| 6yq4-pdb | HEADER HYDROLASE 16-APR-20 6YQ4
TITLE CRYSTAL STRUCTURE OF FUSOBACTERIUM NUCLEATUM TANNASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANNASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSOBACTERIUM NUCLEATUM SUBSP. NUCLEATUM ATCC
SOURCE 3 25586;
SOURCE 4 ORGANISM_TAXID: 190304;
SOURCE 5 GENE: FN0616;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TANNASE, COLORECTAL CANCER, PATHOGEN, GALLOTANNINS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.MANCHENO,J.ANGUITA,H.RODRIGUEZ
REVDAT 1 24-MAR-21 6YQ4 0
JRNL AUTH J.M.MANCHENO,E.ATONDO,J.TOMAS-CORTAZAR,J.LUIS LAVIN,
JRNL AUTH 2 L.PLAZA-VINUESA,I.MARTIN-RUIZ,D.BARRIALES,A.PALACIOS,
JRNL AUTH 3 C.DANIEL NAVO,L.SAMPEDRO,A.PENA-CEARRA,
JRNL AUTH 4 M.ANGEL PASCUAL-ITOIZ,J.CASTELO,A.CARRERAS-GONZALEZ,
JRNL AUTH 5 D.CASTELLANA,A.PELLON,S.DELGADO,P.RUAS-MADIEDO,
JRNL AUTH 6 B.DE LAS RIVAS,L.ABECIA,R.MUNOZ,G.JIMENEZ-OSES,J.ANGUITA,
JRNL AUTH 7 H.RODRIGUEZ
JRNL TITL A STRUCTURALLY UNIQUE FUSOBACTERIUM NUCLEATUM TANNASE
JRNL TITL 2 PROVIDES DETOXICANT ACTIVITY AGAINST GALLOTANNINS AND
JRNL TITL 3 PATHOGEN RESISTANCE.
JRNL REF MICROB BIOTECHNOL 2020
JRNL REFN ISSN 1751-7915
JRNL PMID 33336898
JRNL DOI 10.1111/1751-7915.13732
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 60840
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3103
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 47.7900 - 6.7148 0.99 2731 128 0.1513 0.2093
REMARK 3 2 6.7148 - 5.3320 0.99 2668 142 0.1599 0.2090
REMARK 3 3 5.3320 - 4.6587 0.98 2591 161 0.1322 0.1903
REMARK 3 4 4.6587 - 4.2330 0.99 2661 128 0.1196 0.1813
REMARK 3 5 4.2330 - 3.9298 0.99 2628 150 0.1391 0.2060
REMARK 3 6 3.9298 - 3.6982 1.00 2657 131 0.1528 0.2602
REMARK 3 7 3.6982 - 3.5130 1.00 2636 156 0.1554 0.2295
REMARK 3 8 3.5130 - 3.3601 0.99 2621 142 0.1656 0.2559
REMARK 3 9 3.3601 - 3.2308 0.98 2604 138 0.1751 0.2669
REMARK 3 10 3.2308 - 3.1193 0.99 2559 171 0.1926 0.2997
REMARK 3 11 3.1193 - 3.0218 0.99 2651 132 0.1907 0.2786
REMARK 3 12 3.0218 - 2.9355 0.99 2626 134 0.1920 0.3002
REMARK 3 13 2.9355 - 2.8582 1.00 2645 144 0.2083 0.3116
REMARK 3 14 2.8582 - 2.7885 0.99 2592 154 0.2187 0.2801
REMARK 3 15 2.7885 - 2.7251 0.99 2648 138 0.2110 0.3009
REMARK 3 16 2.7251 - 2.6671 1.00 2632 135 0.2130 0.2854
REMARK 3 17 2.6671 - 2.6138 0.99 2612 138 0.2221 0.3176
REMARK 3 18 2.6138 - 2.5644 0.98 2579 120 0.2117 0.3144
REMARK 3 19 2.5644 - 2.5186 0.99 2632 133 0.2277 0.3160
REMARK 3 20 2.5186 - 2.4759 0.99 2569 140 0.2394 0.3389
REMARK 3 21 2.4759 - 2.4360 0.99 2646 157 0.2496 0.3313
REMARK 3 22 2.4360 - 2.3990 0.97 2549 131 0.2528 0.3654
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.66
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.6560 3.1061 -1.5523
REMARK 3 T TENSOR
REMARK 3 T11: 0.4972 T22: 0.2548
REMARK 3 T33: 0.3757 T12: 0.0445
REMARK 3 T13: -0.0544 T23: -0.1374
REMARK 3 L TENSOR
REMARK 3 L11: 2.6984 L22: 7.3210
REMARK 3 L33: 3.3718 L12: 2.6911
REMARK 3 L13: -0.6376 L23: -3.3494
REMARK 3 S TENSOR
REMARK 3 S11: 0.1123 S12: -0.2190 S13: 0.4777
REMARK 3 S21: 0.2226 S22: -0.1709 S23: 0.2732
REMARK 3 S31: -0.4610 S32: -0.0334 S33: 0.0395
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 59 THROUGH 239 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.6159 -13.3387 -6.0048
REMARK 3 T TENSOR
REMARK 3 T11: 0.2800 T22: 0.2210
REMARK 3 T33: 0.1899 T12: 0.0211
REMARK 3 T13: -0.0155 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 1.6344 L22: 1.9926
REMARK 3 L33: 1.2379 L12: 0.0330
REMARK 3 L13: 0.3015 L23: 0.3587
REMARK 3 S TENSOR
REMARK 3 S11: 0.0446 S12: -0.2152 S13: 0.2294
REMARK 3 S21: -0.0001 S22: -0.1417 S23: 0.1011
REMARK 3 S31: -0.1636 S32: -0.1626 S33: 0.0768
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 240 THROUGH 279 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3642 -34.2624 -6.6488
REMARK 3 T TENSOR
REMARK 3 T11: 0.2627 T22: 0.2119
REMARK 3 T33: 0.1925 T12: -0.0125
REMARK 3 T13: 0.0195 T23: 0.0725
REMARK 3 L TENSOR
REMARK 3 L11: 3.5122 L22: 1.8726
REMARK 3 L33: 3.4919 L12: -2.4461
REMARK 3 L13: 1.4308 L23: -0.5160
REMARK 3 S TENSOR
REMARK 3 S11: 0.0951 S12: 0.1069 S13: -0.0974
REMARK 3 S21: 0.1828 S22: 0.0497 S23: -0.2919
REMARK 3 S31: 0.0525 S32: 0.2286 S33: -0.2030
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 280 THROUGH 494 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2732 -28.4455 -14.5839
REMARK 3 T TENSOR
REMARK 3 T11: 0.2608 T22: 0.1809
REMARK 3 T33: 0.1834 T12: 0.0200
REMARK 3 T13: -0.0161 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 1.5324 L22: 2.0315
REMARK 3 L33: 1.3600 L12: -0.2385
REMARK 3 L13: 0.1519 L23: 0.3824
REMARK 3 S TENSOR
REMARK 3 S11: 0.0766 S12: 0.0244 S13: -0.1163
REMARK 3 S21: -0.1223 S22: -0.1271 S23: -0.0541
REMARK 3 S31: 0.0981 S32: 0.0343 S33: 0.0750
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0147 -37.4642 -51.6785
REMARK 3 T TENSOR
REMARK 3 T11: 0.4921 T22: 0.7992
REMARK 3 T33: 0.2865 T12: 0.2452
REMARK 3 T13: 0.0156 T23: 0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 2.1680 L22: 8.0217
REMARK 3 L33: 5.2905 L12: -1.8575
REMARK 3 L13: -1.4502 L23: 2.6737
REMARK 3 S TENSOR
REMARK 3 S11: -0.1950 S12: -0.1791 S13: -0.0077
REMARK 3 S21: 0.2408 S22: 0.0759 S23: -0.5095
REMARK 3 S31: 0.8807 S32: 1.2144 S33: 0.0609
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 59 THROUGH 211 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.3713 -30.5472 -52.3722
REMARK 3 T TENSOR
REMARK 3 T11: 0.3343 T22: 0.3854
REMARK 3 T33: 0.1793 T12: 0.0419
REMARK 3 T13: 0.0324 T23: 0.0365
REMARK 3 L TENSOR
REMARK 3 L11: 1.1681 L22: 2.3956
REMARK 3 L33: 3.2090 L12: -0.4327
REMARK 3 L13: -0.8675 L23: 0.0303
REMARK 3 S TENSOR
REMARK 3 S11: -0.0948 S12: 0.1511 S13: 0.0581
REMARK 3 S21: -0.1981 S22: 0.0334 S23: -0.2165
REMARK 3 S31: 0.3303 S32: 0.5047 S33: 0.0161
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 212 THROUGH 279 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.0712 -28.4093 -37.3237
REMARK 3 T TENSOR
REMARK 3 T11: 0.4129 T22: 0.3744
REMARK 3 T33: 0.2086 T12: 0.0045
REMARK 3 T13: 0.0401 T23: -0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 4.6186 L22: 1.9287
REMARK 3 L33: 5.1737 L12: 0.3898
REMARK 3 L13: -0.7244 L23: 0.5312
REMARK 3 S TENSOR
REMARK 3 S11: 0.0398 S12: -0.2301 S13: -0.3543
REMARK 3 S21: 0.1289 S22: 0.1003 S23: 0.3382
REMARK 3 S31: 0.5253 S32: -0.7848 S33: -0.0997
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 280 THROUGH 494 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.3016 -28.7582 -48.5036
REMARK 3 T TENSOR
REMARK 3 T11: 0.3762 T22: 0.4449
REMARK 3 T33: 0.2230 T12: -0.0404
REMARK 3 T13: -0.0196 T23: 0.0425
REMARK 3 L TENSOR
REMARK 3 L11: 1.2697 L22: 1.4769
REMARK 3 L33: 3.1590 L12: 0.1333
REMARK 3 L13: -0.1777 L23: 0.1823
REMARK 3 S TENSOR
REMARK 3 S11: -0.0355 S12: 0.1683 S13: 0.0203
REMARK 3 S21: -0.0976 S22: 0.0053 S23: 0.2264
REMARK 3 S31: 0.3348 S32: -0.7685 S33: 0.0551
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 5 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.1766 -84.6652 -42.8040
REMARK 3 T TENSOR
REMARK 3 T11: 0.5821 T22: 0.4272
REMARK 3 T33: 0.3293 T12: 0.1184
REMARK 3 T13: 0.0869 T23: -0.0865
REMARK 3 L TENSOR
REMARK 3 L11: 5.1640 L22: 3.2048
REMARK 3 L33: 2.9049 L12: -0.8245
REMARK 3 L13: -0.3268 L23: 0.9898
REMARK 3 S TENSOR
REMARK 3 S11: -0.1754 S12: 0.3120 S13: -0.3890
REMARK 3 S21: -0.3802 S22: 0.2444 S23: -0.5792
REMARK 3 S31: 0.1864 S32: 0.4272 S33: -0.1166
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 82 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6072 -72.8803 -42.8642
REMARK 3 T TENSOR
REMARK 3 T11: 0.4114 T22: 0.3515
REMARK 3 T33: 0.3061 T12: 0.0927
REMARK 3 T13: 0.0742 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 5.5831 L22: 2.9519
REMARK 3 L33: 1.3204 L12: -1.5685
REMARK 3 L13: -2.1711 L23: 1.4537
REMARK 3 S TENSOR
REMARK 3 S11: -0.1499 S12: -0.2400 S13: 0.6784
REMARK 3 S21: -0.2110 S22: 0.2697 S23: -0.5404
REMARK 3 S31: 0.1186 S32: 0.1961 S33: -0.1386
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 115 THROUGH 279 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8071 -70.3335 -36.8928
REMARK 3 T TENSOR
REMARK 3 T11: 0.3352 T22: 0.3190
REMARK 3 T33: 0.1697 T12: 0.0197
REMARK 3 T13: -0.0397 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 1.8153 L22: 2.3871
REMARK 3 L33: 1.6160 L12: -0.5765
REMARK 3 L13: -0.3216 L23: 0.6750
REMARK 3 S TENSOR
REMARK 3 S11: -0.0874 S12: 0.2669 S13: 0.0190
REMARK 3 S21: -0.3053 S22: 0.0146 S23: 0.1712
REMARK 3 S31: 0.1439 S32: -0.1081 S33: 0.0686
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 280 THROUGH 494 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8842 -60.9138 -29.2238
REMARK 3 T TENSOR
REMARK 3 T11: 0.3017 T22: 0.2506
REMARK 3 T33: 0.2144 T12: 0.0469
REMARK 3 T13: -0.0460 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 2.2025 L22: 1.9256
REMARK 3 L33: 1.3832 L12: -0.8068
REMARK 3 L13: -0.0996 L23: 0.3391
REMARK 3 S TENSOR
REMARK 3 S11: -0.1452 S12: 0.0094 S13: 0.2374
REMARK 3 S21: 0.0023 S22: 0.1170 S23: 0.0126
REMARK 3 S31: 0.0734 S32: -0.0103 S33: 0.0338
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 6YQ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-APR-20.
REMARK 100 THE DEPOSITION ID IS D_1292108062.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60896
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.390
REMARK 200 RESOLUTION RANGE LOW (A) : 47.791
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.620
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.3100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
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 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: 4J0D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, TRIS-HCL, PH 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 45.53350
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 MET A 1
REMARK 465 VAL A 2
REMARK 465 LYS A 3
REMARK 465 ASN A 4
REMARK 465 ARG A 396
REMARK 465 ASN A 397
REMARK 465 GLY A 398
REMARK 465 LYS A 399
REMARK 465 PHE A 400
REMARK 465 ASN A 401
REMARK 465 ASP A 402
REMARK 465 LYS A 403
REMARK 465 ASN A 404
REMARK 465 ASN A 405
REMARK 465 LYS A 406
REMARK 465 ILE A 407
REMARK 465 LYS A 495
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 LYS B 3
REMARK 465 ASN B 4
REMARK 465 GLY B 398
REMARK 465 LYS B 399
REMARK 465 PHE B 400
REMARK 465 ASN B 401
REMARK 465 ASP B 402
REMARK 465 LYS B 403
REMARK 465 ASN B 404
REMARK 465 ASN B 405
REMARK 465 LYS B 406
REMARK 465 ILE B 407
REMARK 465 LYS B 495
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 LYS C 3
REMARK 465 ASN C 4
REMARK 465 PHE C 395
REMARK 465 ARG C 396
REMARK 465 ASN C 397
REMARK 465 GLY C 398
REMARK 465 LYS C 399
REMARK 465 PHE C 400
REMARK 465 ASN C 401
REMARK 465 ASP C 402
REMARK 465 LYS C 403
REMARK 465 ASN C 404
REMARK 465 ASN C 405
REMARK 465 LYS C 406
REMARK 465 LYS C 495
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 NZ LYS B 125 O HOH B 601 1.92
REMARK 500 NZ LYS A 125 O HOH A 601 1.94
REMARK 500 NH1 ARG C 246 OD2 ASP C 446 2.10
REMARK 500 O GLU A 242 O HOH A 602 2.12
REMARK 500 O HOH A 755 O HOH A 771 2.13
REMARK 500 O TYR C 103 OG SER C 106 2.14
REMARK 500 O TYR C 243 NH2 ARG C 246 2.14
REMARK 500 O HOH A 700 O HOH C 704 2.14
REMARK 500 OG SER B 408 O HOH B 602 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 LYS A 373 CD - CE - NZ ANGL. DEV. = -15.1 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 ASN A 23 -12.72 -140.41
REMARK 500 TYR A 37 34.26 -98.08
REMARK 500 ASN A 67 -168.96 -129.45
REMARK 500 SER A 166 -121.51 71.43
REMARK 500 THR A 196 -96.58 -122.01
REMARK 500 CYS A 207 53.44 37.19
REMARK 500 THR A 210 -169.51 -118.89
REMARK 500 ASP A 283 -164.70 -78.88
REMARK 500 SER A 322 -62.89 -25.49
REMARK 500 GLU A 331 -103.74 -114.33
REMARK 500 MET A 350 -73.74 -97.43
REMARK 500 ASP A 481 45.73 -140.97
REMARK 500 ASN B 23 47.13 -164.12
REMARK 500 ASN B 40 72.54 -118.43
REMARK 500 GLN B 47 57.85 -98.75
REMARK 500 ASP B 95 4.81 -174.81
REMARK 500 LYS B 159 61.32 -118.26
REMARK 500 SER B 166 -120.23 64.67
REMARK 500 THR B 196 -122.08 -125.65
REMARK 500 CYS B 207 68.25 18.47
REMARK 500 THR B 249 22.65 43.93
REMARK 500 SER B 251 165.94 64.58
REMARK 500 THR B 252 118.78 -163.78
REMARK 500 PHE B 324 34.52 -84.49
REMARK 500 GLU B 331 -139.90 -95.04
REMARK 500 ASN B 333 -37.73 66.75
REMARK 500 PHE B 395 -20.99 168.16
REMARK 500 ASP B 481 45.90 -150.75
REMARK 500 ASN C 23 -33.48 -157.64
REMARK 500 ASN C 34 31.04 72.41
REMARK 500 ASP C 95 31.61 -78.46
REMARK 500 SER C 166 -116.99 65.65
REMARK 500 THR C 196 -94.77 -128.03
REMARK 500 CYS C 207 61.62 28.34
REMARK 500 GLU C 233 80.69 -35.98
REMARK 500 SER C 247 -75.54 -144.02
REMARK 500 THR C 249 83.09 81.27
REMARK 500 ARG C 250 176.48 75.50
REMARK 500 SER C 251 -152.11 -85.79
REMARK 500 ASP C 283 -167.01 -76.74
REMARK 500 ASP C 292 157.12 -43.31
REMARK 500 GLU C 331 -85.84 -125.82
REMARK 500 MET C 350 -60.95 -94.13
REMARK 500 PHE C 356 -51.37 -122.49
REMARK 500 ASP C 371 -167.15 -125.31
REMARK 500 PHE C 379 17.70 -144.76
REMARK 500 ASP C 481 42.13 -141.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP B 393 TYR B 394 142.83
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 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 150 O
REMARK 620 2 ASP A 150 OD2 74.1
REMARK 620 3 MET A 153 O 74.8 131.5
REMARK 620 4 GLY A 155 O 164.2 97.7 119.6
REMARK 620 5 HOH A 676 O 103.9 73.9 78.6 86.3
REMARK 620 6 HOH A 759 O 90.6 127.2 89.2 83.6 157.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 150 O
REMARK 620 2 ASP B 150 OD2 77.1
REMARK 620 3 MET B 153 O 81.5 139.5
REMARK 620 4 GLY B 155 O 165.5 109.3 100.0
REMARK 620 5 HOH B 680 O 109.5 76.0 79.5 84.8
REMARK 620 6 HOH B 685 O 83.7 120.9 89.9 81.9 161.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 150 O
REMARK 620 2 ASP C 150 OD2 87.8
REMARK 620 3 MET C 153 O 90.1 166.7
REMARK 620 4 GLY C 155 O 149.2 83.0 105.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SPD B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 502
DBREF 6YQ4 A 1 495 UNP Q8RFS1 Q8RFS1_FUSNN 1 495
DBREF 6YQ4 B 1 495 UNP Q8RFS1 Q8RFS1_FUSNN 1 495
DBREF 6YQ4 C 1 495 UNP Q8RFS1 Q8RFS1_FUSNN 1 495
SEQRES 1 A 495 MET VAL LYS ASN ASP TYR ASP LEU LYS PHE ASN PRO ASP
SEQRES 2 A 495 LYS TYR ILE SER LYS GLU ILE LYS ILE ASN GLY LYS LYS
SEQRES 3 A 495 ILE LYS TYR ARG ALA TYR GLU ASN ILE ILE TYR ILE LYS
SEQRES 4 A 495 ASN PRO ILE ASP LYS ASP TYR GLN ASN MET ASN ILE TYR
SEQRES 5 A 495 ILE PRO GLU GLU TYR PHE ASN ASN LEU SER ILE GLY SER
SEQRES 6 A 495 TYR ASN SER ASN ASN ALA PRO ILE PHE PHE PRO ASN THR
SEQRES 7 A 495 VAL GLY GLY TYR MET PRO GLY LYS ALA ASP THR VAL GLY
SEQRES 8 A 495 LEU GLY ARG ASP GLY LYS ALA ASN SER LEU THR TYR ALA
SEQRES 9 A 495 LEU SER LYS GLY TYR VAL VAL ALA ALA PRO GLY ALA ARG
SEQRES 10 A 495 GLY ARG THR LEU THR ASP ASP LYS GLY ASN TYR ILE GLY
SEQRES 11 A 495 LYS ALA PRO ALA ALA ILE VAL ASP LEU LYS ALA ALA VAL
SEQRES 12 A 495 ARG TYR LEU TYR LEU ASN ASP GLU VAL MET PRO GLY ASP
SEQRES 13 A 495 ALA ASN LYS ILE ILE SER ASN GLY THR SER ALA GLY GLY
SEQRES 14 A 495 ALA LEU SER ALA LEU LEU GLY ALA SER GLY ASN SER GLN
SEQRES 15 A 495 ASP TYR LEU PRO TYR LEU LYS GLU ILE GLY ALA ALA GLU
SEQRES 16 A 495 THR ARG ASP ASP ILE PHE ALA VAL SER ALA TYR CYS PRO
SEQRES 17 A 495 ILE THR ASN LEU GLU ASN ALA ASP SER ALA TYR GLU TRP
SEQRES 18 A 495 MET TYR ASN GLY VAL ASN SER TYR SER ARG MET GLU PHE
SEQRES 19 A 495 THR ARG ASN THR SER ALA GLN GLU TYR ASN ASP ARG SER
SEQRES 20 A 495 LEU THR ARG SER THR VAL GLN GLY ASN LEU THR ASN ASP
SEQRES 21 A 495 GLU ILE ASN ILE SER ASN LYS LEU LYS THR LEU PHE PRO
SEQRES 22 A 495 ILE TYR LEU ASN SER LEU LYS LEU THR ASP ASP GLY GLY
SEQRES 23 A 495 ASN LEU LEU THR LEU ASP LYS SER GLY ASN GLY SER PHE
SEQRES 24 A 495 LYS THR TYR LEU SER ILE ILE ILE ARG ASN SER ALA ASN
SEQRES 25 A 495 ARG ALA LEU ARG GLU GLY LYS ASP ILE SER GLN PHE LYS
SEQRES 26 A 495 LYS ALA PHE THR ILE GLU ASN ASN LYS VAL VAL ALA VAL
SEQRES 27 A 495 ASN LEU ASP VAL TYR THR HIS ILE GLY ASP ARG MET LYS
SEQRES 28 A 495 SER PRO PRO ALA PHE ASP SER LEU ASP ALA SER SER GLY
SEQRES 29 A 495 GLU ASN ASN LEU PHE GLY ASP LYS LYS SER ASP SER LYS
SEQRES 30 A 495 HIS PHE THR LYS PHE SER PHE ASP ILE ASN ASN LYS ALA
SEQRES 31 A 495 ALA ILE ASP TYR PHE ARG ASN GLY LYS PHE ASN ASP LYS
SEQRES 32 A 495 ASN ASN LYS ILE SER ILE PRO LYS MET ALA ASP LYS ASN
SEQRES 33 A 495 ILE ILE LYS MET MET ASN PRO MET TYR TYR ILE ASP SER
SEQRES 34 A 495 ASN THR SER THR LYS TYR TRP ARG ILE ARG HIS GLY ALA
SEQRES 35 A 495 ILE ASP LYS ASP THR SER LEU ALA ILE PRO ALA ILE LEU
SEQRES 36 A 495 ALA LEU LYS LEU LYS ASN SER GLY LYS ILE VAL ASN PHE
SEQRES 37 A 495 ALA ALA PRO TRP GLY GLN GLY HIS GLY GLY ASP TYR ASP
SEQRES 38 A 495 LEU GLU GLU LEU PHE ASN TRP ILE ASP ASN VAL VAL LYS
SEQRES 39 A 495 LYS
SEQRES 1 B 495 MET VAL LYS ASN ASP TYR ASP LEU LYS PHE ASN PRO ASP
SEQRES 2 B 495 LYS TYR ILE SER LYS GLU ILE LYS ILE ASN GLY LYS LYS
SEQRES 3 B 495 ILE LYS TYR ARG ALA TYR GLU ASN ILE ILE TYR ILE LYS
SEQRES 4 B 495 ASN PRO ILE ASP LYS ASP TYR GLN ASN MET ASN ILE TYR
SEQRES 5 B 495 ILE PRO GLU GLU TYR PHE ASN ASN LEU SER ILE GLY SER
SEQRES 6 B 495 TYR ASN SER ASN ASN ALA PRO ILE PHE PHE PRO ASN THR
SEQRES 7 B 495 VAL GLY GLY TYR MET PRO GLY LYS ALA ASP THR VAL GLY
SEQRES 8 B 495 LEU GLY ARG ASP GLY LYS ALA ASN SER LEU THR TYR ALA
SEQRES 9 B 495 LEU SER LYS GLY TYR VAL VAL ALA ALA PRO GLY ALA ARG
SEQRES 10 B 495 GLY ARG THR LEU THR ASP ASP LYS GLY ASN TYR ILE GLY
SEQRES 11 B 495 LYS ALA PRO ALA ALA ILE VAL ASP LEU LYS ALA ALA VAL
SEQRES 12 B 495 ARG TYR LEU TYR LEU ASN ASP GLU VAL MET PRO GLY ASP
SEQRES 13 B 495 ALA ASN LYS ILE ILE SER ASN GLY THR SER ALA GLY GLY
SEQRES 14 B 495 ALA LEU SER ALA LEU LEU GLY ALA SER GLY ASN SER GLN
SEQRES 15 B 495 ASP TYR LEU PRO TYR LEU LYS GLU ILE GLY ALA ALA GLU
SEQRES 16 B 495 THR ARG ASP ASP ILE PHE ALA VAL SER ALA TYR CYS PRO
SEQRES 17 B 495 ILE THR ASN LEU GLU ASN ALA ASP SER ALA TYR GLU TRP
SEQRES 18 B 495 MET TYR ASN GLY VAL ASN SER TYR SER ARG MET GLU PHE
SEQRES 19 B 495 THR ARG ASN THR SER ALA GLN GLU TYR ASN ASP ARG SER
SEQRES 20 B 495 LEU THR ARG SER THR VAL GLN GLY ASN LEU THR ASN ASP
SEQRES 21 B 495 GLU ILE ASN ILE SER ASN LYS LEU LYS THR LEU PHE PRO
SEQRES 22 B 495 ILE TYR LEU ASN SER LEU LYS LEU THR ASP ASP GLY GLY
SEQRES 23 B 495 ASN LEU LEU THR LEU ASP LYS SER GLY ASN GLY SER PHE
SEQRES 24 B 495 LYS THR TYR LEU SER ILE ILE ILE ARG ASN SER ALA ASN
SEQRES 25 B 495 ARG ALA LEU ARG GLU GLY LYS ASP ILE SER GLN PHE LYS
SEQRES 26 B 495 LYS ALA PHE THR ILE GLU ASN ASN LYS VAL VAL ALA VAL
SEQRES 27 B 495 ASN LEU ASP VAL TYR THR HIS ILE GLY ASP ARG MET LYS
SEQRES 28 B 495 SER PRO PRO ALA PHE ASP SER LEU ASP ALA SER SER GLY
SEQRES 29 B 495 GLU ASN ASN LEU PHE GLY ASP LYS LYS SER ASP SER LYS
SEQRES 30 B 495 HIS PHE THR LYS PHE SER PHE ASP ILE ASN ASN LYS ALA
SEQRES 31 B 495 ALA ILE ASP TYR PHE ARG ASN GLY LYS PHE ASN ASP LYS
SEQRES 32 B 495 ASN ASN LYS ILE SER ILE PRO LYS MET ALA ASP LYS ASN
SEQRES 33 B 495 ILE ILE LYS MET MET ASN PRO MET TYR TYR ILE ASP SER
SEQRES 34 B 495 ASN THR SER THR LYS TYR TRP ARG ILE ARG HIS GLY ALA
SEQRES 35 B 495 ILE ASP LYS ASP THR SER LEU ALA ILE PRO ALA ILE LEU
SEQRES 36 B 495 ALA LEU LYS LEU LYS ASN SER GLY LYS ILE VAL ASN PHE
SEQRES 37 B 495 ALA ALA PRO TRP GLY GLN GLY HIS GLY GLY ASP TYR ASP
SEQRES 38 B 495 LEU GLU GLU LEU PHE ASN TRP ILE ASP ASN VAL VAL LYS
SEQRES 39 B 495 LYS
SEQRES 1 C 495 MET VAL LYS ASN ASP TYR ASP LEU LYS PHE ASN PRO ASP
SEQRES 2 C 495 LYS TYR ILE SER LYS GLU ILE LYS ILE ASN GLY LYS LYS
SEQRES 3 C 495 ILE LYS TYR ARG ALA TYR GLU ASN ILE ILE TYR ILE LYS
SEQRES 4 C 495 ASN PRO ILE ASP LYS ASP TYR GLN ASN MET ASN ILE TYR
SEQRES 5 C 495 ILE PRO GLU GLU TYR PHE ASN ASN LEU SER ILE GLY SER
SEQRES 6 C 495 TYR ASN SER ASN ASN ALA PRO ILE PHE PHE PRO ASN THR
SEQRES 7 C 495 VAL GLY GLY TYR MET PRO GLY LYS ALA ASP THR VAL GLY
SEQRES 8 C 495 LEU GLY ARG ASP GLY LYS ALA ASN SER LEU THR TYR ALA
SEQRES 9 C 495 LEU SER LYS GLY TYR VAL VAL ALA ALA PRO GLY ALA ARG
SEQRES 10 C 495 GLY ARG THR LEU THR ASP ASP LYS GLY ASN TYR ILE GLY
SEQRES 11 C 495 LYS ALA PRO ALA ALA ILE VAL ASP LEU LYS ALA ALA VAL
SEQRES 12 C 495 ARG TYR LEU TYR LEU ASN ASP GLU VAL MET PRO GLY ASP
SEQRES 13 C 495 ALA ASN LYS ILE ILE SER ASN GLY THR SER ALA GLY GLY
SEQRES 14 C 495 ALA LEU SER ALA LEU LEU GLY ALA SER GLY ASN SER GLN
SEQRES 15 C 495 ASP TYR LEU PRO TYR LEU LYS GLU ILE GLY ALA ALA GLU
SEQRES 16 C 495 THR ARG ASP ASP ILE PHE ALA VAL SER ALA TYR CYS PRO
SEQRES 17 C 495 ILE THR ASN LEU GLU ASN ALA ASP SER ALA TYR GLU TRP
SEQRES 18 C 495 MET TYR ASN GLY VAL ASN SER TYR SER ARG MET GLU PHE
SEQRES 19 C 495 THR ARG ASN THR SER ALA GLN GLU TYR ASN ASP ARG SER
SEQRES 20 C 495 LEU THR ARG SER THR VAL GLN GLY ASN LEU THR ASN ASP
SEQRES 21 C 495 GLU ILE ASN ILE SER ASN LYS LEU LYS THR LEU PHE PRO
SEQRES 22 C 495 ILE TYR LEU ASN SER LEU LYS LEU THR ASP ASP GLY GLY
SEQRES 23 C 495 ASN LEU LEU THR LEU ASP LYS SER GLY ASN GLY SER PHE
SEQRES 24 C 495 LYS THR TYR LEU SER ILE ILE ILE ARG ASN SER ALA ASN
SEQRES 25 C 495 ARG ALA LEU ARG GLU GLY LYS ASP ILE SER GLN PHE LYS
SEQRES 26 C 495 LYS ALA PHE THR ILE GLU ASN ASN LYS VAL VAL ALA VAL
SEQRES 27 C 495 ASN LEU ASP VAL TYR THR HIS ILE GLY ASP ARG MET LYS
SEQRES 28 C 495 SER PRO PRO ALA PHE ASP SER LEU ASP ALA SER SER GLY
SEQRES 29 C 495 GLU ASN ASN LEU PHE GLY ASP LYS LYS SER ASP SER LYS
SEQRES 30 C 495 HIS PHE THR LYS PHE SER PHE ASP ILE ASN ASN LYS ALA
SEQRES 31 C 495 ALA ILE ASP TYR PHE ARG ASN GLY LYS PHE ASN ASP LYS
SEQRES 32 C 495 ASN ASN LYS ILE SER ILE PRO LYS MET ALA ASP LYS ASN
SEQRES 33 C 495 ILE ILE LYS MET MET ASN PRO MET TYR TYR ILE ASP SER
SEQRES 34 C 495 ASN THR SER THR LYS TYR TRP ARG ILE ARG HIS GLY ALA
SEQRES 35 C 495 ILE ASP LYS ASP THR SER LEU ALA ILE PRO ALA ILE LEU
SEQRES 36 C 495 ALA LEU LYS LEU LYS ASN SER GLY LYS ILE VAL ASN PHE
SEQRES 37 C 495 ALA ALA PRO TRP GLY GLN GLY HIS GLY GLY ASP TYR ASP
SEQRES 38 C 495 LEU GLU GLU LEU PHE ASN TRP ILE ASP ASN VAL VAL LYS
SEQRES 39 C 495 LYS
HET GOL A 501 6
HET MG A 502 1
HET GOL B 501 6
HET SPD B 502 10
HET MG B 503 1
HET GOL C 501 6
HET MG C 502 1
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETNAM SPD SPERMIDINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN SPD N-(2-AMINO-PROPYL)-1,4-DIAMINOBUTANE; PA(34)
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 5 MG 3(MG 2+)
FORMUL 7 SPD C7 H19 N3
FORMUL 11 HOH *407(H2 O)
HELIX 1 AA1 GLU A 56 ASN A 59 5 4
HELIX 2 AA2 ASN A 99 LYS A 107 1 9
HELIX 3 AA3 PRO A 133 ASN A 149 1 17
HELIX 4 AA4 SER A 166 SER A 178 1 13
HELIX 5 AA5 SER A 181 ASP A 183 5 3
HELIX 6 AA6 TYR A 184 GLY A 192 1 9
HELIX 7 AA7 ASN A 211 ASN A 224 1 14
HELIX 8 AA8 SER A 239 ASP A 245 1 7
HELIX 9 AA9 THR A 258 LYS A 280 1 23
HELIX 10 AB1 GLY A 297 GLU A 317 1 21
HELIX 11 AB2 ILE A 321 LYS A 326 5 6
HELIX 12 AB3 ASN A 339 HIS A 345 1 7
HELIX 13 AB4 SER A 363 PHE A 369 1 7
HELIX 14 AB5 THR A 380 PHE A 395 1 16
HELIX 15 AB6 ASP A 414 MET A 421 1 8
HELIX 16 AB7 ASN A 422 TYR A 426 5 5
HELIX 17 AB8 LEU A 449 SER A 462 1 14
HELIX 18 AB9 ASP A 481 LYS A 494 1 14
HELIX 19 AC1 GLU B 56 ASN B 59 5 4
HELIX 20 AC2 ASN B 99 LYS B 107 1 9
HELIX 21 AC3 PRO B 133 ASN B 149 1 17
HELIX 22 AC4 SER B 166 SER B 178 1 13
HELIX 23 AC5 SER B 181 ASP B 183 5 3
HELIX 24 AC6 TYR B 184 GLY B 192 1 9
HELIX 25 AC7 ASN B 211 ASN B 224 1 14
HELIX 26 AC8 SER B 239 ASP B 245 1 7
HELIX 27 AC9 ARG B 246 THR B 249 5 4
HELIX 28 AD1 THR B 258 LEU B 279 1 22
HELIX 29 AD2 GLY B 297 GLU B 317 1 21
HELIX 30 AD3 ILE B 321 LYS B 326 5 6
HELIX 31 AD4 ASN B 339 THR B 344 1 6
HELIX 32 AD5 HIS B 345 GLY B 347 5 3
HELIX 33 AD6 SER B 363 PHE B 369 1 7
HELIX 34 AD7 THR B 380 TYR B 394 1 15
HELIX 35 AD8 ASP B 414 ASN B 422 1 9
HELIX 36 AD9 PRO B 423 TYR B 426 5 4
HELIX 37 AE1 LEU B 449 SER B 462 1 14
HELIX 38 AE2 ASP B 481 LYS B 494 1 14
HELIX 39 AE3 GLU C 56 ASN C 59 5 4
HELIX 40 AE4 ASN C 99 GLY C 108 1 10
HELIX 41 AE5 PRO C 133 ASP C 150 1 18
HELIX 42 AE6 SER C 166 SER C 178 1 13
HELIX 43 AE7 SER C 181 ASP C 183 5 3
HELIX 44 AE8 TYR C 184 ILE C 191 1 8
HELIX 45 AE9 ASN C 211 ASN C 224 1 14
HELIX 46 AF1 SER C 239 ARG C 246 1 8
HELIX 47 AF2 THR C 258 LEU C 279 1 22
HELIX 48 AF3 GLY C 297 GLU C 317 1 21
HELIX 49 AF4 ILE C 321 LYS C 326 5 6
HELIX 50 AF5 ASN C 339 HIS C 345 1 7
HELIX 51 AF6 SER C 363 PHE C 369 1 7
HELIX 52 AF7 THR C 380 ASP C 393 1 14
HELIX 53 AF8 ASP C 414 MET C 421 1 8
HELIX 54 AF9 ASN C 422 TYR C 426 5 5
HELIX 55 AG1 LEU C 449 SER C 462 1 14
HELIX 56 AG2 ASP C 481 VAL C 493 1 13
SHEET 1 AA1 9 ILE A 16 LYS A 21 0
SHEET 2 AA1 9 LYS A 26 ILE A 36 -1 O ILE A 27 N ILE A 20
SHEET 3 AA1 9 ASN A 48 PRO A 54 -1 O ILE A 51 N TYR A 32
SHEET 4 AA1 9 VAL A 110 PRO A 114 -1 O VAL A 111 N TYR A 52
SHEET 5 AA1 9 ILE A 73 PRO A 76 1 N PHE A 74 O VAL A 110
SHEET 6 AA1 9 ILE A 160 ASN A 163 1 O ILE A 161 N PHE A 75
SHEET 7 AA1 9 ALA A 202 TYR A 206 1 O ALA A 202 N SER A 162
SHEET 8 AA1 9 TYR A 435 ARG A 439 1 O ARG A 437 N ALA A 205
SHEET 9 AA1 9 ILE A 465 ALA A 469 1 O ASN A 467 N TRP A 436
SHEET 1 AA2 2 SER A 228 MET A 232 0
SHEET 2 AA2 2 THR A 252 ASN A 256 -1 O VAL A 253 N ARG A 231
SHEET 1 AA3 2 PHE A 328 ILE A 330 0
SHEET 2 AA3 2 VAL A 335 VAL A 338 -1 O VAL A 336 N THR A 329
SHEET 1 AA4 9 ILE B 16 LYS B 21 0
SHEET 2 AA4 9 LYS B 26 ILE B 36 -1 O ALA B 31 N ILE B 16
SHEET 3 AA4 9 ASN B 48 PRO B 54 -1 O MET B 49 N ILE B 35
SHEET 4 AA4 9 VAL B 110 PRO B 114 -1 O ALA B 113 N ASN B 50
SHEET 5 AA4 9 ILE B 73 PRO B 76 1 N PHE B 74 O ALA B 112
SHEET 6 AA4 9 ILE B 160 ASN B 163 1 O ILE B 161 N ILE B 73
SHEET 7 AA4 9 ALA B 202 TYR B 206 1 O SER B 204 N SER B 162
SHEET 8 AA4 9 TYR B 435 ARG B 439 1 O ARG B 437 N VAL B 203
SHEET 9 AA4 9 ILE B 465 ALA B 469 1 O ASN B 467 N TRP B 436
SHEET 1 AA5 2 LEU B 92 GLY B 93 0
SHEET 2 AA5 2 LYS B 97 ALA B 98 -1 O LYS B 97 N GLY B 93
SHEET 1 AA6 2 SER B 228 ARG B 231 0
SHEET 2 AA6 2 VAL B 253 ASN B 256 -1 O VAL B 253 N ARG B 231
SHEET 1 AA7 2 PHE B 328 ILE B 330 0
SHEET 2 AA7 2 VAL B 335 VAL B 338 -1 O VAL B 336 N THR B 329
SHEET 1 AA8 9 ILE C 16 LYS C 21 0
SHEET 2 AA8 9 LYS C 26 ILE C 36 -1 O TYR C 29 N LYS C 18
SHEET 3 AA8 9 ASN C 48 PRO C 54 -1 O ILE C 51 N TYR C 32
SHEET 4 AA8 9 VAL C 110 PRO C 114 -1 O ALA C 113 N ASN C 50
SHEET 5 AA8 9 ILE C 73 PRO C 76 1 N PHE C 74 O VAL C 110
SHEET 6 AA8 9 ILE C 160 ASN C 163 1 O ILE C 161 N ILE C 73
SHEET 7 AA8 9 ALA C 202 TYR C 206 1 O SER C 204 N SER C 162
SHEET 8 AA8 9 TYR C 435 ARG C 439 1 O ARG C 437 N VAL C 203
SHEET 9 AA8 9 ILE C 465 ALA C 469 1 O ASN C 467 N TRP C 436
SHEET 1 AA9 2 SER C 228 ARG C 231 0
SHEET 2 AA9 2 VAL C 253 ASN C 256 -1 O VAL C 253 N ARG C 231
SHEET 1 AB1 2 PHE C 328 ILE C 330 0
SHEET 2 AB1 2 VAL C 335 VAL C 338 -1 O VAL C 336 N THR C 329
LINK O ASP A 150 MG MG A 502 1555 1555 2.52
LINK OD2 ASP A 150 MG MG A 502 1555 1555 2.43
LINK O MET A 153 MG MG A 502 1555 1555 2.29
LINK O GLY A 155 MG MG A 502 1555 1555 2.10
LINK MG MG A 502 O HOH A 676 1555 1555 2.66
LINK MG MG A 502 O HOH A 759 1555 1555 2.81
LINK O ASP B 150 MG MG B 503 1555 1555 2.49
LINK OD2 ASP B 150 MG MG B 503 1555 1555 2.18
LINK O MET B 153 MG MG B 503 1555 1555 2.41
LINK O GLY B 155 MG MG B 503 1555 1555 2.19
LINK MG MG B 503 O HOH B 680 1555 1555 2.68
LINK MG MG B 503 O HOH B 685 1555 1555 2.87
LINK O ASP C 150 MG MG C 502 1555 1555 2.47
LINK OD2 ASP C 150 MG MG C 502 1555 1555 2.56
LINK O MET C 153 MG MG C 502 1555 1555 2.37
LINK O GLY C 155 MG MG C 502 1555 1555 2.42
CISPEP 1 ALA A 132 PRO A 133 0 5.90
CISPEP 2 PRO A 353 PRO A 354 0 -2.85
CISPEP 3 ALA B 132 PRO B 133 0 -1.46
CISPEP 4 PRO B 353 PRO B 354 0 -3.99
CISPEP 5 ALA C 132 PRO C 133 0 -1.24
CISPEP 6 PRO C 353 PRO C 354 0 -11.20
SITE 1 AC1 5 GLY A 81 TYR A 82 LYS A 351 GLU A 365
SITE 2 AC1 5 ASP A 446
SITE 1 AC2 6 ASP A 150 MET A 153 PRO A 154 GLY A 155
SITE 2 AC2 6 HOH A 676 HOH A 759
SITE 1 AC3 6 GLY B 81 TYR B 243 LYS B 351 GLU B 365
SITE 2 AC3 6 ASP B 446 SPD B 502
SITE 1 AC4 8 ARG B 231 SER B 352 ALA B 355 GLY B 364
SITE 2 AC4 8 GLU B 365 GOL B 501 HOH B 604 HOH B 626
SITE 1 AC5 5 ASP B 150 MET B 153 GLY B 155 HOH B 680
SITE 2 AC5 5 HOH B 685
SITE 1 AC6 4 GLY C 81 LYS C 351 GLU C 365 ASP C 446
SITE 1 AC7 3 ASP C 150 MET C 153 GLY C 155
CRYST1 71.840 91.067 124.068 90.00 101.70 90.00 P 1 21 1 6
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 0.013920 0.000000 0.002882 0.00000
SCALE2 0.000000 0.010981 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008231 0.00000
TER 3753 LYS A 494
TER 7517 LYS B 494
TER 11267 LYS C 494
MASTER 627 0 7 56 41 0 12 611686 3 49 117
END
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