 460 ALA SER SER MET PRO ASN ALA GLU SER TRP PRO VAL VAL
SEQRES 20 B 460 GLY GLN PHE SER SER VAL GLY SER LEU GLY ALA ASP GLU
SEQRES 21 B 460 SER LYS TRP LEU CYS SER GLU PHE LYS GLU SER MET LEU
SEQRES 22 B 460 THR LEU GLY LYS GLU SER LYS THR PRO GLY LYS SER SER
SEQRES 23 B 460 VAL PRO LEU TYR LEU ILE TYR PRO SER VAL GLU ASN VAL
SEQRES 24 B 460 ARG THR SER LEU GLU GLY TYR PRO ALA GLY GLY SER LEU
SEQRES 25 B 460 PRO TYR SER ILE GLN THR ALA GLU LYS GLN ASN TRP LEU
SEQRES 26 B 460 HIS SER TYR PHE HIS LYS TRP SER ALA GLU THR SER GLY
SEQRES 27 B 460 ARG SER ASN ALA MET PRO HIS ILE LYS THR TYR MET ARG
SEQRES 28 B 460 PRO SER PRO ASP PHE SER LYS ILE ALA TRP PHE LEU VAL
SEQRES 29 B 460 THR SER ALA ASN LEU SER LYS ALA ALA TRP GLY ALA LEU
SEQRES 30 B 460 GLU LYS ASN GLY THR GLN LEU MET ILE ARG SER TYR GLU
SEQRES 31 B 460 LEU GLY VAL LEU PHE LEU PRO SER ALA PHE GLY LEU ASP
SEQRES 32 B 460 SER PHE LYS VAL LYS GLN LYS PHE PHE ALA GLY SER GLN
SEQRES 33 B 460 GLU PRO MET ALA THR PHE PRO VAL PRO TYR ASP LEU PRO
SEQRES 34 B 460 PRO GLU LEU TYR GLY SER LYS ASP ARG PRO TRP ILE TRP
SEQRES 35 B 460 ASN ILE PRO TYR VAL LYS ALA PRO ASP THR HIS GLY ASN
SEQRES 36 B 460 MET TRP VAL PRO SER
HET EDO A 701 4
HET EDO A 702 4
HET EDO A 703 4
HET JTA A 704 17
HET EDO B 701 4
HET EDO B 702 4
HET JTA B 703 17
HETNAM EDO 1,2-ETHANEDIOL
HETNAM JTA 4-HYDROXY-8-NITROQUINOLINE-3-CARBOXYLIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 5(C2 H6 O2)
FORMUL 6 JTA 2(C10 H6 N2 O5)
FORMUL 10 HOH *580(H2 O)
HELIX 1 AA1 LYS A 175 ASN A 179 5 5
HELIX 2 AA2 HIS A 184 LEU A 189 1 6
HELIX 3 AA3 SER A 190 GLY A 194 5 5
HELIX 4 AA4 ASP A 207 TYR A 215 1 9
HELIX 5 AA5 PRO A 216 ARG A 220 5 5
HELIX 6 AA6 LYS A 231 LYS A 243 1 13
HELIX 7 AA7 ILE A 285 HIS A 290 5 6
HELIX 8 AA8 HIS A 318 ALA A 329 1 12
HELIX 9 AA9 ALA A 332 LYS A 344 1 13
HELIX 10 AB1 SER A 365 ASN A 369 5 5
HELIX 11 AB2 TRP A 370 ALA A 383 1 14
HELIX 12 AB3 ASN A 388 TRP A 392 5 5
HELIX 13 AB4 GLU A 415 THR A 422 1 8
HELIX 14 AB5 SER A 443 THR A 449 1 7
HELIX 15 AB6 GLY A 453 LEU A 460 5 8
HELIX 16 AB7 SER A 463 LYS A 469 1 7
HELIX 17 AB8 GLN A 470 SER A 475 5 6
HELIX 18 AB9 ALA A 482 GLY A 486 5 5
HELIX 19 AC1 SER A 518 GLY A 523 1 6
HELIX 20 AC2 LEU A 544 GLY A 549 5 6
HELIX 21 AC3 LYS B 175 ASN B 179 5 5
HELIX 22 AC4 HIS B 184 SER B 190 1 7
HELIX 23 AC5 PRO B 191 GLY B 194 5 4
HELIX 24 AC6 ASP B 207 TYR B 215 1 9
HELIX 25 AC7 PRO B 216 ARG B 220 5 5
HELIX 26 AC8 LYS B 231 LYS B 243 1 13
HELIX 27 AC9 ILE B 285 HIS B 290 5 6
HELIX 28 AD1 HIS B 318 ALA B 329 1 12
HELIX 29 AD2 ALA B 332 LYS B 344 1 13
HELIX 30 AD3 GLN B 363 ASN B 369 5 7
HELIX 31 AD4 TRP B 370 ALA B 383 1 14
HELIX 32 AD5 ASN B 388 TRP B 392 5 5
HELIX 33 AD6 GLU B 415 THR B 422 1 8
HELIX 34 AD7 SER B 443 THR B 449 1 7
HELIX 35 AD8 GLY B 453 LEU B 460 5 8
HELIX 36 AD9 SER B 463 LYS B 469 1 7
HELIX 37 AE1 GLN B 470 SER B 475 5 6
HELIX 38 AE2 ALA B 482 GLY B 486 5 5
HELIX 39 AE3 SER B 518 GLY B 523 1 6
HELIX 40 AE4 LEU B 544 GLY B 549 5 6
SHEET 1 AA1 7 PHE A 166 LEU A 168 0
SHEET 2 AA1 7 GLY A 295 LEU A 298 -1 O ILE A 296 N TYR A 167
SHEET 3 AA1 7 LEU A 275 HIS A 280 -1 N ILE A 279 O TRP A 297
SHEET 4 AA1 7 MET A 266 TYR A 271 -1 N LEU A 269 O ARG A 276
SHEET 5 AA1 7 LEU A 196 PHE A 202 -1 N VAL A 197 O LEU A 270
SHEET 6 AA1 7 ILE A 224 HIS A 228 1 O LEU A 225 N GLN A 201
SHEET 7 AA1 7 ILE A 248 GLN A 252 1 O SER A 249 N LEU A 226
SHEET 1 AA2 2 LYS A 292 THR A 293 0
SHEET 2 AA2 2 MET A 491 PRO A 492 1 O MET A 491 N THR A 293
SHEET 1 AA3 7 TYR A 353 SER A 357 0
SHEET 2 AA3 7 GLU A 538 PHE A 543 -1 O LEU A 542 N TYR A 353
SHEET 3 AA3 7 LYS A 506 THR A 513 -1 N PHE A 510 O PHE A 543
SHEET 4 AA3 7 LYS A 495 PRO A 500 -1 N ARG A 499 O ALA A 508
SHEET 5 AA3 7 VAL A 394 GLN A 397 -1 N VAL A 395 O MET A 498
SHEET 6 AA3 7 LEU A 437 ILE A 440 1 O ILE A 440 N GLY A 396
SHEET 7 AA3 7 PHE A 477 HIS A 478 1 O HIS A 478 N LEU A 439
SHEET 1 AA4 5 TYR A 353 SER A 357 0
SHEET 2 AA4 5 GLU A 538 PHE A 543 -1 O LEU A 542 N TYR A 353
SHEET 3 AA4 5 LYS A 506 THR A 513 -1 N PHE A 510 O PHE A 543
SHEET 4 AA4 5 PHE A 553 VAL A 555 -1 O PHE A 553 N ILE A 507
SHEET 5 AA4 5 THR A 569 PHE A 570 1 O PHE A 570 N LYS A 554
SHEET 1 AA5 3 GLY A 360 GLN A 363 0
SHEET 2 AA5 3 GLN A 531 ILE A 534 -1 O LEU A 532 N PHE A 362
SHEET 3 AA5 3 ALA A 524 GLU A 526 -1 N GLU A 526 O GLN A 531
SHEET 1 AA6 7 PHE B 166 LEU B 168 0
SHEET 2 AA6 7 GLY B 295 LEU B 298 -1 O ILE B 296 N TYR B 167
SHEET 3 AA6 7 LEU B 275 HIS B 280 -1 N ILE B 279 O TRP B 297
SHEET 4 AA6 7 MET B 266 TYR B 271 -1 N LEU B 269 O ARG B 276
SHEET 5 AA6 7 LEU B 196 PHE B 202 -1 N PHE B 202 O MET B 266
SHEET 6 AA6 7 ILE B 224 HIS B 228 1 O LEU B 225 N GLN B 201
SHEET 7 AA6 7 ILE B 248 GLN B 252 1 O SER B 249 N ILE B 224
SHEET 1 AA7 7 TYR B 353 SER B 357 0
SHEET 2 AA7 7 GLU B 538 PHE B 543 -1 O LEU B 542 N TYR B 353
SHEET 3 AA7 7 LYS B 506 THR B 513 -1 N PHE B 510 O PHE B 543
SHEET 4 AA7 7 LYS B 495 PRO B 500 -1 N ARG B 499 O ALA B 508
SHEET 5 AA7 7 VAL B 394 GLN B 397 -1 N GLN B 397 O THR B 496
SHEET 6 AA7 7 LEU B 437 ILE B 440 1 O TYR B 438 N VAL B 394
SHEET 7 AA7 7 PHE B 477 HIS B 478 1 O HIS B 478 N LEU B 439
SHEET 1 AA8 5 TYR B 353 SER B 357 0
SHEET 2 AA8 5 GLU B 538 PHE B 543 -1 O LEU B 542 N TYR B 353
SHEET 3 AA8 5 LYS B 506 THR B 513 -1 N PHE B 510 O PHE B 543
SHEET 4 AA8 5 PHE B 553 VAL B 555 -1 O PHE B 553 N ILE B 507
SHEET 5 AA8 5 THR B 569 PHE B 570 1 O PHE B 570 N LYS B 554
SHEET 1 AA9 3 GLY B 360 PHE B 362 0
SHEET 2 AA9 3 GLN B 531 ILE B 534 -1 O LEU B 532 N PHE B 362
SHEET 3 AA9 3 ALA B 524 GLU B 526 -1 N ALA B 524 O MET B 533
CISPEP 1 LEU A 576 PRO A 577 0 -4.40
CISPEP 2 LEU B 576 PRO B 577 0 -2.53
SITE 1 AC1 5 ASP A 322 ASN A 369 TRP A 370 HOH A 801
SITE 2 AC1 5 HOH A 939
SITE 1 AC2 7 ILE A 355 GLY A 356 SER A 357 THR A 513
SITE 2 AC2 7 ALA A 515 TRP A 522 GLY A 540
SITE 1 AC3 6 THR A 484 LYS A 556 TYR A 574 ASP A 575
SITE 2 AC3 6 LEU A 576 HOH A 869
SITE 1 AC4 11 TYR A 204 HIS A 263 LYS A 265 ASN A 283
SITE 2 AC4 11 GLY A 458 PRO A 461 HIS A 493 HOH A 899
SITE 3 AC4 11 HOH A 942 HOH A 973 HOH A1032
SITE 1 AC5 3 SER B 400 ASN B 516 SER B 518
SITE 1 AC6 7 ILE B 355 GLY B 356 SER B 357 THR B 513
SITE 2 AC6 7 ALA B 515 TRP B 522 GLY B 540
SITE 1 AC7 8 TYR B 204 HIS B 263 LYS B 265 ASN B 283
SITE 2 AC7 8 GLY B 458 PRO B 461 HIS B 493 HOH B 827
CRYST1 50.156 105.686 193.984 90.00 90.00 90.00 P 21 21 21 8
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 0.019938 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009462 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005155 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
