HEADER TRANSFERASE 15-FEB-15 5AIK
TITLE HUMAN DYRK1A IN COMPLEX WITH LDN-211898
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DYRK1A DUAL-SPECIFICITY TYROSINE-PHOSPHORYLATION REGULATED
COMPND 3 KINASE 1A;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 128-485;
COMPND 6 SYNONYM: DUAL SPECIFICITY YAK1-RELATED KINASE, HP86, PROTEIN KINASE
COMPND 7 MINIBRAIN HOMOLOG, MNBH, HMNB;
COMPND 8 EC: 2.7.11.1;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS TRANSFERASE, DYRK1A, KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.ELKINS,M.SOUNDARARAJAN,J.R.C.MUNIZ,G.CUNY,J.HIGGINS,A.EDWARDS,
AUTHOR 2 C.BOUNTRA,S.KNAPP
REVDAT 4 10-JAN-24 5AIK 1 REMARK
REVDAT 3 07-JUL-21 5AIK 1 REMARK LINK
REVDAT 2 12-DEC-18 5AIK 1 JRNL
REVDAT 1 25-FEB-15 5AIK 0
JRNL AUTH J.M.ELKINS,M.SOUNDARARAJAN,J.R.C.MUNIZ,G.CUNY,J.HIGGINS,
JRNL AUTH 2 A.EDWARDS,C.BOUNTRA,S.KNAPP
JRNL TITL DYRK1A WITH LDN-211898
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 116.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 49699
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2665
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3599
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.3270
REMARK 3 BIN FREE R VALUE SET COUNT : 195
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11111
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 146
REMARK 3 SOLVENT ATOMS : 64
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.67000
REMARK 3 B22 (A**2) : -0.66000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.003
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.333
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.288
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.149
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.903
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11519 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10913 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15592 ; 1.443 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25054 ; 1.227 ; 2.991
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1366 ; 7.988 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 537 ;35.835 ;23.966
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2001 ;14.699 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 66 ;17.365 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1658 ; 0.210 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12880 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2714 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5488 ; 0.613 ; 1.859
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5487 ; 0.613 ; 1.859
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6846 ; 1.119 ; 2.784
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6031 ; 0.561 ; 1.954
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 134 481 B 134 481 42982 0.04 0.05
REMARK 3 2 A 134 481 C 134 481 43248 0.04 0.05
REMARK 3 3 A 134 480 D 134 480 43128 0.05 0.05
REMARK 3 4 B 134 481 C 134 481 43142 0.04 0.05
REMARK 3 5 B 134 480 D 134 480 42838 0.04 0.05
REMARK 3 6 C 134 480 D 134 480 43058 0.05 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 134 A 241
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3360 29.5620 38.9260
REMARK 3 T TENSOR
REMARK 3 T11: 0.1154 T22: 0.1328
REMARK 3 T33: 0.0903 T12: -0.0077
REMARK 3 T13: 0.0597 T23: 0.0751
REMARK 3 L TENSOR
REMARK 3 L11: 0.9088 L22: 2.4610
REMARK 3 L33: 3.7257 L12: 0.1009
REMARK 3 L13: -0.0097 L23: -0.3390
REMARK 3 S TENSOR
REMARK 3 S11: 0.0513 S12: -0.2774 S13: -0.1178
REMARK 3 S21: 0.1267 S22: -0.1020 S23: -0.1230
REMARK 3 S31: -0.0021 S32: 0.2209 S33: 0.0506
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 242 A 481
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9470 24.7940 9.4600
REMARK 3 T TENSOR
REMARK 3 T11: 0.1194 T22: 0.0253
REMARK 3 T33: 0.0611 T12: 0.0337
REMARK 3 T13: 0.0407 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 1.2399 L22: 2.7265
REMARK 3 L33: 2.6393 L12: 0.5028
REMARK 3 L13: -0.2771 L23: -0.1094
REMARK 3 S TENSOR
REMARK 3 S11: 0.0154 S12: 0.0775 S13: -0.1008
REMARK 3 S21: -0.2685 S22: -0.1265 S23: 0.0371
REMARK 3 S31: 0.1406 S32: -0.1129 S33: 0.1111
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 134 B 241
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6070 9.1990 77.3830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1530 T22: 0.0835
REMARK 3 T33: 0.2410 T12: 0.0900
REMARK 3 T13: 0.1616 T23: 0.1009
REMARK 3 L TENSOR
REMARK 3 L11: 3.3600 L22: 3.6782
REMARK 3 L33: 4.4475 L12: 0.0116
REMARK 3 L13: 0.3781 L23: -0.7798
REMARK 3 S TENSOR
REMARK 3 S11: -0.0910 S12: 0.1656 S13: -0.1995
REMARK 3 S21: -0.2375 S22: -0.1512 S23: -0.3899
REMARK 3 S31: 0.2606 S32: 0.4104 S33: 0.2423
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 242 B 481
REMARK 3 ORIGIN FOR THE GROUP (A): -8.2690 27.0030 60.7310
REMARK 3 T TENSOR
REMARK 3 T11: 0.1400 T22: 0.0686
REMARK 3 T33: 0.0777 T12: 0.0068
REMARK 3 T13: 0.0706 T23: 0.0412
REMARK 3 L TENSOR
REMARK 3 L11: 1.3920 L22: 1.4086
REMARK 3 L33: 3.0710 L12: -0.0960
REMARK 3 L13: -0.3509 L23: -0.4636
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: 0.1266 S13: 0.0438
REMARK 3 S21: 0.0080 S22: -0.0016 S23: 0.0668
REMARK 3 S31: -0.1908 S32: -0.1645 S33: 0.0018
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 134 C 241
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9440 74.9170 19.8820
REMARK 3 T TENSOR
REMARK 3 T11: 0.0678 T22: 0.0145
REMARK 3 T33: 0.0751 T12: -0.0036
REMARK 3 T13: 0.0249 T23: -0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 1.6220 L22: 5.1446
REMARK 3 L33: 2.9176 L12: -0.1983
REMARK 3 L13: -0.0725 L23: 0.4993
REMARK 3 S TENSOR
REMARK 3 S11: 0.0986 S12: 0.0457 S13: -0.0481
REMARK 3 S21: 0.0076 S22: 0.0571 S23: -0.1064
REMARK 3 S31: -0.0984 S32: 0.1484 S33: -0.1557
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 242 C 481
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8310 55.5860 3.5040
REMARK 3 T TENSOR
REMARK 3 T11: 0.2207 T22: 0.2216
REMARK 3 T33: 0.3031 T12: 0.0638
REMARK 3 T13: -0.1098 T23: -0.2331
REMARK 3 L TENSOR
REMARK 3 L11: 2.3401 L22: 1.7876
REMARK 3 L33: 1.8600 L12: 0.2763
REMARK 3 L13: -0.1694 L23: 0.4504
REMARK 3 S TENSOR
REMARK 3 S11: -0.0219 S12: 0.4875 S13: -0.3162
REMARK 3 S21: -0.2894 S22: -0.3012 S23: 0.4541
REMARK 3 S31: -0.0413 S32: -0.3480 S33: 0.3231
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 134 D 241
REMARK 3 ORIGIN FOR THE GROUP (A): 36.4240 50.9640 18.6470
REMARK 3 T TENSOR
REMARK 3 T11: 0.2400 T22: 0.1071
REMARK 3 T33: 0.1414 T12: -0.0616
REMARK 3 T13: 0.1294 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 2.5573 L22: 2.2410
REMARK 3 L33: 2.4187 L12: 1.3016
REMARK 3 L13: 0.6013 L23: 1.2772
REMARK 3 S TENSOR
REMARK 3 S11: -0.0272 S12: -0.0811 S13: 0.0640
REMARK 3 S21: -0.3316 S22: 0.0890 S23: -0.1415
REMARK 3 S31: -0.4084 S32: 0.0651 S33: -0.0618
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 242 D 480
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0510 57.0620 47.9760
REMARK 3 T TENSOR
REMARK 3 T11: 0.1804 T22: 0.4659
REMARK 3 T33: 0.2136 T12: -0.0620
REMARK 3 T13: 0.0586 T23: -0.1634
REMARK 3 L TENSOR
REMARK 3 L11: 1.7659 L22: 2.3112
REMARK 3 L33: 3.0237 L12: -0.1520
REMARK 3 L13: 0.4751 L23: -0.3213
REMARK 3 S TENSOR
REMARK 3 S11: -0.0261 S12: -0.6208 S13: 0.0201
REMARK 3 S21: 0.2103 S22: 0.2245 S23: -0.3454
REMARK 3 S31: -0.2424 S32: 0.1078 S33: -0.1984
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 5AIK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1290053296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9245
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PIXEL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52473
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 45.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.18000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: PDB ENTRY 2VX3
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NA/KPO4, 20% PEG 3350, 10%
REMARK 280 ETHYLENE GLYCOL, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 44.97750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 116.23400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.44550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 116.23400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.97750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.44550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
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: 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 350
REMARK 350 BIOMOLECULE: 4
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: 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 MET A 104
REMARK 465 HIS A 105
REMARK 465 HIS A 106
REMARK 465 HIS A 107
REMARK 465 HIS A 108
REMARK 465 HIS A 109
REMARK 465 HIS A 110
REMARK 465 SER A 111
REMARK 465 SER A 112
REMARK 465 GLY A 113
REMARK 465 VAL A 114
REMARK 465 ASP A 115
REMARK 465 LEU A 116
REMARK 465 GLY A 117
REMARK 465 THR A 118
REMARK 465 GLU A 119
REMARK 465 ASN A 120
REMARK 465 LEU A 121
REMARK 465 TYR A 122
REMARK 465 PHE A 123
REMARK 465 GLN A 124
REMARK 465 SER A 125
REMARK 465 MET A 126
REMARK 465 SER A 127
REMARK 465 SER A 128
REMARK 465 HIS A 129
REMARK 465 LYS A 130
REMARK 465 LYS A 131
REMARK 465 GLU A 132
REMARK 465 ARG A 133
REMARK 465 LYS A 409
REMARK 465 ASP A 410
REMARK 465 GLY A 411
REMARK 465 THR A 482
REMARK 465 ALA A 483
REMARK 465 ASP A 484
REMARK 465 GLU A 485
REMARK 465 MET B 104
REMARK 465 HIS B 105
REMARK 465 HIS B 106
REMARK 465 HIS B 107
REMARK 465 HIS B 108
REMARK 465 HIS B 109
REMARK 465 HIS B 110
REMARK 465 SER B 111
REMARK 465 SER B 112
REMARK 465 GLY B 113
REMARK 465 VAL B 114
REMARK 465 ASP B 115
REMARK 465 LEU B 116
REMARK 465 GLY B 117
REMARK 465 THR B 118
REMARK 465 GLU B 119
REMARK 465 ASN B 120
REMARK 465 LEU B 121
REMARK 465 TYR B 122
REMARK 465 PHE B 123
REMARK 465 GLN B 124
REMARK 465 SER B 125
REMARK 465 MET B 126
REMARK 465 SER B 127
REMARK 465 SER B 128
REMARK 465 HIS B 129
REMARK 465 LYS B 130
REMARK 465 LYS B 131
REMARK 465 GLU B 132
REMARK 465 ARG B 133
REMARK 465 LYS B 409
REMARK 465 ASP B 410
REMARK 465 GLY B 411
REMARK 465 LYS B 412
REMARK 465 ARG B 413
REMARK 465 THR B 482
REMARK 465 ALA B 483
REMARK 465 ASP B 484
REMARK 465 GLU B 485
REMARK 465 MET C 104
REMARK 465 HIS C 105
REMARK 465 HIS C 106
REMARK 465 HIS C 107
REMARK 465 HIS C 108
REMARK 465 HIS C 109
REMARK 465 HIS C 110
REMARK 465 SER C 111
REMARK 465 SER C 112
REMARK 465 GLY C 113
REMARK 465 VAL C 114
REMARK 465 ASP C 115
REMARK 465 LEU C 116
REMARK 465 GLY C 117
REMARK 465 THR C 118
REMARK 465 GLU C 119
REMARK 465 ASN C 120
REMARK 465 LEU C 121
REMARK 465 TYR C 122
REMARK 465 PHE C 123
REMARK 465 GLN C 124
REMARK 465 SER C 125
REMARK 465 MET C 126
REMARK 465 SER C 127
REMARK 465 SER C 128
REMARK 465 HIS C 129
REMARK 465 LYS C 130
REMARK 465 LYS C 131
REMARK 465 GLU C 132
REMARK 465 ARG C 133
REMARK 465 LYS C 409
REMARK 465 ASP C 410
REMARK 465 GLY C 411
REMARK 465 LYS C 412
REMARK 465 ARG C 413
REMARK 465 THR C 482
REMARK 465 ALA C 483
REMARK 465 ASP C 484
REMARK 465 GLU C 485
REMARK 465 MET D 104
REMARK 465 HIS D 105
REMARK 465 HIS D 106
REMARK 465 HIS D 107
REMARK 465 HIS D 108
REMARK 465 HIS D 109
REMARK 465 HIS D 110
REMARK 465 SER D 111
REMARK 465 SER D 112
REMARK 465 GLY D 113
REMARK 465 VAL D 114
REMARK 465 ASP D 115
REMARK 465 LEU D 116
REMARK 465 GLY D 117
REMARK 465 THR D 118
REMARK 465 GLU D 119
REMARK 465 ASN D 120
REMARK 465 LEU D 121
REMARK 465 TYR D 122
REMARK 465 PHE D 123
REMARK 465 GLN D 124
REMARK 465 SER D 125
REMARK 465 MET D 126
REMARK 465 SER D 127
REMARK 465 SER D 128
REMARK 465 HIS D 129
REMARK 465 LYS D 130
REMARK 465 LYS D 131
REMARK 465 GLU D 132
REMARK 465 ARG D 133
REMARK 465 ASP D 410
REMARK 465 GLY D 411
REMARK 465 LYS D 412
REMARK 465 ARG D 413
REMARK 465 LYS D 481
REMARK 465 THR D 482
REMARK 465 ALA D 483
REMARK 465 ASP D 484
REMARK 465 GLU D 485
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 150 NZ
REMARK 470 LYS A 193 CD CE NZ
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 ARG A 250 NE CZ NH1 NH2
REMARK 470 LYS A 299 CG CD CE NZ
REMARK 470 LYS A 407 CG CD CE NZ
REMARK 470 LYS A 412 CG CD CE NZ
REMARK 470 ARG A 413 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 480 CD CE NZ
REMARK 470 LYS A 481 CG CD CE NZ
REMARK 470 LYS B 134 CG CD CE NZ
REMARK 470 LYS B 150 CE NZ
REMARK 470 LYS B 154 CG CD CE NZ
REMARK 470 LYS B 167 CE NZ
REMARK 470 LYS B 212 CE NZ
REMARK 470 GLU B 216 CG CD OE1 OE2
REMARK 470 GLN B 316 CD OE1 NE2
REMARK 470 LYS B 397 CE NZ
REMARK 470 LYS B 407 CG CD CE NZ
REMARK 470 GLU B 414 CG CD OE1 OE2
REMARK 470 LYS B 416 CE NZ
REMARK 470 LYS B 465 NZ
REMARK 470 LYS B 480 CD CE NZ
REMARK 470 LYS B 481 CG CD CE NZ
REMARK 470 LYS C 134 CG CD CE NZ
REMARK 470 LYS C 150 CE NZ
REMARK 470 LYS C 212 CE NZ
REMARK 470 ARG C 255 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 317 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 407 CG CD CE NZ
REMARK 470 LYS C 416 CD CE NZ
REMARK 470 LYS C 480 CD CE NZ
REMARK 470 LYS C 481 CG CD CE NZ
REMARK 470 LYS D 134 CG CD CE NZ
REMARK 470 LYS D 154 CG CD CE NZ
REMARK 470 ARG D 179 NE CZ NH1 NH2
REMARK 470 LYS D 194 CE NZ
REMARK 470 GLU D 216 CG CD OE1 OE2
REMARK 470 ARG D 250 NE CZ NH1 NH2
REMARK 470 GLN D 316 CD OE1 NE2
REMARK 470 ARG D 317 NE CZ NH1 NH2
REMARK 470 LYS D 406 CE NZ
REMARK 470 LYS D 407 CG CD CE NZ
REMARK 470 LYS D 409 CG CD CE NZ
REMARK 470 LYS D 480 CE NZ
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 ARG A 458 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 317 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 179 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG D 458 NE - CZ - NH1 ANGL. DEV. = 3.0 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 ASP A 138 -127.71 57.06
REMARK 500 ASP A 143 9.15 -68.54
REMARK 500 ARG A 158 -55.59 -153.75
REMARK 500 PHE A 170 -73.39 62.70
REMARK 500 SER A 242 -149.15 -99.70
REMARK 500 LEU A 281 -65.19 -95.89
REMARK 500 ASP A 287 42.09 -165.52
REMARK 500 ASP A 307 89.37 68.96
REMARK 500 ILE A 318 -62.30 -108.14
REMARK 500 GLN A 323 139.90 72.45
REMARK 500 GLU A 414 -58.10 -135.82
REMARK 500 HIS A 444 42.08 -143.64
REMARK 500 ASP B 138 -127.82 58.73
REMARK 500 ASP B 143 9.76 -69.25
REMARK 500 ARG B 158 -54.54 -153.92
REMARK 500 PHE B 170 -72.40 62.33
REMARK 500 SER B 242 -148.91 -99.25
REMARK 500 LEU B 281 -63.95 -96.49
REMARK 500 ASP B 287 40.36 -164.92
REMARK 500 ASP B 307 88.91 67.89
REMARK 500 ILE B 318 -62.73 -98.39
REMARK 500 GLN B 323 141.73 73.88
REMARK 500 PRO B 418 116.53 -37.61
REMARK 500 ASP C 138 -128.07 59.27
REMARK 500 ASP C 143 9.86 -69.44
REMARK 500 ARG C 158 -54.24 -155.43
REMARK 500 PHE C 170 -73.07 63.13
REMARK 500 SER C 242 -149.69 -98.88
REMARK 500 LEU C 281 -65.43 -97.16
REMARK 500 ASP C 287 40.12 -163.42
REMARK 500 ASP C 307 87.60 69.38
REMARK 500 ARG C 317 14.43 51.85
REMARK 500 GLN C 323 141.71 71.77
REMARK 500 ASP D 138 -128.69 58.57
REMARK 500 ASP D 143 8.59 -69.18
REMARK 500 ARG D 158 -54.07 -153.65
REMARK 500 PHE D 170 -74.02 63.48
REMARK 500 SER D 242 -148.73 -97.38
REMARK 500 LEU D 281 -64.73 -96.77
REMARK 500 ASP D 287 41.35 -164.39
REMARK 500 ASP D 307 87.65 68.79
REMARK 500 GLN D 323 141.73 72.86
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 GLY A 139 TYR A 140 -99.61
REMARK 500 SER A 169 PHE A 170 59.24
REMARK 500 GLY B 139 TYR B 140 -99.26
REMARK 500 SER B 169 PHE B 170 59.06
REMARK 500 GLY C 139 TYR C 140 -121.71
REMARK 500 SER C 169 PHE C 170 57.87
REMARK 500 GLY D 139 TYR D 140 -120.94
REMARK 500 SER D 169 PHE D 170 58.05
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 AWR A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AWR B 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AWR C 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AWR D 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1485
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1484
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AIL RELATED DB: PDB
REMARK 900 HUMAN PARP9 2ND MACRODOMAIN
DBREF 5AIK A 128 485 UNP Q13627 DYR1A_HUMAN 128 485
DBREF 5AIK B 128 485 UNP Q13627 DYR1A_HUMAN 128 485
DBREF 5AIK C 128 485 UNP Q13627 DYR1A_HUMAN 128 485
DBREF 5AIK D 128 485 UNP Q13627 DYR1A_HUMAN 128 485
SEQADV 5AIK MET A 104 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS A 105 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS A 106 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS A 107 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS A 108 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS A 109 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS A 110 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER A 111 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER A 112 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLY A 113 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK VAL A 114 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK ASP A 115 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK LEU A 116 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLY A 117 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK THR A 118 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLU A 119 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK ASN A 120 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK LEU A 121 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK TYR A 122 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK PHE A 123 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLN A 124 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER A 125 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK MET A 126 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER A 127 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK MET B 104 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS B 105 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS B 106 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS B 107 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS B 108 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS B 109 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS B 110 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER B 111 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER B 112 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLY B 113 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK VAL B 114 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK ASP B 115 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK LEU B 116 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLY B 117 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK THR B 118 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLU B 119 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK ASN B 120 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK LEU B 121 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK TYR B 122 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK PHE B 123 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLN B 124 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER B 125 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK MET B 126 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER B 127 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK MET C 104 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS C 105 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS C 106 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS C 107 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS C 108 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS C 109 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS C 110 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER C 111 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER C 112 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLY C 113 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK VAL C 114 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK ASP C 115 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK LEU C 116 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLY C 117 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK THR C 118 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLU C 119 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK ASN C 120 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK LEU C 121 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK TYR C 122 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK PHE C 123 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLN C 124 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER C 125 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK MET C 126 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER C 127 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK MET D 104 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS D 105 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS D 106 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS D 107 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS D 108 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS D 109 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK HIS D 110 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER D 111 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER D 112 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLY D 113 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK VAL D 114 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK ASP D 115 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK LEU D 116 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLY D 117 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK THR D 118 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLU D 119 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK ASN D 120 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK LEU D 121 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK TYR D 122 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK PHE D 123 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK GLN D 124 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER D 125 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK MET D 126 UNP Q13627 EXPRESSION TAG
SEQADV 5AIK SER D 127 UNP Q13627 EXPRESSION TAG
SEQRES 1 A 382 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 382 GLY THR GLU ASN LEU TYR PHE GLN SER MET SER SER HIS
SEQRES 3 A 382 LYS LYS GLU ARG LYS VAL TYR ASN ASP GLY TYR ASP ASP
SEQRES 4 A 382 ASP ASN TYR ASP TYR ILE VAL LYS ASN GLY GLU LYS TRP
SEQRES 5 A 382 MET ASP ARG TYR GLU ILE ASP SER LEU ILE GLY LYS GLY
SEQRES 6 A 382 SER PHE GLY GLN VAL VAL LYS ALA TYR ASP ARG VAL GLU
SEQRES 7 A 382 GLN GLU TRP VAL ALA ILE LYS ILE ILE LYS ASN LYS LYS
SEQRES 8 A 382 ALA PHE LEU ASN GLN ALA GLN ILE GLU VAL ARG LEU LEU
SEQRES 9 A 382 GLU LEU MET ASN LYS HIS ASP THR GLU MET LYS TYR TYR
SEQRES 10 A 382 ILE VAL HIS LEU LYS ARG HIS PHE MET PHE ARG ASN HIS
SEQRES 11 A 382 LEU CYS LEU VAL PHE GLU MET LEU SER TYR ASN LEU TYR
SEQRES 12 A 382 ASP LEU LEU ARG ASN THR ASN PHE ARG GLY VAL SER LEU
SEQRES 13 A 382 ASN LEU THR ARG LYS PHE ALA GLN GLN MET CYS THR ALA
SEQRES 14 A 382 LEU LEU PHE LEU ALA THR PRO GLU LEU SER ILE ILE HIS
SEQRES 15 A 382 CYS ASP LEU LYS PRO GLU ASN ILE LEU LEU CYS ASN PRO
SEQRES 16 A 382 LYS ARG SER ALA ILE LYS ILE VAL ASP PHE GLY SER SER
SEQRES 17 A 382 CYS GLN LEU GLY GLN ARG ILE TYR GLN PTR ILE GLN SER
SEQRES 18 A 382 ARG PHE TYR ARG SER PRO GLU VAL LEU LEU GLY MET PRO
SEQRES 19 A 382 TYR ASP LEU ALA ILE ASP MET TRP SER LEU GLY CYS ILE
SEQRES 20 A 382 LEU VAL GLU MET HIS THR GLY GLU PRO LEU PHE SER GLY
SEQRES 21 A 382 ALA ASN GLU VAL ASP GLN MET ASN LYS ILE VAL GLU VAL
SEQRES 22 A 382 LEU GLY ILE PRO PRO ALA HIS ILE LEU ASP GLN ALA PRO
SEQRES 23 A 382 LYS ALA ARG LYS PHE PHE GLU LYS LEU PRO ASP GLY THR
SEQRES 24 A 382 TRP ASN LEU LYS LYS THR LYS ASP GLY LYS ARG GLU TYR
SEQRES 25 A 382 LYS PRO PRO GLY THR ARG LYS LEU HIS ASN ILE LEU GLY
SEQRES 26 A 382 VAL GLU THR GLY GLY PRO GLY GLY ARG ARG ALA GLY GLU
SEQRES 27 A 382 SER GLY HIS THR VAL ALA ASP TYR LEU LYS PHE LYS ASP
SEQRES 28 A 382 LEU ILE LEU ARG MET LEU ASP TYR ASP PRO LYS THR ARG
SEQRES 29 A 382 ILE GLN PRO TYR TYR ALA LEU GLN HIS SER PHE PHE LYS
SEQRES 30 A 382 LYS THR ALA ASP GLU
SEQRES 1 B 382 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 382 GLY THR GLU ASN LEU TYR PHE GLN SER MET SER SER HIS
SEQRES 3 B 382 LYS LYS GLU ARG LYS VAL TYR ASN ASP GLY TYR ASP ASP
SEQRES 4 B 382 ASP ASN TYR ASP TYR ILE VAL LYS ASN GLY GLU LYS TRP
SEQRES 5 B 382 MET ASP ARG TYR GLU ILE ASP SER LEU ILE GLY LYS GLY
SEQRES 6 B 382 SER PHE GLY GLN VAL VAL LYS ALA TYR ASP ARG VAL GLU
SEQRES 7 B 382 GLN GLU TRP VAL ALA ILE LYS ILE ILE LYS ASN LYS LYS
SEQRES 8 B 382 ALA PHE LEU ASN GLN ALA GLN ILE GLU VAL ARG LEU LEU
SEQRES 9 B 382 GLU LEU MET ASN LYS HIS ASP THR GLU MET LYS TYR TYR
SEQRES 10 B 382 ILE VAL HIS LEU LYS ARG HIS PHE MET PHE ARG ASN HIS
SEQRES 11 B 382 LEU CYS LEU VAL PHE GLU MET LEU SER TYR ASN LEU TYR
SEQRES 12 B 382 ASP LEU LEU ARG ASN THR ASN PHE ARG GLY VAL SER LEU
SEQRES 13 B 382 ASN LEU THR ARG LYS PHE ALA GLN GLN MET CYS THR ALA
SEQRES 14 B 382 LEU LEU PHE LEU ALA THR PRO GLU LEU SER ILE ILE HIS
SEQRES 15 B 382 CYS ASP LEU LYS PRO GLU ASN ILE LEU LEU CYS ASN PRO
SEQRES 16 B 382 LYS ARG SER ALA ILE LYS ILE VAL ASP PHE GLY SER SER
SEQRES 17 B 382 CYS GLN LEU GLY GLN ARG ILE TYR GLN PTR ILE GLN SER
SEQRES 18 B 382 ARG PHE TYR ARG SER PRO GLU VAL LEU LEU GLY MET PRO
SEQRES 19 B 382 TYR ASP LEU ALA ILE ASP MET TRP SER LEU GLY CYS ILE
SEQRES 20 B 382 LEU VAL GLU MET HIS THR GLY GLU PRO LEU PHE SER GLY
SEQRES 21 B 382 ALA ASN GLU VAL ASP GLN MET ASN LYS ILE VAL GLU VAL
SEQRES 22 B 382 LEU GLY ILE PRO PRO ALA HIS ILE LEU ASP GLN ALA PRO
SEQRES 23 B 382 LYS ALA ARG LYS PHE PHE GLU LYS LEU PRO ASP GLY THR
SEQRES 24 B 382 TRP ASN LEU LYS LYS THR LYS ASP GLY LYS ARG GLU TYR
SEQRES 25 B 382 LYS PRO PRO GLY THR ARG LYS LEU HIS ASN ILE LEU GLY
SEQRES 26 B 382 VAL GLU THR GLY GLY PRO GLY GLY ARG ARG ALA GLY GLU
SEQRES 27 B 382 SER GLY HIS THR VAL ALA ASP TYR LEU LYS PHE LYS ASP
SEQRES 28 B 382 LEU ILE LEU ARG MET LEU ASP TYR ASP PRO LYS THR ARG
SEQRES 29 B 382 ILE GLN PRO TYR TYR ALA LEU GLN HIS SER PHE PHE LYS
SEQRES 30 B 382 LYS THR ALA ASP GLU
SEQRES 1 C 382 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 382 GLY THR GLU ASN LEU TYR PHE GLN SER MET SER SER HIS
SEQRES 3 C 382 LYS LYS GLU ARG LYS VAL TYR ASN ASP GLY TYR ASP ASP
SEQRES 4 C 382 ASP ASN TYR ASP TYR ILE VAL LYS ASN GLY GLU LYS TRP
SEQRES 5 C 382 MET ASP ARG TYR GLU ILE ASP SER LEU ILE GLY LYS GLY
SEQRES 6 C 382 SER PHE GLY GLN VAL VAL LYS ALA TYR ASP ARG VAL GLU
SEQRES 7 C 382 GLN GLU TRP VAL ALA ILE LYS ILE ILE LYS ASN LYS LYS
SEQRES 8 C 382 ALA PHE LEU ASN GLN ALA GLN ILE GLU VAL ARG LEU LEU
SEQRES 9 C 382 GLU LEU MET ASN LYS HIS ASP THR GLU MET LYS TYR TYR
SEQRES 10 C 382 ILE VAL HIS LEU LYS ARG HIS PHE MET PHE ARG ASN HIS
SEQRES 11 C 382 LEU CYS LEU VAL PHE GLU MET LEU SER TYR ASN LEU TYR
SEQRES 12 C 382 ASP LEU LEU ARG ASN THR ASN PHE ARG GLY VAL SER LEU
SEQRES 13 C 382 ASN LEU THR ARG LYS PHE ALA GLN GLN MET CYS THR ALA
SEQRES 14 C 382 LEU LEU PHE LEU ALA THR PRO GLU LEU SER ILE ILE HIS
SEQRES 15 C 382 CYS ASP LEU LYS PRO GLU ASN ILE LEU LEU CYS ASN PRO
SEQRES 16 C 382 LYS ARG SER ALA ILE LYS ILE VAL ASP PHE GLY SER SER
SEQRES 17 C 382 CYS GLN LEU GLY GLN ARG ILE TYR GLN PTR ILE GLN SER
SEQRES 18 C 382 ARG PHE TYR ARG SER PRO GLU VAL LEU LEU GLY MET PRO
SEQRES 19 C 382 TYR ASP LEU ALA ILE ASP MET TRP SER LEU GLY CYS ILE
SEQRES 20 C 382 LEU VAL GLU MET HIS THR GLY GLU PRO LEU PHE SER GLY
SEQRES 21 C 382 ALA ASN GLU VAL ASP GLN MET ASN LYS ILE VAL GLU VAL
SEQRES 22 C 382 LEU GLY ILE PRO PRO ALA HIS ILE LEU ASP GLN ALA PRO
SEQRES 23 C 382 LYS ALA ARG LYS PHE PHE GLU LYS LEU PRO ASP GLY THR
SEQRES 24 C 382 TRP ASN LEU LYS LYS THR LYS ASP GLY LYS ARG GLU TYR
SEQRES 25 C 382 LYS PRO PRO GLY THR ARG LYS LEU HIS ASN ILE LEU GLY
SEQRES 26 C 382 VAL GLU THR GLY GLY PRO GLY GLY ARG ARG ALA GLY GLU
SEQRES 27 C 382 SER GLY HIS THR VAL ALA ASP TYR LEU LYS PHE LYS ASP
SEQRES 28 C 382 LEU ILE LEU ARG MET LEU ASP TYR ASP PRO LYS THR ARG
SEQRES 29 C 382 ILE GLN PRO TYR TYR ALA LEU GLN HIS SER PHE PHE LYS
SEQRES 30 C 382 LYS THR ALA ASP GLU
SEQRES 1 D 382 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 382 GLY THR GLU ASN LEU TYR PHE GLN SER MET SER SER HIS
SEQRES 3 D 382 LYS LYS GLU ARG LYS VAL TYR ASN ASP GLY TYR ASP ASP
SEQRES 4 D 382 ASP ASN TYR ASP TYR ILE VAL LYS ASN GLY GLU LYS TRP
SEQRES 5 D 382 MET ASP ARG TYR GLU ILE ASP SER LEU ILE GLY LYS GLY
SEQRES 6 D 382 SER PHE GLY GLN VAL VAL LYS ALA TYR ASP ARG VAL GLU
SEQRES 7 D 382 GLN GLU TRP VAL ALA ILE LYS ILE ILE LYS ASN LYS LYS
SEQRES 8 D 382 ALA PHE LEU ASN GLN ALA GLN ILE GLU VAL ARG LEU LEU
SEQRES 9 D 382 GLU LEU MET ASN LYS HIS ASP THR GLU MET LYS TYR TYR
SEQRES 10 D 382 ILE VAL HIS LEU LYS ARG HIS PHE MET PHE ARG ASN HIS
SEQRES 11 D 382 LEU CYS LEU VAL PHE GLU MET LEU SER TYR ASN LEU TYR
SEQRES 12 D 382 ASP LEU LEU ARG ASN THR ASN PHE ARG GLY VAL SER LEU
SEQRES 13 D 382 ASN LEU THR ARG LYS PHE ALA GLN GLN MET CYS THR ALA
SEQRES 14 D 382 LEU LEU PHE LEU ALA THR PRO GLU LEU SER ILE ILE HIS
SEQRES 15 D 382 CYS ASP LEU LYS PRO GLU ASN ILE LEU LEU CYS ASN PRO
SEQRES 16 D 382 LYS ARG SER ALA ILE LYS ILE VAL ASP PHE GLY SER SER
SEQRES 17 D 382 CYS GLN LEU GLY GLN ARG ILE TYR GLN PTR ILE GLN SER
SEQRES 18 D 382 ARG PHE TYR ARG SER PRO GLU VAL LEU LEU GLY MET PRO
SEQRES 19 D 382 TYR ASP LEU ALA ILE ASP MET TRP SER LEU GLY CYS ILE
SEQRES 20 D 382 LEU VAL GLU MET HIS THR GLY GLU PRO LEU PHE SER GLY
SEQRES 21 D 382 ALA ASN GLU VAL ASP GLN MET ASN LYS ILE VAL GLU VAL
SEQRES 22 D 382 LEU GLY ILE PRO PRO ALA HIS ILE LEU ASP GLN ALA PRO
SEQRES 23 D 382 LYS ALA ARG LYS PHE PHE GLU LYS LEU PRO ASP GLY THR
SEQRES 24 D 382 TRP ASN LEU LYS LYS THR LYS ASP GLY LYS ARG GLU TYR
SEQRES 25 D 382 LYS PRO PRO GLY THR ARG LYS LEU HIS ASN ILE LEU GLY
SEQRES 26 D 382 VAL GLU THR GLY GLY PRO GLY GLY ARG ARG ALA GLY GLU
SEQRES 27 D 382 SER GLY HIS THR VAL ALA ASP TYR LEU LYS PHE LYS ASP
SEQRES 28 D 382 LEU ILE LEU ARG MET LEU ASP TYR ASP PRO LYS THR ARG
SEQRES 29 D 382 ILE GLN PRO TYR TYR ALA LEU GLN HIS SER PHE PHE LYS
SEQRES 30 D 382 LYS THR ALA ASP GLU
MODRES 5AIK PTR A 321 TYR O-PHOSPHOTYROSINE
MODRES 5AIK PTR B 321 TYR O-PHOSPHOTYROSINE
MODRES 5AIK PTR C 321 TYR O-PHOSPHOTYROSINE
MODRES 5AIK PTR D 321 TYR O-PHOSPHOTYROSINE
HET PTR A 321 16
HET PTR B 321 16
HET PTR C 321 16
HET PTR D 321 16
HET AWR A 900 24
HET PO4 A1483 5
HET PO4 A1484 5
HET AWR B 900 24
HET PO4 B1483 5
HET PO4 B1484 5
HET PO4 B1485 5
HET AWR C 900 24
HET PO4 C1483 5
HET PO4 C1484 5
HET AWR D 900 24
HET PO4 D1482 5
HET PO4 D1483 5
HET PO4 D1484 5
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM AWR 4-(7-METHOXY-1-(TRIFLUOROMETHYL)-9H-PYRIDO[3,4-B]INDOL-
HETNAM 2 AWR 9-YL)BUTAN-1-AMINE
HETNAM PO4 PHOSPHATE ION
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR 4(C9 H12 N O6 P)
FORMUL 5 AWR 4(C17 H18 F3 N3 O)
FORMUL 6 PO4 10(O4 P 3-)
FORMUL 19 HOH *64(H2 O)
HELIX 1 1 LYS A 193 LYS A 212 1 20
HELIX 2 2 THR A 215 TYR A 220 5 6
HELIX 3 3 ASN A 244 THR A 252 1 9
HELIX 4 4 SER A 258 ALA A 277 1 20
HELIX 5 5 LYS A 289 GLU A 291 5 3
HELIX 6 6 SER A 324 ARG A 328 5 5
HELIX 7 7 SER A 329 LEU A 334 1 6
HELIX 8 8 LEU A 340 GLY A 357 1 18
HELIX 9 9 ASN A 365 GLY A 378 1 14
HELIX 10 10 PRO A 381 ASP A 386 1 6
HELIX 11 11 LYS A 390 PHE A 394 1 5
HELIX 12 12 LYS A 422 GLY A 428 1 7
HELIX 13 13 GLY A 433 ARG A 437 5 5
HELIX 14 14 THR A 445 LEU A 460 1 16
HELIX 15 15 GLN A 469 LEU A 474 1 6
HELIX 16 16 HIS A 476 LYS A 480 5 5
HELIX 17 17 LYS B 193 LYS B 212 1 20
HELIX 18 18 THR B 215 TYR B 220 5 6
HELIX 19 19 ASN B 244 THR B 252 1 9
HELIX 20 20 SER B 258 ALA B 277 1 20
HELIX 21 21 LYS B 289 GLU B 291 5 3
HELIX 22 22 SER B 324 ARG B 328 5 5
HELIX 23 23 SER B 329 LEU B 334 1 6
HELIX 24 24 LEU B 340 GLY B 357 1 18
HELIX 25 25 ASN B 365 GLY B 378 1 14
HELIX 26 26 PRO B 381 ASP B 386 1 6
HELIX 27 27 LYS B 390 PHE B 394 1 5
HELIX 28 28 LYS B 422 GLY B 428 1 7
HELIX 29 29 GLY B 433 ARG B 437 5 5
HELIX 30 30 THR B 445 LEU B 460 1 16
HELIX 31 31 GLN B 469 LEU B 474 1 6
HELIX 32 32 LYS C 193 LYS C 212 1 20
HELIX 33 33 THR C 215 TYR C 220 5 6
HELIX 34 34 ASN C 244 THR C 252 1 9
HELIX 35 35 SER C 258 ALA C 277 1 20
HELIX 36 36 LYS C 289 GLU C 291 5 3
HELIX 37 37 SER C 324 ARG C 328 5 5
HELIX 38 38 SER C 329 LEU C 334 1 6
HELIX 39 39 LEU C 340 GLY C 357 1 18
HELIX 40 40 ASN C 365 GLY C 378 1 14
HELIX 41 41 PRO C 381 ASP C 386 1 6
HELIX 42 42 LYS C 390 PHE C 394 1 5
HELIX 43 43 LYS C 422 GLY C 428 1 7
HELIX 44 44 GLY C 433 ARG C 437 5 5
HELIX 45 45 THR C 445 LEU C 460 1 16
HELIX 46 46 GLN C 469 LEU C 474 1 6
HELIX 47 47 LYS D 193 LYS D 212 1 20
HELIX 48 48 THR D 215 TYR D 220 5 6
HELIX 49 49 ASN D 244 THR D 252 1 9
HELIX 50 50 SER D 258 ALA D 277 1 20
HELIX 51 51 LYS D 289 GLU D 291 5 3
HELIX 52 52 SER D 324 ARG D 328 5 5
HELIX 53 53 SER D 329 LEU D 334 1 6
HELIX 54 54 LEU D 340 GLY D 357 1 18
HELIX 55 55 ASN D 365 GLY D 378 1 14
HELIX 56 56 PRO D 381 ASP D 386 1 6
HELIX 57 57 LYS D 390 PHE D 394 1 5
HELIX 58 58 LYS D 422 GLY D 428 1 7
HELIX 59 59 GLY D 433 ARG D 437 5 5
HELIX 60 60 THR D 445 LEU D 460 1 16
HELIX 61 61 GLN D 469 LEU D 474 1 6
HELIX 62 62 HIS D 476 LYS D 480 5 5
SHEET 1 AA 6 LYS A 154 TRP A 155 0
SHEET 2 AA 6 TYR A 159 GLY A 168 -1 O TYR A 159 N TRP A 155
SHEET 3 AA 6 GLY A 171 ASP A 178 -1 O GLY A 171 N GLY A 168
SHEET 4 AA 6 GLU A 183 ILE A 190 -1 O GLU A 183 N ASP A 178
SHEET 5 AA 6 HIS A 233 GLU A 239 -1 O LEU A 234 N ILE A 190
SHEET 6 AA 6 LEU A 224 PHE A 230 -1 N LYS A 225 O VAL A 237
SHEET 1 AB 2 ILE A 283 ILE A 284 0
SHEET 2 AB 2 CYS A 312 GLN A 313 -1 O CYS A 312 N ILE A 284
SHEET 1 AC 2 ILE A 293 LEU A 295 0
SHEET 2 AC 2 ILE A 303 ILE A 305 -1 O LYS A 304 N LEU A 294
SHEET 1 AD 2 PHE A 395 LYS A 397 0
SHEET 2 AD 2 TRP A 403 LEU A 405 -1 O ASN A 404 N GLU A 396
SHEET 1 BA 6 LYS B 154 TRP B 155 0
SHEET 2 BA 6 TYR B 159 LYS B 167 -1 O TYR B 159 N TRP B 155
SHEET 3 BA 6 GLY B 171 ASP B 178 -1 O VAL B 173 N ILE B 165
SHEET 4 BA 6 GLU B 183 ILE B 190 -1 O GLU B 183 N ASP B 178
SHEET 5 BA 6 HIS B 233 GLU B 239 -1 O LEU B 234 N ILE B 190
SHEET 6 BA 6 LEU B 224 PHE B 230 -1 N LYS B 225 O VAL B 237
SHEET 1 BB 2 ILE B 283 ILE B 284 0
SHEET 2 BB 2 CYS B 312 GLN B 313 -1 O CYS B 312 N ILE B 284
SHEET 1 BC 2 ILE B 293 LEU B 295 0
SHEET 2 BC 2 ILE B 303 ILE B 305 -1 O LYS B 304 N LEU B 294
SHEET 1 BD 2 PHE B 395 LYS B 397 0
SHEET 2 BD 2 TRP B 403 LEU B 405 -1 O ASN B 404 N GLU B 396
SHEET 1 CA 6 LYS C 154 TRP C 155 0
SHEET 2 CA 6 TYR C 159 LYS C 167 -1 O TYR C 159 N TRP C 155
SHEET 3 CA 6 GLY C 171 ASP C 178 -1 O VAL C 173 N ILE C 165
SHEET 4 CA 6 GLU C 183 ILE C 190 -1 O GLU C 183 N ASP C 178
SHEET 5 CA 6 HIS C 233 GLU C 239 -1 O LEU C 234 N ILE C 190
SHEET 6 CA 6 LEU C 224 PHE C 230 -1 N LYS C 225 O VAL C 237
SHEET 1 CB 2 ILE C 283 ILE C 284 0
SHEET 2 CB 2 CYS C 312 GLN C 313 -1 O CYS C 312 N ILE C 284
SHEET 1 CC 2 ILE C 293 LEU C 295 0
SHEET 2 CC 2 ILE C 303 ILE C 305 -1 O LYS C 304 N LEU C 294
SHEET 1 CD 2 PHE C 395 LYS C 397 0
SHEET 2 CD 2 TRP C 403 LEU C 405 -1 O ASN C 404 N GLU C 396
SHEET 1 DA 6 LYS D 154 TRP D 155 0
SHEET 2 DA 6 TYR D 159 GLY D 168 -1 O TYR D 159 N TRP D 155
SHEET 3 DA 6 GLY D 171 ASP D 178 -1 O GLY D 171 N GLY D 168
SHEET 4 DA 6 GLU D 183 ILE D 190 -1 O GLU D 183 N ASP D 178
SHEET 5 DA 6 HIS D 233 GLU D 239 -1 O LEU D 234 N ILE D 190
SHEET 6 DA 6 LEU D 224 PHE D 230 -1 N LYS D 225 O VAL D 237
SHEET 1 DB 2 ILE D 283 ILE D 284 0
SHEET 2 DB 2 CYS D 312 GLN D 313 -1 O CYS D 312 N ILE D 284
SHEET 1 DC 2 ILE D 293 LEU D 295 0
SHEET 2 DC 2 ILE D 303 ILE D 305 -1 O LYS D 304 N LEU D 294
SHEET 1 DD 2 PHE D 395 LYS D 397 0
SHEET 2 DD 2 TRP D 403 LEU D 405 -1 O ASN D 404 N GLU D 396
LINK C GLN A 320 N PTR A 321 1555 1555 1.33
LINK C PTR A 321 N ILE A 322 1555 1555 1.33
LINK C GLN B 320 N PTR B 321 1555 1555 1.33
LINK C PTR B 321 N ILE B 322 1555 1555 1.34
LINK C GLN C 320 N PTR C 321 1555 1555 1.33
LINK C PTR C 321 N ILE C 322 1555 1555 1.33
LINK C GLN D 320 N PTR D 321 1555 1555 1.33
LINK C PTR D 321 N ILE D 322 1555 1555 1.33
CISPEP 1 THR D 408 LYS D 409 0 -17.01
SITE 1 AC1 8 PHE A 170 VAL A 173 LYS A 188 GLU A 203
SITE 2 AC1 8 PHE A 238 GLU A 239 LEU A 241 ASP A 307
SITE 1 AC2 12 GLY B 166 PHE B 170 VAL B 173 ALA B 186
SITE 2 AC2 12 LYS B 188 GLU B 203 PHE B 238 GLU B 239
SITE 3 AC2 12 LEU B 241 SER B 242 LEU B 294 ASP B 307
SITE 1 AC3 9 LYS C 167 PHE C 170 VAL C 173 ALA C 186
SITE 2 AC3 9 LYS C 188 PHE C 238 GLU C 239 LEU C 241
SITE 3 AC3 9 ASP C 307
SITE 1 AC4 12 ILE D 165 PHE D 170 VAL D 173 ALA D 186
SITE 2 AC4 12 LYS D 188 GLU D 203 PHE D 238 GLU D 239
SITE 3 AC4 12 LEU D 241 SER D 242 LEU D 294 ASP D 307
SITE 1 AC5 4 GLY B 168 SER B 169 TYR C 145 LYS C 193
SITE 1 AC6 3 LYS B 193 LYS B 194 SER C 310
SITE 1 AC7 4 TYR B 145 LYS B 193 GLY C 168 SER C 169
SITE 1 AC8 4 GLY A 168 SER A 169 TYR D 145 LYS D 193
SITE 1 AC9 3 SER A 310 LYS D 193 LYS D 194
SITE 1 BC1 3 TYR A 145 GLY D 168 SER D 169
SITE 1 BC2 3 LYS A 264 ARG A 300 SER A 301
SITE 1 BC3 3 LYS B 264 ARG B 300 SER B 301
SITE 1 BC4 3 LYS C 264 ARG C 300 SER C 301
SITE 1 BC5 3 LYS D 264 ARG D 300 SER D 301
CRYST1 89.955 90.891 232.468 90.00 90.00 90.00 P 21 21 21 16
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 0.011117 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011002 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004302 0.00000
MTRIX1 1 0.454070 -0.628240 0.631770 -5.22992 1
MTRIX2 1 0.673430 -0.222270 -0.705040 30.03312 1
MTRIX3 1 0.583360 0.745590 0.322150 31.16370 1
MTRIX1 2 -0.703660 0.251880 0.664400 -9.69246 1
MTRIX2 2 0.419620 -0.607270 0.674640 58.36529 1
MTRIX3 2 0.573400 0.753510 0.321620 -26.22789 1
MTRIX1 3 0.220310 -0.975180 -0.022180 61.96759 1
MTRIX2 3 -0.974880 -0.220890 0.028430 75.63342 1
MTRIX3 3 -0.032630 0.015360 -0.999350 57.62270 1
(ATOM LINES ARE NOT SHOWN.)
END
