HEADER HYDROLASE 01-JUL-18 6DXY
TITLE MURINE N-ACYLETHANOLAMINE-HYDROLYZING ACID AMIDASE (NAAA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-ACYLETHANOLAMINE-HYDROLYZING ACID AMIDASE SUBUNIT ALPHA;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: N-ACYLSPHINGOSINE AMIDOHYDROLASE-LIKE,ASAH-LIKE PROTEIN;
COMPND 5 EC: 3.5.1.60;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: N-ACYLETHANOLAMINE-HYDROLYZING ACID AMIDASE SUBUNIT BETA;
COMPND 9 CHAIN: B, D;
COMPND 10 SYNONYM: N-ACYLSPHINGOSINE AMIDOHYDROLASE-LIKE,ASAH-LIKE PROTEIN;
COMPND 11 EC: 3.5.1.60;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: NAAA, ASAHL;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 GENE: NAAA, ASAHL;
SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS ENDOCANNABINOID, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GORELIK,A.GEBAI,K.ILLES,D.PIOMELLI,B.NAGAR
REVDAT 9 15-NOV-23 6DXY 1 REMARK
REVDAT 8 11-OCT-23 6DXY 1 HETSYN
REVDAT 7 29-JUL-20 6DXY 1 COMPND REMARK HETNAM HETSYN
REVDAT 7 2 1 LINK SITE
REVDAT 6 08-JAN-20 6DXY 1 REMARK
REVDAT 5 17-APR-19 6DXY 1 COMPND
REVDAT 4 07-NOV-18 6DXY 1 JRNL
REVDAT 3 24-OCT-18 6DXY 1 COMPND JRNL
REVDAT 2 10-OCT-18 6DXY 1 COMPND JRNL
REVDAT 1 26-SEP-18 6DXY 0
JRNL AUTH A.GORELIK,A.GEBAI,K.ILLES,D.PIOMELLI,B.NAGAR
JRNL TITL MOLECULAR MECHANISM OF ACTIVATION OF THE IMMUNOREGULATORY
JRNL TITL 2 AMIDASE NAAA.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 10032 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 30301806
JRNL DOI 10.1073/PNAS.1811759115
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155)
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) : 40.44
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 61.4
REMARK 3 NUMBER OF REFLECTIONS : 72758
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.890
REMARK 3 FREE R VALUE TEST SET COUNT : 2831
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 40.4506 - 5.0223 0.99 5658 215 0.1826 0.1723
REMARK 3 2 5.0223 - 3.9875 0.97 5521 224 0.1365 0.1622
REMARK 3 3 3.9875 - 3.4838 0.98 5567 225 0.1443 0.1859
REMARK 3 4 3.4838 - 3.1654 0.98 5573 229 0.1522 0.1940
REMARK 3 5 3.1654 - 2.9386 0.99 5616 231 0.1587 0.1892
REMARK 3 6 2.9386 - 2.7654 0.97 5543 227 0.1650 0.1911
REMARK 3 7 2.7654 - 2.6269 0.87 4941 198 0.1708 0.2285
REMARK 3 8 2.6269 - 2.5126 0.70 3945 164 0.1706 0.1729
REMARK 3 9 2.5126 - 2.4158 0.60 3424 135 0.1782 0.1936
REMARK 3 10 2.4158 - 2.3325 0.55 3137 125 0.1712 0.1879
REMARK 3 11 2.3325 - 2.2596 0.52 2939 120 0.1863 0.1986
REMARK 3 12 2.2596 - 2.1950 0.50 2832 115 0.1957 0.2072
REMARK 3 13 2.1950 - 2.1372 0.50 2852 117 0.1952 0.2051
REMARK 3 14 2.1372 - 2.0851 0.50 2805 112 0.2133 0.2316
REMARK 3 15 2.0851 - 2.0377 0.49 2847 116 0.2363 0.2930
REMARK 3 16 2.0377 - 1.9943 0.45 2548 109 0.2383 0.2397
REMARK 3 17 1.9943 - 1.9544 0.31 1806 72 0.2626 0.2921
REMARK 3 18 1.9544 - 1.9175 0.20 1132 45 0.2639 0.2933
REMARK 3 19 1.9175 - 1.8833 0.13 761 35 0.2711 0.3535
REMARK 3 20 1.8833 - 1.8514 0.08 480 17 0.3097 0.3390
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.910
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 : 0.004 5438
REMARK 3 ANGLE : 0.750 7424
REMARK 3 CHIRALITY : 0.047 826
REMARK 3 PLANARITY : 0.004 938
REMARK 3 DIHEDRAL : 10.315 3203
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 34 THROUGH 53 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.3809 160.9561 -22.4467
REMARK 3 T TENSOR
REMARK 3 T11: 0.2746 T22: 0.2007
REMARK 3 T33: 0.1475 T12: 0.0427
REMARK 3 T13: -0.0180 T23: 0.0405
REMARK 3 L TENSOR
REMARK 3 L11: 1.4735 L22: 4.9087
REMARK 3 L33: 1.5537 L12: -0.1018
REMARK 3 L13: 0.5620 L23: -1.1898
REMARK 3 S TENSOR
REMARK 3 S11: -0.0122 S12: 0.3899 S13: 0.3356
REMARK 3 S21: 0.0196 S22: -0.0838 S23: -0.2701
REMARK 3 S31: -0.1708 S32: -0.1012 S33: -0.0293
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 54 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): -54.2497 148.3567 -21.5172
REMARK 3 T TENSOR
REMARK 3 T11: 0.2935 T22: 0.4362
REMARK 3 T33: 0.3385 T12: -0.0958
REMARK 3 T13: -0.0865 T23: 0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 4.8665 L22: 6.2372
REMARK 3 L33: 2.7934 L12: 0.3804
REMARK 3 L13: -1.7687 L23: 0.3032
REMARK 3 S TENSOR
REMARK 3 S11: 0.0976 S12: -0.2096 S13: -0.8305
REMARK 3 S21: -0.1876 S22: -0.1345 S23: 0.4689
REMARK 3 S31: 0.6753 S32: -0.7037 S33: 0.0407
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): -67.4445 153.8569 -7.4348
REMARK 3 T TENSOR
REMARK 3 T11: 0.7907 T22: 1.8660
REMARK 3 T33: 0.7533 T12: -0.2615
REMARK 3 T13: 0.2178 T23: -0.0811
REMARK 3 L TENSOR
REMARK 3 L11: 1.4390 L22: 4.2192
REMARK 3 L33: 2.9910 L12: 1.7797
REMARK 3 L13: -0.4089 L23: -1.2014
REMARK 3 S TENSOR
REMARK 3 S11: 0.4845 S12: -0.1985 S13: 0.3613
REMARK 3 S21: 0.1925 S22: -0.2042 S23: 1.2175
REMARK 3 S31: -0.2864 S32: -2.0098 S33: -0.1987
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 96 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.2199 156.5974 -15.5018
REMARK 3 T TENSOR
REMARK 3 T11: 0.2057 T22: 0.5208
REMARK 3 T33: 0.2329 T12: 0.0324
REMARK 3 T13: 0.0001 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 5.4967 L22: 4.8660
REMARK 3 L33: 4.0451 L12: 1.1170
REMARK 3 L13: 0.4126 L23: 0.4942
REMARK 3 S TENSOR
REMARK 3 S11: 0.0852 S12: -0.3070 S13: 0.2199
REMARK 3 S21: 0.4684 S22: 0.0746 S23: 0.0904
REMARK 3 S31: -0.0927 S32: -0.7752 S33: -0.0669
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 132 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.6869 155.0029 -7.9073
REMARK 3 T TENSOR
REMARK 3 T11: 0.1418 T22: 0.1645
REMARK 3 T33: 0.1552 T12: -0.0035
REMARK 3 T13: -0.0055 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 2.1555 L22: 1.7089
REMARK 3 L33: 3.8758 L12: -0.9331
REMARK 3 L13: 1.4802 L23: 0.3200
REMARK 3 S TENSOR
REMARK 3 S11: 0.0616 S12: -0.1667 S13: -0.0680
REMARK 3 S21: -0.0149 S22: -0.0343 S23: 0.1613
REMARK 3 S31: -0.0050 S32: -0.5312 S33: -0.0392
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 217 THROUGH 360 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.8731 154.2056 -0.3170
REMARK 3 T TENSOR
REMARK 3 T11: 0.1188 T22: 0.0982
REMARK 3 T33: 0.1285 T12: -0.0126
REMARK 3 T13: -0.0384 T23: -0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 2.0568 L22: 2.6763
REMARK 3 L33: 3.4777 L12: -0.4784
REMARK 3 L13: 0.1283 L23: 0.3797
REMARK 3 S TENSOR
REMARK 3 S11: -0.0101 S12: -0.1973 S13: 0.0484
REMARK 3 S21: 0.1668 S22: 0.0559 S23: -0.1004
REMARK 3 S31: -0.0955 S32: -0.1105 S33: 0.0127
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 34 THROUGH 43 )
REMARK 3 ORIGIN FOR THE GROUP (A): -95.6706 153.9183 25.4062
REMARK 3 T TENSOR
REMARK 3 T11: 0.3221 T22: 0.3534
REMARK 3 T33: 0.2772 T12: -0.0102
REMARK 3 T13: 0.0712 T23: -0.0761
REMARK 3 L TENSOR
REMARK 3 L11: 1.4888 L22: 2.0461
REMARK 3 L33: 7.0088 L12: 0.1186
REMARK 3 L13: 2.5132 L23: 1.8191
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: -0.5606 S13: 0.3522
REMARK 3 S21: 0.5914 S22: -0.4343 S23: 0.8569
REMARK 3 S31: 0.0880 S32: -0.6445 S33: 0.2572
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 44 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -80.6833 153.4715 25.4556
REMARK 3 T TENSOR
REMARK 3 T11: 0.3020 T22: 0.3743
REMARK 3 T33: 0.2387 T12: -0.0704
REMARK 3 T13: -0.0276 T23: -0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 5.6925 L22: 4.6060
REMARK 3 L33: 2.5703 L12: -1.9010
REMARK 3 L13: 0.1601 L23: -0.7675
REMARK 3 S TENSOR
REMARK 3 S11: -0.1073 S12: -0.2304 S13: -0.2226
REMARK 3 S21: 0.1233 S22: 0.0476 S23: -0.4205
REMARK 3 S31: -0.0891 S32: 0.3570 S33: 0.1020
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 77 THROUGH 97 )
REMARK 3 ORIGIN FOR THE GROUP (A): -67.3914 153.6103 10.3929
REMARK 3 T TENSOR
REMARK 3 T11: 0.5685 T22: 1.2359
REMARK 3 T33: 0.6825 T12: -0.1013
REMARK 3 T13: -0.0054 T23: -0.0687
REMARK 3 L TENSOR
REMARK 3 L11: 5.0755 L22: 8.1559
REMARK 3 L33: 3.2876 L12: -1.1356
REMARK 3 L13: -0.3971 L23: 2.9942
REMARK 3 S TENSOR
REMARK 3 S11: 0.2780 S12: 0.6919 S13: 0.4673
REMARK 3 S21: 0.4018 S22: -0.0379 S23: -2.0246
REMARK 3 S31: -0.0924 S32: 1.6322 S33: -0.2473
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 98 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): -74.6938 155.2204 18.8613
REMARK 3 T TENSOR
REMARK 3 T11: 0.2016 T22: 0.4323
REMARK 3 T33: 0.3141 T12: -0.0658
REMARK 3 T13: -0.0444 T23: -0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 4.7141 L22: 3.7005
REMARK 3 L33: 5.4611 L12: -1.9913
REMARK 3 L13: 0.0913 L23: -0.8311
REMARK 3 S TENSOR
REMARK 3 S11: 0.0826 S12: 0.2927 S13: -0.1384
REMARK 3 S21: -0.1901 S22: -0.1922 S23: -0.0438
REMARK 3 S31: -0.1555 S32: 0.3821 S33: 0.1169
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 132 THROUGH 168 )
REMARK 3 ORIGIN FOR THE GROUP (A): -95.9193 152.1158 12.1418
REMARK 3 T TENSOR
REMARK 3 T11: 0.1276 T22: 0.1682
REMARK 3 T33: 0.1757 T12: -0.0197
REMARK 3 T13: 0.0263 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 2.6565 L22: 2.9046
REMARK 3 L33: 3.8327 L12: 0.5093
REMARK 3 L13: 1.6266 L23: -0.0374
REMARK 3 S TENSOR
REMARK 3 S11: 0.1466 S12: -0.2195 S13: -0.2487
REMARK 3 S21: 0.1008 S22: 0.0063 S23: -0.0869
REMARK 3 S31: 0.0365 S32: 0.0443 S33: -0.0535
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 169 THROUGH 231 )
REMARK 3 ORIGIN FOR THE GROUP (A): -84.9450 157.9453 9.3709
REMARK 3 T TENSOR
REMARK 3 T11: 0.1919 T22: 0.3224
REMARK 3 T33: 0.2127 T12: -0.0678
REMARK 3 T13: -0.0034 T23: -0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 2.4720 L22: 3.2662
REMARK 3 L33: 3.3172 L12: 0.2087
REMARK 3 L13: 1.7923 L23: -0.4493
REMARK 3 S TENSOR
REMARK 3 S11: 0.0304 S12: 0.1052 S13: 0.1824
REMARK 3 S21: -0.0925 S22: -0.0006 S23: -0.5151
REMARK 3 S31: -0.1412 S32: 0.7704 S33: -0.2259
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 232 THROUGH 316 )
REMARK 3 ORIGIN FOR THE GROUP (A): -94.7440 154.7891 -2.4478
REMARK 3 T TENSOR
REMARK 3 T11: 0.1986 T22: 0.1782
REMARK 3 T33: 0.1355 T12: -0.0182
REMARK 3 T13: -0.0243 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 2.4219 L22: 2.8690
REMARK 3 L33: 2.5740 L12: 0.4495
REMARK 3 L13: -0.2871 L23: 0.2950
REMARK 3 S TENSOR
REMARK 3 S11: -0.0575 S12: 0.2278 S13: 0.0842
REMARK 3 S21: -0.3801 S22: 0.0308 S23: 0.0263
REMARK 3 S31: -0.1514 S32: 0.0018 S33: 0.0028
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 317 THROUGH 360 )
REMARK 3 ORIGIN FOR THE GROUP (A):-102.4917 148.6100 11.2946
REMARK 3 T TENSOR
REMARK 3 T11: 0.1175 T22: 0.1864
REMARK 3 T33: 0.2137 T12: -0.0303
REMARK 3 T13: 0.0202 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 1.7595 L22: 3.1058
REMARK 3 L33: 3.2650 L12: 1.1522
REMARK 3 L13: 0.2518 L23: 0.1682
REMARK 3 S TENSOR
REMARK 3 S11: 0.0434 S12: -0.1991 S13: 0.0547
REMARK 3 S21: 0.1465 S22: 0.0193 S23: 0.3459
REMARK 3 S31: -0.0055 S32: -0.2595 S33: -0.0386
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 6DXY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1000235419.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58028
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.851
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 (%) : 98.0
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
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) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 5U7Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NACL, 0.1 M BIS-TRIS PH 5 AND 20
REMARK 280 % PEG 3350, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 101.10250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 58.37156
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 15.19867
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 101.10250
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 58.37156
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 15.19867
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 101.10250
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 58.37156
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 15.19867
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 116.74311
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 30.39733
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 116.74311
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 30.39733
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 116.74311
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 30.39733
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 5300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 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 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 ASP A 24
REMARK 465 ARG A 25
REMARK 465 HIS A 26
REMARK 465 HIS A 27
REMARK 465 HIS A 28
REMARK 465 HIS A 29
REMARK 465 HIS A 30
REMARK 465 HIS A 31
REMARK 465 LYS A 32
REMARK 465 LEU A 33
REMARK 465 ALA A 129
REMARK 465 PHE A 130
REMARK 465 PRO B 361
REMARK 465 SER B 362
REMARK 465 ASP C 24
REMARK 465 ARG C 25
REMARK 465 HIS C 26
REMARK 465 HIS C 27
REMARK 465 HIS C 28
REMARK 465 HIS C 29
REMARK 465 HIS C 30
REMARK 465 HIS C 31
REMARK 465 LYS C 32
REMARK 465 LEU C 33
REMARK 465 ALA C 129
REMARK 465 PHE C 130
REMARK 465 PRO D 361
REMARK 465 SER D 362
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 HH22 ARG A 76 O ALA A 127 1.59
REMARK 500 O ALA B 212 HG SER D 215 1.60
REMARK 500 O HOH D 518 O HOH D 521 1.95
REMARK 500 OE2 GLU A 126 O HOH A 301 1.95
REMARK 500 O HOH B 539 O HOH B 569 2.01
REMARK 500 OE1 GLU A 93 O HOH A 302 2.04
REMARK 500 O HOH D 505 O HOH D 648 2.04
REMARK 500 O HOH C 326 O HOH C 340 2.06
REMARK 500 O HOH B 638 O HOH B 647 2.07
REMARK 500 O HOH B 621 O HOH B 670 2.09
REMARK 500 O HOH B 580 O HOH B 581 2.09
REMARK 500 O HOH C 307 O HOH C 344 2.10
REMARK 500 O HOH C 335 O HOH C 345 2.10
REMARK 500 O HOH D 615 O HOH D 628 2.11
REMARK 500 OE2 GLU B 200 O HOH B 501 2.11
REMARK 500 O HOH D 644 O HOH D 657 2.13
REMARK 500 OD3 OCS B 131 O HOH B 502 2.13
REMARK 500 O HOH A 329 O HOH A 346 2.13
REMARK 500 O HOH D 592 O HOH D 614 2.13
REMARK 500 O HOH B 553 O HOH B 605 2.13
REMARK 500 O6 NAG B 401 O HOH B 503 2.14
REMARK 500 O HOH A 332 O HOH A 346 2.14
REMARK 500 OD1 ASP C 117 O HOH C 301 2.16
REMARK 500 O HOH B 662 O HOH B 665 2.17
REMARK 500 O HOH D 507 O HOH D 549 2.18
REMARK 500 O HOH B 533 O HOH B 648 2.18
REMARK 500 O HOH A 330 O HOH A 340 2.18
REMARK 500 NZ LYS D 297 O HOH D 501 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 O HOH D 506 O HOH D 642 2675 2.04
REMARK 500 O HOH B 607 O HOH B 633 6465 2.11
REMARK 500 O HOH C 330 O HOH D 501 1556 2.11
REMARK 500 O HOH D 527 O HOH D 658 2675 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 LYS B 193 -66.56 -131.55
REMARK 500 SER B 215 28.27 -75.48
REMARK 500 LYS B 261 -2.93 76.97
REMARK 500 THR B 291 -100.51 -110.95
REMARK 500 PHE D 153 67.46 32.72
REMARK 500 LYS D 193 -64.56 -128.00
REMARK 500 LYS D 261 -3.21 76.22
REMARK 500 GLU D 285 79.06 -100.63
REMARK 500 THR D 291 -100.84 -108.00
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 B 683 DISTANCE = 6.37 ANGSTROMS
DBREF 6DXY A 34 130 UNP Q9D7V9 NAAA_MOUSE 34 130
DBREF 6DXY B 131 362 UNP Q9D7V9 NAAA_MOUSE 131 362
DBREF 6DXY C 34 130 UNP Q9D7V9 NAAA_MOUSE 34 130
DBREF 6DXY D 131 362 UNP Q9D7V9 NAAA_MOUSE 131 362
SEQADV 6DXY ASP A 24 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY ARG A 25 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY HIS A 26 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY HIS A 27 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY HIS A 28 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY HIS A 29 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY HIS A 30 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY HIS A 31 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY LYS A 32 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY LEU A 33 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY VAL A 47 UNP Q9D7V9 ALA 47 CONFLICT
SEQADV 6DXY SER A 112 UNP Q9D7V9 ASN 112 CONFLICT
SEQADV 6DXY ARG B 142 UNP Q9D7V9 HIS 142 CONFLICT
SEQADV 6DXY ASP B 163 UNP Q9D7V9 ASN 163 CONFLICT
SEQADV 6DXY SER B 338 UNP Q9D7V9 ASN 338 CONFLICT
SEQADV 6DXY ASP C 24 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY ARG C 25 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY HIS C 26 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY HIS C 27 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY HIS C 28 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY HIS C 29 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY HIS C 30 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY HIS C 31 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY LYS C 32 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY LEU C 33 UNP Q9D7V9 EXPRESSION TAG
SEQADV 6DXY VAL C 47 UNP Q9D7V9 ALA 47 CONFLICT
SEQADV 6DXY SER C 112 UNP Q9D7V9 ASN 112 CONFLICT
SEQADV 6DXY ARG D 142 UNP Q9D7V9 HIS 142 CONFLICT
SEQADV 6DXY ASP D 163 UNP Q9D7V9 ASN 163 CONFLICT
SEQADV 6DXY SER D 338 UNP Q9D7V9 ASN 338 CONFLICT
SEQRES 1 A 107 ASP ARG HIS HIS HIS HIS HIS HIS LYS LEU VAL PRO GLY
SEQRES 2 A 107 THR PRO PRO LEU PHE ASN VAL SER LEU ASP VAL ALA PRO
SEQRES 3 A 107 GLU GLN ARG TRP LEU PRO MET LEU ARG HIS TYR ASP PRO
SEQRES 4 A 107 ASP PHE LEU ARG THR ALA VAL ALA GLN VAL ILE GLY ASP
SEQRES 5 A 107 ARG VAL PRO GLN TRP VAL LEU GLY MET VAL GLY GLU ILE
SEQRES 6 A 107 VAL SER LYS VAL GLU SER PHE LEU PRO GLN PRO PHE THR
SEQRES 7 A 107 ASP GLU ILE ARG SER ILE CYS ASP SER LEU SER LEU SER
SEQRES 8 A 107 LEU ALA ASP GLY ILE LEU VAL ASN LEU ALA TYR GLU ALA
SEQRES 9 A 107 SER ALA PHE
SEQRES 1 B 232 OCS THR SER ILE VAL ALA GLN ASP SER GLN GLY ARG ILE
SEQRES 2 B 232 TYR HIS GLY ARG ASN LEU ASP TYR PRO PHE GLY LYS ILE
SEQRES 3 B 232 LEU ARG LYS LEU THR ALA ASP VAL GLN PHE ILE LYS ASN
SEQRES 4 B 232 GLY GLN ILE ALA PHE THR GLY THR THR PHE VAL GLY TYR
SEQRES 5 B 232 VAL GLY LEU TRP THR GLY GLN SER PRO HIS LYS PHE THR
SEQRES 6 B 232 ILE SER GLY ASP GLU ARG ASP LYS GLY TRP TRP TRP GLU
SEQRES 7 B 232 ASN MET ILE ALA ALA LEU SER LEU GLY HIS SER PRO ILE
SEQRES 8 B 232 SER TRP LEU ILE ARG LYS THR LEU SER GLU SER GLU SER
SEQRES 9 B 232 PHE GLU ALA ALA VAL TYR THR LEU ALA LYS THR PRO LEU
SEQRES 10 B 232 ILE ALA ASP VAL TYR TYR ILE VAL GLY GLY THR SER PRO
SEQRES 11 B 232 LYS GLU GLY VAL VAL ILE THR ARG ASP ARG GLY GLY PRO
SEQRES 12 B 232 ALA ASP ILE TRP PRO LEU ASP PRO LEU ASN GLY GLU TRP
SEQRES 13 B 232 PHE ARG VAL GLU THR ASN TYR ASP HIS TRP LYS PRO ALA
SEQRES 14 B 232 PRO LYS VAL ASP ASP ARG ARG THR PRO ALA ILE LYS ALA
SEQRES 15 B 232 LEU ASN ALA THR GLY GLN ALA HIS LEU ASN LEU GLU THR
SEQRES 16 B 232 LEU PHE GLN VAL LEU SER LEU PHE PRO VAL TYR ASN SER
SEQRES 17 B 232 TYR THR ILE TYR THR THR VAL MET SER ALA ALA GLU PRO
SEQRES 18 B 232 ASP LYS TYR LEU THR MET ILE ARG ASN PRO SER
SEQRES 1 C 107 ASP ARG HIS HIS HIS HIS HIS HIS LYS LEU VAL PRO GLY
SEQRES 2 C 107 THR PRO PRO LEU PHE ASN VAL SER LEU ASP VAL ALA PRO
SEQRES 3 C 107 GLU GLN ARG TRP LEU PRO MET LEU ARG HIS TYR ASP PRO
SEQRES 4 C 107 ASP PHE LEU ARG THR ALA VAL ALA GLN VAL ILE GLY ASP
SEQRES 5 C 107 ARG VAL PRO GLN TRP VAL LEU GLY MET VAL GLY GLU ILE
SEQRES 6 C 107 VAL SER LYS VAL GLU SER PHE LEU PRO GLN PRO PHE THR
SEQRES 7 C 107 ASP GLU ILE ARG SER ILE CYS ASP SER LEU SER LEU SER
SEQRES 8 C 107 LEU ALA ASP GLY ILE LEU VAL ASN LEU ALA TYR GLU ALA
SEQRES 9 C 107 SER ALA PHE
SEQRES 1 D 232 OCS THR SER ILE VAL ALA GLN ASP SER GLN GLY ARG ILE
SEQRES 2 D 232 TYR HIS GLY ARG ASN LEU ASP TYR PRO PHE GLY LYS ILE
SEQRES 3 D 232 LEU ARG LYS LEU THR ALA ASP VAL GLN PHE ILE LYS ASN
SEQRES 4 D 232 GLY GLN ILE ALA PHE THR GLY THR THR PHE VAL GLY TYR
SEQRES 5 D 232 VAL GLY LEU TRP THR GLY GLN SER PRO HIS LYS PHE THR
SEQRES 6 D 232 ILE SER GLY ASP GLU ARG ASP LYS GLY TRP TRP TRP GLU
SEQRES 7 D 232 ASN MET ILE ALA ALA LEU SER LEU GLY HIS SER PRO ILE
SEQRES 8 D 232 SER TRP LEU ILE ARG LYS THR LEU SER GLU SER GLU SER
SEQRES 9 D 232 PHE GLU ALA ALA VAL TYR THR LEU ALA LYS THR PRO LEU
SEQRES 10 D 232 ILE ALA ASP VAL TYR TYR ILE VAL GLY GLY THR SER PRO
SEQRES 11 D 232 LYS GLU GLY VAL VAL ILE THR ARG ASP ARG GLY GLY PRO
SEQRES 12 D 232 ALA ASP ILE TRP PRO LEU ASP PRO LEU ASN GLY GLU TRP
SEQRES 13 D 232 PHE ARG VAL GLU THR ASN TYR ASP HIS TRP LYS PRO ALA
SEQRES 14 D 232 PRO LYS VAL ASP ASP ARG ARG THR PRO ALA ILE LYS ALA
SEQRES 15 D 232 LEU ASN ALA THR GLY GLN ALA HIS LEU ASN LEU GLU THR
SEQRES 16 D 232 LEU PHE GLN VAL LEU SER LEU PHE PRO VAL TYR ASN SER
SEQRES 17 D 232 TYR THR ILE TYR THR THR VAL MET SER ALA ALA GLU PRO
SEQRES 18 D 232 ASP LYS TYR LEU THR MET ILE ARG ASN PRO SER
MODRES 6DXY OCS B 131 CYS MODIFIED RESIDUE
MODRES 6DXY OCS D 131 CYS MODIFIED RESIDUE
HET OCS B 131 14
HET OCS D 131 14
HET NAG A 201 28
HET CL A 202 1
HET NAG B 401 28
HET CL B 402 1
HET CL B 403 1
HET CL B 404 1
HET CL B 405 1
HET PG4 B 406 31
HET CL C 201 1
HET NAG D 401 28
HET CL D 402 1
HET CL D 403 1
HET CL D 404 1
HET CL D 405 1
HET CL D 406 1
HET PG4 D 407 31
HET P33 D 408 52
HETNAM OCS CYSTEINESULFONIC ACID
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CL CHLORIDE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM P33 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN P33 HEPTAETHYLENE GLYCOL; PEG330
FORMUL 2 OCS 2(C3 H7 N O5 S)
FORMUL 5 NAG 3(C8 H15 N O6)
FORMUL 6 CL 11(CL 1-)
FORMUL 12 PG4 2(C8 H18 O5)
FORMUL 21 P33 C14 H30 O8
FORMUL 22 HOH *458(H2 O)
HELIX 1 AA1 TRP A 53 ARG A 58 1 6
HELIX 2 AA2 ASP A 61 VAL A 77 1 17
HELIX 3 AA3 PRO A 78 MET A 84 1 7
HELIX 4 AA4 MET A 84 LEU A 96 1 13
HELIX 5 AA5 PRO A 97 SER A 112 1 16
HELIX 6 AA6 SER A 114 ALA A 124 1 11
HELIX 7 AA7 ILE B 156 LYS B 159 5 4
HELIX 8 AA8 TRP B 205 SER B 215 1 11
HELIX 9 AA9 PRO B 220 SER B 232 1 13
HELIX 10 AB1 SER B 234 THR B 245 1 12
HELIX 11 AB2 ASP B 280 GLY B 284 5 5
HELIX 12 AB3 PRO B 300 ASP B 304 5 5
HELIX 13 AB4 ARG B 305 GLY B 317 1 13
HELIX 14 AB5 GLN B 318 LEU B 321 5 4
HELIX 15 AB6 ASN B 322 LEU B 330 1 9
HELIX 16 AB7 GLU B 350 TYR B 354 5 5
HELIX 17 AB8 ALA C 48 TRP C 53 1 6
HELIX 18 AB9 TRP C 53 ARG C 58 1 6
HELIX 19 AC1 ASP C 61 VAL C 77 1 17
HELIX 20 AC2 PRO C 78 MET C 84 1 7
HELIX 21 AC3 MET C 84 LEU C 96 1 13
HELIX 22 AC4 PRO C 97 SER C 112 1 16
HELIX 23 AC5 SER C 114 TYR C 125 1 12
HELIX 24 AC6 GLY D 154 LEU D 160 1 7
HELIX 25 AC7 TRP D 205 LEU D 214 1 10
HELIX 26 AC8 PRO D 220 SER D 232 1 13
HELIX 27 AC9 SER D 234 THR D 245 1 12
HELIX 28 AD1 ASP D 280 GLY D 284 5 5
HELIX 29 AD2 PRO D 300 ASP D 304 5 5
HELIX 30 AD3 ARG D 305 GLY D 317 1 13
HELIX 31 AD4 GLN D 318 LEU D 321 5 4
HELIX 32 AD5 ASN D 322 LEU D 330 1 9
HELIX 33 AD6 GLU D 350 TYR D 354 5 5
SHEET 1 AA1 8 LEU A 40 SER A 44 0
SHEET 2 AA1 8 THR B 161 LYS B 168 1 O GLN B 165 N PHE A 41
SHEET 3 AA1 8 GLN B 171 PHE B 179 -1 O PHE B 174 N PHE B 166
SHEET 4 AA1 8 THR B 187 SER B 190 -1 O GLN B 189 N THR B 175
SHEET 5 AA1 8 PHE B 194 GLU B 200 -1 O PHE B 194 N SER B 190
SHEET 6 AA1 8 VAL B 251 GLY B 256 -1 O ILE B 254 N SER B 197
SHEET 7 AA1 8 GLY B 263 ARG B 268 -1 O ILE B 266 N TYR B 253
SHEET 8 AA1 8 PRO B 273 PRO B 278 -1 O ALA B 274 N THR B 267
SHEET 1 AA2 5 PHE B 287 GLU B 290 0
SHEET 2 AA2 5 THR B 132 GLN B 137 -1 N SER B 133 O GLU B 290
SHEET 3 AA2 5 ILE B 143 ASP B 150 -1 O GLY B 146 N ILE B 134
SHEET 4 AA2 5 THR B 340 MET B 346 -1 O ILE B 341 N LEU B 149
SHEET 5 AA2 5 LEU B 355 ILE B 358 -1 O MET B 357 N THR B 343
SHEET 1 AA3 8 LEU C 40 SER C 44 0
SHEET 2 AA3 8 THR D 161 LYS D 168 1 O GLN D 165 N PHE C 41
SHEET 3 AA3 8 GLN D 171 PHE D 179 -1 O GLN D 171 N LYS D 168
SHEET 4 AA3 8 THR D 187 SER D 190 -1 O GLN D 189 N THR D 175
SHEET 5 AA3 8 PHE D 194 GLU D 200 -1 O PHE D 194 N SER D 190
SHEET 6 AA3 8 VAL D 251 GLY D 256 -1 O ILE D 254 N SER D 197
SHEET 7 AA3 8 GLY D 263 ARG D 268 -1 O ILE D 266 N TYR D 253
SHEET 8 AA3 8 PRO D 273 PRO D 278 -1 O ALA D 274 N THR D 267
SHEET 1 AA4 5 PHE D 287 GLU D 290 0
SHEET 2 AA4 5 THR D 132 GLN D 137 -1 N SER D 133 O GLU D 290
SHEET 3 AA4 5 ILE D 143 ASP D 150 -1 O TYR D 144 N ALA D 136
SHEET 4 AA4 5 THR D 340 MET D 346 -1 O ILE D 341 N LEU D 149
SHEET 5 AA4 5 LEU D 355 ILE D 358 -1 O MET D 357 N THR D 343
LINK ND2 ASN A 42 C1 NAG A 201 1555 1555 1.43
LINK C OCS B 131 N THR B 132 1555 1555 1.32
LINK ND2 ASN B 314 C1 NAG B 401 1555 1555 1.43
LINK C OCS D 131 N THR D 132 1555 1555 1.33
LINK ND2 ASN D 314 C1 NAG D 401 1555 1555 1.44
CISPEP 1 PHE B 333 PRO B 334 0 1.55
CISPEP 2 PHE D 333 PRO D 334 0 0.17
CRYST1 202.205 202.205 45.596 90.00 90.00 120.00 H 3 18
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 0.004945 0.002855 0.000000 0.00000
SCALE2 0.000000 0.005711 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021932 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
