HEADER TRANSFERASE, HYDROLASE 26-AUG-09 3ISN
TITLE CRYSTAL STRUCTURE OF HIV-1 RT BOUND TO A 6-VINYLPYRIMIDINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REVERSE TRANSCRIPTASE/RIBONUCLEASE H;
COMPND 3 CHAIN: C;
COMPND 4 SYNONYM: HIV-1 REVERSE TRANSCRIPTASE, P66 RT;
COMPND 5 EC: 2.7.7.49, 2.7.7.7, 3.1.26.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: P51 RT;
COMPND 9 CHAIN: D;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS;
SOURCE 3 ORGANISM_COMMON: HIV-1;
SOURCE 4 ORGANISM_TAXID: 11678;
SOURCE 5 STRAIN: TYPE 1 BH10;
SOURCE 6 GENE: GAG-POL;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS;
SOURCE 12 ORGANISM_COMMON: HIV-1;
SOURCE 13 ORGANISM_TAXID: 11678;
SOURCE 14 STRAIN: TYPE 1 BH10;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HIV-1, INHIBITOR, RT, TRANSFERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.ENNIFAR,S.FREISZ,G.BEC,P.DUMAS,M.BOTTA,M.RADI
REVDAT 2 01-NOV-23 3ISN 1 REMARK
REVDAT 1 16-MAR-10 3ISN 0
JRNL AUTH S.FREISZ,G.BEC,M.RADI,P.WOLFF,E.CRESPAN,L.ANGELI,P.DUMAS,
JRNL AUTH 2 G.MAGA,M.BOTTA,E.ENNIFAR
JRNL TITL CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE BOUND TO A
JRNL TITL 2 NON-NUCLEOSIDE INHIBITOR WITH A NOVEL MECHANISM OF ACTION
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 49 1805 2010
JRNL REFN ISSN 1433-7851
JRNL PMID 20135654
JRNL DOI 10.1002/ANIE.200905651
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.4_57)
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.8
REMARK 3 NUMBER OF REFLECTIONS : 43911
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.550
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 49.1117 - 6.0202 1.00 3479 165 0.1878 0.2397
REMARK 3 2 6.0202 - 4.7797 1.00 3412 163 0.1852 0.2343
REMARK 3 3 4.7797 - 4.1759 1.00 3380 161 0.1707 0.2126
REMARK 3 4 4.1759 - 3.7942 0.81 2737 131 0.1912 0.2744
REMARK 3 5 3.7942 - 3.5223 0.77 2600 123 0.2144 0.2685
REMARK 3 6 3.5223 - 3.3147 0.70 2352 113 0.2455 0.2833
REMARK 3 7 3.3147 - 3.1487 0.99 3323 159 0.2412 0.3254
REMARK 3 8 3.1487 - 3.0117 1.00 3350 159 0.2349 0.3135
REMARK 3 9 3.0117 - 2.8958 1.00 3348 159 0.2365 0.3036
REMARK 3 10 2.8958 - 2.7959 1.00 3381 162 0.2618 0.4177
REMARK 3 11 2.7959 - 2.7084 1.00 3359 160 0.2926 0.3767
REMARK 3 12 2.7084 - 2.6310 0.20 668 32 0.3237 0.2880
REMARK 3 13 2.6310 - 2.5618 1.00 3319 158 0.3091 0.3828
REMARK 3 14 2.5618 - 2.4993 0.95 3205 153 0.4562 0.4468
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 : 0.32
REMARK 3 B_SOL : 50.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.050
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.29200
REMARK 3 B22 (A**2) : 8.35000
REMARK 3 B33 (A**2) : 1.62700
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 6.84000
REMARK 3 B23 (A**2) : 0.00000
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 8173
REMARK 3 ANGLE : 1.353 11109
REMARK 3 CHIRALITY : 0.085 1205
REMARK 3 PLANARITY : 0.007 1399
REMARK 3 DIHEDRAL : 19.756 3072
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 3ISN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054815.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2824
REMARK 200 MONOCHROMATOR : CRYSTAL
REMARK 200 OPTICS : CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49675
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.3
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : 0.06200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.4900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54200
REMARK 200 R SYM FOR SHELL (I) : 0.73700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.530
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: PDB ID 1DLO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BIS-TRIS , 25% PEG 3350, 200MM
REMARK 280 AMMONIUM SULFATE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 112.56050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.09100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 112.56050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.09100
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: 5230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 C 586 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 ARG C 557
REMARK 465 LYS C 558
REMARK 465 ILE C 559
REMARK 465 LEU C 560
REMARK 465 LYS D 219
REMARK 465 LYS D 220
REMARK 465 HIS D 221
REMARK 465 GLN D 222
REMARK 465 LYS D 223
REMARK 465 GLU D 224
REMARK 465 PRO D 225
REMARK 465 PRO D 226
REMARK 465 PHE D 227
REMARK 465 LEU D 228
REMARK 465 TRP D 229
REMARK 465 MET D 230
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 52 C - N - CA ANGL. DEV. = 10.7 DEGREES
REMARK 500 PRO D 420 C - N - CA ANGL. DEV. = 11.7 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 LYS C 20 55.71 -148.81
REMARK 500 PRO C 25 -159.03 -83.28
REMARK 500 LEU C 26 -165.57 150.94
REMARK 500 THR C 27 133.17 -28.97
REMARK 500 ALA C 33 -61.13 71.59
REMARK 500 PRO C 52 -7.25 -40.31
REMARK 500 LYS C 66 -118.78 51.55
REMARK 500 LYS C 70 -113.09 12.22
REMARK 500 TRP C 71 -81.71 -125.64
REMARK 500 ARG C 72 122.72 85.15
REMARK 500 GLN C 91 127.94 -37.82
REMARK 500 SER C 117 21.72 178.93
REMARK 500 ASP C 121 107.73 -54.85
REMARK 500 ILE C 135 -76.28 -24.07
REMARK 500 ASN C 137 67.65 -104.74
REMARK 500 MET C 184 -123.44 42.65
REMARK 500 THR C 216 86.89 -173.26
REMARK 500 ASP C 218 100.02 -55.53
REMARK 500 LYS C 220 -91.60 4.93
REMARK 500 HIS C 221 -120.48 61.24
REMARK 500 GLN C 222 38.24 -149.93
REMARK 500 PHE C 227 97.74 96.46
REMARK 500 LYS C 249 -172.51 -175.92
REMARK 500 ALA C 267 -47.85 133.17
REMARK 500 LEU C 283 -74.60 -89.50
REMARK 500 THR C 286 -158.47 -115.00
REMARK 500 LYS C 287 -157.24 -161.61
REMARK 500 ALA C 288 89.30 44.90
REMARK 500 THR C 296 170.96 -58.20
REMARK 500 GLN C 334 91.51 60.09
REMARK 500 PHE C 346 -6.84 81.34
REMARK 500 ARG C 358 -97.36 -57.64
REMARK 500 GLU C 413 115.35 -39.92
REMARK 500 ASN C 418 87.41 -65.74
REMARK 500 THR C 419 -99.53 -123.41
REMARK 500 PRO C 420 -120.14 -80.84
REMARK 500 LYS C 451 -11.54 82.09
REMARK 500 ASN C 471 59.24 34.34
REMARK 500 THR C 472 -168.19 -127.03
REMARK 500 ILE C 542 85.97 32.97
REMARK 500 SER C 553 54.60 -112.97
REMARK 500 PRO D 4 4.47 -58.06
REMARK 500 LYS D 65 -120.90 -77.60
REMARK 500 THR D 69 -103.42 -61.93
REMARK 500 GLN D 85 152.12 -44.46
REMARK 500 TRP D 88 -122.02 50.42
REMARK 500 VAL D 90 45.00 -87.11
REMARK 500 PRO D 95 160.68 -39.75
REMARK 500 PHE D 116 9.85 -67.29
REMARK 500 ASP D 121 128.67 -32.15
REMARK 500
REMARK 500 THIS ENTRY HAS 73 RAMACHANDRAN OUTLIERS.
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 EDM C 561
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ITH RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 E465Q IS MUTAGENESIS ACCORDING TO REFERENCE 9 OF DATABASE UNIPROTKB/
REMARK 999 SWISS-PROT P03366 (POL_HV1B1).
DBREF 3ISN C 1 560 UNP P03366 POL_HV1B1 600 1159
DBREF 3ISN D 1 427 UNP P03366 POL_HV1B1 600 1026
SEQADV 3ISN GLN C 478 UNP P03366 GLU 1077 SEE REMARK 999
SEQRES 1 C 560 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 C 560 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 C 560 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 C 560 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 C 560 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 C 560 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 C 560 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 C 560 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS
SEQRES 9 C 560 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 C 560 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 C 560 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 C 560 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 C 560 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 C 560 PRO PHE LYS LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 C 560 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 C 560 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 C 560 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 C 560 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 C 560 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 C 560 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 C 560 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 C 560 ILE LYS VAL ARG GLN LEU CYS LYS LEU LEU ARG GLY THR
SEQRES 23 C 560 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 C 560 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 C 560 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 C 560 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 C 560 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 C 560 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 C 560 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 C 560 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 C 560 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 C 560 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 C 560 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU
SEQRES 34 C 560 GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE TYR VAL
SEQRES 35 C 560 ASP GLY ALA ALA ASN ARG GLU THR LYS LEU GLY LYS ALA
SEQRES 36 C 560 GLY TYR VAL THR ASN LYS GLY ARG GLN LYS VAL VAL PRO
SEQRES 37 C 560 LEU THR ASN THR THR ASN GLN LYS THR GLN LEU GLN ALA
SEQRES 38 C 560 ILE TYR LEU ALA LEU GLN ASP SER GLY LEU GLU VAL ASN
SEQRES 39 C 560 ILE VAL THR ASP SER GLN TYR ALA LEU GLY ILE ILE GLN
SEQRES 40 C 560 ALA GLN PRO ASP LYS SER GLU SER GLU LEU VAL ASN GLN
SEQRES 41 C 560 ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS VAL TYR LEU
SEQRES 42 C 560 ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY GLY ASN GLU
SEQRES 43 C 560 GLN VAL ASP LYS LEU VAL SER ALA GLY ILE ARG LYS ILE
SEQRES 44 C 560 LEU
SEQRES 1 D 427 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 D 427 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 D 427 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 D 427 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 D 427 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 D 427 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 D 427 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 D 427 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS
SEQRES 9 D 427 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 D 427 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 D 427 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 D 427 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 D 427 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 D 427 PRO PHE LYS LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 D 427 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 D 427 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 D 427 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 D 427 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 D 427 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 D 427 GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU
SEQRES 21 D 427 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 D 427 ILE LYS VAL ARG GLN LEU CYS LYS LEU LEU ARG GLY THR
SEQRES 23 D 427 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 D 427 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 D 427 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 D 427 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 D 427 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 D 427 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 D 427 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 D 427 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 D 427 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 D 427 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 D 427 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR
HET EDM C 561 15
HETNAM EDM 6-ETHENYL-N,N-DIMETHYL-2-(METHYLSULFONYL)PYRIMIDIN-4-
HETNAM 2 EDM AMINE
FORMUL 3 EDM C9 H13 N3 O2 S
FORMUL 4 HOH *204(H2 O)
HELIX 1 1 THR C 27 GLU C 44 1 18
HELIX 2 2 PHE C 77 THR C 84 1 8
HELIX 3 3 HIS C 96 LEU C 100 5 5
HELIX 4 4 ASP C 121 ALA C 129 5 9
HELIX 5 5 GLY C 155 GLN C 174 1 20
HELIX 6 6 GLU C 194 TRP C 212 1 19
HELIX 7 7 THR C 253 GLN C 269 1 17
HELIX 8 8 VAL C 276 LEU C 282 1 7
HELIX 9 9 THR C 296 LEU C 310 1 15
HELIX 10 10 ASN C 363 GLY C 384 1 22
HELIX 11 11 GLN C 394 TYR C 405 1 12
HELIX 12 12 THR C 473 ASP C 488 1 16
HELIX 13 13 SER C 499 ALA C 508 1 10
HELIX 14 14 SER C 515 LYS C 528 1 14
HELIX 15 15 ILE C 542 SER C 553 1 12
HELIX 16 16 THR D 27 GLU D 44 1 18
HELIX 17 17 LYS D 66 THR D 69 5 4
HELIX 18 18 PHE D 77 THR D 84 1 8
HELIX 19 19 PHE D 87 GLN D 91 5 5
HELIX 20 20 GLY D 99 LYS D 103 5 5
HELIX 21 21 GLY D 112 VAL D 118 5 7
HELIX 22 22 ASP D 121 ALA D 129 5 9
HELIX 23 23 SER D 134 GLU D 138 5 5
HELIX 24 24 LYS D 154 PHE D 160 1 7
HELIX 25 25 PHE D 160 GLN D 174 1 15
HELIX 26 26 GLU D 194 ARG D 211 1 18
HELIX 27 27 VAL D 254 ALA D 267 1 14
HELIX 28 28 VAL D 276 ARG D 284 1 9
HELIX 29 29 THR D 296 LEU D 310 1 15
HELIX 30 30 ASN D 363 GLY D 384 1 22
HELIX 31 31 GLN D 394 TRP D 402 1 9
HELIX 32 32 THR D 403 TYR D 405 5 3
SHEET 1 A 3 ILE C 47 LYS C 49 0
SHEET 2 A 3 ILE C 142 TYR C 146 -1 O GLN C 145 N SER C 48
SHEET 3 A 3 PHE C 130 ILE C 132 -1 N ILE C 132 O ILE C 142
SHEET 1 B 2 VAL C 60 ALA C 62 0
SHEET 2 B 2 LYS C 73 VAL C 75 -1 O LEU C 74 N PHE C 61
SHEET 1 C 3 SER C 105 ASP C 110 0
SHEET 2 C 3 ASP C 186 SER C 191 -1 O VAL C 189 N THR C 107
SHEET 3 C 3 VAL C 179 TYR C 183 -1 N TYR C 183 O ASP C 186
SHEET 1 D 4 LEU C 228 TRP C 229 0
SHEET 2 D 4 TYR C 232 LEU C 234 -1 O TYR C 232 N TRP C 229
SHEET 3 D 4 TRP C 239 VAL C 241 -1 O THR C 240 N GLU C 233
SHEET 4 D 4 VAL C 314 GLY C 316 -1 O VAL C 314 N VAL C 241
SHEET 1 E 5 ASN C 348 ALA C 355 0
SHEET 2 E 5 GLN C 336 TYR C 342 -1 N ILE C 341 O LYS C 350
SHEET 3 E 5 ILE C 326 LYS C 331 -1 N ILE C 326 O TYR C 342
SHEET 4 E 5 LYS C 388 LEU C 391 1 O LYS C 390 N ALA C 327
SHEET 5 E 5 TRP C 414 PHE C 416 1 O GLU C 415 N LEU C 391
SHEET 1 F 2 HIS C 361 THR C 362 0
SHEET 2 F 2 LYS C 512 SER C 513 -1 O LYS C 512 N THR C 362
SHEET 1 G 5 GLN C 464 LEU C 469 0
SHEET 2 G 5 GLY C 453 THR C 459 -1 N GLY C 453 O LEU C 469
SHEET 3 G 5 GLU C 438 ALA C 446 -1 N TYR C 441 O VAL C 458
SHEET 4 G 5 GLU C 492 THR C 497 1 O ASN C 494 N GLU C 438
SHEET 5 G 5 LYS C 530 TRP C 535 1 O TYR C 532 N ILE C 495
SHEET 1 H 3 ILE D 47 LYS D 49 0
SHEET 2 H 3 ILE D 142 TYR D 146 -1 O GLN D 145 N SER D 48
SHEET 3 H 3 PHE D 130 ILE D 132 -1 N ILE D 132 O ILE D 142
SHEET 1 I 2 VAL D 60 LYS D 64 0
SHEET 2 I 2 TRP D 71 VAL D 75 -1 O ARG D 72 N ILE D 63
SHEET 1 J 3 SER D 105 ASP D 110 0
SHEET 2 J 3 ASP D 186 SER D 191 -1 O VAL D 189 N THR D 107
SHEET 3 J 3 ILE D 178 TYR D 183 -1 N TYR D 181 O TYR D 188
SHEET 1 K 2 TRP D 252 THR D 253 0
SHEET 2 K 2 VAL D 292 ILE D 293 -1 O ILE D 293 N TRP D 252
SHEET 1 L 5 LYS D 347 ALA D 355 0
SHEET 2 L 5 GLN D 336 GLU D 344 -1 N ILE D 341 O LYS D 350
SHEET 3 L 5 ILE D 326 LYS D 331 -1 N GLN D 330 O THR D 338
SHEET 4 L 5 LYS D 388 LEU D 391 1 O LYS D 390 N ALA D 327
SHEET 5 L 5 TRP D 414 PHE D 416 1 O GLU D 415 N PHE D 389
SITE 1 AC1 9 MET C 184 ASP C 186 MET C 230 GLY C 231
SITE 2 AC1 9 LYS C 263 TRP C 266 HOH C 578 HOH C 631
SITE 3 AC1 9 HOH C 672
CRYST1 225.121 72.182 93.516 90.00 108.97 90.00 C 1 2 1 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 0.004442 0.000000 0.001527 0.00000
SCALE2 0.000000 0.013854 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011308 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
