HEADER OXIDOREDUCTASE 29-APR-13 4BKP
TITLE CRYSTAL STRUCTURE OF HUMAN GDP-L-FUCOSE SYNTHASE WITH BOUND NADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GDP-L-FUCOSE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: GDP-4-KETO-6-DEOXY-D-MANNOSE-3,5-EPIMERASE-4-REDUCTASE,
COMPND 5 PROTEIN FX, RED CELL NADP(H)-BINDING PROTEIN, SHORT-CHAIN
COMPND 6 DEHYDROGENASE/REDUCTASE FAMILY 4E MEMBER 1;
COMPND 7 EC: 1.1.1.271;
COMPND 8 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_VARIANT: R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.VOLLMAR,N.SHAFQAT,A.ROJKOVA,T.KROJER,A.BRADLEY,J.W.RAYNOR,
AUTHOR 2 K.KAVANAGH,F.VON DELFT,C.H.ARROWSMITH,C.BOUNTRA,A.EDWARDS,
AUTHOR 3 U.OPPERMANN,W.W.YUE
REVDAT 3 20-DEC-23 4BKP 1 REMARK
REVDAT 2 24-JAN-18 4BKP 1 JRNL
REVDAT 1 12-JUN-13 4BKP 0
JRNL AUTH M.VOLLMAR,N.SHAFQAT,A.ROJKOVA,T.KROJER,A.BRADLEY,J.W.RAYNOR,
JRNL AUTH 2 K.KAVANAGH,F.VON DELFT,C.H.ARROWSMITH,C.BOUNTRA,A.EDWARDS,
JRNL AUTH 3 U.OPPERMANN,W.W.YUE
JRNL TITL CRYSTAL STRUCTURE OF HUMAN GDP-L-FUCOSE SYNTHASE WITH BOUND
JRNL TITL 2 NADP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 49.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 45196
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2408
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) : 3334
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.3320
REMARK 3 BIN FREE R VALUE SET COUNT : 169
REMARK 3 BIN FREE R VALUE : 0.4030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9797
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 209
REMARK 3 SOLVENT ATOMS : 50
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.94000
REMARK 3 B22 (A**2) : 0.47000
REMARK 3 B33 (A**2) : -1.40000
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): 0.766
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.299
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.223
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.103
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10274 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9116 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14057 ; 1.198 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20799 ; 0.868 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1290 ; 5.228 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 455 ;35.989 ;24.044
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1413 ;15.524 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;15.904 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1567 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11894 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2540 ; 0.003 ; 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): 5172 ; 5.044 ; 8.838
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5171 ; 5.042 ; 8.838
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6458 ; 7.215 ;16.582
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5100 ; 6.098 ; 9.119
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 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 -11 A 80
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3488 -17.2929 -53.5008
REMARK 3 T TENSOR
REMARK 3 T11: 0.1213 T22: 0.2293
REMARK 3 T33: 0.0864 T12: -0.0254
REMARK 3 T13: -0.0251 T23: -0.0479
REMARK 3 L TENSOR
REMARK 3 L11: 0.4466 L22: 0.4184
REMARK 3 L33: 3.2603 L12: 0.2707
REMARK 3 L13: 0.3511 L23: 1.0783
REMARK 3 S TENSOR
REMARK 3 S11: 0.1105 S12: -0.0929 S13: -0.0594
REMARK 3 S21: 0.0716 S22: -0.1719 S23: -0.0013
REMARK 3 S31: 0.0970 S32: -0.3757 S33: 0.0614
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 81 A 208
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9069 -28.9014 -66.1789
REMARK 3 T TENSOR
REMARK 3 T11: 0.2136 T22: 0.2157
REMARK 3 T33: 0.1436 T12: -0.0102
REMARK 3 T13: -0.0494 T23: -0.0776
REMARK 3 L TENSOR
REMARK 3 L11: 2.1160 L22: 1.0036
REMARK 3 L33: 0.7401 L12: 1.0226
REMARK 3 L13: 0.1536 L23: -0.0246
REMARK 3 S TENSOR
REMARK 3 S11: 0.1956 S12: -0.0124 S13: -0.2851
REMARK 3 S21: -0.0785 S22: -0.1355 S23: -0.1857
REMARK 3 S31: 0.1103 S32: -0.1182 S33: -0.0600
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 : A 209 A 320
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6841 -38.7305 -56.8707
REMARK 3 T TENSOR
REMARK 3 T11: 0.2230 T22: 0.1421
REMARK 3 T33: 0.1407 T12: -0.0967
REMARK 3 T13: -0.1467 T23: 0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 2.9010 L22: 1.4402
REMARK 3 L33: 1.8391 L12: 1.8582
REMARK 3 L13: 1.0613 L23: 0.4472
REMARK 3 S TENSOR
REMARK 3 S11: 0.5876 S12: -0.3596 S13: -0.3773
REMARK 3 S21: 0.3676 S22: -0.3565 S23: -0.2425
REMARK 3 S31: 0.4512 S32: -0.1940 S33: -0.2311
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 -11 B 78
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0726 -10.1301 -94.4036
REMARK 3 T TENSOR
REMARK 3 T11: 0.2350 T22: 0.3482
REMARK 3 T33: 0.0770 T12: -0.1078
REMARK 3 T13: 0.0290 T23: -0.0654
REMARK 3 L TENSOR
REMARK 3 L11: 0.4866 L22: 0.4490
REMARK 3 L33: 4.5726 L12: -0.2156
REMARK 3 L13: 1.2024 L23: 0.1497
REMARK 3 S TENSOR
REMARK 3 S11: -0.0892 S12: 0.0836 S13: 0.0951
REMARK 3 S21: -0.0599 S22: 0.0747 S23: -0.1790
REMARK 3 S31: -0.3580 S32: 0.1213 S33: 0.0145
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 : B 79 B 210
REMARK 3 ORIGIN FOR THE GROUP (A): 20.2234 -20.8570 -81.5200
REMARK 3 T TENSOR
REMARK 3 T11: 0.2142 T22: 0.3050
REMARK 3 T33: 0.1764 T12: -0.0276
REMARK 3 T13: 0.0146 T23: -0.1508
REMARK 3 L TENSOR
REMARK 3 L11: 1.2160 L22: 0.4314
REMARK 3 L33: 1.2776 L12: 0.5815
REMARK 3 L13: -1.1635 L23: -0.4694
REMARK 3 S TENSOR
REMARK 3 S11: -0.1633 S12: 0.0593 S13: -0.2459
REMARK 3 S21: -0.0516 S22: 0.0435 S23: -0.2039
REMARK 3 S31: 0.0425 S32: 0.0919 S33: 0.1198
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 : B 211 B 320
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8288 -23.5959 -91.9697
REMARK 3 T TENSOR
REMARK 3 T11: 0.0939 T22: 0.3551
REMARK 3 T33: 0.2940 T12: -0.0128
REMARK 3 T13: 0.0998 T23: -0.2563
REMARK 3 L TENSOR
REMARK 3 L11: 5.4274 L22: 1.7510
REMARK 3 L33: 1.9518 L12: 0.9695
REMARK 3 L13: 0.0840 L23: -0.3320
REMARK 3 S TENSOR
REMARK 3 S11: -0.2344 S12: 0.6701 S13: -0.5816
REMARK 3 S21: -0.2171 S22: 0.2140 S23: -0.4932
REMARK 3 S31: 0.3279 S32: 0.4258 S33: 0.0204
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 : C -12 C 78
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1041 -2.5073 -45.0844
REMARK 3 T TENSOR
REMARK 3 T11: 0.0973 T22: 0.0706
REMARK 3 T33: 0.1660 T12: -0.0011
REMARK 3 T13: 0.0677 T23: -0.0565
REMARK 3 L TENSOR
REMARK 3 L11: 1.1482 L22: 0.3550
REMARK 3 L33: 3.9601 L12: 0.4075
REMARK 3 L13: -0.6004 L23: -0.2008
REMARK 3 S TENSOR
REMARK 3 S11: -0.1774 S12: 0.2375 S13: -0.3220
REMARK 3 S21: -0.1443 S22: 0.0335 S23: -0.0823
REMARK 3 S31: 0.2250 S32: -0.0057 S33: 0.1439
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 : C 79 C 183
REMARK 3 ORIGIN FOR THE GROUP (A): -26.4288 4.7865 -32.1299
REMARK 3 T TENSOR
REMARK 3 T11: 0.0850 T22: 0.1385
REMARK 3 T33: 0.1563 T12: -0.0172
REMARK 3 T13: 0.0166 T23: 0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 1.3315 L22: 1.6032
REMARK 3 L33: 0.5532 L12: 0.3184
REMARK 3 L13: 0.4009 L23: 0.7868
REMARK 3 S TENSOR
REMARK 3 S11: -0.0867 S12: -0.0260 S13: -0.1470
REMARK 3 S21: -0.1010 S22: -0.0358 S23: 0.0623
REMARK 3 S31: -0.0446 S32: -0.0306 S33: 0.1225
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 : C 184 C 321
REMARK 3 ORIGIN FOR THE GROUP (A): -40.4248 -7.0248 -40.2757
REMARK 3 T TENSOR
REMARK 3 T11: 0.0851 T22: 0.1785
REMARK 3 T33: 0.2760 T12: -0.0523
REMARK 3 T13: 0.0249 T23: -0.1129
REMARK 3 L TENSOR
REMARK 3 L11: 3.0483 L22: 3.0242
REMARK 3 L33: 1.2217 L12: 0.8417
REMARK 3 L13: -0.5883 L23: -0.4849
REMARK 3 S TENSOR
REMARK 3 S11: -0.3747 S12: 0.5680 S13: -0.6873
REMARK 3 S21: -0.1890 S22: 0.2147 S23: 0.1161
REMARK 3 S31: -0.0460 S32: -0.3790 S33: 0.1600
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 : D -7 D 35
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1590 15.9009 2.7143
REMARK 3 T TENSOR
REMARK 3 T11: 0.7738 T22: 0.2358
REMARK 3 T33: 0.4133 T12: -0.1799
REMARK 3 T13: -0.1966 T23: 0.1774
REMARK 3 L TENSOR
REMARK 3 L11: 0.4345 L22: 1.9021
REMARK 3 L33: 1.5435 L12: -0.7430
REMARK 3 L13: 0.6070 L23: -1.6985
REMARK 3 S TENSOR
REMARK 3 S11: -0.1807 S12: 0.0204 S13: -0.0593
REMARK 3 S21: 0.7237 S22: -0.2974 S23: -0.3821
REMARK 3 S31: -0.6421 S32: 0.3310 S33: 0.4780
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 : D 36 D 92
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0846 13.5718 -15.7318
REMARK 3 T TENSOR
REMARK 3 T11: 0.0997 T22: 0.1185
REMARK 3 T33: 0.1423 T12: -0.0146
REMARK 3 T13: -0.0643 T23: 0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 1.0420 L22: 3.2653
REMARK 3 L33: 5.5131 L12: 0.7930
REMARK 3 L13: 0.6574 L23: -1.2202
REMARK 3 S TENSOR
REMARK 3 S11: 0.1700 S12: -0.0641 S13: -0.1994
REMARK 3 S21: 0.1185 S22: -0.0310 S23: -0.4639
REMARK 3 S31: -0.0922 S32: 0.2121 S33: -0.1390
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 : D 93 D 320
REMARK 3 ORIGIN FOR THE GROUP (A): -20.6252 26.9152 -11.3509
REMARK 3 T TENSOR
REMARK 3 T11: 0.2697 T22: 0.1171
REMARK 3 T33: 0.0794 T12: 0.0732
REMARK 3 T13: -0.0896 T23: -0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 1.2460 L22: 2.7867
REMARK 3 L33: 1.7551 L12: 0.4228
REMARK 3 L13: 1.0039 L23: 0.6423
REMARK 3 S TENSOR
REMARK 3 S11: -0.1875 S12: -0.2931 S13: 0.1802
REMARK 3 S21: 0.4394 S22: -0.1268 S23: -0.0352
REMARK 3 S31: -0.2928 S32: -0.2845 S33: 0.3143
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. U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 4BKP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1290056674.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47605
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 49.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9000
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) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 1.07000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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: PDB ENTRY 4B8W
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M CITRATE PH 5.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 53.29800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 81.54750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 98.79050
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 53.29800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 81.54750
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 98.79050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 53.29800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 81.54750
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 98.79050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 53.29800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 81.54750
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 98.79050
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 SER A -15
REMARK 465 SER A -14
REMARK 465 GLY A -13
REMARK 465 VAL A -12
REMARK 465 LYS A 321
REMARK 465 MET B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 SER B -15
REMARK 465 SER B -14
REMARK 465 GLY B -13
REMARK 465 VAL B -12
REMARK 465 LYS B 321
REMARK 465 MET C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 SER C -15
REMARK 465 SER C -14
REMARK 465 GLY C -13
REMARK 465 MET D -22
REMARK 465 HIS D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 SER D -15
REMARK 465 SER D -14
REMARK 465 GLY D -13
REMARK 465 VAL D -12
REMARK 465 ASP D -11
REMARK 465 LEU D -10
REMARK 465 GLY D -9
REMARK 465 THR D -8
REMARK 465 LYS D 321
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 ASP A -11 CG OD1 OD2
REMARK 470 LYS A 44 CG CD CE NZ
REMARK 470 GLU A 59 CG CD OE1 OE2
REMARK 470 LEU A 76 CG CD1 CD2
REMARK 470 PHE A 77 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 78 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 79 CG OD1 ND2
REMARK 470 ILE A 80 CG1 CG2 CD1
REMARK 470 VAL A 104 CG1 CG2
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 GLU A 183 CG CD OE1 OE2
REMARK 470 ASP A 184 CG OD1 OD2
REMARK 470 LYS A 199 CE NZ
REMARK 470 SER A 200 OG
REMARK 470 SER A 201 OG
REMARK 470 SER A 203 OG
REMARK 470 LYS A 253 CG CD CE NZ
REMARK 470 VAL A 260 CG1 CG2
REMARK 470 ASP A 264 CG OD1 OD2
REMARK 470 GLU A 268 CG CD OE1 OE2
REMARK 470 THR A 270 OG1 CG2
REMARK 470 LYS A 275 CE NZ
REMARK 470 SER A 276 OG
REMARK 470 LYS A 282 CG CD CE NZ
REMARK 470 SER A 287 OG
REMARK 470 ARG A 297 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 302 CG CD CE NZ
REMARK 470 LYS A 306 CG CD CE NZ
REMARK 470 GLU A 317 CG CD OE1 OE2
REMARK 470 GLN A 318 CG CD OE1 NE2
REMARK 470 ASP B -11 CG OD1 OD2
REMARK 470 LEU B -10 CG CD1 CD2
REMARK 470 GLU B -7 CG CD OE1 OE2
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 LEU B 76 CG CD1 CD2
REMARK 470 PHE B 77 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 78 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 79 CG OD1 ND2
REMARK 470 ILE B 80 CG1 CG2 CD1
REMARK 470 VAL B 104 CG1 CG2
REMARK 470 ARG B 107 NE CZ NH1 NH2
REMARK 470 LYS B 121 CG CD CE NZ
REMARK 470 SER B 139 OG
REMARK 470 GLU B 183 CG CD OE1 OE2
REMARK 470 ASP B 184 CG OD1 OD2
REMARK 470 LYS B 194 CG CD CE NZ
REMARK 470 LEU B 197 CG CD1 CD2
REMARK 470 LYS B 199 CE NZ
REMARK 470 SER B 200 OG
REMARK 470 SER B 201 OG
REMARK 470 SER B 203 OG
REMARK 470 LEU B 205 CG CD1 CD2
REMARK 470 THR B 206 OG1 CG2
REMARK 470 TRP B 208 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 208 CZ3 CH2
REMARK 470 THR B 210 OG1 CG2
REMARK 470 ARG B 214 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 246 CG CD OE1 OE2
REMARK 470 ILE B 252 CG1 CG2 CD1
REMARK 470 LYS B 253 CG CD CE NZ
REMARK 470 GLU B 254 CG CD OE1 OE2
REMARK 470 GLU B 257 CG CD OE1 OE2
REMARK 470 VAL B 260 CG1 CG2
REMARK 470 GLU B 268 CG CD OE1 OE2
REMARK 470 VAL B 269 CG1 CG2
REMARK 470 THR B 270 OG1 CG2
REMARK 470 PHE B 271 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 272 CG OD1 OD2
REMARK 470 THR B 273 OG1 CG2
REMARK 470 THR B 274 OG1 CG2
REMARK 470 LYS B 275 CG CD CE NZ
REMARK 470 SER B 276 OG
REMARK 470 GLN B 279 CG CD OE1 NE2
REMARK 470 LYS B 281 CG CD CE NZ
REMARK 470 LYS B 282 CG CD CE NZ
REMARK 470 SER B 287 OG
REMARK 470 ARG B 297 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 302 CG CD CE NZ
REMARK 470 LYS B 306 CG CD CE NZ
REMARK 470 ASP B 314 CG OD1 OD2
REMARK 470 GLU B 317 CG CD OE1 OE2
REMARK 470 GLN B 318 CG CD OE1 NE2
REMARK 470 GLU C -7 CG CD OE1 OE2
REMARK 470 LYS C 25 CG CD CE NZ
REMARK 470 LYS C 44 CG CD CE NZ
REMARK 470 ARG C 78 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 79 CG OD1 ND2
REMARK 470 ILE C 80 CG1 CG2 CD1
REMARK 470 LYS C 121 CG CD CE NZ
REMARK 470 GLU C 183 CG CD OE1 OE2
REMARK 470 SER C 200 OG
REMARK 470 SER C 201 OG
REMARK 470 SER C 203 OG
REMARK 470 GLU C 246 CG CD OE1 OE2
REMARK 470 VAL C 260 CG1 CG2
REMARK 470 GLU C 268 CG CD OE1 OE2
REMARK 470 THR C 270 OG1 CG2
REMARK 470 THR C 274 OG1 CG2
REMARK 470 LYS C 275 CG CD CE NZ
REMARK 470 SER C 276 OG
REMARK 470 SER C 287 OG
REMARK 470 ASP C 295 CG OD1 OD2
REMARK 470 ARG C 297 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 306 CG CD CE NZ
REMARK 470 GLU C 317 CG CD OE1 OE2
REMARK 470 GLN C 318 CG CD OE1 NE2
REMARK 470 LYS C 321 CG CD CE NZ
REMARK 470 GLU D -7 CG CD OE1 OE2
REMARK 470 SER D -1 OG
REMARK 470 LYS D 25 CG CD CE NZ
REMARK 470 LYS D 44 CG CD CE NZ
REMARK 470 PHE D 77 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 78 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 79 CG OD1 ND2
REMARK 470 ILE D 80 CG1 CG2 CD1
REMARK 470 LYS D 121 CG CD CE NZ
REMARK 470 SER D 139 OG
REMARK 470 GLU D 183 CG CD OE1 OE2
REMARK 470 LYS D 199 CE NZ
REMARK 470 SER D 200 OG
REMARK 470 SER D 201 OG
REMARK 470 SER D 203 OG
REMARK 470 THR D 206 OG1 CG2
REMARK 470 GLN D 225 CG CD OE1 NE2
REMARK 470 LYS D 253 CG CD CE NZ
REMARK 470 GLU D 257 CG CD OE1 OE2
REMARK 470 VAL D 260 CG1 CG2
REMARK 470 GLU D 261 CG CD OE1 OE2
REMARK 470 GLU D 268 CG CD OE1 OE2
REMARK 470 VAL D 269 CG1 CG2
REMARK 470 THR D 274 OG1 CG2
REMARK 470 LYS D 275 CG CD CE NZ
REMARK 470 LYS D 281 CE NZ
REMARK 470 SER D 287 OG
REMARK 470 ASP D 295 CG OD1 OD2
REMARK 470 ARG D 297 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 302 CG CD CE NZ
REMARK 470 LYS D 306 CG CD CE NZ
REMARK 470 GLU D 317 CG CD OE1 OE2
REMARK 470 GLN D 318 CG CD OE1 NE2
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 ALA A 46 134.08 -179.84
REMARK 500 PHE A 77 -4.14 84.55
REMARK 500 THR A 171 -143.58 -83.12
REMARK 500 ALA B 46 133.47 179.68
REMARK 500 PHE B 77 -3.63 84.47
REMARK 500 THR B 171 -144.29 -83.90
REMARK 500 ALA C 46 134.35 179.95
REMARK 500 PHE C 77 -3.58 83.50
REMARK 500 THR C 171 -144.19 -83.09
REMARK 500 LYS C 282 40.34 -140.08
REMARK 500 ALA D 46 133.71 -179.53
REMARK 500 PHE D 77 -2.93 83.55
REMARK 500 THR D 171 -143.98 -83.12
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 NAP A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 1321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1321
DBREF 4BKP A 8 321 UNP Q13630 FCL_HUMAN 8 321
DBREF 4BKP B 8 321 UNP Q13630 FCL_HUMAN 8 321
DBREF 4BKP C 8 321 UNP Q13630 FCL_HUMAN 8 321
DBREF 4BKP D 8 321 UNP Q13630 FCL_HUMAN 8 321
SEQADV 4BKP MET A -22 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS A -21 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS A -20 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS A -19 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS A -18 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS A -17 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS A -16 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP SER A -15 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP SER A -14 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLY A -13 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP VAL A -12 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP ASP A -11 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP LEU A -10 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLY A -9 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP THR A -8 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLU A -7 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP ASN A -6 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP LEU A -5 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP TYR A -4 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP PHE A -3 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLN A -2 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP SER A -1 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP MET B -22 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS B -21 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS B -20 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS B -19 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS B -18 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS B -17 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS B -16 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP SER B -15 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP SER B -14 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLY B -13 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP VAL B -12 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP ASP B -11 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP LEU B -10 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLY B -9 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP THR B -8 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLU B -7 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP ASN B -6 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP LEU B -5 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP TYR B -4 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP PHE B -3 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLN B -2 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP SER B -1 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP MET C -22 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS C -21 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS C -20 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS C -19 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS C -18 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS C -17 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS C -16 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP SER C -15 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP SER C -14 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLY C -13 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP VAL C -12 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP ASP C -11 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP LEU C -10 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLY C -9 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP THR C -8 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLU C -7 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP ASN C -6 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP LEU C -5 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP TYR C -4 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP PHE C -3 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLN C -2 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP SER C -1 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP MET D -22 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS D -21 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS D -20 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS D -19 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS D -18 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS D -17 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP HIS D -16 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP SER D -15 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP SER D -14 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLY D -13 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP VAL D -12 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP ASP D -11 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP LEU D -10 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLY D -9 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP THR D -8 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLU D -7 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP ASN D -6 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP LEU D -5 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP TYR D -4 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP PHE D -3 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP GLN D -2 UNP Q13630 EXPRESSION TAG
SEQADV 4BKP SER D -1 UNP Q13630 EXPRESSION TAG
SEQRES 1 A 336 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 336 GLY THR GLU ASN LEU TYR PHE GLN SER MET ARG ILE LEU
SEQRES 3 A 336 VAL THR GLY GLY SER GLY LEU VAL GLY LYS ALA ILE GLN
SEQRES 4 A 336 LYS VAL VAL ALA ASP GLY ALA GLY LEU PRO GLY GLU ASP
SEQRES 5 A 336 TRP VAL PHE VAL SER SER LYS ASP ALA ASP LEU THR ASP
SEQRES 6 A 336 THR ALA GLN THR ARG ALA LEU PHE GLU LYS VAL GLN PRO
SEQRES 7 A 336 THR HIS VAL ILE HIS LEU ALA ALA MET VAL GLY GLY LEU
SEQRES 8 A 336 PHE ARG ASN ILE LYS TYR ASN LEU ASP PHE TRP ARG LYS
SEQRES 9 A 336 ASN VAL HIS MET ASN ASP ASN VAL LEU HIS SER ALA PHE
SEQRES 10 A 336 GLU VAL GLY ALA ARG LYS VAL VAL SER CYS LEU SER THR
SEQRES 11 A 336 CYS ILE PHE PRO ASP LYS THR THR TYR PRO ILE ASP GLU
SEQRES 12 A 336 THR MET ILE HIS ASN GLY PRO PRO HIS ASN SER ASN PHE
SEQRES 13 A 336 GLY TYR SER TYR ALA LYS ARG MET ILE ASP VAL GLN ASN
SEQRES 14 A 336 ARG ALA TYR PHE GLN GLN TYR GLY CYS THR PHE THR ALA
SEQRES 15 A 336 VAL ILE PRO THR ASN VAL PHE GLY PRO HIS ASP ASN PHE
SEQRES 16 A 336 ASN ILE GLU ASP GLY HIS VAL LEU PRO GLY LEU ILE HIS
SEQRES 17 A 336 LYS VAL HIS LEU ALA LYS SER SER GLY SER ALA LEU THR
SEQRES 18 A 336 VAL TRP GLY THR GLY ASN PRO ARG ARG GLN PHE ILE TYR
SEQRES 19 A 336 SER LEU ASP LEU ALA GLN LEU PHE ILE TRP VAL LEU ARG
SEQRES 20 A 336 GLU TYR ASN GLU VAL GLU PRO ILE ILE LEU SER VAL GLY
SEQRES 21 A 336 GLU GLU ASP GLU VAL SER ILE LYS GLU ALA ALA GLU ALA
SEQRES 22 A 336 VAL VAL GLU ALA MET ASP PHE HIS GLY GLU VAL THR PHE
SEQRES 23 A 336 ASP THR THR LYS SER ASP GLY GLN PHE LYS LYS THR ALA
SEQRES 24 A 336 SER ASN SER LYS LEU ARG THR TYR LEU PRO ASP PHE ARG
SEQRES 25 A 336 PHE THR PRO PHE LYS GLN ALA VAL LYS GLU THR CYS ALA
SEQRES 26 A 336 TRP PHE THR ASP ASN TYR GLU GLN ALA ARG LYS
SEQRES 1 B 336 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 336 GLY THR GLU ASN LEU TYR PHE GLN SER MET ARG ILE LEU
SEQRES 3 B 336 VAL THR GLY GLY SER GLY LEU VAL GLY LYS ALA ILE GLN
SEQRES 4 B 336 LYS VAL VAL ALA ASP GLY ALA GLY LEU PRO GLY GLU ASP
SEQRES 5 B 336 TRP VAL PHE VAL SER SER LYS ASP ALA ASP LEU THR ASP
SEQRES 6 B 336 THR ALA GLN THR ARG ALA LEU PHE GLU LYS VAL GLN PRO
SEQRES 7 B 336 THR HIS VAL ILE HIS LEU ALA ALA MET VAL GLY GLY LEU
SEQRES 8 B 336 PHE ARG ASN ILE LYS TYR ASN LEU ASP PHE TRP ARG LYS
SEQRES 9 B 336 ASN VAL HIS MET ASN ASP ASN VAL LEU HIS SER ALA PHE
SEQRES 10 B 336 GLU VAL GLY ALA ARG LYS VAL VAL SER CYS LEU SER THR
SEQRES 11 B 336 CYS ILE PHE PRO ASP LYS THR THR TYR PRO ILE ASP GLU
SEQRES 12 B 336 THR MET ILE HIS ASN GLY PRO PRO HIS ASN SER ASN PHE
SEQRES 13 B 336 GLY TYR SER TYR ALA LYS ARG MET ILE ASP VAL GLN ASN
SEQRES 14 B 336 ARG ALA TYR PHE GLN GLN TYR GLY CYS THR PHE THR ALA
SEQRES 15 B 336 VAL ILE PRO THR ASN VAL PHE GLY PRO HIS ASP ASN PHE
SEQRES 16 B 336 ASN ILE GLU ASP GLY HIS VAL LEU PRO GLY LEU ILE HIS
SEQRES 17 B 336 LYS VAL HIS LEU ALA LYS SER SER GLY SER ALA LEU THR
SEQRES 18 B 336 VAL TRP GLY THR GLY ASN PRO ARG ARG GLN PHE ILE TYR
SEQRES 19 B 336 SER LEU ASP LEU ALA GLN LEU PHE ILE TRP VAL LEU ARG
SEQRES 20 B 336 GLU TYR ASN GLU VAL GLU PRO ILE ILE LEU SER VAL GLY
SEQRES 21 B 336 GLU GLU ASP GLU VAL SER ILE LYS GLU ALA ALA GLU ALA
SEQRES 22 B 336 VAL VAL GLU ALA MET ASP PHE HIS GLY GLU VAL THR PHE
SEQRES 23 B 336 ASP THR THR LYS SER ASP GLY GLN PHE LYS LYS THR ALA
SEQRES 24 B 336 SER ASN SER LYS LEU ARG THR TYR LEU PRO ASP PHE ARG
SEQRES 25 B 336 PHE THR PRO PHE LYS GLN ALA VAL LYS GLU THR CYS ALA
SEQRES 26 B 336 TRP PHE THR ASP ASN TYR GLU GLN ALA ARG LYS
SEQRES 1 C 336 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 336 GLY THR GLU ASN LEU TYR PHE GLN SER MET ARG ILE LEU
SEQRES 3 C 336 VAL THR GLY GLY SER GLY LEU VAL GLY LYS ALA ILE GLN
SEQRES 4 C 336 LYS VAL VAL ALA ASP GLY ALA GLY LEU PRO GLY GLU ASP
SEQRES 5 C 336 TRP VAL PHE VAL SER SER LYS ASP ALA ASP LEU THR ASP
SEQRES 6 C 336 THR ALA GLN THR ARG ALA LEU PHE GLU LYS VAL GLN PRO
SEQRES 7 C 336 THR HIS VAL ILE HIS LEU ALA ALA MET VAL GLY GLY LEU
SEQRES 8 C 336 PHE ARG ASN ILE LYS TYR ASN LEU ASP PHE TRP ARG LYS
SEQRES 9 C 336 ASN VAL HIS MET ASN ASP ASN VAL LEU HIS SER ALA PHE
SEQRES 10 C 336 GLU VAL GLY ALA ARG LYS VAL VAL SER CYS LEU SER THR
SEQRES 11 C 336 CYS ILE PHE PRO ASP LYS THR THR TYR PRO ILE ASP GLU
SEQRES 12 C 336 THR MET ILE HIS ASN GLY PRO PRO HIS ASN SER ASN PHE
SEQRES 13 C 336 GLY TYR SER TYR ALA LYS ARG MET ILE ASP VAL GLN ASN
SEQRES 14 C 336 ARG ALA TYR PHE GLN GLN TYR GLY CYS THR PHE THR ALA
SEQRES 15 C 336 VAL ILE PRO THR ASN VAL PHE GLY PRO HIS ASP ASN PHE
SEQRES 16 C 336 ASN ILE GLU ASP GLY HIS VAL LEU PRO GLY LEU ILE HIS
SEQRES 17 C 336 LYS VAL HIS LEU ALA LYS SER SER GLY SER ALA LEU THR
SEQRES 18 C 336 VAL TRP GLY THR GLY ASN PRO ARG ARG GLN PHE ILE TYR
SEQRES 19 C 336 SER LEU ASP LEU ALA GLN LEU PHE ILE TRP VAL LEU ARG
SEQRES 20 C 336 GLU TYR ASN GLU VAL GLU PRO ILE ILE LEU SER VAL GLY
SEQRES 21 C 336 GLU GLU ASP GLU VAL SER ILE LYS GLU ALA ALA GLU ALA
SEQRES 22 C 336 VAL VAL GLU ALA MET ASP PHE HIS GLY GLU VAL THR PHE
SEQRES 23 C 336 ASP THR THR LYS SER ASP GLY GLN PHE LYS LYS THR ALA
SEQRES 24 C 336 SER ASN SER LYS LEU ARG THR TYR LEU PRO ASP PHE ARG
SEQRES 25 C 336 PHE THR PRO PHE LYS GLN ALA VAL LYS GLU THR CYS ALA
SEQRES 26 C 336 TRP PHE THR ASP ASN TYR GLU GLN ALA ARG LYS
SEQRES 1 D 336 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 336 GLY THR GLU ASN LEU TYR PHE GLN SER MET ARG ILE LEU
SEQRES 3 D 336 VAL THR GLY GLY SER GLY LEU VAL GLY LYS ALA ILE GLN
SEQRES 4 D 336 LYS VAL VAL ALA ASP GLY ALA GLY LEU PRO GLY GLU ASP
SEQRES 5 D 336 TRP VAL PHE VAL SER SER LYS ASP ALA ASP LEU THR ASP
SEQRES 6 D 336 THR ALA GLN THR ARG ALA LEU PHE GLU LYS VAL GLN PRO
SEQRES 7 D 336 THR HIS VAL ILE HIS LEU ALA ALA MET VAL GLY GLY LEU
SEQRES 8 D 336 PHE ARG ASN ILE LYS TYR ASN LEU ASP PHE TRP ARG LYS
SEQRES 9 D 336 ASN VAL HIS MET ASN ASP ASN VAL LEU HIS SER ALA PHE
SEQRES 10 D 336 GLU VAL GLY ALA ARG LYS VAL VAL SER CYS LEU SER THR
SEQRES 11 D 336 CYS ILE PHE PRO ASP LYS THR THR TYR PRO ILE ASP GLU
SEQRES 12 D 336 THR MET ILE HIS ASN GLY PRO PRO HIS ASN SER ASN PHE
SEQRES 13 D 336 GLY TYR SER TYR ALA LYS ARG MET ILE ASP VAL GLN ASN
SEQRES 14 D 336 ARG ALA TYR PHE GLN GLN TYR GLY CYS THR PHE THR ALA
SEQRES 15 D 336 VAL ILE PRO THR ASN VAL PHE GLY PRO HIS ASP ASN PHE
SEQRES 16 D 336 ASN ILE GLU ASP GLY HIS VAL LEU PRO GLY LEU ILE HIS
SEQRES 17 D 336 LYS VAL HIS LEU ALA LYS SER SER GLY SER ALA LEU THR
SEQRES 18 D 336 VAL TRP GLY THR GLY ASN PRO ARG ARG GLN PHE ILE TYR
SEQRES 19 D 336 SER LEU ASP LEU ALA GLN LEU PHE ILE TRP VAL LEU ARG
SEQRES 20 D 336 GLU TYR ASN GLU VAL GLU PRO ILE ILE LEU SER VAL GLY
SEQRES 21 D 336 GLU GLU ASP GLU VAL SER ILE LYS GLU ALA ALA GLU ALA
SEQRES 22 D 336 VAL VAL GLU ALA MET ASP PHE HIS GLY GLU VAL THR PHE
SEQRES 23 D 336 ASP THR THR LYS SER ASP GLY GLN PHE LYS LYS THR ALA
SEQRES 24 D 336 SER ASN SER LYS LEU ARG THR TYR LEU PRO ASP PHE ARG
SEQRES 25 D 336 PHE THR PRO PHE LYS GLN ALA VAL LYS GLU THR CYS ALA
SEQRES 26 D 336 TRP PHE THR ASP ASN TYR GLU GLN ALA ARG LYS
HET NAP A 901 48
HET FLC A1321 13
HET NAP B 901 48
HET NAP C 901 48
HET NAP D 901 48
HET EDO D1321 4
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM FLC CITRATE ANION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 NAP 4(C21 H28 N7 O17 P3)
FORMUL 6 FLC C6 H5 O7 3-
FORMUL 10 EDO C2 H6 O2
FORMUL 11 HOH *50(H2 O)
HELIX 1 1 GLY A 17 ASP A 29 1 13
HELIX 2 2 ASP A 50 GLN A 62 1 13
HELIX 3 3 TYR A 82 GLY A 105 1 24
HELIX 4 4 SER A 114 PHE A 118 5 5
HELIX 5 5 ASN A 140 GLY A 162 1 23
HELIX 6 6 HIS A 186 GLY A 202 1 17
HELIX 7 7 SER A 220 TYR A 234 1 15
HELIX 8 8 GLY A 245 GLU A 249 5 5
HELIX 9 9 ILE A 252 MET A 263 1 12
HELIX 10 10 ASN A 286 LEU A 293 1 8
HELIX 11 11 PRO A 300 ASN A 315 1 16
HELIX 12 12 GLY B 17 ASP B 29 1 13
HELIX 13 13 ASP B 50 GLN B 62 1 13
HELIX 14 14 TYR B 82 GLY B 105 1 24
HELIX 15 15 SER B 114 PHE B 118 5 5
HELIX 16 16 ASN B 140 GLY B 162 1 23
HELIX 17 17 HIS B 186 GLY B 202 1 17
HELIX 18 18 SER B 220 TYR B 234 1 15
HELIX 19 19 GLY B 245 GLU B 249 5 5
HELIX 20 20 ILE B 252 MET B 263 1 12
HELIX 21 21 ASN B 286 LEU B 293 1 8
HELIX 22 22 PRO B 300 ASN B 315 1 16
HELIX 23 23 GLY C 17 ASP C 29 1 13
HELIX 24 24 ASP C 50 GLN C 62 1 13
HELIX 25 25 TYR C 82 GLY C 105 1 24
HELIX 26 26 SER C 114 PHE C 118 5 5
HELIX 27 27 ASN C 140 GLY C 162 1 23
HELIX 28 28 HIS C 186 GLY C 202 1 17
HELIX 29 29 SER C 220 TYR C 234 1 15
HELIX 30 30 GLY C 245 GLU C 249 5 5
HELIX 31 31 ILE C 252 MET C 263 1 12
HELIX 32 32 ASN C 286 LEU C 293 1 8
HELIX 33 33 PRO C 300 ASN C 315 1 16
HELIX 34 34 GLY D 17 ASP D 29 1 13
HELIX 35 35 ASP D 50 GLN D 62 1 13
HELIX 36 36 TYR D 82 GLY D 105 1 24
HELIX 37 37 SER D 114 PHE D 118 5 5
HELIX 38 38 ASN D 140 GLY D 162 1 23
HELIX 39 39 HIS D 186 GLY D 202 1 17
HELIX 40 40 SER D 220 TYR D 234 1 15
HELIX 41 41 GLY D 245 GLU D 249 5 5
HELIX 42 42 ILE D 252 MET D 263 1 12
HELIX 43 43 ASN D 286 LEU D 293 1 8
HELIX 44 44 PRO D 300 ASN D 315 1 16
SHEET 1 AA 6 GLU A 36 PHE A 40 0
SHEET 2 AA 6 MET A 8 THR A 13 1 O MET A 8 N ASP A 37
SHEET 3 AA 6 HIS A 65 HIS A 68 1 O HIS A 65 N LEU A 11
SHEET 4 AA 6 LYS A 108 CYS A 112 1 O LYS A 108 N VAL A 66
SHEET 5 AA 6 THR A 164 PRO A 170 1 O THR A 164 N VAL A 109
SHEET 6 AA 6 ILE A 240 LEU A 242 1 O ILE A 240 N ILE A 169
SHEET 1 AB 2 ASN A 172 PHE A 174 0
SHEET 2 AB 2 PHE A 217 TYR A 219 1 O ILE A 218 N PHE A 174
SHEET 1 AC 2 LEU A 205 TRP A 208 0
SHEET 2 AC 2 VAL A 269 ASP A 272 1 O THR A 270 N VAL A 207
SHEET 1 AD 2 ARG A 214 ARG A 215 0
SHEET 2 AD 2 VAL A 250 SER A 251 -1 O VAL A 250 N ARG A 215
SHEET 1 BA 6 GLU B 36 PHE B 40 0
SHEET 2 BA 6 MET B 8 THR B 13 1 O MET B 8 N ASP B 37
SHEET 3 BA 6 HIS B 65 HIS B 68 1 O HIS B 65 N LEU B 11
SHEET 4 BA 6 LYS B 108 CYS B 112 1 O LYS B 108 N VAL B 66
SHEET 5 BA 6 THR B 164 PRO B 170 1 O THR B 164 N VAL B 109
SHEET 6 BA 6 ILE B 240 LEU B 242 1 O ILE B 240 N ILE B 169
SHEET 1 BB 2 ASN B 172 PHE B 174 0
SHEET 2 BB 2 PHE B 217 TYR B 219 1 O ILE B 218 N PHE B 174
SHEET 1 BC 2 LEU B 205 TRP B 208 0
SHEET 2 BC 2 VAL B 269 ASP B 272 1 O THR B 270 N VAL B 207
SHEET 1 BD 2 ARG B 214 ARG B 215 0
SHEET 2 BD 2 VAL B 250 SER B 251 -1 O VAL B 250 N ARG B 215
SHEET 1 CA 6 GLU C 36 PHE C 40 0
SHEET 2 CA 6 MET C 8 THR C 13 1 O MET C 8 N ASP C 37
SHEET 3 CA 6 HIS C 65 HIS C 68 1 O HIS C 65 N LEU C 11
SHEET 4 CA 6 LYS C 108 CYS C 112 1 O LYS C 108 N VAL C 66
SHEET 5 CA 6 THR C 164 PRO C 170 1 O THR C 164 N VAL C 109
SHEET 6 CA 6 ILE C 240 LEU C 242 1 O ILE C 240 N ILE C 169
SHEET 1 CB 2 ASN C 172 PHE C 174 0
SHEET 2 CB 2 PHE C 217 TYR C 219 1 O ILE C 218 N PHE C 174
SHEET 1 CC 2 LEU C 205 TRP C 208 0
SHEET 2 CC 2 VAL C 269 ASP C 272 1 O THR C 270 N VAL C 207
SHEET 1 CD 2 ARG C 214 ARG C 215 0
SHEET 2 CD 2 VAL C 250 SER C 251 -1 O VAL C 250 N ARG C 215
SHEET 1 DA 6 GLU D 36 PHE D 40 0
SHEET 2 DA 6 MET D 8 THR D 13 1 O MET D 8 N ASP D 37
SHEET 3 DA 6 HIS D 65 HIS D 68 1 O HIS D 65 N LEU D 11
SHEET 4 DA 6 LYS D 108 CYS D 112 1 O LYS D 108 N VAL D 66
SHEET 5 DA 6 THR D 164 PRO D 170 1 O THR D 164 N VAL D 109
SHEET 6 DA 6 ILE D 240 LEU D 242 1 O ILE D 240 N ILE D 169
SHEET 1 DB 2 ASN D 172 PHE D 174 0
SHEET 2 DB 2 PHE D 217 TYR D 219 1 O ILE D 218 N PHE D 174
SHEET 1 DC 2 LEU D 205 TRP D 208 0
SHEET 2 DC 2 VAL D 269 ASP D 272 1 O THR D 270 N VAL D 207
SHEET 1 DD 2 ARG D 214 ARG D 215 0
SHEET 2 DD 2 VAL D 250 SER D 251 -1 O VAL D 250 N ARG D 215
CISPEP 1 GLY A 74 GLY A 75 0 -1.37
CISPEP 2 TYR A 124 PRO A 125 0 -2.73
CISPEP 3 GLY B 74 GLY B 75 0 -1.54
CISPEP 4 TYR B 124 PRO B 125 0 -3.55
CISPEP 5 GLY C 74 GLY C 75 0 -1.47
CISPEP 6 TYR C 124 PRO C 125 0 -2.96
CISPEP 7 GLY D 74 GLY D 75 0 -1.12
CISPEP 8 TYR D 124 PRO D 125 0 -1.88
SITE 1 AC1 22 GLY A 14 SER A 16 GLY A 17 LEU A 18
SITE 2 AC1 22 VAL A 19 SER A 42 SER A 43 ALA A 46
SITE 3 AC1 22 ASP A 47 LEU A 48 LEU A 69 ALA A 70
SITE 4 AC1 22 ALA A 71 MET A 93 CYS A 112 LEU A 113
SITE 5 AC1 22 TYR A 143 LYS A 147 THR A 171 VAL A 173
SITE 6 AC1 22 HIS A 186 ARG A 320
SITE 1 AC2 23 GLY B 14 SER B 16 GLY B 17 LEU B 18
SITE 2 AC2 23 VAL B 19 SER B 42 SER B 43 ALA B 46
SITE 3 AC2 23 ASP B 47 LEU B 48 LEU B 69 ALA B 70
SITE 4 AC2 23 ALA B 71 VAL B 73 MET B 93 CYS B 112
SITE 5 AC2 23 LEU B 113 TYR B 143 LYS B 147 THR B 171
SITE 6 AC2 23 VAL B 173 HIS B 186 ARG B 320
SITE 1 AC3 23 GLY C 14 SER C 16 GLY C 17 LEU C 18
SITE 2 AC3 23 VAL C 19 SER C 42 SER C 43 ALA C 46
SITE 3 AC3 23 ASP C 47 LEU C 48 LEU C 69 ALA C 70
SITE 4 AC3 23 ALA C 71 VAL C 73 MET C 93 CYS C 112
SITE 5 AC3 23 LEU C 113 TYR C 143 LYS C 147 THR C 171
SITE 6 AC3 23 VAL C 173 HIS C 186 ARG C 320
SITE 1 AC4 25 GLY D 14 SER D 16 GLY D 17 LEU D 18
SITE 2 AC4 25 VAL D 19 SER D 42 SER D 43 ALA D 46
SITE 3 AC4 25 ASP D 47 LEU D 48 THR D 49 LEU D 69
SITE 4 AC4 25 ALA D 70 ALA D 71 VAL D 73 MET D 93
SITE 5 AC4 25 CYS D 112 LEU D 113 TYR D 143 LYS D 147
SITE 6 AC4 25 THR D 171 VAL D 173 HIS D 186 ARG D 320
SITE 7 AC4 25 HOH D2001
SITE 1 AC5 6 THR A 49 ARG A 88 LYS A 89 HIS A 92
SITE 2 AC5 6 TYR B -4 ARG B 55
SITE 1 AC6 2 TYR A -4 LYS D 89
CRYST1 106.596 163.095 197.581 90.00 90.00 90.00 I 2 2 2 32
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 0.009381 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006131 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005061 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
