HEADER TRANSFERASE 30-JUN-10 3NRU
TITLE LIGAND BINDING DOMAIN OF EPHA7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPHRIN RECEPTOR;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 FRAGMENT: RESIDUES 29-204;
COMPND 5 EC: 2.7.10.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EPHA7;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFHMSP-LIC-C
KEYWDS KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WALKER,L.YERMEKBAYEVA,A.SEITOVA,J.KANIA,C.BOUNTRA,J.WEIGELT,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,S.DHE-PAGANON
REVDAT 2 06-SEP-23 3NRU 1 REMARK SEQADV
REVDAT 1 08-DEC-10 3NRU 0
JRNL AUTH J.R.WALKER,L.YERMEKBAYEVA,A.SEITOVA,J.KANIA,C.BOUNTRA,
JRNL AUTH 2 J.WEIGELT,C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,
JRNL AUTH 3 S.DHE-PAGANON
JRNL TITL EPHRIN A7 LIGAND BINDING DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 117396
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) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6230
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8469
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 448
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15203
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.64000
REMARK 3 B22 (A**2) : -0.19000
REMARK 3 B33 (A**2) : -0.45000
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): 0.300
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.232
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.164
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.606
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15671 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21293 ; 0.967 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1877 ; 6.052 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 749 ;36.343 ;24.927
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2626 ;14.127 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 75 ;12.118 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2353 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11819 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 9497 ; 0.348 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15320 ; 0.654 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6174 ; 0.792 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5973 ; 1.330 ; 4.500
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1747 -35.7298 -9.4755
REMARK 3 T TENSOR
REMARK 3 T11: 0.0181 T22: 0.0950
REMARK 3 T33: 0.1079 T12: 0.0112
REMARK 3 T13: 0.0084 T23: -0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 1.8024 L22: 2.8533
REMARK 3 L33: 2.4668 L12: -0.4887
REMARK 3 L13: -0.5616 L23: -0.3211
REMARK 3 S TENSOR
REMARK 3 S11: -0.0245 S12: -0.0348 S13: 0.0694
REMARK 3 S21: -0.1800 S22: 0.0599 S23: -0.0047
REMARK 3 S31: 0.1031 S32: 0.1411 S33: -0.0354
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 : B -10 B 9999
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6514 -36.9205 8.4968
REMARK 3 T TENSOR
REMARK 3 T11: 0.0221 T22: 0.1019
REMARK 3 T33: 0.1221 T12: 0.0126
REMARK 3 T13: 0.0193 T23: 0.0428
REMARK 3 L TENSOR
REMARK 3 L11: 1.9750 L22: 2.7301
REMARK 3 L33: 2.8155 L12: -0.0136
REMARK 3 L13: -0.6890 L23: -0.0660
REMARK 3 S TENSOR
REMARK 3 S11: -0.0609 S12: -0.0565 S13: -0.0255
REMARK 3 S21: 0.1854 S22: 0.0381 S23: 0.0003
REMARK 3 S31: 0.1258 S32: -0.0720 S33: 0.0228
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 : C -10 C 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4978 -64.5202 -33.5881
REMARK 3 T TENSOR
REMARK 3 T11: 0.1469 T22: 0.0604
REMARK 3 T33: 0.0864 T12: -0.0520
REMARK 3 T13: -0.0607 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 2.7026 L22: 2.2615
REMARK 3 L33: 2.9080 L12: 0.3833
REMARK 3 L13: -0.1535 L23: 0.3020
REMARK 3 S TENSOR
REMARK 3 S11: 0.1119 S12: -0.1208 S13: 0.0876
REMARK 3 S21: 0.0419 S22: -0.0615 S23: 0.0728
REMARK 3 S31: 0.0525 S32: 0.2382 S33: -0.0504
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 : D -10 D 9999
REMARK 3 ORIGIN FOR THE GROUP (A): -9.3945 -60.3566 39.4302
REMARK 3 T TENSOR
REMARK 3 T11: 0.0556 T22: 0.0746
REMARK 3 T33: 0.0480 T12: -0.0036
REMARK 3 T13: -0.0187 T23: 0.0473
REMARK 3 L TENSOR
REMARK 3 L11: 2.7003 L22: 3.0920
REMARK 3 L33: 3.6621 L12: -0.6043
REMARK 3 L13: 0.0686 L23: -0.8900
REMARK 3 S TENSOR
REMARK 3 S11: -0.0022 S12: 0.0073 S13: 0.0038
REMARK 3 S21: 0.1589 S22: 0.0171 S23: 0.0861
REMARK 3 S31: -0.0840 S32: -0.2428 S33: -0.0150
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 : E -10 E 9999
REMARK 3 ORIGIN FOR THE GROUP (A): -34.4107 -62.1065 12.5795
REMARK 3 T TENSOR
REMARK 3 T11: 0.0381 T22: 0.1273
REMARK 3 T33: 0.0293 T12: 0.0046
REMARK 3 T13: 0.0063 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 4.0585 L22: 2.4899
REMARK 3 L33: 1.9706 L12: -0.0863
REMARK 3 L13: 0.9561 L23: 0.0538
REMARK 3 S TENSOR
REMARK 3 S11: 0.2816 S12: 0.2076 S13: 0.0817
REMARK 3 S21: 0.1097 S22: -0.2766 S23: -0.0410
REMARK 3 S31: 0.2103 S32: 0.1884 S33: -0.0050
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 : F -10 F 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7231 -12.9348 -36.9913
REMARK 3 T TENSOR
REMARK 3 T11: 0.2044 T22: 0.0923
REMARK 3 T33: 0.1110 T12: 0.1093
REMARK 3 T13: -0.0353 T23: -0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 4.0984 L22: 2.4274
REMARK 3 L33: 4.3615 L12: -1.0978
REMARK 3 L13: 1.6189 L23: -0.8226
REMARK 3 S TENSOR
REMARK 3 S11: 0.2745 S12: 0.3950 S13: -0.2367
REMARK 3 S21: -0.3779 S22: -0.2037 S23: 0.0791
REMARK 3 S31: 0.2835 S32: 0.4738 S33: -0.0708
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 : G -10 G 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 40.5890 -58.5582 -11.1787
REMARK 3 T TENSOR
REMARK 3 T11: 0.0255 T22: 0.0634
REMARK 3 T33: 0.1240 T12: 0.0199
REMARK 3 T13: -0.0308 T23: -0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 2.5557 L22: 2.1674
REMARK 3 L33: 2.8058 L12: 0.3828
REMARK 3 L13: 0.0212 L23: -0.5789
REMARK 3 S TENSOR
REMARK 3 S11: 0.1140 S12: -0.0331 S13: 0.0245
REMARK 3 S21: -0.1246 S22: -0.0613 S23: 0.1152
REMARK 3 S31: 0.1246 S32: -0.0122 S33: -0.0527
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 : H -10 H 9999
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2073 -11.9110 34.6364
REMARK 3 T TENSOR
REMARK 3 T11: 0.1299 T22: 0.0695
REMARK 3 T33: 0.0167 T12: -0.0431
REMARK 3 T13: 0.0196 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 2.5800 L22: 2.7817
REMARK 3 L33: 3.1904 L12: 0.7346
REMARK 3 L13: 0.5445 L23: 1.1333
REMARK 3 S TENSOR
REMARK 3 S11: 0.1253 S12: -0.3395 S13: -0.0710
REMARK 3 S21: 0.5084 S22: -0.1561 S23: 0.0491
REMARK 3 S31: 0.2357 S32: -0.2948 S33: 0.0308
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I -10 I 9999
REMARK 3 ORIGIN FOR THE GROUP (A): -34.9326 -78.8240 -6.5434
REMARK 3 T TENSOR
REMARK 3 T11: 0.3236 T22: 0.2910
REMARK 3 T33: 0.1770 T12: 0.2844
REMARK 3 T13: -0.1838 T23: -0.1815
REMARK 3 L TENSOR
REMARK 3 L11: 3.6075 L22: 3.4992
REMARK 3 L33: 4.2876 L12: 0.2200
REMARK 3 L13: 1.0705 L23: 1.2211
REMARK 3 S TENSOR
REMARK 3 S11: 0.4746 S12: 0.3960 S13: -0.5940
REMARK 3 S21: -0.3457 S22: -0.0584 S23: -0.0165
REMARK 3 S31: 0.5458 S32: 0.4335 S33: -0.4162
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J -10 J 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 29.8094 -68.5176 -59.3271
REMARK 3 T TENSOR
REMARK 3 T11: 0.0547 T22: 0.1790
REMARK 3 T33: 0.1428 T12: -0.0737
REMARK 3 T13: -0.0367 T23: -0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 2.8250 L22: 2.7886
REMARK 3 L33: 4.4053 L12: -0.7897
REMARK 3 L13: -1.3695 L23: 1.4531
REMARK 3 S TENSOR
REMARK 3 S11: 0.0388 S12: -0.2673 S13: 0.1375
REMARK 3 S21: 0.1824 S22: 0.1371 S23: -0.3671
REMARK 3 S31: -0.1697 S32: 0.5993 S33: -0.1760
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K -10 K 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7852 -40.9393 -60.1722
REMARK 3 T TENSOR
REMARK 3 T11: 0.4251 T22: 0.0260
REMARK 3 T33: 0.1186 T12: -0.0096
REMARK 3 T13: -0.0488 T23: -0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 2.5456 L22: 3.8745
REMARK 3 L33: 4.9121 L12: -0.2348
REMARK 3 L13: 0.9805 L23: -0.3580
REMARK 3 S TENSOR
REMARK 3 S11: -0.2264 S12: -0.0583 S13: 0.2113
REMARK 3 S21: 0.1548 S22: 0.0402 S23: -0.0749
REMARK 3 S31: -1.0363 S32: 0.0860 S33: 0.1862
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L -10 L 9999
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3038 -38.9363 -76.8974
REMARK 3 T TENSOR
REMARK 3 T11: 0.4816 T22: 0.1655
REMARK 3 T33: 0.2625 T12: 0.1457
REMARK 3 T13: -0.0619 T23: 0.1105
REMARK 3 L TENSOR
REMARK 3 L11: 3.8080 L22: 3.8572
REMARK 3 L33: 4.3612 L12: 0.8653
REMARK 3 L13: 0.3565 L23: 0.2180
REMARK 3 S TENSOR
REMARK 3 S11: -0.5186 S12: 0.0585 S13: 0.5025
REMARK 3 S21: -0.0370 S22: 0.4377 S23: 0.4182
REMARK 3 S31: -0.6196 S32: -0.5375 S33: 0.0809
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3NRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060201.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123900
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.55500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
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: 2WO1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 M NH4SO4, 0.6 M LISO4, 0.1 M TRI
REMARK 280 -NACITRATE PH 4.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
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 68.80850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.89150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.34950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.89150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 68.80850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.34950
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, 5, 6, 7, 8, 9, 10, 11, 12
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J
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: 11
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K
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: 12
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L
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 ALA A 30
REMARK 465 ALA A 31
REMARK 465 GLN A 41
REMARK 465 GLN A 42
REMARK 465 THR A 43
REMARK 465 GLU A 44
REMARK 465 LEU A 45
REMARK 465 GLN A 157
REMARK 465 GLY A 158
REMARK 465 ASP A 159
REMARK 465 LEU A 160
REMARK 465 GLY A 161
REMARK 465 GLU A 162
REMARK 465 ARG A 163
REMARK 465 LYS A 164
REMARK 465 MET A 165
REMARK 465 GLU A 205
REMARK 465 PHE A 206
REMARK 465 VAL A 207
REMARK 465 GLU A 208
REMARK 465 HIS A 209
REMARK 465 HIS A 210
REMARK 465 HIS A 211
REMARK 465 HIS A 212
REMARK 465 HIS A 213
REMARK 465 HIS A 214
REMARK 465 HIS A 215
REMARK 465 HIS A 216
REMARK 465 ALA B 30
REMARK 465 ALA B 31
REMARK 465 THR B 43
REMARK 465 GLU B 44
REMARK 465 LEU B 45
REMARK 465 GLY B 117
REMARK 465 THR B 118
REMARK 465 PHE B 155
REMARK 465 THR B 156
REMARK 465 GLN B 157
REMARK 465 GLY B 158
REMARK 465 ASP B 159
REMARK 465 LEU B 160
REMARK 465 GLY B 161
REMARK 465 GLU B 162
REMARK 465 ARG B 163
REMARK 465 LYS B 164
REMARK 465 GLU B 205
REMARK 465 PHE B 206
REMARK 465 VAL B 207
REMARK 465 GLU B 208
REMARK 465 HIS B 209
REMARK 465 HIS B 210
REMARK 465 HIS B 211
REMARK 465 HIS B 212
REMARK 465 HIS B 213
REMARK 465 HIS B 214
REMARK 465 HIS B 215
REMARK 465 HIS B 216
REMARK 465 ALA C 30
REMARK 465 GLN C 41
REMARK 465 GLN C 42
REMARK 465 THR C 43
REMARK 465 GLU C 44
REMARK 465 LEU C 45
REMARK 465 PHE C 155
REMARK 465 THR C 156
REMARK 465 GLN C 157
REMARK 465 GLY C 158
REMARK 465 ASP C 159
REMARK 465 LEU C 160
REMARK 465 GLY C 161
REMARK 465 GLU C 162
REMARK 465 ARG C 163
REMARK 465 GLU C 205
REMARK 465 PHE C 206
REMARK 465 VAL C 207
REMARK 465 GLU C 208
REMARK 465 HIS C 209
REMARK 465 HIS C 210
REMARK 465 HIS C 211
REMARK 465 HIS C 212
REMARK 465 HIS C 213
REMARK 465 HIS C 214
REMARK 465 HIS C 215
REMARK 465 HIS C 216
REMARK 465 ALA D 30
REMARK 465 LEU D 116
REMARK 465 GLY D 117
REMARK 465 THR D 118
REMARK 465 PHE D 155
REMARK 465 THR D 156
REMARK 465 GLN D 157
REMARK 465 GLY D 158
REMARK 465 ASP D 159
REMARK 465 LEU D 160
REMARK 465 GLY D 161
REMARK 465 GLU D 162
REMARK 465 ARG D 163
REMARK 465 LYS D 164
REMARK 465 MET D 165
REMARK 465 GLU D 205
REMARK 465 PHE D 206
REMARK 465 VAL D 207
REMARK 465 GLU D 208
REMARK 465 HIS D 209
REMARK 465 HIS D 210
REMARK 465 HIS D 211
REMARK 465 HIS D 212
REMARK 465 HIS D 213
REMARK 465 HIS D 214
REMARK 465 HIS D 215
REMARK 465 HIS D 216
REMARK 465 ALA E 30
REMARK 465 THR E 43
REMARK 465 GLU E 44
REMARK 465 LEU E 45
REMARK 465 LEU E 116
REMARK 465 GLN E 157
REMARK 465 GLY E 158
REMARK 465 ASP E 159
REMARK 465 LEU E 160
REMARK 465 GLY E 161
REMARK 465 GLU E 162
REMARK 465 ARG E 163
REMARK 465 GLU E 205
REMARK 465 PHE E 206
REMARK 465 VAL E 207
REMARK 465 GLU E 208
REMARK 465 HIS E 209
REMARK 465 HIS E 210
REMARK 465 HIS E 211
REMARK 465 HIS E 212
REMARK 465 HIS E 213
REMARK 465 HIS E 214
REMARK 465 HIS E 215
REMARK 465 HIS E 216
REMARK 465 ALA F 30
REMARK 465 THR F 43
REMARK 465 GLU F 44
REMARK 465 LEU F 45
REMARK 465 GLY F 114
REMARK 465 VAL F 115
REMARK 465 LEU F 116
REMARK 465 SER F 154
REMARK 465 PHE F 155
REMARK 465 THR F 156
REMARK 465 GLN F 157
REMARK 465 GLY F 158
REMARK 465 ASP F 159
REMARK 465 LEU F 160
REMARK 465 GLY F 161
REMARK 465 GLU F 162
REMARK 465 ARG F 163
REMARK 465 LYS F 164
REMARK 465 MET F 165
REMARK 465 GLU F 205
REMARK 465 PHE F 206
REMARK 465 VAL F 207
REMARK 465 GLU F 208
REMARK 465 HIS F 209
REMARK 465 HIS F 210
REMARK 465 HIS F 211
REMARK 465 HIS F 212
REMARK 465 HIS F 213
REMARK 465 HIS F 214
REMARK 465 HIS F 215
REMARK 465 HIS F 216
REMARK 465 VAL G 115
REMARK 465 LEU G 116
REMARK 465 GLY G 117
REMARK 465 SER G 154
REMARK 465 PHE G 155
REMARK 465 THR G 156
REMARK 465 GLN G 157
REMARK 465 GLY G 158
REMARK 465 ASP G 159
REMARK 465 LEU G 160
REMARK 465 GLY G 161
REMARK 465 GLU G 162
REMARK 465 ARG G 163
REMARK 465 LYS G 164
REMARK 465 MET G 165
REMARK 465 GLU G 205
REMARK 465 PHE G 206
REMARK 465 VAL G 207
REMARK 465 GLU G 208
REMARK 465 HIS G 209
REMARK 465 HIS G 210
REMARK 465 HIS G 211
REMARK 465 HIS G 212
REMARK 465 HIS G 213
REMARK 465 HIS G 214
REMARK 465 HIS G 215
REMARK 465 HIS G 216
REMARK 465 ALA H 30
REMARK 465 GLN H 41
REMARK 465 GLN H 42
REMARK 465 THR H 43
REMARK 465 GLU H 44
REMARK 465 LEU H 45
REMARK 465 PRO H 113
REMARK 465 GLY H 114
REMARK 465 PHE H 155
REMARK 465 THR H 156
REMARK 465 GLN H 157
REMARK 465 GLY H 158
REMARK 465 ASP H 159
REMARK 465 LEU H 160
REMARK 465 GLY H 161
REMARK 465 GLU H 162
REMARK 465 ARG H 163
REMARK 465 LYS H 164
REMARK 465 GLU H 205
REMARK 465 PHE H 206
REMARK 465 VAL H 207
REMARK 465 GLU H 208
REMARK 465 HIS H 209
REMARK 465 HIS H 210
REMARK 465 HIS H 211
REMARK 465 HIS H 212
REMARK 465 HIS H 213
REMARK 465 HIS H 214
REMARK 465 HIS H 215
REMARK 465 HIS H 216
REMARK 465 ALA I 30
REMARK 465 GLN I 41
REMARK 465 GLN I 42
REMARK 465 THR I 43
REMARK 465 GLU I 44
REMARK 465 LEU I 45
REMARK 465 LEU I 116
REMARK 465 GLY I 117
REMARK 465 THR I 118
REMARK 465 GLN I 157
REMARK 465 GLY I 158
REMARK 465 ASP I 159
REMARK 465 LEU I 160
REMARK 465 GLY I 161
REMARK 465 GLU I 162
REMARK 465 GLU I 205
REMARK 465 PHE I 206
REMARK 465 VAL I 207
REMARK 465 GLU I 208
REMARK 465 HIS I 209
REMARK 465 HIS I 210
REMARK 465 HIS I 211
REMARK 465 HIS I 212
REMARK 465 HIS I 213
REMARK 465 HIS I 214
REMARK 465 HIS I 215
REMARK 465 HIS I 216
REMARK 465 ALA J 30
REMARK 465 GLY J 114
REMARK 465 VAL J 115
REMARK 465 PHE J 155
REMARK 465 THR J 156
REMARK 465 GLN J 157
REMARK 465 GLY J 158
REMARK 465 ASP J 159
REMARK 465 LEU J 160
REMARK 465 GLY J 161
REMARK 465 GLU J 162
REMARK 465 ARG J 163
REMARK 465 LYS J 164
REMARK 465 MET J 165
REMARK 465 GLU J 205
REMARK 465 PHE J 206
REMARK 465 VAL J 207
REMARK 465 GLU J 208
REMARK 465 HIS J 209
REMARK 465 HIS J 210
REMARK 465 HIS J 211
REMARK 465 HIS J 212
REMARK 465 HIS J 213
REMARK 465 HIS J 214
REMARK 465 HIS J 215
REMARK 465 HIS J 216
REMARK 465 ALA K 30
REMARK 465 GLN K 42
REMARK 465 THR K 43
REMARK 465 GLU K 44
REMARK 465 LEU K 45
REMARK 465 LEU K 116
REMARK 465 GLY K 117
REMARK 465 THR K 118
REMARK 465 SER K 154
REMARK 465 PHE K 155
REMARK 465 THR K 156
REMARK 465 GLN K 157
REMARK 465 GLY K 158
REMARK 465 ASP K 159
REMARK 465 LEU K 160
REMARK 465 GLY K 161
REMARK 465 GLU K 162
REMARK 465 ARG K 163
REMARK 465 LYS K 164
REMARK 465 MET K 165
REMARK 465 GLU K 205
REMARK 465 PHE K 206
REMARK 465 VAL K 207
REMARK 465 GLU K 208
REMARK 465 HIS K 209
REMARK 465 HIS K 210
REMARK 465 HIS K 211
REMARK 465 HIS K 212
REMARK 465 HIS K 213
REMARK 465 HIS K 214
REMARK 465 HIS K 215
REMARK 465 HIS K 216
REMARK 465 ALA L 30
REMARK 465 ALA L 31
REMARK 465 GLN L 41
REMARK 465 GLN L 42
REMARK 465 THR L 43
REMARK 465 GLU L 44
REMARK 465 LEU L 45
REMARK 465 VAL L 115
REMARK 465 LEU L 116
REMARK 465 TYR L 132
REMARK 465 GLY L 135
REMARK 465 ARG L 136
REMARK 465 ASN L 137
REMARK 465 GLN L 157
REMARK 465 GLY L 158
REMARK 465 ASP L 159
REMARK 465 LEU L 160
REMARK 465 GLY L 161
REMARK 465 GLU L 162
REMARK 465 ARG L 163
REMARK 465 LYS L 203
REMARK 465 LYS L 204
REMARK 465 GLU L 205
REMARK 465 PHE L 206
REMARK 465 VAL L 207
REMARK 465 GLU L 208
REMARK 465 HIS L 209
REMARK 465 HIS L 210
REMARK 465 HIS L 211
REMARK 465 HIS L 212
REMARK 465 HIS L 213
REMARK 465 HIS L 214
REMARK 465 HIS L 215
REMARK 465 HIS L 216
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 GLU A 46 CG CD OE1 OE2
REMARK 470 ARG A 69 CZ NH1 NH2
REMARK 470 LEU A 116 CG CD1 CD2
REMARK 470 LYS A 203 CD CE NZ
REMARK 470 LYS A 204 CG CD CE NZ
REMARK 470 GLU B 46 CG CD OE1 OE2
REMARK 470 MET B 77 CG SD CE
REMARK 470 ARG B 97 CZ NH1 NH2
REMARK 470 LYS B 120 NZ
REMARK 470 ARG B 136 NE CZ NH1 NH2
REMARK 470 LYS B 166 CG CD CE NZ
REMARK 470 LYS B 204 CE NZ
REMARK 470 GLU C 46 CD OE1 OE2
REMARK 470 ASN C 80 CG OD1 ND2
REMARK 470 ARG C 136 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 164 CG CD CE NZ
REMARK 470 GLN D 41 CG CD OE1 NE2
REMARK 470 THR D 43 OG1 CG2
REMARK 470 GLU D 44 CG CD OE1 OE2
REMARK 470 GLU D 46 CG CD OE1 OE2
REMARK 470 GLU D 63 CG CD OE1 OE2
REMARK 470 ARG D 107 NE CZ NH1 NH2
REMARK 470 LYS D 166 CD CE NZ
REMARK 470 GLN E 41 CG CD OE1 NE2
REMARK 470 GLU E 46 CG CD OE1 OE2
REMARK 470 GLU E 57 OE1 OE2
REMARK 470 LYS E 164 CE NZ
REMARK 470 LYS E 203 CD CE NZ
REMARK 470 GLN F 41 CG CD OE1 NE2
REMARK 470 GLU F 46 CG CD OE1 OE2
REMARK 470 GLU F 63 OE1 OE2
REMARK 470 LYS F 204 CG CD CE NZ
REMARK 470 LYS G 39 CG CD CE NZ
REMARK 470 GLU G 63 OE1 OE2
REMARK 470 ARG H 69 CZ NH1 NH2
REMARK 470 ASN H 94 CG OD1 ND2
REMARK 470 GLN H 96 CG CD OE1 NE2
REMARK 470 LEU H 112 CG CD1 CD2
REMARK 470 VAL H 115 CG1 CG2
REMARK 470 LEU H 116 CG CD1 CD2
REMARK 470 ARG H 136 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 139 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 180 CG CD CE NZ
REMARK 470 GLU I 46 CG CD OE1 OE2
REMARK 470 GLU I 63 CG CD OE1 OE2
REMARK 470 GLU I 78 CG CD OE1 OE2
REMARK 470 ARG I 86 CG CD NE CZ NH1 NH2
REMARK 470 ASN I 88 CG OD1 ND2
REMARK 470 ASN I 94 CG OD1 ND2
REMARK 470 ARG I 136 CG CD NE CZ NH1 NH2
REMARK 470 ARG I 139 CG CD NE CZ NH1 NH2
REMARK 470 SER I 154 OG
REMARK 470 THR I 156 OG1 CG2
REMARK 470 LYS I 166 CG CD CE NZ
REMARK 470 GLU J 46 CG CD OE1 OE2
REMARK 470 GLU J 63 CG CD OE1 OE2
REMARK 470 LYS J 180 CG CD CE NZ
REMARK 470 GLU K 32 CG CD OE1 OE2
REMARK 470 GLN K 41 CG CD OE1 NE2
REMARK 470 GLU K 46 CG CD OE1 OE2
REMARK 470 MET K 77 CG SD CE
REMARK 470 ASN K 88 CG OD1 ND2
REMARK 470 ASP K 108 CG OD1 OD2
REMARK 470 LYS K 120 CG CD CE NZ
REMARK 470 TYR K 132 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG K 136 CG CD NE CZ NH1 NH2
REMARK 470 ASN K 137 CG OD1 ND2
REMARK 470 LYS K 166 CG CD CE NZ
REMARK 470 LYS K 179 CG CD CE NZ
REMARK 470 GLU L 46 CG CD OE1 OE2
REMARK 470 ILE L 48 CG1 CG2 CD1
REMARK 470 GLU L 78 CG CD OE1 OE2
REMARK 470 ARG L 139 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 166 CG CD CE NZ
REMARK 470 LYS L 179 CG CD CE NZ
REMARK 470 LYS L 180 CG CD CE NZ
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 CYS A 74 56.91 -152.59
REMARK 500 GLN A 96 -85.30 -105.85
REMARK 500 PRO A 113 88.94 -61.61
REMARK 500 LEU A 116 -158.97 51.24
REMARK 500 GLN B 41 -145.00 -98.39
REMARK 500 CYS B 74 61.44 -155.75
REMARK 500 GLN B 75 59.95 -97.27
REMARK 500 GLN B 96 -90.76 -106.10
REMARK 500 CYS B 109 38.00 -71.93
REMARK 500 VAL B 115 -38.60 -137.28
REMARK 500 ASP B 133 93.24 -69.06
REMARK 500 CYS C 74 55.40 -159.89
REMARK 500 GLN C 96 -91.36 -103.52
REMARK 500 ASP C 133 94.08 -63.66
REMARK 500 ARG C 136 48.94 -93.42
REMARK 500 CYS D 74 54.33 -148.41
REMARK 500 ASN D 82 74.43 -155.35
REMARK 500 GLN D 96 -97.02 -102.16
REMARK 500 GLN D 96 -97.01 -102.16
REMARK 500 GLN E 75 41.99 -95.35
REMARK 500 GLN E 96 -89.11 -105.62
REMARK 500 GLN F 41 -101.33 62.29
REMARK 500 CYS F 74 59.43 -154.66
REMARK 500 GLN F 96 -87.65 -103.18
REMARK 500 ASP G 62 -169.73 -71.41
REMARK 500 CYS G 74 63.92 -154.12
REMARK 500 GLN G 75 50.76 -101.00
REMARK 500 GLN G 96 -82.95 -109.50
REMARK 500 CYS H 74 56.12 -153.14
REMARK 500 GLN H 96 -90.64 -108.64
REMARK 500 THR H 118 -47.07 66.46
REMARK 500 LYS I 39 62.19 -101.21
REMARK 500 GLU I 63 -35.34 76.14
REMARK 500 CYS I 74 82.99 -155.19
REMARK 500 GLN I 96 -93.60 -95.57
REMARK 500 THR I 134 125.71 -35.02
REMARK 500 CYS J 74 61.51 -151.79
REMARK 500 GLN J 75 61.50 -100.48
REMARK 500 GLN J 96 -89.56 -105.31
REMARK 500 THR J 134 -151.50 -96.98
REMARK 500 CYS K 74 63.52 -155.22
REMARK 500 GLN K 96 -86.43 -106.40
REMARK 500 CYS K 109 -40.45 67.93
REMARK 500 ASP L 62 -167.20 -78.74
REMARK 500 CYS L 74 52.93 -148.46
REMARK 500 ASN L 88 -170.75 -68.83
REMARK 500 GLN L 96 -82.83 -106.28
REMARK 500 THR L 118 51.95 -104.18
REMARK 500 SER L 154 -46.61 74.96
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 SO4 G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3H8M RELATED DB: PDB
REMARK 900 SAM DOMAIN OF HUMAN EPHRIN TYPE-A RECEPTOR 7 (EPHA7)
REMARK 900 RELATED ID: 3DKO RELATED DB: PDB
REMARK 900 COMPLEX BETWEEN THE KINASE DOMAIN OF HUMAN EPHRIN TYPE-A RECEPTOR 7
REMARK 900 (EPHA7) AND INHIBITOR ALW-II-49-7
REMARK 900 RELATED ID: 2REI RELATED DB: PDB
REMARK 900 KINASE DOMAIN OF HUMAN EPHRIN TYPE-A RECEPTOR 7 (EPHA7)
DBREF 3NRU A 32 204 UNP B7ZLK0 B7ZLK0_HUMAN 32 204
DBREF 3NRU B 32 204 UNP B7ZLK0 B7ZLK0_HUMAN 32 204
DBREF 3NRU C 32 204 UNP B7ZLK0 B7ZLK0_HUMAN 32 204
DBREF 3NRU D 32 204 UNP B7ZLK0 B7ZLK0_HUMAN 32 204
DBREF 3NRU E 32 204 UNP B7ZLK0 B7ZLK0_HUMAN 32 204
DBREF 3NRU F 32 204 UNP B7ZLK0 B7ZLK0_HUMAN 32 204
DBREF 3NRU G 32 204 UNP B7ZLK0 B7ZLK0_HUMAN 32 204
DBREF 3NRU H 32 204 UNP B7ZLK0 B7ZLK0_HUMAN 32 204
DBREF 3NRU I 32 204 UNP B7ZLK0 B7ZLK0_HUMAN 32 204
DBREF 3NRU J 32 204 UNP B7ZLK0 B7ZLK0_HUMAN 32 204
DBREF 3NRU K 32 204 UNP B7ZLK0 B7ZLK0_HUMAN 32 204
DBREF 3NRU L 32 204 UNP B7ZLK0 B7ZLK0_HUMAN 32 204
SEQADV 3NRU ALA A 30 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA A 31 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU A 205 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU PHE A 206 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU VAL A 207 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU A 208 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS A 209 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS A 210 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS A 211 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS A 212 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS A 213 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS A 214 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS A 215 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS A 216 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA B 30 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA B 31 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU B 205 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU PHE B 206 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU VAL B 207 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU B 208 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS B 209 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS B 210 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS B 211 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS B 212 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS B 213 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS B 214 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS B 215 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS B 216 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA C 30 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA C 31 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU C 205 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU PHE C 206 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU VAL C 207 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU C 208 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS C 209 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS C 210 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS C 211 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS C 212 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS C 213 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS C 214 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS C 215 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS C 216 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA D 30 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA D 31 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU D 205 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU PHE D 206 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU VAL D 207 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU D 208 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS D 209 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS D 210 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS D 211 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS D 212 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS D 213 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS D 214 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS D 215 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS D 216 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA E 30 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA E 31 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU E 205 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU PHE E 206 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU VAL E 207 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU E 208 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS E 209 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS E 210 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS E 211 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS E 212 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS E 213 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS E 214 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS E 215 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS E 216 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA F 30 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA F 31 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU F 205 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU PHE F 206 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU VAL F 207 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU F 208 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS F 209 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS F 210 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS F 211 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS F 212 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS F 213 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS F 214 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS F 215 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS F 216 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA G 30 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA G 31 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU G 205 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU PHE G 206 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU VAL G 207 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU G 208 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS G 209 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS G 210 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS G 211 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS G 212 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS G 213 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS G 214 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS G 215 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS G 216 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA H 30 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA H 31 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU H 205 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU PHE H 206 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU VAL H 207 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU H 208 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS H 209 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS H 210 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS H 211 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS H 212 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS H 213 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS H 214 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS H 215 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS H 216 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA I 30 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA I 31 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU I 205 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU PHE I 206 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU VAL I 207 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU I 208 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS I 209 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS I 210 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS I 211 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS I 212 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS I 213 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS I 214 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS I 215 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS I 216 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA J 30 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA J 31 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU J 205 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU PHE J 206 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU VAL J 207 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU J 208 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS J 209 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS J 210 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS J 211 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS J 212 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS J 213 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS J 214 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS J 215 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS J 216 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA K 30 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA K 31 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU K 205 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU PHE K 206 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU VAL K 207 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU K 208 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS K 209 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS K 210 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS K 211 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS K 212 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS K 213 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS K 214 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS K 215 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS K 216 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA L 30 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU ALA L 31 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU L 205 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU PHE L 206 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU VAL L 207 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU GLU L 208 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS L 209 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS L 210 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS L 211 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS L 212 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS L 213 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS L 214 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS L 215 UNP B7ZLK0 EXPRESSION TAG
SEQADV 3NRU HIS L 216 UNP B7ZLK0 EXPRESSION TAG
SEQRES 1 A 187 ALA ALA GLU VAL LEU LEU LEU ASP SER LYS ALA GLN GLN
SEQRES 2 A 187 THR GLU LEU GLU TRP ILE SER SER PRO PRO ASN GLY TRP
SEQRES 3 A 187 GLU GLU ILE SER GLY LEU ASP GLU ASN TYR THR PRO ILE
SEQRES 4 A 187 ARG THR TYR GLN VAL CYS GLN VAL MET GLU PRO ASN GLN
SEQRES 5 A 187 ASN ASN TRP LEU ARG THR ASN TRP ILE SER LYS GLY ASN
SEQRES 6 A 187 ALA GLN ARG ILE PHE VAL GLU LEU LYS PHE THR LEU ARG
SEQRES 7 A 187 ASP CYS ASN SER LEU PRO GLY VAL LEU GLY THR CYS LYS
SEQRES 8 A 187 GLU THR PHE ASN LEU TYR TYR TYR GLU THR ASP TYR ASP
SEQRES 9 A 187 THR GLY ARG ASN ILE ARG GLU ASN LEU TYR VAL LYS ILE
SEQRES 10 A 187 ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN GLY ASP
SEQRES 11 A 187 LEU GLY GLU ARG LYS MET LYS LEU ASN THR GLU VAL ARG
SEQRES 12 A 187 GLU ILE GLY PRO LEU SER LYS LYS GLY PHE TYR LEU ALA
SEQRES 13 A 187 PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL SER VAL
SEQRES 14 A 187 LYS VAL TYR TYR LYS LYS GLU PHE VAL GLU HIS HIS HIS
SEQRES 15 A 187 HIS HIS HIS HIS HIS
SEQRES 1 B 187 ALA ALA GLU VAL LEU LEU LEU ASP SER LYS ALA GLN GLN
SEQRES 2 B 187 THR GLU LEU GLU TRP ILE SER SER PRO PRO ASN GLY TRP
SEQRES 3 B 187 GLU GLU ILE SER GLY LEU ASP GLU ASN TYR THR PRO ILE
SEQRES 4 B 187 ARG THR TYR GLN VAL CYS GLN VAL MET GLU PRO ASN GLN
SEQRES 5 B 187 ASN ASN TRP LEU ARG THR ASN TRP ILE SER LYS GLY ASN
SEQRES 6 B 187 ALA GLN ARG ILE PHE VAL GLU LEU LYS PHE THR LEU ARG
SEQRES 7 B 187 ASP CYS ASN SER LEU PRO GLY VAL LEU GLY THR CYS LYS
SEQRES 8 B 187 GLU THR PHE ASN LEU TYR TYR TYR GLU THR ASP TYR ASP
SEQRES 9 B 187 THR GLY ARG ASN ILE ARG GLU ASN LEU TYR VAL LYS ILE
SEQRES 10 B 187 ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN GLY ASP
SEQRES 11 B 187 LEU GLY GLU ARG LYS MET LYS LEU ASN THR GLU VAL ARG
SEQRES 12 B 187 GLU ILE GLY PRO LEU SER LYS LYS GLY PHE TYR LEU ALA
SEQRES 13 B 187 PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL SER VAL
SEQRES 14 B 187 LYS VAL TYR TYR LYS LYS GLU PHE VAL GLU HIS HIS HIS
SEQRES 15 B 187 HIS HIS HIS HIS HIS
SEQRES 1 C 187 ALA ALA GLU VAL LEU LEU LEU ASP SER LYS ALA GLN GLN
SEQRES 2 C 187 THR GLU LEU GLU TRP ILE SER SER PRO PRO ASN GLY TRP
SEQRES 3 C 187 GLU GLU ILE SER GLY LEU ASP GLU ASN TYR THR PRO ILE
SEQRES 4 C 187 ARG THR TYR GLN VAL CYS GLN VAL MET GLU PRO ASN GLN
SEQRES 5 C 187 ASN ASN TRP LEU ARG THR ASN TRP ILE SER LYS GLY ASN
SEQRES 6 C 187 ALA GLN ARG ILE PHE VAL GLU LEU LYS PHE THR LEU ARG
SEQRES 7 C 187 ASP CYS ASN SER LEU PRO GLY VAL LEU GLY THR CYS LYS
SEQRES 8 C 187 GLU THR PHE ASN LEU TYR TYR TYR GLU THR ASP TYR ASP
SEQRES 9 C 187 THR GLY ARG ASN ILE ARG GLU ASN LEU TYR VAL LYS ILE
SEQRES 10 C 187 ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN GLY ASP
SEQRES 11 C 187 LEU GLY GLU ARG LYS MET LYS LEU ASN THR GLU VAL ARG
SEQRES 12 C 187 GLU ILE GLY PRO LEU SER LYS LYS GLY PHE TYR LEU ALA
SEQRES 13 C 187 PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL SER VAL
SEQRES 14 C 187 LYS VAL TYR TYR LYS LYS GLU PHE VAL GLU HIS HIS HIS
SEQRES 15 C 187 HIS HIS HIS HIS HIS
SEQRES 1 D 187 ALA ALA GLU VAL LEU LEU LEU ASP SER LYS ALA GLN GLN
SEQRES 2 D 187 THR GLU LEU GLU TRP ILE SER SER PRO PRO ASN GLY TRP
SEQRES 3 D 187 GLU GLU ILE SER GLY LEU ASP GLU ASN TYR THR PRO ILE
SEQRES 4 D 187 ARG THR TYR GLN VAL CYS GLN VAL MET GLU PRO ASN GLN
SEQRES 5 D 187 ASN ASN TRP LEU ARG THR ASN TRP ILE SER LYS GLY ASN
SEQRES 6 D 187 ALA GLN ARG ILE PHE VAL GLU LEU LYS PHE THR LEU ARG
SEQRES 7 D 187 ASP CYS ASN SER LEU PRO GLY VAL LEU GLY THR CYS LYS
SEQRES 8 D 187 GLU THR PHE ASN LEU TYR TYR TYR GLU THR ASP TYR ASP
SEQRES 9 D 187 THR GLY ARG ASN ILE ARG GLU ASN LEU TYR VAL LYS ILE
SEQRES 10 D 187 ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN GLY ASP
SEQRES 11 D 187 LEU GLY GLU ARG LYS MET LYS LEU ASN THR GLU VAL ARG
SEQRES 12 D 187 GLU ILE GLY PRO LEU SER LYS LYS GLY PHE TYR LEU ALA
SEQRES 13 D 187 PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL SER VAL
SEQRES 14 D 187 LYS VAL TYR TYR LYS LYS GLU PHE VAL GLU HIS HIS HIS
SEQRES 15 D 187 HIS HIS HIS HIS HIS
SEQRES 1 E 187 ALA ALA GLU VAL LEU LEU LEU ASP SER LYS ALA GLN GLN
SEQRES 2 E 187 THR GLU LEU GLU TRP ILE SER SER PRO PRO ASN GLY TRP
SEQRES 3 E 187 GLU GLU ILE SER GLY LEU ASP GLU ASN TYR THR PRO ILE
SEQRES 4 E 187 ARG THR TYR GLN VAL CYS GLN VAL MET GLU PRO ASN GLN
SEQRES 5 E 187 ASN ASN TRP LEU ARG THR ASN TRP ILE SER LYS GLY ASN
SEQRES 6 E 187 ALA GLN ARG ILE PHE VAL GLU LEU LYS PHE THR LEU ARG
SEQRES 7 E 187 ASP CYS ASN SER LEU PRO GLY VAL LEU GLY THR CYS LYS
SEQRES 8 E 187 GLU THR PHE ASN LEU TYR TYR TYR GLU THR ASP TYR ASP
SEQRES 9 E 187 THR GLY ARG ASN ILE ARG GLU ASN LEU TYR VAL LYS ILE
SEQRES 10 E 187 ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN GLY ASP
SEQRES 11 E 187 LEU GLY GLU ARG LYS MET LYS LEU ASN THR GLU VAL ARG
SEQRES 12 E 187 GLU ILE GLY PRO LEU SER LYS LYS GLY PHE TYR LEU ALA
SEQRES 13 E 187 PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL SER VAL
SEQRES 14 E 187 LYS VAL TYR TYR LYS LYS GLU PHE VAL GLU HIS HIS HIS
SEQRES 15 E 187 HIS HIS HIS HIS HIS
SEQRES 1 F 187 ALA ALA GLU VAL LEU LEU LEU ASP SER LYS ALA GLN GLN
SEQRES 2 F 187 THR GLU LEU GLU TRP ILE SER SER PRO PRO ASN GLY TRP
SEQRES 3 F 187 GLU GLU ILE SER GLY LEU ASP GLU ASN TYR THR PRO ILE
SEQRES 4 F 187 ARG THR TYR GLN VAL CYS GLN VAL MET GLU PRO ASN GLN
SEQRES 5 F 187 ASN ASN TRP LEU ARG THR ASN TRP ILE SER LYS GLY ASN
SEQRES 6 F 187 ALA GLN ARG ILE PHE VAL GLU LEU LYS PHE THR LEU ARG
SEQRES 7 F 187 ASP CYS ASN SER LEU PRO GLY VAL LEU GLY THR CYS LYS
SEQRES 8 F 187 GLU THR PHE ASN LEU TYR TYR TYR GLU THR ASP TYR ASP
SEQRES 9 F 187 THR GLY ARG ASN ILE ARG GLU ASN LEU TYR VAL LYS ILE
SEQRES 10 F 187 ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN GLY ASP
SEQRES 11 F 187 LEU GLY GLU ARG LYS MET LYS LEU ASN THR GLU VAL ARG
SEQRES 12 F 187 GLU ILE GLY PRO LEU SER LYS LYS GLY PHE TYR LEU ALA
SEQRES 13 F 187 PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL SER VAL
SEQRES 14 F 187 LYS VAL TYR TYR LYS LYS GLU PHE VAL GLU HIS HIS HIS
SEQRES 15 F 187 HIS HIS HIS HIS HIS
SEQRES 1 G 187 ALA ALA GLU VAL LEU LEU LEU ASP SER LYS ALA GLN GLN
SEQRES 2 G 187 THR GLU LEU GLU TRP ILE SER SER PRO PRO ASN GLY TRP
SEQRES 3 G 187 GLU GLU ILE SER GLY LEU ASP GLU ASN TYR THR PRO ILE
SEQRES 4 G 187 ARG THR TYR GLN VAL CYS GLN VAL MET GLU PRO ASN GLN
SEQRES 5 G 187 ASN ASN TRP LEU ARG THR ASN TRP ILE SER LYS GLY ASN
SEQRES 6 G 187 ALA GLN ARG ILE PHE VAL GLU LEU LYS PHE THR LEU ARG
SEQRES 7 G 187 ASP CYS ASN SER LEU PRO GLY VAL LEU GLY THR CYS LYS
SEQRES 8 G 187 GLU THR PHE ASN LEU TYR TYR TYR GLU THR ASP TYR ASP
SEQRES 9 G 187 THR GLY ARG ASN ILE ARG GLU ASN LEU TYR VAL LYS ILE
SEQRES 10 G 187 ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN GLY ASP
SEQRES 11 G 187 LEU GLY GLU ARG LYS MET LYS LEU ASN THR GLU VAL ARG
SEQRES 12 G 187 GLU ILE GLY PRO LEU SER LYS LYS GLY PHE TYR LEU ALA
SEQRES 13 G 187 PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL SER VAL
SEQRES 14 G 187 LYS VAL TYR TYR LYS LYS GLU PHE VAL GLU HIS HIS HIS
SEQRES 15 G 187 HIS HIS HIS HIS HIS
SEQRES 1 H 187 ALA ALA GLU VAL LEU LEU LEU ASP SER LYS ALA GLN GLN
SEQRES 2 H 187 THR GLU LEU GLU TRP ILE SER SER PRO PRO ASN GLY TRP
SEQRES 3 H 187 GLU GLU ILE SER GLY LEU ASP GLU ASN TYR THR PRO ILE
SEQRES 4 H 187 ARG THR TYR GLN VAL CYS GLN VAL MET GLU PRO ASN GLN
SEQRES 5 H 187 ASN ASN TRP LEU ARG THR ASN TRP ILE SER LYS GLY ASN
SEQRES 6 H 187 ALA GLN ARG ILE PHE VAL GLU LEU LYS PHE THR LEU ARG
SEQRES 7 H 187 ASP CYS ASN SER LEU PRO GLY VAL LEU GLY THR CYS LYS
SEQRES 8 H 187 GLU THR PHE ASN LEU TYR TYR TYR GLU THR ASP TYR ASP
SEQRES 9 H 187 THR GLY ARG ASN ILE ARG GLU ASN LEU TYR VAL LYS ILE
SEQRES 10 H 187 ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN GLY ASP
SEQRES 11 H 187 LEU GLY GLU ARG LYS MET LYS LEU ASN THR GLU VAL ARG
SEQRES 12 H 187 GLU ILE GLY PRO LEU SER LYS LYS GLY PHE TYR LEU ALA
SEQRES 13 H 187 PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL SER VAL
SEQRES 14 H 187 LYS VAL TYR TYR LYS LYS GLU PHE VAL GLU HIS HIS HIS
SEQRES 15 H 187 HIS HIS HIS HIS HIS
SEQRES 1 I 187 ALA ALA GLU VAL LEU LEU LEU ASP SER LYS ALA GLN GLN
SEQRES 2 I 187 THR GLU LEU GLU TRP ILE SER SER PRO PRO ASN GLY TRP
SEQRES 3 I 187 GLU GLU ILE SER GLY LEU ASP GLU ASN TYR THR PRO ILE
SEQRES 4 I 187 ARG THR TYR GLN VAL CYS GLN VAL MET GLU PRO ASN GLN
SEQRES 5 I 187 ASN ASN TRP LEU ARG THR ASN TRP ILE SER LYS GLY ASN
SEQRES 6 I 187 ALA GLN ARG ILE PHE VAL GLU LEU LYS PHE THR LEU ARG
SEQRES 7 I 187 ASP CYS ASN SER LEU PRO GLY VAL LEU GLY THR CYS LYS
SEQRES 8 I 187 GLU THR PHE ASN LEU TYR TYR TYR GLU THR ASP TYR ASP
SEQRES 9 I 187 THR GLY ARG ASN ILE ARG GLU ASN LEU TYR VAL LYS ILE
SEQRES 10 I 187 ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN GLY ASP
SEQRES 11 I 187 LEU GLY GLU ARG LYS MET LYS LEU ASN THR GLU VAL ARG
SEQRES 12 I 187 GLU ILE GLY PRO LEU SER LYS LYS GLY PHE TYR LEU ALA
SEQRES 13 I 187 PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL SER VAL
SEQRES 14 I 187 LYS VAL TYR TYR LYS LYS GLU PHE VAL GLU HIS HIS HIS
SEQRES 15 I 187 HIS HIS HIS HIS HIS
SEQRES 1 J 187 ALA ALA GLU VAL LEU LEU LEU ASP SER LYS ALA GLN GLN
SEQRES 2 J 187 THR GLU LEU GLU TRP ILE SER SER PRO PRO ASN GLY TRP
SEQRES 3 J 187 GLU GLU ILE SER GLY LEU ASP GLU ASN TYR THR PRO ILE
SEQRES 4 J 187 ARG THR TYR GLN VAL CYS GLN VAL MET GLU PRO ASN GLN
SEQRES 5 J 187 ASN ASN TRP LEU ARG THR ASN TRP ILE SER LYS GLY ASN
SEQRES 6 J 187 ALA GLN ARG ILE PHE VAL GLU LEU LYS PHE THR LEU ARG
SEQRES 7 J 187 ASP CYS ASN SER LEU PRO GLY VAL LEU GLY THR CYS LYS
SEQRES 8 J 187 GLU THR PHE ASN LEU TYR TYR TYR GLU THR ASP TYR ASP
SEQRES 9 J 187 THR GLY ARG ASN ILE ARG GLU ASN LEU TYR VAL LYS ILE
SEQRES 10 J 187 ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN GLY ASP
SEQRES 11 J 187 LEU GLY GLU ARG LYS MET LYS LEU ASN THR GLU VAL ARG
SEQRES 12 J 187 GLU ILE GLY PRO LEU SER LYS LYS GLY PHE TYR LEU ALA
SEQRES 13 J 187 PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL SER VAL
SEQRES 14 J 187 LYS VAL TYR TYR LYS LYS GLU PHE VAL GLU HIS HIS HIS
SEQRES 15 J 187 HIS HIS HIS HIS HIS
SEQRES 1 K 187 ALA ALA GLU VAL LEU LEU LEU ASP SER LYS ALA GLN GLN
SEQRES 2 K 187 THR GLU LEU GLU TRP ILE SER SER PRO PRO ASN GLY TRP
SEQRES 3 K 187 GLU GLU ILE SER GLY LEU ASP GLU ASN TYR THR PRO ILE
SEQRES 4 K 187 ARG THR TYR GLN VAL CYS GLN VAL MET GLU PRO ASN GLN
SEQRES 5 K 187 ASN ASN TRP LEU ARG THR ASN TRP ILE SER LYS GLY ASN
SEQRES 6 K 187 ALA GLN ARG ILE PHE VAL GLU LEU LYS PHE THR LEU ARG
SEQRES 7 K 187 ASP CYS ASN SER LEU PRO GLY VAL LEU GLY THR CYS LYS
SEQRES 8 K 187 GLU THR PHE ASN LEU TYR TYR TYR GLU THR ASP TYR ASP
SEQRES 9 K 187 THR GLY ARG ASN ILE ARG GLU ASN LEU TYR VAL LYS ILE
SEQRES 10 K 187 ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN GLY ASP
SEQRES 11 K 187 LEU GLY GLU ARG LYS MET LYS LEU ASN THR GLU VAL ARG
SEQRES 12 K 187 GLU ILE GLY PRO LEU SER LYS LYS GLY PHE TYR LEU ALA
SEQRES 13 K 187 PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL SER VAL
SEQRES 14 K 187 LYS VAL TYR TYR LYS LYS GLU PHE VAL GLU HIS HIS HIS
SEQRES 15 K 187 HIS HIS HIS HIS HIS
SEQRES 1 L 187 ALA ALA GLU VAL LEU LEU LEU ASP SER LYS ALA GLN GLN
SEQRES 2 L 187 THR GLU LEU GLU TRP ILE SER SER PRO PRO ASN GLY TRP
SEQRES 3 L 187 GLU GLU ILE SER GLY LEU ASP GLU ASN TYR THR PRO ILE
SEQRES 4 L 187 ARG THR TYR GLN VAL CYS GLN VAL MET GLU PRO ASN GLN
SEQRES 5 L 187 ASN ASN TRP LEU ARG THR ASN TRP ILE SER LYS GLY ASN
SEQRES 6 L 187 ALA GLN ARG ILE PHE VAL GLU LEU LYS PHE THR LEU ARG
SEQRES 7 L 187 ASP CYS ASN SER LEU PRO GLY VAL LEU GLY THR CYS LYS
SEQRES 8 L 187 GLU THR PHE ASN LEU TYR TYR TYR GLU THR ASP TYR ASP
SEQRES 9 L 187 THR GLY ARG ASN ILE ARG GLU ASN LEU TYR VAL LYS ILE
SEQRES 10 L 187 ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN GLY ASP
SEQRES 11 L 187 LEU GLY GLU ARG LYS MET LYS LEU ASN THR GLU VAL ARG
SEQRES 12 L 187 GLU ILE GLY PRO LEU SER LYS LYS GLY PHE TYR LEU ALA
SEQRES 13 L 187 PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL SER VAL
SEQRES 14 L 187 LYS VAL TYR TYR LYS LYS GLU PHE VAL GLU HIS HIS HIS
SEQRES 15 L 187 HIS HIS HIS HIS HIS
HET SO4 A 301 5
HET CL B 300 1
HET SO4 B 301 5
HET SO4 B 302 5
HET SO4 B 303 5
HET CL C 300 1
HET SO4 C 302 5
HET SO4 D 301 5
HET SO4 D 302 5
HET SO4 G 301 5
HET SO4 G 217 5
HET SO4 J 301 5
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 13 SO4 10(O4 S 2-)
FORMUL 14 CL 2(CL 1-)
FORMUL 25 HOH *610(H2 O)
HELIX 1 1 ARG A 139 TYR A 143 5 5
HELIX 2 2 ARG B 139 TYR B 143 5 5
HELIX 3 3 ASP C 108 LEU C 112 5 5
HELIX 4 4 ARG C 139 TYR C 143 5 5
HELIX 5 5 ASP D 108 LEU D 112 5 5
HELIX 6 6 ARG D 139 TYR D 143 5 5
HELIX 7 7 ASP E 108 LEU E 112 5 5
HELIX 8 8 ARG E 139 TYR E 143 5 5
HELIX 9 9 ARG F 139 TYR F 143 5 5
HELIX 10 10 LYS G 39 GLN G 41 5 3
HELIX 11 11 ASP G 108 LEU G 112 5 5
HELIX 12 12 ARG G 139 TYR G 143 5 5
HELIX 13 13 ASP H 108 LEU H 112 5 5
HELIX 14 14 ARG H 139 TYR H 143 5 5
HELIX 15 15 ASP I 108 LEU I 112 5 5
HELIX 16 16 ARG I 139 TYR I 143 5 5
HELIX 17 17 LYS J 39 GLN J 41 5 3
HELIX 18 18 ASP J 108 LEU J 112 5 5
HELIX 19 19 ARG J 139 TYR J 143 5 5
HELIX 20 20 LYS K 39 GLN K 41 5 3
HELIX 21 21 ARG K 139 TYR K 143 5 5
HELIX 22 22 ASP L 108 LEU L 112 5 5
HELIX 23 23 ARG L 139 TYR L 143 5 5
SHEET 1 A 4 VAL A 33 ASP A 37 0
SHEET 2 A 4 CYS A 192 TYR A 202 -1 O VAL A 200 N LEU A 35
SHEET 3 A 4 PRO A 67 CYS A 74 -1 N TYR A 71 O LEU A 195
SHEET 4 A 4 GLU A 56 LEU A 61 -1 N GLU A 56 O GLN A 72
SHEET 1 B 4 VAL A 33 ASP A 37 0
SHEET 2 B 4 CYS A 192 TYR A 202 -1 O VAL A 200 N LEU A 35
SHEET 3 B 4 ILE A 98 LEU A 106 -1 N GLU A 101 O LYS A 199
SHEET 4 B 4 ASN A 168 ILE A 174 -1 O ILE A 174 N ILE A 98
SHEET 1 C 4 ILE A 48 SER A 50 0
SHEET 2 C 4 ASN A 83 ARG A 86 -1 O TRP A 84 N SER A 50
SHEET 3 C 4 GLY A 181 ASP A 188 -1 O ASP A 188 N ASN A 83
SHEET 4 C 4 ILE A 90 SER A 91 -1 N ILE A 90 O PHE A 182
SHEET 1 D 5 ILE A 48 SER A 50 0
SHEET 2 D 5 ASN A 83 ARG A 86 -1 O TRP A 84 N SER A 50
SHEET 3 D 5 GLY A 181 ASP A 188 -1 O ASP A 188 N ASN A 83
SHEET 4 D 5 THR A 122 THR A 130 -1 N TYR A 126 O ALA A 185
SHEET 5 D 5 VAL A 144 ALA A 150 -1 O VAL A 144 N TYR A 127
SHEET 1 E 4 VAL B 33 ASP B 37 0
SHEET 2 E 4 CYS B 192 TYR B 202 -1 O VAL B 200 N LEU B 35
SHEET 3 E 4 PRO B 67 CYS B 74 -1 N TYR B 71 O LEU B 195
SHEET 4 E 4 GLU B 56 LEU B 61 -1 N GLU B 56 O GLN B 72
SHEET 1 F 4 VAL B 33 ASP B 37 0
SHEET 2 F 4 CYS B 192 TYR B 202 -1 O VAL B 200 N LEU B 35
SHEET 3 F 4 ILE B 98 THR B 105 -1 N PHE B 99 O TYR B 201
SHEET 4 F 4 ASN B 168 ILE B 174 -1 O ILE B 174 N ILE B 98
SHEET 1 G 4 ILE B 48 SER B 50 0
SHEET 2 G 4 ASN B 83 ARG B 86 -1 O TRP B 84 N SER B 50
SHEET 3 G 4 GLY B 181 ASP B 188 -1 O ASP B 188 N ASN B 83
SHEET 4 G 4 ILE B 90 SER B 91 -1 N ILE B 90 O PHE B 182
SHEET 1 H 5 ILE B 48 SER B 50 0
SHEET 2 H 5 ASN B 83 ARG B 86 -1 O TRP B 84 N SER B 50
SHEET 3 H 5 GLY B 181 ASP B 188 -1 O ASP B 188 N ASN B 83
SHEET 4 H 5 THR B 122 THR B 130 -1 N TYR B 126 O ALA B 185
SHEET 5 H 5 VAL B 144 ALA B 150 -1 O ILE B 149 N PHE B 123
SHEET 1 I 4 GLU C 32 ASP C 37 0
SHEET 2 I 4 ILE C 193 LYS C 203 -1 O VAL C 200 N LEU C 35
SHEET 3 I 4 PRO C 67 VAL C 73 -1 N TYR C 71 O LEU C 195
SHEET 4 I 4 GLU C 56 LEU C 61 -1 N ILE C 58 O THR C 70
SHEET 1 J 4 GLU C 32 ASP C 37 0
SHEET 2 J 4 ILE C 193 LYS C 203 -1 O VAL C 200 N LEU C 35
SHEET 3 J 4 ILE C 98 LEU C 106 -1 N GLU C 101 O LYS C 199
SHEET 4 J 4 ASN C 168 ILE C 174 -1 O ILE C 174 N ILE C 98
SHEET 1 K 4 ILE C 48 SER C 50 0
SHEET 2 K 4 ASN C 83 ARG C 86 -1 O TRP C 84 N SER C 50
SHEET 3 K 4 GLY C 181 ASP C 188 -1 O ASP C 188 N ASN C 83
SHEET 4 K 4 ILE C 90 SER C 91 -1 N ILE C 90 O PHE C 182
SHEET 1 L 5 ILE C 48 SER C 50 0
SHEET 2 L 5 ASN C 83 ARG C 86 -1 O TRP C 84 N SER C 50
SHEET 3 L 5 GLY C 181 ASP C 188 -1 O ASP C 188 N ASN C 83
SHEET 4 L 5 THR C 122 THR C 130 -1 N TYR C 126 O ALA C 185
SHEET 5 L 5 VAL C 144 ALA C 150 -1 O ILE C 149 N PHE C 123
SHEET 1 M 4 GLU D 32 ASP D 37 0
SHEET 2 M 4 ILE D 193 LYS D 203 -1 O VAL D 200 N LEU D 35
SHEET 3 M 4 PRO D 67 VAL D 73 -1 N TYR D 71 O LEU D 195
SHEET 4 M 4 GLU D 56 LEU D 61 -1 N GLU D 56 O GLN D 72
SHEET 1 N 4 GLU D 32 ASP D 37 0
SHEET 2 N 4 ILE D 193 LYS D 203 -1 O VAL D 200 N LEU D 35
SHEET 3 N 4 ILE D 98 LEU D 106 -1 N GLU D 101 O LYS D 199
SHEET 4 N 4 ASN D 168 ILE D 174 -1 O ILE D 174 N ILE D 98
SHEET 1 O 4 ILE D 48 SER D 50 0
SHEET 2 O 4 ASN D 83 ARG D 86 -1 O TRP D 84 N SER D 50
SHEET 3 O 4 GLY D 181 ASP D 188 -1 O ASP D 188 N ASN D 83
SHEET 4 O 4 ILE D 90 SER D 91 -1 N ILE D 90 O PHE D 182
SHEET 1 P 5 ILE D 48 SER D 50 0
SHEET 2 P 5 ASN D 83 ARG D 86 -1 O TRP D 84 N SER D 50
SHEET 3 P 5 GLY D 181 ASP D 188 -1 O ASP D 188 N ASN D 83
SHEET 4 P 5 THR D 122 THR D 130 -1 N TYR D 126 O ALA D 185
SHEET 5 P 5 VAL D 144 ALA D 150 -1 O ILE D 149 N PHE D 123
SHEET 1 Q 4 GLU E 32 ASP E 37 0
SHEET 2 Q 4 CYS E 192 LYS E 203 -1 O VAL E 200 N LEU E 35
SHEET 3 Q 4 PRO E 67 CYS E 74 -1 N TYR E 71 O LEU E 195
SHEET 4 Q 4 GLU E 56 LEU E 61 -1 N ILE E 58 O THR E 70
SHEET 1 R 4 GLU E 32 ASP E 37 0
SHEET 2 R 4 CYS E 192 LYS E 203 -1 O VAL E 200 N LEU E 35
SHEET 3 R 4 ILE E 98 LEU E 106 -1 N GLU E 101 O LYS E 199
SHEET 4 R 4 ASN E 168 ILE E 174 -1 O ILE E 174 N ILE E 98
SHEET 1 S 4 ILE E 48 SER E 50 0
SHEET 2 S 4 ASN E 83 ARG E 86 -1 O TRP E 84 N SER E 50
SHEET 3 S 4 GLY E 181 ASP E 188 -1 O ASP E 188 N ASN E 83
SHEET 4 S 4 ILE E 90 SER E 91 -1 N ILE E 90 O PHE E 182
SHEET 1 T 5 ILE E 48 SER E 50 0
SHEET 2 T 5 ASN E 83 ARG E 86 -1 O TRP E 84 N SER E 50
SHEET 3 T 5 GLY E 181 ASP E 188 -1 O ASP E 188 N ASN E 83
SHEET 4 T 5 THR E 122 THR E 130 -1 N TYR E 126 O ALA E 185
SHEET 5 T 5 VAL E 144 ALA E 150 -1 O ILE E 149 N PHE E 123
SHEET 1 U 4 GLU F 32 ASP F 37 0
SHEET 2 U 4 CYS F 192 LYS F 203 -1 O VAL F 200 N LEU F 35
SHEET 3 U 4 PRO F 67 CYS F 74 -1 N TYR F 71 O LEU F 195
SHEET 4 U 4 GLU F 56 LEU F 61 -1 N GLU F 56 O GLN F 72
SHEET 1 V 4 GLU F 32 ASP F 37 0
SHEET 2 V 4 CYS F 192 LYS F 203 -1 O VAL F 200 N LEU F 35
SHEET 3 V 4 ILE F 98 LEU F 106 -1 N GLU F 101 O LYS F 199
SHEET 4 V 4 ASN F 168 ILE F 174 -1 O ILE F 174 N ILE F 98
SHEET 1 W 4 ILE F 48 SER F 50 0
SHEET 2 W 4 ASN F 83 ARG F 86 -1 O TRP F 84 N SER F 50
SHEET 3 W 4 GLY F 181 ASP F 188 -1 O ASP F 188 N ASN F 83
SHEET 4 W 4 ILE F 90 SER F 91 -1 N ILE F 90 O PHE F 182
SHEET 1 X 5 ILE F 48 SER F 50 0
SHEET 2 X 5 ASN F 83 ARG F 86 -1 O TRP F 84 N SER F 50
SHEET 3 X 5 GLY F 181 ASP F 188 -1 O ASP F 188 N ASN F 83
SHEET 4 X 5 THR F 122 THR F 130 -1 N TYR F 126 O ALA F 185
SHEET 5 X 5 VAL F 144 ALA F 150 -1 O ILE F 149 N PHE F 123
SHEET 1 Y 4 GLU G 32 ASP G 37 0
SHEET 2 Y 4 CYS G 192 LYS G 203 -1 O VAL G 200 N LEU G 35
SHEET 3 Y 4 PRO G 67 CYS G 74 -1 N TYR G 71 O LEU G 195
SHEET 4 Y 4 GLU G 56 LEU G 61 -1 N ILE G 58 O THR G 70
SHEET 1 Z 4 GLU G 32 ASP G 37 0
SHEET 2 Z 4 CYS G 192 LYS G 203 -1 O VAL G 200 N LEU G 35
SHEET 3 Z 4 ILE G 98 LEU G 106 -1 N GLU G 101 O LYS G 199
SHEET 4 Z 4 ASN G 168 ILE G 174 -1 O GLU G 170 N LEU G 102
SHEET 1 AA 4 ILE G 48 SER G 50 0
SHEET 2 AA 4 ASN G 83 ARG G 86 -1 O TRP G 84 N SER G 50
SHEET 3 AA 4 GLY G 181 ASP G 188 -1 O ASP G 188 N ASN G 83
SHEET 4 AA 4 ILE G 90 SER G 91 -1 N ILE G 90 O PHE G 182
SHEET 1 AB 5 ILE G 48 SER G 50 0
SHEET 2 AB 5 ASN G 83 ARG G 86 -1 O TRP G 84 N SER G 50
SHEET 3 AB 5 GLY G 181 ASP G 188 -1 O ASP G 188 N ASN G 83
SHEET 4 AB 5 THR G 122 THR G 130 -1 N TYR G 126 O ALA G 185
SHEET 5 AB 5 VAL G 144 ALA G 150 -1 O ILE G 149 N PHE G 123
SHEET 1 AC 4 GLU H 32 ASP H 37 0
SHEET 2 AC 4 ILE H 193 LYS H 203 -1 O VAL H 200 N LEU H 35
SHEET 3 AC 4 PRO H 67 VAL H 73 -1 N TYR H 71 O LEU H 195
SHEET 4 AC 4 GLU H 56 LEU H 61 -1 N ILE H 58 O THR H 70
SHEET 1 AD 4 GLU H 32 ASP H 37 0
SHEET 2 AD 4 ILE H 193 LYS H 203 -1 O VAL H 200 N LEU H 35
SHEET 3 AD 4 ILE H 98 LEU H 106 -1 N GLU H 101 O LYS H 199
SHEET 4 AD 4 ASN H 168 ILE H 174 -1 O ILE H 174 N ILE H 98
SHEET 1 AE 4 ILE H 48 SER H 50 0
SHEET 2 AE 4 ASN H 83 ARG H 86 -1 O TRP H 84 N SER H 50
SHEET 3 AE 4 GLY H 181 ASP H 188 -1 O ASP H 188 N ASN H 83
SHEET 4 AE 4 ILE H 90 SER H 91 -1 N ILE H 90 O PHE H 182
SHEET 1 AF 5 ILE H 48 SER H 50 0
SHEET 2 AF 5 ASN H 83 ARG H 86 -1 O TRP H 84 N SER H 50
SHEET 3 AF 5 GLY H 181 ASP H 188 -1 O ASP H 188 N ASN H 83
SHEET 4 AF 5 THR H 122 THR H 130 -1 N TYR H 126 O ALA H 185
SHEET 5 AF 5 VAL H 144 ALA H 150 -1 O ILE H 149 N PHE H 123
SHEET 1 AG 4 VAL I 33 ASP I 37 0
SHEET 2 AG 4 CYS I 192 TYR I 202 -1 O VAL I 200 N LEU I 35
SHEET 3 AG 4 PRO I 67 CYS I 74 -1 N TYR I 71 O LEU I 195
SHEET 4 AG 4 GLU I 56 LEU I 61 -1 N ILE I 58 O THR I 70
SHEET 1 AH 4 VAL I 33 ASP I 37 0
SHEET 2 AH 4 CYS I 192 TYR I 202 -1 O VAL I 200 N LEU I 35
SHEET 3 AH 4 ILE I 98 LEU I 106 -1 N GLU I 101 O LYS I 199
SHEET 4 AH 4 ASN I 168 ILE I 174 -1 O ILE I 174 N ILE I 98
SHEET 1 AI 4 ILE I 48 SER I 50 0
SHEET 2 AI 4 ASN I 83 ARG I 86 -1 O TRP I 84 N SER I 50
SHEET 3 AI 4 GLY I 181 ASP I 188 -1 O ASP I 188 N ASN I 83
SHEET 4 AI 4 ILE I 90 SER I 91 -1 N ILE I 90 O PHE I 182
SHEET 1 AJ 5 ILE I 48 SER I 50 0
SHEET 2 AJ 5 ASN I 83 ARG I 86 -1 O TRP I 84 N SER I 50
SHEET 3 AJ 5 GLY I 181 ASP I 188 -1 O ASP I 188 N ASN I 83
SHEET 4 AJ 5 THR I 122 THR I 130 -1 N TYR I 126 O ALA I 185
SHEET 5 AJ 5 VAL I 144 ALA I 150 -1 O ILE I 149 N PHE I 123
SHEET 1 AK 4 GLU J 32 ASP J 37 0
SHEET 2 AK 4 CYS J 192 LYS J 203 -1 O VAL J 200 N LEU J 35
SHEET 3 AK 4 PRO J 67 CYS J 74 -1 N VAL J 73 O ILE J 193
SHEET 4 AK 4 GLU J 56 LEU J 61 -1 N ILE J 58 O THR J 70
SHEET 1 AL 4 GLU J 32 ASP J 37 0
SHEET 2 AL 4 CYS J 192 LYS J 203 -1 O VAL J 200 N LEU J 35
SHEET 3 AL 4 ILE J 98 LEU J 106 -1 N PHE J 99 O TYR J 201
SHEET 4 AL 4 ASN J 168 ILE J 174 -1 O ILE J 174 N ILE J 98
SHEET 1 AM 4 ILE J 48 SER J 50 0
SHEET 2 AM 4 ASN J 83 ARG J 86 -1 O ARG J 86 N ILE J 48
SHEET 3 AM 4 GLY J 181 ASP J 188 -1 O ASP J 188 N ASN J 83
SHEET 4 AM 4 ILE J 90 SER J 91 -1 N ILE J 90 O PHE J 182
SHEET 1 AN 5 ILE J 48 SER J 50 0
SHEET 2 AN 5 ASN J 83 ARG J 86 -1 O ARG J 86 N ILE J 48
SHEET 3 AN 5 GLY J 181 ASP J 188 -1 O ASP J 188 N ASN J 83
SHEET 4 AN 5 THR J 122 THR J 130 -1 N TYR J 126 O ALA J 185
SHEET 5 AN 5 VAL J 144 ALA J 150 -1 O ILE J 149 N PHE J 123
SHEET 1 AO 4 GLU K 32 ASP K 37 0
SHEET 2 AO 4 CYS K 192 LYS K 203 -1 O VAL K 200 N LEU K 35
SHEET 3 AO 4 PRO K 67 CYS K 74 -1 N TYR K 71 O LEU K 195
SHEET 4 AO 4 GLU K 56 LEU K 61 -1 N GLU K 56 O GLN K 72
SHEET 1 AP 4 GLU K 32 ASP K 37 0
SHEET 2 AP 4 CYS K 192 LYS K 203 -1 O VAL K 200 N LEU K 35
SHEET 3 AP 4 ILE K 98 LEU K 106 -1 N GLU K 101 O LYS K 199
SHEET 4 AP 4 ASN K 168 ILE K 174 -1 O ILE K 174 N ILE K 98
SHEET 1 AQ 4 ILE K 48 SER K 50 0
SHEET 2 AQ 4 ASN K 83 ARG K 86 -1 O TRP K 84 N SER K 50
SHEET 3 AQ 4 GLY K 181 ASP K 188 -1 O PHE K 186 N LEU K 85
SHEET 4 AQ 4 ILE K 90 SER K 91 -1 N ILE K 90 O PHE K 182
SHEET 1 AR 5 ILE K 48 SER K 50 0
SHEET 2 AR 5 ASN K 83 ARG K 86 -1 O TRP K 84 N SER K 50
SHEET 3 AR 5 GLY K 181 ASP K 188 -1 O PHE K 186 N LEU K 85
SHEET 4 AR 5 THR K 122 THR K 130 -1 N ASN K 124 O GLN K 187
SHEET 5 AR 5 VAL K 144 ALA K 150 -1 O ILE K 149 N PHE K 123
SHEET 1 AS 4 VAL L 33 ASP L 37 0
SHEET 2 AS 4 ILE L 193 TYR L 202 -1 O VAL L 200 N LEU L 35
SHEET 3 AS 4 PRO L 67 VAL L 73 -1 N TYR L 71 O LEU L 195
SHEET 4 AS 4 GLU L 56 LEU L 61 -1 N GLY L 60 O ILE L 68
SHEET 1 AT 4 VAL L 33 ASP L 37 0
SHEET 2 AT 4 ILE L 193 TYR L 202 -1 O VAL L 200 N LEU L 35
SHEET 3 AT 4 ILE L 98 LEU L 106 -1 N GLU L 101 O LYS L 199
SHEET 4 AT 4 ASN L 168 ILE L 174 -1 O ASN L 168 N PHE L 104
SHEET 1 AU 4 ILE L 48 SER L 50 0
SHEET 2 AU 4 ASN L 83 ARG L 86 -1 O TRP L 84 N SER L 50
SHEET 3 AU 4 GLY L 181 ASP L 188 -1 O ASP L 188 N ASN L 83
SHEET 4 AU 4 ILE L 90 SER L 91 -1 N ILE L 90 O PHE L 182
SHEET 1 AV 5 ILE L 48 SER L 50 0
SHEET 2 AV 5 ASN L 83 ARG L 86 -1 O TRP L 84 N SER L 50
SHEET 3 AV 5 GLY L 181 ASP L 188 -1 O ASP L 188 N ASN L 83
SHEET 4 AV 5 THR L 122 THR L 130 -1 N TYR L 126 O ALA L 185
SHEET 5 AV 5 VAL L 144 ALA L 150 -1 O ILE L 149 N PHE L 123
SSBOND 1 CYS A 74 CYS A 192 1555 1555 2.05
SSBOND 2 CYS A 109 CYS A 119 1555 1555 2.04
SSBOND 3 CYS B 74 CYS B 192 1555 1555 2.05
SSBOND 4 CYS B 109 CYS B 119 1555 1555 2.04
SSBOND 5 CYS C 74 CYS C 192 1555 1555 2.05
SSBOND 6 CYS C 109 CYS C 119 1555 1555 2.04
SSBOND 7 CYS D 74 CYS D 192 1555 1555 2.03
SSBOND 8 CYS D 109 CYS D 119 1555 1555 2.03
SSBOND 9 CYS E 74 CYS E 192 1555 1555 2.04
SSBOND 10 CYS E 109 CYS E 119 1555 1555 2.04
SSBOND 11 CYS F 74 CYS F 192 1555 1555 2.04
SSBOND 12 CYS F 109 CYS F 119 1555 1555 2.04
SSBOND 13 CYS G 74 CYS G 192 1555 1555 2.04
SSBOND 14 CYS G 109 CYS G 119 1555 1555 2.04
SSBOND 15 CYS H 74 CYS H 192 1555 1555 2.04
SSBOND 16 CYS H 109 CYS H 119 1555 1555 2.03
SSBOND 17 CYS I 109 CYS I 119 1555 1555 2.04
SSBOND 18 CYS J 74 CYS J 192 1555 1555 2.04
SSBOND 19 CYS J 109 CYS J 119 1555 1555 2.03
SSBOND 20 CYS K 74 CYS K 192 1555 1555 2.04
SSBOND 21 CYS K 109 CYS K 119 1555 1555 2.03
SSBOND 22 CYS L 74 CYS L 192 1555 1555 2.04
SSBOND 23 CYS L 109 CYS L 119 1555 1555 2.03
CISPEP 1 SER A 50 PRO A 51 0 -0.44
CISPEP 2 GLY A 175 PRO A 176 0 -1.74
CISPEP 3 SER B 50 PRO B 51 0 1.95
CISPEP 4 GLY B 175 PRO B 176 0 -1.30
CISPEP 5 SER C 50 PRO C 51 0 1.36
CISPEP 6 GLY C 175 PRO C 176 0 -0.94
CISPEP 7 SER D 50 PRO D 51 0 -1.60
CISPEP 8 GLY D 175 PRO D 176 0 -0.48
CISPEP 9 SER E 50 PRO E 51 0 0.36
CISPEP 10 GLY E 175 PRO E 176 0 -1.14
CISPEP 11 SER F 50 PRO F 51 0 -3.49
CISPEP 12 GLY F 175 PRO F 176 0 0.04
CISPEP 13 SER G 50 PRO G 51 0 -4.53
CISPEP 14 GLY G 175 PRO G 176 0 -2.18
CISPEP 15 SER H 50 PRO H 51 0 -1.45
CISPEP 16 GLY H 117 THR H 118 0 -8.67
CISPEP 17 GLY H 175 PRO H 176 0 0.03
CISPEP 18 SER I 50 PRO I 51 0 2.98
CISPEP 19 GLY I 175 PRO I 176 0 -1.92
CISPEP 20 SER J 50 PRO J 51 0 2.04
CISPEP 21 GLY J 175 PRO J 176 0 2.90
CISPEP 22 SER K 50 PRO K 51 0 0.76
CISPEP 23 GLY K 175 PRO K 176 0 1.68
CISPEP 24 SER L 50 PRO L 51 0 0.31
CISPEP 25 GLY L 175 PRO L 176 0 1.76
SITE 1 AC1 4 ARG A 139 HOH A 341 ASN C 137 ARG G 139
SITE 1 AC2 1 THR B 130
SITE 1 AC3 4 ASN B 137 ARG B 139 ARG E 139 ASN E 141
SITE 1 AC4 4 ARG B 139 GLU B 140 ASN B 141 LYS D 179
SITE 1 AC5 5 THR A 156 LYS B 39 LYS B 199 HOH B 384
SITE 2 AC5 5 ARG G 107
SITE 1 AC6 1 THR C 130
SITE 1 AC7 6 ARG A 139 ASN A 141 HOH A 313 HOH A 360
SITE 2 AC7 6 ASN C 137 ARG C 139
SITE 1 AC8 8 ARG D 139 GLU D 140 ASN D 141 HOH D 337
SITE 2 AC8 8 ASN E 137 ARG E 139 LEU E 142 HOH E 342
SITE 1 AC9 3 ASN B 137 ARG D 139 ARG E 139
SITE 1 BC1 6 ASN A 137 ARG A 139 HOH A 364 ARG G 139
SITE 2 BC1 6 GLU G 140 ASN G 141
SITE 1 BC2 4 ARG C 139 GLU C 140 ASN C 141 LYS G 179
SITE 1 BC3 4 ARG J 107 LYS K 39 LYS K 199 THR L 156
CRYST1 137.617 140.699 143.783 90.00 90.00 90.00 P 21 21 21 48
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 0.007267 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007107 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006955 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
