HEADER HYDROLASE/HYDROLASE INHIBITOR 08-OCT-11 3U4H
TITLE CD38 STRUCTURE-BASED INHIBITOR DESIGN USING THE N1-CYCLIC INOSINE 5'-
TITLE 2 DIPHOSPHATE RIBOSE TEMPLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADP-RIBOSYL CYCLASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN, ENZYMATIC DOMAIN;
COMPND 5 SYNONYM: CYCLIC ADP-RIBOSE HYDROLASE 1, CADPR HYDROLASE 1, T10;
COMPND 6 EC: 3.2.2.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CD38;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS NON-HYDROLYZABLE INHIBITOR, TWO DOMAINS, CADPR CYCLIZATION,
KEYWDS 2 HYDROLYSIS, 8-AMINO-N1-CIDPR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.LIU,Q.HAO,H.C.LEE,R.GRAEFF
REVDAT 3 01-NOV-23 3U4H 1 REMARK SEQADV
REVDAT 2 24-JUL-13 3U4H 1 JRNL
REVDAT 1 10-OCT-12 3U4H 0
JRNL AUTH C.MOREAU,Q.LIU,R.GRAEFF,G.K.WAGNER,M.P.THOMAS,J.M.SWARBRICK,
JRNL AUTH 2 S.SHUTO,H.C.LEE,Q.HAO,B.V.L.POTTER
JRNL TITL CD38 STRUCTURE-BASED INHIBITOR DESIGN USING THE N1-CYCLIC
JRNL TITL 2 INOSINE 5'-DIPHOSPHATE RIBOSE TEMPLATE
JRNL REF PLOS ONE V. 8 66247 2013
JRNL REFN ESSN 1932-6203
JRNL PMID 23840430
JRNL DOI 10.1371/JOURNAL.PONE.0066247
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
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) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.1
REMARK 3 NUMBER OF REFLECTIONS : 38873
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1948
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 25.2479 - 4.5174 0.99 2944 149 0.1797 0.2303
REMARK 3 2 4.5174 - 3.5889 0.99 2939 157 0.1551 0.1972
REMARK 3 3 3.5889 - 3.1362 0.99 2914 168 0.1742 0.2071
REMARK 3 4 3.1362 - 2.8499 0.99 2913 151 0.1845 0.2629
REMARK 3 5 2.8499 - 2.6459 0.98 2939 144 0.1880 0.2762
REMARK 3 6 2.6459 - 2.4900 0.98 2877 157 0.1817 0.2115
REMARK 3 7 2.4900 - 2.3654 0.98 2902 173 0.1879 0.2603
REMARK 3 8 2.3654 - 2.2625 0.97 2864 133 0.1926 0.2515
REMARK 3 9 2.2625 - 2.1755 0.94 2780 153 0.1940 0.2492
REMARK 3 10 2.1755 - 2.1004 0.90 2684 133 0.1984 0.2618
REMARK 3 11 2.1004 - 2.0348 0.83 2461 132 0.2143 0.2716
REMARK 3 12 2.0348 - 1.9766 0.77 2259 115 0.2128 0.3083
REMARK 3 13 1.9766 - 1.9246 0.69 2058 100 0.2244 0.2748
REMARK 3 14 1.9246 - 1.8777 0.47 1391 83 0.2478 0.3575
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 : 0.40
REMARK 3 B_SOL : 60.10
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.400
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.98430
REMARK 3 B22 (A**2) : -0.76230
REMARK 3 B33 (A**2) : 10.74670
REMARK 3 B12 (A**2) : -0.27570
REMARK 3 B13 (A**2) : 1.57100
REMARK 3 B23 (A**2) : -7.14100
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 4223
REMARK 3 ANGLE : 1.125 5724
REMARK 3 CHIRALITY : 0.072 618
REMARK 3 PLANARITY : 0.004 726
REMARK 3 DIHEDRAL : 20.902 1564
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 48:117)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1939 -13.5476 4.3522
REMARK 3 T TENSOR
REMARK 3 T11: 0.1388 T22: 0.0707
REMARK 3 T33: 0.3978 T12: -0.0085
REMARK 3 T13: -0.0611 T23: 0.0509
REMARK 3 L TENSOR
REMARK 3 L11: 2.5945 L22: 1.4410
REMARK 3 L33: 0.8500 L12: 0.7236
REMARK 3 L13: 0.3481 L23: 0.4175
REMARK 3 S TENSOR
REMARK 3 S11: 0.2309 S12: -0.0378 S13: -0.9546
REMARK 3 S21: 0.0772 S22: -0.0333 S23: -0.2245
REMARK 3 S31: 0.1329 S32: 0.0081 S33: -0.1118
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 118:146)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0493 3.1432 -3.4854
REMARK 3 T TENSOR
REMARK 3 T11: 0.1748 T22: 0.0783
REMARK 3 T33: 0.1082 T12: 0.0321
REMARK 3 T13: 0.0142 T23: 0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 0.6864 L22: 1.6785
REMARK 3 L33: 0.2209 L12: 0.6953
REMARK 3 L13: -0.0048 L23: 0.4138
REMARK 3 S TENSOR
REMARK 3 S11: 0.0728 S12: 0.0332 S13: -0.2455
REMARK 3 S21: -0.1176 S22: 0.0040 S23: -0.2709
REMARK 3 S31: 0.0969 S32: -0.0094 S33: -0.0636
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 147:193)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1828 -9.6914 -0.2796
REMARK 3 T TENSOR
REMARK 3 T11: 0.1383 T22: 0.0692
REMARK 3 T33: 0.3265 T12: -0.0010
REMARK 3 T13: -0.0410 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 2.3966 L22: 0.7412
REMARK 3 L33: 0.4251 L12: -0.6807
REMARK 3 L13: 0.0245 L23: 0.3367
REMARK 3 S TENSOR
REMARK 3 S11: 0.2182 S12: 0.0593 S13: -0.8379
REMARK 3 S21: -0.0069 S22: -0.1258 S23: 0.2179
REMARK 3 S31: 0.0232 S32: -0.0695 S33: -0.0626
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 194:244)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7300 10.6547 1.0198
REMARK 3 T TENSOR
REMARK 3 T11: 0.1260 T22: 0.1168
REMARK 3 T33: 0.1060 T12: 0.0036
REMARK 3 T13: -0.0035 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 1.3225 L22: 1.2206
REMARK 3 L33: 0.6207 L12: -0.0343
REMARK 3 L13: -0.2062 L23: 0.6913
REMARK 3 S TENSOR
REMARK 3 S11: 0.0613 S12: 0.0754 S13: 0.0880
REMARK 3 S21: -0.0745 S22: -0.1498 S23: 0.1442
REMARK 3 S31: 0.0346 S32: -0.1205 S33: 0.0930
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 250:275)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.5756 20.6396 -2.0826
REMARK 3 T TENSOR
REMARK 3 T11: 0.1914 T22: -0.0072
REMARK 3 T33: 0.1585 T12: 0.1674
REMARK 3 T13: -0.0592 T23: 0.1798
REMARK 3 L TENSOR
REMARK 3 L11: 1.0062 L22: 0.3744
REMARK 3 L33: 0.5041 L12: 0.5113
REMARK 3 L13: 0.2588 L23: -0.0406
REMARK 3 S TENSOR
REMARK 3 S11: 0.2926 S12: -0.3739 S13: 1.0508
REMARK 3 S21: 0.1117 S22: -0.1950 S23: 0.2839
REMARK 3 S31: -0.3879 S32: -0.4269 S33: -0.0476
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 276:296)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2651 11.6160 -14.6477
REMARK 3 T TENSOR
REMARK 3 T11: 0.3911 T22: 0.4312
REMARK 3 T33: 0.1991 T12: 0.0193
REMARK 3 T13: 0.1550 T23: 0.1110
REMARK 3 L TENSOR
REMARK 3 L11: 1.8399 L22: 0.9339
REMARK 3 L33: 0.6278 L12: -0.5965
REMARK 3 L13: 0.1206 L23: 0.6139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0370 S12: 0.8156 S13: 0.1341
REMARK 3 S21: -0.4676 S22: -0.0687 S23: -0.4828
REMARK 3 S31: -0.0122 S32: 0.3251 S33: -0.0293
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 48:117)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9410 22.7733 22.0216
REMARK 3 T TENSOR
REMARK 3 T11: 0.1736 T22: 0.4078
REMARK 3 T33: 0.4407 T12: -0.1405
REMARK 3 T13: 0.1382 T23: -0.3234
REMARK 3 L TENSOR
REMARK 3 L11: 2.0166 L22: 0.8252
REMARK 3 L33: 2.4418 L12: -0.1896
REMARK 3 L13: -1.5552 L23: -0.1812
REMARK 3 S TENSOR
REMARK 3 S11: 0.3950 S12: -0.7928 S13: 0.9264
REMARK 3 S21: 0.0752 S22: -0.0796 S23: 0.2466
REMARK 3 S31: -0.3139 S32: 0.4695 S33: -0.3313
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 118:146)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7825 9.0026 37.8183
REMARK 3 T TENSOR
REMARK 3 T11: 0.3928 T22: 1.1123
REMARK 3 T33: 0.0467 T12: -0.1125
REMARK 3 T13: 0.0284 T23: -0.3045
REMARK 3 L TENSOR
REMARK 3 L11: 2.0992 L22: 0.4762
REMARK 3 L33: 0.5124 L12: 0.5745
REMARK 3 L13: -0.7132 L23: -0.4862
REMARK 3 S TENSOR
REMARK 3 S11: 0.5643 S12: -0.7645 S13: 0.0767
REMARK 3 S21: 0.5826 S22: -0.2054 S23: 0.1573
REMARK 3 S31: 0.0273 S32: 1.6548 S33: -0.2910
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 147:193)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.2750 14.4552 16.5636
REMARK 3 T TENSOR
REMARK 3 T11: 0.1205 T22: 0.2626
REMARK 3 T33: 0.2062 T12: -0.0054
REMARK 3 T13: 0.0198 T23: -0.1016
REMARK 3 L TENSOR
REMARK 3 L11: 3.8521 L22: 0.5953
REMARK 3 L33: 1.0433 L12: 1.0369
REMARK 3 L13: -1.1628 L23: 0.0570
REMARK 3 S TENSOR
REMARK 3 S11: 0.3100 S12: -0.7608 S13: 0.4681
REMARK 3 S21: -0.0074 S22: -0.0613 S23: 0.1108
REMARK 3 S31: 0.0138 S32: 0.3368 S33: -0.1941
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 194:275)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.6586 -1.0259 36.3922
REMARK 3 T TENSOR
REMARK 3 T11: 0.3470 T22: 1.3207
REMARK 3 T33: 0.1023 T12: 0.0097
REMARK 3 T13: -0.0478 T23: -0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 1.5800 L22: 1.6254
REMARK 3 L33: 0.4883 L12: 0.8261
REMARK 3 L13: -0.5274 L23: -0.7592
REMARK 3 S TENSOR
REMARK 3 S11: 0.2449 S12: -0.8662 S13: -0.1004
REMARK 3 S21: 0.0942 S22: -0.6543 S23: -0.2959
REMARK 3 S31: 0.1509 S32: 1.1323 S33: 0.2088
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 276:296)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.5556 -1.7374 46.5876
REMARK 3 T TENSOR
REMARK 3 T11: 0.4472 T22: 0.9713
REMARK 3 T33: 0.2748 T12: 0.0517
REMARK 3 T13: 0.1104 T23: -0.2392
REMARK 3 L TENSOR
REMARK 3 L11: 0.5808 L22: 0.0465
REMARK 3 L33: 3.1960 L12: -0.0394
REMARK 3 L13: -0.7246 L23: -0.2889
REMARK 3 S TENSOR
REMARK 3 S11: -0.1467 S12: 0.6775 S13: -0.1469
REMARK 3 S21: 0.0594 S22: -0.0429 S23: 0.3879
REMARK 3 S31: -0.1799 S32: 0.9451 S33: 0.0639
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 3U4H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068294.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9778
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38912
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870
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 (%) : 90.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2PGJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, 12% PEG 4000, PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 LYS A 39
REMARK 465 ARG A 40
REMARK 465 GLU A 41
REMARK 465 ALA A 42
REMARK 465 GLU A 43
REMARK 465 ALA A 44
REMARK 465 ARG A 45
REMARK 465 TRP A 46
REMARK 465 ARG A 47
REMARK 465 GLY A 246
REMARK 465 ARG A 247
REMARK 465 GLU A 248
REMARK 465 ASP A 249
REMARK 465 THR A 297
REMARK 465 SER A 298
REMARK 465 GLU A 299
REMARK 465 ILE A 300
REMARK 465 LYS B 39
REMARK 465 ARG B 40
REMARK 465 GLU B 41
REMARK 465 ALA B 42
REMARK 465 GLU B 43
REMARK 465 ALA B 44
REMARK 465 THR B 297
REMARK 465 SER B 298
REMARK 465 GLU B 299
REMARK 465 ILE B 300
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 ILE A 128 43.22 -152.17
REMARK 500 GLN A 139 18.08 -152.76
REMARK 500 ASP A 179 -69.68 -103.39
REMARK 500 ASN A 182 47.32 -91.31
REMARK 500 ASP A 202 -124.51 59.29
REMARK 500 ASN A 270 41.47 77.35
REMARK 500 ASN A 290 71.25 -113.28
REMARK 500 GLU A 292 23.38 44.03
REMARK 500 SER A 294 -162.29 -113.22
REMARK 500 PRO B 118 104.72 -47.30
REMARK 500 ILE B 128 41.48 -147.52
REMARK 500 CYS B 180 140.80 -170.65
REMARK 500 ASN B 182 58.21 -94.63
REMARK 500 ASP B 202 -116.81 60.36
REMARK 500 VAL B 225 -58.08 -125.39
REMARK 500 GLU B 248 108.62 -43.27
REMARK 500 GLU B 292 40.97 37.82
REMARK 500 ASP B 293 -79.23 -118.61
REMARK 500 SER B 295 74.63 38.42
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 C8R A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8R B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3U4I RELATED DB: PDB
DBREF 3U4H A 45 300 UNP P28907 CD38_HUMAN 45 300
DBREF 3U4H B 45 300 UNP P28907 CD38_HUMAN 45 300
SEQADV 3U4H LYS A 39 UNP P28907 EXPRESSION TAG
SEQADV 3U4H ARG A 40 UNP P28907 EXPRESSION TAG
SEQADV 3U4H GLU A 41 UNP P28907 EXPRESSION TAG
SEQADV 3U4H ALA A 42 UNP P28907 EXPRESSION TAG
SEQADV 3U4H GLU A 43 UNP P28907 EXPRESSION TAG
SEQADV 3U4H ALA A 44 UNP P28907 EXPRESSION TAG
SEQADV 3U4H THR A 49 UNP P28907 GLN 49 ENGINEERED MUTATION
SEQADV 3U4H ASP A 100 UNP P28907 ASN 100 ENGINEERED MUTATION
SEQADV 3U4H ASP A 164 UNP P28907 ASN 164 ENGINEERED MUTATION
SEQADV 3U4H ASP A 209 UNP P28907 ASN 209 ENGINEERED MUTATION
SEQADV 3U4H ASP A 219 UNP P28907 ASN 219 ENGINEERED MUTATION
SEQADV 3U4H LYS B 39 UNP P28907 EXPRESSION TAG
SEQADV 3U4H ARG B 40 UNP P28907 EXPRESSION TAG
SEQADV 3U4H GLU B 41 UNP P28907 EXPRESSION TAG
SEQADV 3U4H ALA B 42 UNP P28907 EXPRESSION TAG
SEQADV 3U4H GLU B 43 UNP P28907 EXPRESSION TAG
SEQADV 3U4H ALA B 44 UNP P28907 EXPRESSION TAG
SEQADV 3U4H THR B 49 UNP P28907 GLN 49 ENGINEERED MUTATION
SEQADV 3U4H ASP B 100 UNP P28907 ASN 100 ENGINEERED MUTATION
SEQADV 3U4H ASP B 164 UNP P28907 ASN 164 ENGINEERED MUTATION
SEQADV 3U4H ASP B 209 UNP P28907 ASN 209 ENGINEERED MUTATION
SEQADV 3U4H ASP B 219 UNP P28907 ASN 219 ENGINEERED MUTATION
SEQRES 1 A 262 LYS ARG GLU ALA GLU ALA ARG TRP ARG GLN THR TRP SER
SEQRES 2 A 262 GLY PRO GLY THR THR LYS ARG PHE PRO GLU THR VAL LEU
SEQRES 3 A 262 ALA ARG CYS VAL LYS TYR THR GLU ILE HIS PRO GLU MET
SEQRES 4 A 262 ARG HIS VAL ASP CYS GLN SER VAL TRP ASP ALA PHE LYS
SEQRES 5 A 262 GLY ALA PHE ILE SER LYS HIS PRO CYS ASP ILE THR GLU
SEQRES 6 A 262 GLU ASP TYR GLN PRO LEU MET LYS LEU GLY THR GLN THR
SEQRES 7 A 262 VAL PRO CYS ASN LYS ILE LEU LEU TRP SER ARG ILE LYS
SEQRES 8 A 262 ASP LEU ALA HIS GLN PHE THR GLN VAL GLN ARG ASP MET
SEQRES 9 A 262 PHE THR LEU GLU ASP THR LEU LEU GLY TYR LEU ALA ASP
SEQRES 10 A 262 ASP LEU THR TRP CYS GLY GLU PHE ASP THR SER LYS ILE
SEQRES 11 A 262 ASN TYR GLN SER CYS PRO ASP TRP ARG LYS ASP CYS SER
SEQRES 12 A 262 ASN ASN PRO VAL SER VAL PHE TRP LYS THR VAL SER ARG
SEQRES 13 A 262 ARG PHE ALA GLU ALA ALA CYS ASP VAL VAL HIS VAL MET
SEQRES 14 A 262 LEU ASP GLY SER ARG SER LYS ILE PHE ASP LYS ASP SER
SEQRES 15 A 262 THR PHE GLY SER VAL GLU VAL HIS ASN LEU GLN PRO GLU
SEQRES 16 A 262 LYS VAL GLN THR LEU GLU ALA TRP VAL ILE HIS GLY GLY
SEQRES 17 A 262 ARG GLU ASP SER ARG ASP LEU CYS GLN ASP PRO THR ILE
SEQRES 18 A 262 LYS GLU LEU GLU SER ILE ILE SER LYS ARG ASN ILE GLN
SEQRES 19 A 262 PHE SER CYS LYS ASN ILE TYR ARG PRO ASP LYS PHE LEU
SEQRES 20 A 262 GLN CYS VAL LYS ASN PRO GLU ASP SER SER CYS THR SER
SEQRES 21 A 262 GLU ILE
SEQRES 1 B 262 LYS ARG GLU ALA GLU ALA ARG TRP ARG GLN THR TRP SER
SEQRES 2 B 262 GLY PRO GLY THR THR LYS ARG PHE PRO GLU THR VAL LEU
SEQRES 3 B 262 ALA ARG CYS VAL LYS TYR THR GLU ILE HIS PRO GLU MET
SEQRES 4 B 262 ARG HIS VAL ASP CYS GLN SER VAL TRP ASP ALA PHE LYS
SEQRES 5 B 262 GLY ALA PHE ILE SER LYS HIS PRO CYS ASP ILE THR GLU
SEQRES 6 B 262 GLU ASP TYR GLN PRO LEU MET LYS LEU GLY THR GLN THR
SEQRES 7 B 262 VAL PRO CYS ASN LYS ILE LEU LEU TRP SER ARG ILE LYS
SEQRES 8 B 262 ASP LEU ALA HIS GLN PHE THR GLN VAL GLN ARG ASP MET
SEQRES 9 B 262 PHE THR LEU GLU ASP THR LEU LEU GLY TYR LEU ALA ASP
SEQRES 10 B 262 ASP LEU THR TRP CYS GLY GLU PHE ASP THR SER LYS ILE
SEQRES 11 B 262 ASN TYR GLN SER CYS PRO ASP TRP ARG LYS ASP CYS SER
SEQRES 12 B 262 ASN ASN PRO VAL SER VAL PHE TRP LYS THR VAL SER ARG
SEQRES 13 B 262 ARG PHE ALA GLU ALA ALA CYS ASP VAL VAL HIS VAL MET
SEQRES 14 B 262 LEU ASP GLY SER ARG SER LYS ILE PHE ASP LYS ASP SER
SEQRES 15 B 262 THR PHE GLY SER VAL GLU VAL HIS ASN LEU GLN PRO GLU
SEQRES 16 B 262 LYS VAL GLN THR LEU GLU ALA TRP VAL ILE HIS GLY GLY
SEQRES 17 B 262 ARG GLU ASP SER ARG ASP LEU CYS GLN ASP PRO THR ILE
SEQRES 18 B 262 LYS GLU LEU GLU SER ILE ILE SER LYS ARG ASN ILE GLN
SEQRES 19 B 262 PHE SER CYS LYS ASN ILE TYR ARG PRO ASP LYS PHE LEU
SEQRES 20 B 262 GLN CYS VAL LYS ASN PRO GLU ASP SER SER CYS THR SER
SEQRES 21 B 262 GLU ILE
HET C8R A 401 36
HET C8R B 401 36
HETNAM C8R 8-AMINO-N1-CYCLIC INOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 C8R 2(C15 H21 N5 O14 P2)
FORMUL 5 HOH *251(H2 O)
HELIX 1 1 ARG A 58 HIS A 74 1 17
HELIX 2 2 PRO A 75 ARG A 78 5 4
HELIX 3 3 ASP A 81 ALA A 92 1 12
HELIX 4 4 GLU A 103 ASP A 105 5 3
HELIX 5 5 TYR A 106 GLY A 113 1 8
HELIX 6 6 PRO A 118 LYS A 121 5 4
HELIX 7 7 ILE A 128 VAL A 138 1 11
HELIX 8 8 THR A 144 ASP A 147 5 4
HELIX 9 9 THR A 148 ASP A 155 1 8
HELIX 10 10 ASN A 183 ALA A 200 1 18
HELIX 11 11 SER A 220 VAL A 225 1 6
HELIX 12 12 ASP A 252 GLN A 255 5 4
HELIX 13 13 ASP A 256 LYS A 268 1 13
HELIX 14 14 ARG A 280 ASN A 290 1 11
HELIX 15 15 ARG B 58 HIS B 74 1 17
HELIX 16 16 PRO B 75 ARG B 78 5 4
HELIX 17 17 ASP B 81 ILE B 94 1 14
HELIX 18 18 THR B 102 ASP B 105 5 4
HELIX 19 19 TYR B 106 GLY B 113 1 8
HELIX 20 20 ILE B 128 GLN B 139 1 12
HELIX 21 21 THR B 144 ASP B 147 5 4
HELIX 22 22 THR B 148 ASP B 155 1 8
HELIX 23 23 ASN B 183 ALA B 200 1 18
HELIX 24 24 SER B 220 VAL B 225 1 6
HELIX 25 25 ASP B 252 GLN B 255 5 4
HELIX 26 26 ASP B 256 LYS B 268 1 13
HELIX 27 27 ARG B 280 ASN B 290 1 11
SHEET 1 A 2 GLY A 52 PRO A 53 0
SHEET 2 A 2 SER A 172 CYS A 173 -1 O CYS A 173 N GLY A 52
SHEET 1 B 4 LEU A 123 SER A 126 0
SHEET 2 B 4 ASP A 202 ASP A 209 1 O HIS A 205 N LEU A 124
SHEET 3 B 4 VAL A 235 ILE A 243 1 O ILE A 243 N LEU A 208
SHEET 4 B 4 GLN A 272 ILE A 278 1 O LYS A 276 N VAL A 242
SHEET 1 C 2 GLY A 161 GLU A 162 0
SHEET 2 C 2 THR A 165 ILE A 168 -1 O THR A 165 N GLU A 162
SHEET 1 D 2 GLY B 52 PRO B 53 0
SHEET 2 D 2 SER B 172 CYS B 173 -1 O CYS B 173 N GLY B 52
SHEET 1 E 4 LEU B 123 SER B 126 0
SHEET 2 E 4 ASP B 202 ASP B 209 1 O HIS B 205 N LEU B 124
SHEET 3 E 4 VAL B 235 ILE B 243 1 O TRP B 241 N VAL B 206
SHEET 4 E 4 GLN B 272 ILE B 278 1 O GLN B 272 N GLN B 236
SSBOND 1 CYS A 67 CYS A 82 1555 1555 2.07
SSBOND 2 CYS A 99 CYS A 180 1555 1555 2.06
SSBOND 3 CYS A 119 CYS A 201 1555 1555 2.06
SSBOND 4 CYS A 160 CYS A 173 1555 1555 2.07
SSBOND 5 CYS A 254 CYS A 275 1555 1555 2.06
SSBOND 6 CYS A 287 CYS A 296 1555 1555 2.02
SSBOND 7 CYS B 67 CYS B 82 1555 1555 2.04
SSBOND 8 CYS B 99 CYS B 180 1555 1555 2.04
SSBOND 9 CYS B 119 CYS B 201 1555 1555 2.03
SSBOND 10 CYS B 160 CYS B 173 1555 1555 2.08
SSBOND 11 CYS B 254 CYS B 275 1555 1555 2.04
SSBOND 12 CYS B 287 CYS B 296 1555 1555 2.03
SITE 1 AC1 22 LEU A 124 TRP A 125 SER A 126 ARG A 127
SITE 2 AC1 22 LEU A 145 GLU A 146 ASP A 155 TRP A 189
SITE 3 AC1 22 SER A 193 SER A 220 THR A 221 PHE A 222
SITE 4 AC1 22 GLU A 226 HOH A 503 HOH A 515 HOH A 519
SITE 5 AC1 22 HOH A 533 HOH A 535 HOH A 541 HOH A 557
SITE 6 AC1 22 HOH A 564 HOH A 603
SITE 1 AC2 18 LEU B 124 TRP B 125 SER B 126 ARG B 127
SITE 2 AC2 18 LEU B 145 GLU B 146 ASP B 155 TRP B 189
SITE 3 AC2 18 SER B 193 SER B 220 THR B 221 PHE B 222
SITE 4 AC2 18 GLU B 226 HOH B 516 HOH B 529 HOH B 533
SITE 5 AC2 18 HOH B 543 HOH B 553
CRYST1 41.713 51.459 67.755 72.85 89.13 83.18 P 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 0.023973 -0.002867 0.000505 0.00000
SCALE2 0.000000 0.019571 -0.006047 0.00000
SCALE3 0.000000 0.000000 0.015449 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
