HEADER TRANSFERASE/TRANSFERASE INHIBITOR 10-DEC-12 4ICL
TITLE HIV-1 REVERSE TRANSCRIPTASE WITH BOUND FRAGMENT AT THE INCOMING DNTP
TITLE 2 BINDING SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REVERSE TRANSCRIPTASE/RIBONUCLEASE H;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: P66 (UNP RESIDUES 600-1154);
COMPND 5 SYNONYM: EXORIBONUCLEASE H, P66 RT;
COMPND 6 EC: 2.7.7.49, 2.7.7.7, 3.1.26.13;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: P51 RT;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: P51 (UNP RESIDUES 600-1027);
COMPND 13 SYNONYM: GAG-POL POLYPROTEIN;
COMPND 14 EC: 2.7.7.49, 2.7.7.7, 3.1.26.13;
COMPND 15 ENGINEERED: YES;
COMPND 16 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1;
SOURCE 3 ORGANISM_COMMON: HIV-1;
SOURCE 4 ORGANISM_TAXID: 11678;
SOURCE 5 STRAIN: BH10;
SOURCE 6 GENE: GAG-POL, POL;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(RIL);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCDF-2;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1;
SOURCE 14 ORGANISM_COMMON: HIV-1;
SOURCE 15 ORGANISM_TAXID: 11678;
SOURCE 16 STRAIN: BH10;
SOURCE 17 GENE: GAG-POL, POL;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: BL21(RIL);
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PCDF-2
KEYWDS RNA-DIRECTED DNA POLYMERASE, DNA POLYMERASE, ENDONUCLEASE, HYDROLASE,
KEYWDS 2 MULTIFUNCTIONAL ENZYME, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.BAUMAN,D.PATEL,E.ARNOLD
REVDAT 5 28-FEB-24 4ICL 1 REMARK SEQADV LINK
REVDAT 4 15-NOV-17 4ICL 1 REMARK
REVDAT 3 17-JUN-15 4ICL 1 HETATM
REVDAT 2 24-APR-13 4ICL 1 JRNL
REVDAT 1 06-FEB-13 4ICL 0
JRNL AUTH J.D.BAUMAN,D.PATEL,C.DHARIA,M.W.FROMER,S.AHMED,Y.FRENKEL,
JRNL AUTH 2 R.S.VIJAYAN,J.T.ECK,W.C.HO,K.DAS,A.J.SHATKIN,E.ARNOLD
JRNL TITL DETECTING ALLOSTERIC SITES OF HIV-1 REVERSE TRANSCRIPTASE BY
JRNL TITL 2 X-RAY CRYSTALLOGRAPHIC FRAGMENT SCREENING.
JRNL REF J.MED.CHEM. V. 56 2738 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23342998
JRNL DOI 10.1021/JM301271J
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 114627
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) : 0.179
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2123
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 38.0082 - 4.5333 0.98 7223 123 0.1688 0.1637
REMARK 3 2 4.5333 - 3.5991 1.00 7235 123 0.1556 0.1564
REMARK 3 3 3.5991 - 3.1444 1.00 7165 135 0.1757 0.1977
REMARK 3 4 3.1444 - 2.8570 1.00 7128 173 0.1840 0.2275
REMARK 3 5 2.8570 - 2.6523 1.00 7098 164 0.1806 0.2222
REMARK 3 6 2.6523 - 2.4960 1.00 7074 144 0.1751 0.2079
REMARK 3 7 2.4960 - 2.3710 1.00 7094 162 0.1797 0.2206
REMARK 3 8 2.3710 - 2.2678 0.99 7001 163 0.1781 0.1889
REMARK 3 9 2.2678 - 2.1805 0.99 7049 140 0.1814 0.2262
REMARK 3 10 2.1805 - 2.1053 0.98 7004 150 0.1888 0.2352
REMARK 3 11 2.1053 - 2.0394 0.98 6951 137 0.1956 0.2428
REMARK 3 12 2.0394 - 1.9811 0.98 6913 139 0.2075 0.2208
REMARK 3 13 1.9811 - 1.9290 0.97 6945 140 0.2281 0.2124
REMARK 3 14 1.9290 - 1.8819 0.97 6871 137 0.2454 0.2603
REMARK 3 15 1.8819 - 1.8391 0.96 6799 129 0.2716 0.2703
REMARK 3 16 1.8391 - 1.8000 0.96 6786 132 0.2953 0.3098
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.000
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 : 0.014 8252
REMARK 3 ANGLE : 1.441 11205
REMARK 3 CHIRALITY : 0.084 1215
REMARK 3 PLANARITY : 0.010 1408
REMARK 3 DIHEDRAL : 14.680 3129
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 296 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6541 -21.1103 52.8672
REMARK 3 T TENSOR
REMARK 3 T11: 0.3216 T22: 0.2900
REMARK 3 T33: 0.2863 T12: -0.0282
REMARK 3 T13: 0.0462 T23: 0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 0.4373 L22: 0.3803
REMARK 3 L33: 1.5574 L12: 0.1209
REMARK 3 L13: 0.3597 L23: 0.3667
REMARK 3 S TENSOR
REMARK 3 S11: 0.1036 S12: -0.1874 S13: -0.1294
REMARK 3 S21: 0.1330 S22: 0.0225 S23: 0.1357
REMARK 3 S31: 0.2130 S32: -0.2073 S33: -0.1369
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 297 THROUGH 383 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6307 -19.0268 20.9858
REMARK 3 T TENSOR
REMARK 3 T11: 0.1983 T22: 0.1928
REMARK 3 T33: 0.2875 T12: -0.0185
REMARK 3 T13: 0.0041 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 1.4862 L22: 1.8137
REMARK 3 L33: 2.5765 L12: -0.0456
REMARK 3 L13: 0.7229 L23: -0.7033
REMARK 3 S TENSOR
REMARK 3 S11: 0.1260 S12: -0.0029 S13: -0.2915
REMARK 3 S21: -0.0118 S22: 0.1866 S23: 0.5321
REMARK 3 S31: 0.2084 S32: -0.4503 S33: -0.1145
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 384 THROUGH 554 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3035 4.6688 6.8146
REMARK 3 T TENSOR
REMARK 3 T11: 0.1627 T22: 0.2773
REMARK 3 T33: 0.2276 T12: 0.0009
REMARK 3 T13: 0.0760 T23: 0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 2.5624 L22: 0.2321
REMARK 3 L33: 0.7604 L12: -1.0046
REMARK 3 L13: 1.5311 L23: -0.3678
REMARK 3 S TENSOR
REMARK 3 S11: -0.0811 S12: -0.3121 S13: -0.1269
REMARK 3 S21: 0.0744 S22: 0.1451 S23: 0.1681
REMARK 3 S31: 0.0255 S32: -0.2627 S33: 0.0038
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.4073 1.4790 36.6419
REMARK 3 T TENSOR
REMARK 3 T11: 0.2286 T22: 0.1919
REMARK 3 T33: 0.1366 T12: -0.0614
REMARK 3 T13: 0.0017 T23: 0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 3.0499 L22: 3.6842
REMARK 3 L33: 2.5568 L12: -0.3270
REMARK 3 L13: 0.8135 L23: -0.3678
REMARK 3 S TENSOR
REMARK 3 S11: -0.0705 S12: 0.0775 S13: 0.2900
REMARK 3 S21: 0.1479 S22: -0.0890 S23: -0.1583
REMARK 3 S31: -0.4171 S32: 0.3615 S33: -0.0060
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 194 )
REMARK 3 ORIGIN FOR THE GROUP (A): 60.9113 15.0887 34.6602
REMARK 3 T TENSOR
REMARK 3 T11: 0.4550 T22: 0.3443
REMARK 3 T33: 0.4715 T12: -0.2927
REMARK 3 T13: -0.1305 T23: 0.1222
REMARK 3 L TENSOR
REMARK 3 L11: 1.7114 L22: 3.1134
REMARK 3 L33: 2.2537 L12: -0.3673
REMARK 3 L13: 0.6278 L23: -0.9827
REMARK 3 S TENSOR
REMARK 3 S11: -0.2805 S12: 0.2958 S13: 0.7657
REMARK 3 S21: 0.5513 S22: 0.0217 S23: -0.4453
REMARK 3 S31: -0.7704 S32: 0.6760 S33: -0.0706
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 195 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): 60.1713 20.3631 15.1473
REMARK 3 T TENSOR
REMARK 3 T11: 0.2790 T22: 1.0937
REMARK 3 T33: 0.7820 T12: -0.1702
REMARK 3 T13: -0.0597 T23: 0.2687
REMARK 3 L TENSOR
REMARK 3 L11: 3.5983 L22: 0.4653
REMARK 3 L33: 1.9788 L12: -0.4788
REMARK 3 L13: 2.5859 L23: -0.2832
REMARK 3 S TENSOR
REMARK 3 S11: -0.0321 S12: -0.0582 S13: -0.2197
REMARK 3 S21: 0.0669 S22: -0.1421 S23: -0.6096
REMARK 3 S31: -0.2493 S32: 0.7581 S33: -0.0021
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 254 THROUGH 325 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8174 30.0218 5.4214
REMARK 3 T TENSOR
REMARK 3 T11: 0.2881 T22: 0.2397
REMARK 3 T33: 0.2674 T12: -0.0211
REMARK 3 T13: 0.0515 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 2.4797 L22: 2.4728
REMARK 3 L33: 5.3668 L12: 0.2967
REMARK 3 L13: 2.2626 L23: 0.4948
REMARK 3 S TENSOR
REMARK 3 S11: -0.3630 S12: 0.0252 S13: 0.5752
REMARK 3 S21: 0.1385 S22: 0.1181 S23: 0.1425
REMARK 3 S31: -0.8854 S32: -0.0672 S33: 0.3548
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 326 THROUGH 428 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.9153 12.3962 18.1642
REMARK 3 T TENSOR
REMARK 3 T11: 0.2431 T22: 0.1872
REMARK 3 T33: 0.1484 T12: -0.0171
REMARK 3 T13: 0.0616 T23: -0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 2.4419 L22: 4.2576
REMARK 3 L33: 2.3606 L12: -0.1182
REMARK 3 L13: 1.6261 L23: -0.4668
REMARK 3 S TENSOR
REMARK 3 S11: -0.0408 S12: 0.1669 S13: 0.0864
REMARK 3 S21: -0.0425 S22: -0.1615 S23: -0.0472
REMARK 3 S31: -0.1527 S32: 0.0726 S33: 0.1299
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 4ICL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1000076582.
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) : 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.917
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117469
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 97.9
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.0100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.73500
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: PHENIX 1.8_1069
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000, 4% PEG 400, 50 MM
REMARK 280 IMIDAZOLE, 10 MM SPERMINE, 15 MM MGSO4, 100 MM AMMONIUM SULFATE,
REMARK 280 AND 5 MM TRIS(2-CARBOXYETHYL)PHOSPHINE, PH 6.7, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 277.0K , VAPOR DIFFUSION, HANGING DROP
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 81.52650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.32400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 81.52650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.32400
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: 8080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 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 555
REMARK 465 GLY B 0
REMARK 465 PRO B 1
REMARK 465 ILE B 2
REMARK 465 SER B 3
REMARK 465 PRO B 4
REMARK 465 THR B 215
REMARK 465 THR B 216
REMARK 465 PRO B 217
REMARK 465 ASP B 218
REMARK 465 LYS B 219
REMARK 465 LYS B 220
REMARK 465 HIS B 221
REMARK 465 GLN B 222
REMARK 465 LYS B 223
REMARK 465 GLU B 224
REMARK 465 PRO B 225
REMARK 465 PRO B 226
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 HE21 GLN A 373 O HOH A 939 1.38
REMARK 500 OE1 GLN A 373 HG1 THR B 397 1.50
REMARK 500 O HOH B 737 O HOH B 842 1.90
REMARK 500 O LYS B 166 OE1 GLU B 169 2.04
REMARK 500 O HIS B 361 O HOH B 841 2.04
REMARK 500 O HOH A 1127 O HOH A 1128 2.06
REMARK 500 O HOH A 948 O HOH A 1090 2.12
REMARK 500 O LEU A 193 O HOH A 1031 2.12
REMARK 500 O HOH B 761 O HOH B 854 2.14
REMARK 500 NE2 GLN A 373 O HOH A 939 2.14
REMARK 500 O HOH B 744 O HOH B 854 2.14
REMARK 500 NZ LYS A 220 O HOH A 1022 2.16
REMARK 500 O HOH B 745 O HOH B 758 2.16
REMARK 500 O HOH A 1047 O HOH A 1091 2.16
REMARK 500 O HOH A 1086 O HOH A 1105 2.17
REMARK 500 N PHE B 227 O HOH B 764 2.17
REMARK 500 O HOH B 815 O HOH B 855 2.18
REMARK 500 O HOH A 766 O HOH A 929 2.18
REMARK 500 O HOH B 823 O HOH B 830 2.19
REMARK 500 O HOH A 940 O HOH A 985 2.19
REMARK 500 O HOH A 994 O HOH B 811 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 OE2 GLU A 529 HZ1 LYS B 104 4545 1.40
REMARK 500 OE2 GLU A 529 NZ LYS B 104 4545 2.11
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 MET A 184 -129.76 57.63
REMARK 500 LYS A 219 108.44 -57.26
REMARK 500 HIS A 221 151.25 -49.35
REMARK 500 ILE A 270 -24.42 -143.10
REMARK 500 PHE B 77 21.41 -79.77
REMARK 500 GLN B 85 154.63 -44.16
REMARK 500 ASN B 136 19.14 58.05
REMARK 500 MET B 184 -120.45 52.19
REMARK 500 ARG B 356 41.35 -93.25
REMARK 500 ALA B 360 33.86 -141.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 443 OD2
REMARK 620 2 ASP A 498 OD2 93.6
REMARK 620 3 ASP A 549 OD1 80.8 140.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T27 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 14N A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 507
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ID5 RELATED DB: PDB
REMARK 900 RELATED ID: 4IDK RELATED DB: PDB
REMARK 900 RELATED ID: 4IFV RELATED DB: PDB
REMARK 900 RELATED ID: 4IFY RELATED DB: PDB
REMARK 900 RELATED ID: 4IG0 RELATED DB: PDB
REMARK 900 RELATED ID: 4IG3 RELATED DB: PDB
REMARK 900 RELATED ID: 4I7G RELATED DB: PDB
DBREF 4ICL A 1 555 UNP P03366 POL_HV1B1 600 1154
DBREF 4ICL B 1 428 UNP P03366 POL_HV1B1 600 1027
SEQADV 4ICL MET A -1 UNP P03366 EXPRESSION TAG
SEQADV 4ICL VAL A 0 UNP P03366 EXPRESSION TAG
SEQADV 4ICL ALA A 172 UNP P03366 LYS 771 ENGINEERED MUTATION
SEQADV 4ICL ALA A 173 UNP P03366 LYS 772 ENGINEERED MUTATION
SEQADV 4ICL SER A 280 UNP P03366 CYS 879 ENGINEERED MUTATION
SEQADV 4ICL GLY B 0 UNP P03366 EXPRESSION TAG
SEQADV 4ICL SER B 280 UNP P03366 CYS 879 ENGINEERED MUTATION
SEQRES 1 A 557 MET VAL PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS
SEQRES 2 A 557 LEU LYS PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP
SEQRES 3 A 557 PRO LEU THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE
SEQRES 4 A 557 CYS THR GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE
SEQRES 5 A 557 GLY PRO GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE
SEQRES 6 A 557 LYS LYS LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP
SEQRES 7 A 557 PHE ARG GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU
SEQRES 8 A 557 VAL GLN LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS
SEQRES 9 A 557 LYS LYS SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR
SEQRES 10 A 557 PHE SER VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR
SEQRES 11 A 557 ALA PHE THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY
SEQRES 12 A 557 ILE ARG TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS
SEQRES 13 A 557 GLY SER PRO ALA ILE PHE GLN SER SER MET THR LYS ILE
SEQRES 14 A 557 LEU GLU PRO PHE ALA ALA GLN ASN PRO ASP ILE VAL ILE
SEQRES 15 A 557 TYR GLN TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU
SEQRES 16 A 557 GLU ILE GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG
SEQRES 17 A 557 GLN HIS LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS
SEQRES 18 A 557 LYS HIS GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR
SEQRES 19 A 557 GLU LEU HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL
SEQRES 20 A 557 LEU PRO GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN
SEQRES 21 A 557 LYS LEU VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR
SEQRES 22 A 557 PRO GLY ILE LYS VAL ARG GLN LEU SER LYS LEU LEU ARG
SEQRES 23 A 557 GLY THR LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU
SEQRES 24 A 557 GLU ALA GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU
SEQRES 25 A 557 LYS GLU PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS
SEQRES 26 A 557 ASP LEU ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN
SEQRES 27 A 557 TRP THR TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU
SEQRES 28 A 557 LYS THR GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR
SEQRES 29 A 557 ASN ASP VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE
SEQRES 30 A 557 THR THR GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS
SEQRES 31 A 557 PHE LYS LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP
SEQRES 32 A 557 TRP THR GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP
SEQRES 33 A 557 GLU PHE VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR
SEQRES 34 A 557 GLN LEU GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE
SEQRES 35 A 557 TYR VAL ASP GLY ALA ALA ASN ARG GLU THR LYS LEU GLY
SEQRES 36 A 557 LYS ALA GLY TYR VAL THR ASN LYS GLY ARG GLN LYS VAL
SEQRES 37 A 557 VAL PRO LEU THR ASN THR THR ASN GLN LYS THR GLU LEU
SEQRES 38 A 557 GLN ALA ILE TYR LEU ALA LEU GLN ASP SER GLY LEU GLU
SEQRES 39 A 557 VAL ASN ILE VAL THR ASP SER GLN TYR ALA LEU GLY ILE
SEQRES 40 A 557 ILE GLN ALA GLN PRO ASP LYS SER GLU SER GLU LEU VAL
SEQRES 41 A 557 ASN GLN ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS VAL
SEQRES 42 A 557 TYR LEU ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY GLY
SEQRES 43 A 557 ASN GLU GLN VAL ASP LYS LEU VAL SER ALA GLY
SEQRES 1 B 429 GLY PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU
SEQRES 2 B 429 LYS PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO
SEQRES 3 B 429 LEU THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS
SEQRES 4 B 429 THR GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY
SEQRES 5 B 429 PRO GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS
SEQRES 6 B 429 LYS LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE
SEQRES 7 B 429 ARG GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL
SEQRES 8 B 429 GLN LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS
SEQRES 9 B 429 LYS SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE
SEQRES 10 B 429 SER VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA
SEQRES 11 B 429 PHE THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE
SEQRES 12 B 429 ARG TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY
SEQRES 13 B 429 SER PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU
SEQRES 14 B 429 GLU PRO PHE LYS LYS GLN ASN PRO ASP ILE VAL ILE TYR
SEQRES 15 B 429 GLN TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU
SEQRES 16 B 429 ILE GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN
SEQRES 17 B 429 HIS LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS
SEQRES 18 B 429 HIS GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU
SEQRES 19 B 429 LEU HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU
SEQRES 20 B 429 PRO GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS
SEQRES 21 B 429 LEU VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO
SEQRES 22 B 429 GLY ILE LYS VAL ARG GLN LEU SER LYS LEU LEU ARG GLY
SEQRES 23 B 429 THR LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU
SEQRES 24 B 429 ALA GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS
SEQRES 25 B 429 GLU PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP
SEQRES 26 B 429 LEU ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP
SEQRES 27 B 429 THR TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS
SEQRES 28 B 429 THR GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN
SEQRES 29 B 429 ASP VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR
SEQRES 30 B 429 THR GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE
SEQRES 31 B 429 LYS LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP
SEQRES 32 B 429 THR GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU
SEQRES 33 B 429 PHE VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN
HET T27 A 601 46
HET MG A 602 1
HET DMS A 603 4
HET DMS A 604 4
HET DMS A 605 4
HET DMS A 606 4
HET 14N A 607 16
HET DMS B 501 4
HET DMS B 502 4
HET DMS B 503 4
HET DMS B 504 4
HET DMS B 505 4
HET DMS B 506 4
HET DMS B 507 4
HETNAM T27 4-{[4-({4-[(E)-2-CYANOETHENYL]-2,6-
HETNAM 2 T27 DIMETHYLPHENYL}AMINO)PYRIMIDIN-2-YL]AMINO}BENZONITRILE
HETNAM MG MAGNESIUM ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM 14N 4-(4-METHYLPIPERAZIN-1-YL)BENZOIC ACID
HETSYN T27 RILPIVIRINE
FORMUL 3 T27 C22 H18 N6
FORMUL 4 MG MG 2+
FORMUL 5 DMS 11(C2 H6 O S)
FORMUL 9 14N C12 H16 N2 O2
FORMUL 17 HOH *689(H2 O)
HELIX 1 1 THR A 27 GLU A 44 1 18
HELIX 2 2 PHE A 77 THR A 84 1 8
HELIX 3 3 GLU A 89 GLY A 93 5 5
HELIX 4 4 HIS A 96 LEU A 100 5 5
HELIX 5 5 ASP A 113 VAL A 118 5 6
HELIX 6 6 PHE A 124 ALA A 129 5 6
HELIX 7 7 SER A 134 GLU A 138 5 5
HELIX 8 8 GLY A 155 ASN A 175 1 21
HELIX 9 9 GLU A 194 LEU A 210 1 17
HELIX 10 10 ARG A 211 GLY A 213 5 3
HELIX 11 11 THR A 253 SER A 268 1 16
HELIX 12 12 VAL A 276 LYS A 281 1 6
HELIX 13 13 LEU A 282 ARG A 284 5 3
HELIX 14 14 THR A 296 LEU A 310 1 15
HELIX 15 15 ASN A 363 GLY A 384 1 22
HELIX 16 16 GLN A 394 TYR A 405 1 12
HELIX 17 17 THR A 473 SER A 489 1 17
HELIX 18 18 SER A 499 ALA A 508 1 10
HELIX 19 19 SER A 515 LYS A 528 1 14
HELIX 20 20 GLY A 544 SER A 553 1 10
HELIX 21 21 THR B 27 GLU B 44 1 18
HELIX 22 22 PHE B 77 THR B 84 1 8
HELIX 23 23 GLY B 99 LYS B 103 5 5
HELIX 24 24 GLY B 112 VAL B 118 5 7
HELIX 25 25 PHE B 124 ALA B 129 5 6
HELIX 26 26 SER B 134 GLU B 138 5 5
HELIX 27 27 LYS B 154 ASN B 175 1 22
HELIX 28 28 GLU B 194 LEU B 214 1 21
HELIX 29 29 HIS B 235 TRP B 239 5 5
HELIX 30 30 VAL B 254 SER B 268 1 15
HELIX 31 31 VAL B 276 LEU B 282 1 7
HELIX 32 32 THR B 296 LEU B 310 1 15
HELIX 33 33 ASN B 363 GLY B 384 1 22
HELIX 34 34 GLN B 394 TRP B 402 1 9
HELIX 35 35 THR B 403 TYR B 405 5 3
HELIX 36 36 VAL B 423 GLN B 428 1 6
SHEET 1 A 3 ILE A 47 LYS A 49 0
SHEET 2 A 3 ILE A 142 TYR A 146 -1 O GLN A 145 N SER A 48
SHEET 3 A 3 PHE A 130 ILE A 132 -1 N ILE A 132 O ILE A 142
SHEET 1 B 2 VAL A 60 LYS A 64 0
SHEET 2 B 2 TRP A 71 VAL A 75 -1 O ARG A 72 N ILE A 63
SHEET 1 C 3 SER A 105 ASP A 110 0
SHEET 2 C 3 ASP A 186 SER A 191 -1 O LEU A 187 N LEU A 109
SHEET 3 C 3 ILE A 178 TYR A 183 -1 N TYR A 181 O TYR A 188
SHEET 1 D 3 PHE A 227 TRP A 229 0
SHEET 2 D 3 TYR A 232 LEU A 234 -1 O LEU A 234 N PHE A 227
SHEET 3 D 3 TRP A 239 VAL A 241 -1 O THR A 240 N GLU A 233
SHEET 1 E 5 LYS A 347 ALA A 355 0
SHEET 2 E 5 GLN A 336 GLU A 344 -1 N ILE A 341 O LYS A 350
SHEET 3 E 5 ILE A 326 GLY A 333 -1 N ILE A 326 O TYR A 342
SHEET 4 E 5 LYS A 388 LEU A 391 1 O LYS A 388 N ALA A 327
SHEET 5 E 5 TRP A 414 PHE A 416 1 O GLU A 415 N PHE A 389
SHEET 1 F 2 HIS A 361 THR A 362 0
SHEET 2 F 2 LYS A 512 SER A 513 -1 O LYS A 512 N THR A 362
SHEET 1 G 5 GLN A 464 LEU A 469 0
SHEET 2 G 5 GLY A 453 THR A 459 -1 N ALA A 455 O VAL A 467
SHEET 3 G 5 THR A 439 ALA A 446 -1 N TYR A 441 O VAL A 458
SHEET 4 G 5 GLU A 492 THR A 497 1 O VAL A 496 N PHE A 440
SHEET 5 G 5 LYS A 530 TRP A 535 1 O ALA A 534 N ILE A 495
SHEET 1 H 3 ILE B 47 LYS B 49 0
SHEET 2 H 3 ILE B 142 TYR B 146 -1 O GLN B 145 N SER B 48
SHEET 3 H 3 PHE B 130 ILE B 132 -1 N ILE B 132 O ILE B 142
SHEET 1 I 2 VAL B 60 ILE B 63 0
SHEET 2 I 2 ARG B 72 VAL B 75 -1 O ARG B 72 N ILE B 63
SHEET 1 J 4 VAL B 179 TYR B 183 0
SHEET 2 J 4 ASP B 186 SER B 191 -1 O TYR B 188 N TYR B 181
SHEET 3 J 4 SER B 105 ASP B 110 -1 N LEU B 109 O LEU B 187
SHEET 4 J 4 TYR B 232 LEU B 234 -1 O LEU B 234 N VAL B 106
SHEET 1 K 2 TRP B 252 THR B 253 0
SHEET 2 K 2 VAL B 292 ILE B 293 -1 O ILE B 293 N TRP B 252
SHEET 1 L 5 ASN B 348 TYR B 354 0
SHEET 2 L 5 GLN B 336 TYR B 342 -1 N ILE B 341 O LYS B 350
SHEET 3 L 5 ILE B 326 GLY B 333 -1 N GLN B 330 O THR B 338
SHEET 4 L 5 LYS B 388 LEU B 391 1 O LYS B 390 N ALA B 327
SHEET 5 L 5 GLU B 413 PHE B 416 1 O GLU B 415 N LEU B 391
LINK OD2 ASP A 443 MG MG A 602 1555 1555 2.34
LINK OD2 ASP A 498 MG MG A 602 1555 1555 2.98
LINK OD1 ASP A 549 MG MG A 602 1555 1555 2.35
CISPEP 1 PRO A 225 PRO A 226 0 0.31
CISPEP 2 PRO A 420 PRO A 421 0 2.38
SITE 1 AC1 14 LEU A 100 LYS A 101 LYS A 103 TYR A 181
SITE 2 AC1 14 TYR A 188 PHE A 227 TRP A 229 LEU A 234
SITE 3 AC1 14 HIS A 235 PRO A 236 TYR A 318 HOH A 857
SITE 4 AC1 14 GLU B 138 HOH B 719
SITE 1 AC2 3 ASP A 443 ASP A 498 ASP A 549
SITE 1 AC3 7 ASN A 363 TRP A 401 LEU A 425 TRP A 426
SITE 2 AC3 7 TYR A 427 GLN A 509 HOH A 885
SITE 1 AC4 7 TRP A 426 TYR A 427 GLN A 428 LEU A 525
SITE 2 AC4 7 ILE A 526 LYS A 528 GLU A 529
SITE 1 AC5 4 LYS A 331 GLY A 333 GLN A 334 LYS A 512
SITE 1 AC6 3 THR A 473 ASN A 474 GLN A 475
SITE 1 AC7 11 MET A 41 LYS A 73 GLY A 112 TYR A 115
SITE 2 AC7 11 TYR A 146 LEU A 149 PRO A 150 GLN A 151
SITE 3 AC7 11 ASP A 185 HOH A1032 HOH A1058
SITE 1 AC8 4 THR B 27 THR B 400 TRP B 401 GLU B 404
SITE 1 AC9 5 GLN A 85 PRO B 55 TYR B 56 LYS B 126
SITE 2 AC9 5 HOH B 642
SITE 1 BC1 8 ILE A 380 VAL A 381 PRO B 25 LEU B 26
SITE 2 BC1 8 PRO B 133 SER B 134 ILE B 135 ASN B 136
SITE 1 BC2 2 HIS B 235 TRP B 239
SITE 1 BC3 6 TRP B 24 GLU B 399 TRP B 402 HOH B 619
SITE 2 BC3 6 HOH B 687 HOH B 697
SITE 1 BC4 4 GLU A 138 LEU B 422 TRP B 426 HOH B 773
SITE 1 BC5 7 PRO B 243 ILE B 244 VAL B 245 LYS B 263
SITE 2 BC5 7 TRP B 426 TYR B 427 GLN B 428
CRYST1 163.053 72.648 109.480 90.00 100.85 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 0.006133 0.000000 0.001176 0.00000
SCALE2 0.000000 0.013765 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009300 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
