HEADER HYDROLASE/HYDROLASE INHIBITOR 01-JUL-16 5KOT
TITLE DISCOVERY OF TAK-272: A NOVEL, POTENT AND ORALLY ACTIVE RENIN IN-
TITLE 2 HIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RENIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 70-406;
COMPND 5 SYNONYM: ANGIOTENSINOGENASE;
COMPND 6 EC: 3.4.23.15;
COMPND 7 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: REN;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK 293
KEYWDS PROTEIN-INHIBITOR COMPLEX, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.P.SNELL,C.A.BEHNKE,K.OKADA,O.HIDEYUKI,B.-C.SANG,W.LANE
REVDAT 2 29-JUL-20 5KOT 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE
REVDAT 1 05-JUL-17 5KOT 0
JRNL AUTH Y.IMAEDA,H.TOKUHARA,Y.FUKASE,R.KANAGAWA,Y.KAJIMOTO,
JRNL AUTH 2 K.KUSUMOTO,M.KONDO,G.P.SNELL,C.A.BEHNKE,T.KUROITA
JRNL TITL DISCOVERY OF TAK-272: A NOVEL, POTENT AND ORALLY ACTIVE
JRNL TITL 2 RENIN INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 49705
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2669
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3633
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 188
REMARK 3 BIN FREE R VALUE : 0.2330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5053
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 204
REMARK 3 SOLVENT ATOMS : 290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.171
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.146
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.688
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5412 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4929 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7328 ; 1.332 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11355 ; 0.868 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 675 ; 7.126 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 214 ;34.757 ;24.393
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 813 ;13.254 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;18.067 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 829 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6020 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1199 ; 0.001 ; 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): 2670 ; 0.949 ; 2.664
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2669 ; 0.944 ; 2.663
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3334 ; 1.515 ; 3.989
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 10
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 78
REMARK 3 RESIDUE RANGE : A 92 A 154
REMARK 3 ORIGIN FOR THE GROUP (A): -21.4410 -46.6255 -16.5997
REMARK 3 T TENSOR
REMARK 3 T11: 0.0430 T22: 0.0048
REMARK 3 T33: 0.0656 T12: 0.0038
REMARK 3 T13: 0.0190 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 1.2220 L22: 1.9961
REMARK 3 L33: 3.3252 L12: 0.1036
REMARK 3 L13: 0.0576 L23: 0.7019
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: -0.0699 S13: -0.1835
REMARK 3 S21: 0.1083 S22: -0.0189 S23: -0.1077
REMARK 3 S31: 0.3121 S32: 0.0231 S33: 0.0112
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 79 A 91
REMARK 3 ORIGIN FOR THE GROUP (A): -32.0981 -39.9884 -19.3412
REMARK 3 T TENSOR
REMARK 3 T11: 0.0684 T22: 0.1213
REMARK 3 T33: 0.0861 T12: -0.0077
REMARK 3 T13: 0.0084 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 2.2219 L22: 10.1704
REMARK 3 L33: 7.4812 L12: -2.1622
REMARK 3 L13: -1.8558 L23: 6.0141
REMARK 3 S TENSOR
REMARK 3 S11: -0.0595 S12: -0.0928 S13: -0.1001
REMARK 3 S21: 0.2302 S22: -0.3040 S23: 0.6432
REMARK 3 S31: 0.4795 S32: -0.4919 S33: 0.3635
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 155 A 248
REMARK 3 RESIDUE RANGE : A 266 A 280
REMARK 3 RESIDUE RANGE : A 299 A 302
REMARK 3 RESIDUE RANGE : A 313 A 340
REMARK 3 ORIGIN FOR THE GROUP (A): -25.5685 -36.2753 4.5955
REMARK 3 T TENSOR
REMARK 3 T11: 0.0756 T22: 0.1693
REMARK 3 T33: 0.0112 T12: -0.0021
REMARK 3 T13: 0.0088 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 2.0178 L22: 4.5082
REMARK 3 L33: 2.8666 L12: -0.5895
REMARK 3 L13: 0.5675 L23: 0.1359
REMARK 3 S TENSOR
REMARK 3 S11: -0.0712 S12: -0.3842 S13: 0.0527
REMARK 3 S21: 0.4190 S22: 0.0305 S23: 0.0843
REMARK 3 S31: 0.0366 S32: -0.2919 S33: 0.0407
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 249 A 265
REMARK 3 RESIDUE RANGE : A 281 A 298
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0099 -16.2575 -1.9403
REMARK 3 T TENSOR
REMARK 3 T11: 0.2756 T22: 0.0877
REMARK 3 T33: 0.1781 T12: 0.0436
REMARK 3 T13: -0.0877 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 6.3438 L22: 3.5373
REMARK 3 L33: 4.1370 L12: 1.0578
REMARK 3 L13: 0.9697 L23: -0.5278
REMARK 3 S TENSOR
REMARK 3 S11: -0.2966 S12: 0.2180 S13: 0.7021
REMARK 3 S21: -0.1673 S22: 0.1275 S23: 0.0035
REMARK 3 S31: -0.7817 S32: 0.0856 S33: 0.1691
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 : A 303 A 312
REMARK 3 ORIGIN FOR THE GROUP (A): -38.4190 -33.9760 -5.6743
REMARK 3 T TENSOR
REMARK 3 T11: 0.1550 T22: 0.2544
REMARK 3 T33: 0.2199 T12: 0.0182
REMARK 3 T13: 0.0045 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 1.9218 L22: 6.1960
REMARK 3 L33: 5.9045 L12: 2.4945
REMARK 3 L13: 1.5596 L23: -0.3568
REMARK 3 S TENSOR
REMARK 3 S11: -0.1594 S12: 0.0541 S13: -0.0439
REMARK 3 S21: -0.3734 S22: 0.1106 S23: 0.1419
REMARK 3 S31: 0.1878 S32: -0.1566 S33: 0.0488
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 78
REMARK 3 RESIDUE RANGE : B 92 B 154
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5079 -24.5831 23.5488
REMARK 3 T TENSOR
REMARK 3 T11: 0.1210 T22: 0.1882
REMARK 3 T33: 0.0596 T12: 0.0819
REMARK 3 T13: 0.0283 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 3.2032 L22: 2.8924
REMARK 3 L33: 2.5950 L12: -0.6077
REMARK 3 L13: -0.6067 L23: -1.0408
REMARK 3 S TENSOR
REMARK 3 S11: -0.0843 S12: -0.2486 S13: -0.0824
REMARK 3 S21: 0.3743 S22: 0.1892 S23: 0.3427
REMARK 3 S31: -0.1840 S32: -0.4245 S33: -0.1049
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 : B 79 B 91
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3784 -14.8401 29.5149
REMARK 3 T TENSOR
REMARK 3 T11: 0.5690 T22: 0.2277
REMARK 3 T33: 0.1266 T12: 0.1660
REMARK 3 T13: -0.0907 T23: -0.1162
REMARK 3 L TENSOR
REMARK 3 L11: 9.3506 L22: 0.9785
REMARK 3 L33: 3.9984 L12: 1.8925
REMARK 3 L13: -6.0293 L23: -1.1434
REMARK 3 S TENSOR
REMARK 3 S11: 0.1217 S12: -0.2789 S13: 0.1134
REMARK 3 S21: 0.4424 S22: -0.1105 S23: -0.0000
REMARK 3 S31: -0.1892 S32: 0.0377 S33: -0.0113
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 155 B 248
REMARK 3 RESIDUE RANGE : B 266 B 280
REMARK 3 RESIDUE RANGE : B 299 B 302
REMARK 3 RESIDUE RANGE : B 313 B 340
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5157 -24.6656 14.3010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0520 T22: 0.1256
REMARK 3 T33: 0.0985 T12: 0.0459
REMARK 3 T13: -0.0128 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 2.5052 L22: 4.5513
REMARK 3 L33: 2.6057 L12: -0.1070
REMARK 3 L13: -0.7577 L23: -1.6330
REMARK 3 S TENSOR
REMARK 3 S11: 0.0241 S12: 0.1108 S13: 0.0119
REMARK 3 S21: -0.0521 S22: -0.2108 S23: -0.4823
REMARK 3 S31: -0.1274 S32: 0.2181 S33: 0.1867
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 249 B 265
REMARK 3 RESIDUE RANGE : B 281 B 298
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0678 -8.2198 -0.2815
REMARK 3 T TENSOR
REMARK 3 T11: 0.1769 T22: 0.2379
REMARK 3 T33: 0.2199 T12: 0.0546
REMARK 3 T13: 0.0212 T23: 0.1242
REMARK 3 L TENSOR
REMARK 3 L11: 3.4804 L22: 7.2979
REMARK 3 L33: 6.5346 L12: 0.2323
REMARK 3 L13: -0.1701 L23: -3.8640
REMARK 3 S TENSOR
REMARK 3 S11: 0.1042 S12: 0.0948 S13: 0.3896
REMARK 3 S21: -0.3318 S22: -0.0578 S23: 0.0956
REMARK 3 S31: -0.3000 S32: -0.2859 S33: -0.0463
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 : B 303 B 312
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7539 -13.2508 26.6849
REMARK 3 T TENSOR
REMARK 3 T11: 0.2892 T22: 0.2517
REMARK 3 T33: 0.2540 T12: -0.0202
REMARK 3 T13: -0.0374 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 2.0429 L22: 3.9162
REMARK 3 L33: 9.2261 L12: -1.6813
REMARK 3 L13: -2.1707 L23: -2.3954
REMARK 3 S TENSOR
REMARK 3 S11: -0.1233 S12: -0.1662 S13: -0.0580
REMARK 3 S21: 0.3283 S22: 0.2293 S23: 0.1722
REMARK 3 S31: -0.2270 S32: -0.0201 S33: -0.1059
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 5KOT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1000222568.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52521
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.76500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% PEG600, 100 MM CITRATE, BUFFER: 25
REMARK 280 MM TRIS PH 7.9, 150 MM NACL, LIGAND WAS SOAKED FOR 18H AT 2MM,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+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 69.65850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.65850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 69.65850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.65850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 69.65850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 69.65850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 69.65850
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 69.65850
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 69.65850
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 69.65850
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 69.65850
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 69.65850
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 69.65850
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 69.65850
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 69.65850
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 69.65850
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 69.65850
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 69.65850
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 69030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 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 GLU A 167
REMARK 465 ASN A 168
REMARK 465 SER A 169
REMARK 465 GLN A 170
REMARK 465 SER A 171
REMARK 465 GLU B 167
REMARK 465 ASN B 168
REMARK 465 SER B 169
REMARK 465 GLN B 170
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 ASN A 5 CG OD1 ND2
REMARK 470 ARG A 139 CG CD NE CZ NH1 NH2
REMARK 470 SER A 212 OG
REMARK 470 LYS A 258 CG CD CE NZ
REMARK 470 GLU A 288 CG CD OE1 OE2
REMARK 470 LYS A 294 CE NZ
REMARK 470 ARG A 330 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 73 CG CD CE NZ
REMARK 470 ARG B 82 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 139 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 154 CG CD CE NZ
REMARK 470 ARG B 164 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 218 CG CD OE1 OE2
REMARK 470 LYS B 249 CG CD CE NZ
REMARK 470 LYS B 250 CG CD CE NZ
REMARK 470 LEU B 252 CG CD1 CD2
REMARK 470 PHE B 253 CG CD1 CD2 CE1 CE2 CZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 75 -60.41 -127.15
REMARK 500 ALA A 299 43.19 -85.87
REMARK 500 ASN B 5 17.10 -145.85
REMARK 500 ASP B 17 14.56 59.51
REMARK 500 ASN B 75 -65.72 -123.24
REMARK 500 ASP B 165 160.85 89.65
REMARK 500 LEU B 172 122.92 -24.66
REMARK 500 ARG B 251 -88.89 -76.07
REMARK 500 LEU B 252 -61.81 -121.39
REMARK 500 ALA B 299 43.97 -87.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KOQ RELATED DB: PDB
REMARK 900 RELATED ID: 5KOS RELATED DB: PDB
DBREF 5KOT A 4 340 UNP P00797 RENI_HUMAN 70 406
DBREF 5KOT B 4 340 UNP P00797 RENI_HUMAN 70 406
SEQRES 1 A 337 GLY ASN THR THR SER SER VAL ILE LEU THR ASN TYR MET
SEQRES 2 A 337 ASP THR GLN TYR TYR GLY GLU ILE GLY ILE GLY THR PRO
SEQRES 3 A 337 PRO GLN THR PHE LYS VAL VAL PHE ASP THR GLY SER SER
SEQRES 4 A 337 ASN VAL TRP VAL PRO SER SER LYS CYS SER ARG LEU TYR
SEQRES 5 A 337 THR ALA CYS VAL TYR HIS LYS LEU PHE ASP ALA SER ASP
SEQRES 6 A 337 SER SER SER TYR LYS HIS ASN GLY THR GLU LEU THR LEU
SEQRES 7 A 337 ARG TYR SER THR GLY THR VAL SER GLY PHE LEU SER GLN
SEQRES 8 A 337 ASP ILE ILE THR VAL GLY GLY ILE THR VAL THR GLN MET
SEQRES 9 A 337 PHE GLY GLU VAL THR GLU MET PRO ALA LEU PRO PHE MET
SEQRES 10 A 337 LEU ALA GLU PHE ASP GLY VAL VAL GLY MET GLY PHE ILE
SEQRES 11 A 337 GLU GLN ALA ILE GLY ARG VAL THR PRO ILE PHE ASP ASN
SEQRES 12 A 337 ILE ILE SER GLN GLY VAL LEU LYS GLU ASP VAL PHE SER
SEQRES 13 A 337 PHE TYR TYR ASN ARG ASP SER GLU ASN SER GLN SER LEU
SEQRES 14 A 337 GLY GLY GLN ILE VAL LEU GLY GLY SER ASP PRO GLN HIS
SEQRES 15 A 337 TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU ILE LYS THR
SEQRES 16 A 337 GLY VAL TRP GLN ILE GLN MET LYS GLY VAL SER VAL GLY
SEQRES 17 A 337 SER SER THR LEU LEU CYS GLU ASP GLY CYS LEU ALA LEU
SEQRES 18 A 337 VAL ASP THR GLY ALA SER TYR ILE SER GLY SER THR SER
SEQRES 19 A 337 SER ILE GLU LYS LEU MET GLU ALA LEU GLY ALA LYS LYS
SEQRES 20 A 337 ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN GLU GLY PRO
SEQRES 21 A 337 THR LEU PRO ASP ILE SER PHE HIS LEU GLY GLY LYS GLU
SEQRES 22 A 337 TYR THR LEU THR SER ALA ASP TYR VAL PHE GLN GLU SER
SEQRES 23 A 337 TYR SER SER LYS LYS LEU CYS THR LEU ALA ILE HIS ALA
SEQRES 24 A 337 MET ASP ILE PRO PRO PRO THR GLY PRO THR TRP ALA LEU
SEQRES 25 A 337 GLY ALA THR PHE ILE ARG LYS PHE TYR THR GLU PHE ASP
SEQRES 26 A 337 ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU ALA ARG
SEQRES 1 B 337 GLY ASN THR THR SER SER VAL ILE LEU THR ASN TYR MET
SEQRES 2 B 337 ASP THR GLN TYR TYR GLY GLU ILE GLY ILE GLY THR PRO
SEQRES 3 B 337 PRO GLN THR PHE LYS VAL VAL PHE ASP THR GLY SER SER
SEQRES 4 B 337 ASN VAL TRP VAL PRO SER SER LYS CYS SER ARG LEU TYR
SEQRES 5 B 337 THR ALA CYS VAL TYR HIS LYS LEU PHE ASP ALA SER ASP
SEQRES 6 B 337 SER SER SER TYR LYS HIS ASN GLY THR GLU LEU THR LEU
SEQRES 7 B 337 ARG TYR SER THR GLY THR VAL SER GLY PHE LEU SER GLN
SEQRES 8 B 337 ASP ILE ILE THR VAL GLY GLY ILE THR VAL THR GLN MET
SEQRES 9 B 337 PHE GLY GLU VAL THR GLU MET PRO ALA LEU PRO PHE MET
SEQRES 10 B 337 LEU ALA GLU PHE ASP GLY VAL VAL GLY MET GLY PHE ILE
SEQRES 11 B 337 GLU GLN ALA ILE GLY ARG VAL THR PRO ILE PHE ASP ASN
SEQRES 12 B 337 ILE ILE SER GLN GLY VAL LEU LYS GLU ASP VAL PHE SER
SEQRES 13 B 337 PHE TYR TYR ASN ARG ASP SER GLU ASN SER GLN SER LEU
SEQRES 14 B 337 GLY GLY GLN ILE VAL LEU GLY GLY SER ASP PRO GLN HIS
SEQRES 15 B 337 TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU ILE LYS THR
SEQRES 16 B 337 GLY VAL TRP GLN ILE GLN MET LYS GLY VAL SER VAL GLY
SEQRES 17 B 337 SER SER THR LEU LEU CYS GLU ASP GLY CYS LEU ALA LEU
SEQRES 18 B 337 VAL ASP THR GLY ALA SER TYR ILE SER GLY SER THR SER
SEQRES 19 B 337 SER ILE GLU LYS LEU MET GLU ALA LEU GLY ALA LYS LYS
SEQRES 20 B 337 ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN GLU GLY PRO
SEQRES 21 B 337 THR LEU PRO ASP ILE SER PHE HIS LEU GLY GLY LYS GLU
SEQRES 22 B 337 TYR THR LEU THR SER ALA ASP TYR VAL PHE GLN GLU SER
SEQRES 23 B 337 TYR SER SER LYS LYS LEU CYS THR LEU ALA ILE HIS ALA
SEQRES 24 B 337 MET ASP ILE PRO PRO PRO THR GLY PRO THR TRP ALA LEU
SEQRES 25 B 337 GLY ALA THR PHE ILE ARG LYS PHE TYR THR GLU PHE ASP
SEQRES 26 B 337 ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU ALA ARG
HET NAG A 401 14
HET 6VU A 402 36
HET PGE A 403 10
HET PEG A 404 7
HET PEG A 405 7
HET PEG A 406 7
HET DMS A 407 4
HET DMS A 408 4
HET DMS A 409 4
HET DMS A 410 4
HET DMS A 411 4
HET DMS A 412 4
HET DMS A 413 4
HET DMS A 414 4
HET NAG B 401 14
HET 6VU B 402 36
HET PGE B 403 10
HET PEG B 404 7
HET DMS B 405 4
HET DMS B 406 4
HET DMS B 407 4
HET DMS B 408 4
HET DMS B 409 4
HET DMS B 410 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM 6VU 1-(4-METHOXYBUTYL)-~{N}-(2-METHYLPROPYL)-~{N}-[(3~{S},
HETNAM 2 6VU 5~{R})-5-MORPHOLIN-4-YLCARBONYLPIPERIDIN-3-
HETNAM 3 6VU YL]BENZIMIDAZOLE-2-CARBOXAMIDE
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 6VU 2(C27 H41 N5 O4)
FORMUL 5 PGE 2(C6 H14 O4)
FORMUL 6 PEG 4(C4 H10 O3)
FORMUL 9 DMS 14(C2 H6 O S)
FORMUL 27 HOH *290(H2 O)
HELIX 1 AA1 TYR A 55 HIS A 61 1 7
HELIX 2 AA2 ASP A 65 SER A 69 5 5
HELIX 3 AA3 PRO A 115 MET A 120 1 6
HELIX 4 AA4 PHE A 132 VAL A 140 5 9
HELIX 5 AA5 PRO A 142 GLN A 150 1 9
HELIX 6 AA6 ASP A 182 GLN A 184 5 3
HELIX 7 AA7 SER A 235 GLY A 247 1 13
HELIX 8 AA8 ASN A 260 LEU A 265 5 6
HELIX 9 AA9 THR A 280 VAL A 285 1 6
HELIX 10 AB1 GLY A 316 ARG A 321 1 6
HELIX 11 AB2 TYR B 55 HIS B 61 1 7
HELIX 12 AB3 ASP B 65 SER B 69 5 5
HELIX 13 AB4 PRO B 115 MET B 120 1 6
HELIX 14 AB5 PHE B 132 VAL B 140 5 9
HELIX 15 AB6 PRO B 142 GLN B 150 1 9
HELIX 16 AB7 ASP B 182 GLN B 184 5 3
HELIX 17 AB8 SER B 235 GLY B 247 1 13
HELIX 18 AB9 ASN B 260 LEU B 265 5 6
HELIX 19 AC1 THR B 280 VAL B 285 1 6
HELIX 20 AC2 GLY B 316 LYS B 322 1 7
SHEET 1 AA1 9 LYS A 73 TYR A 83 0
SHEET 2 AA1 9 GLY A 86 VAL A 99 -1 O LEU A 92 N GLY A 76
SHEET 3 AA1 9 GLN A 19 ILE A 26 -1 N GLY A 25 O THR A 98
SHEET 4 AA1 9 SER A 8 TYR A 15 -1 N TYR A 15 O GLN A 19
SHEET 5 AA1 9 GLY A 174 LEU A 178 -1 O LEU A 178 N SER A 8
SHEET 6 AA1 9 VAL A 157 TYR A 162 -1 N TYR A 161 O GLN A 175
SHEET 7 AA1 9 PHE A 323 ASP A 328 -1 O PHE A 327 N PHE A 158
SHEET 8 AA1 9 ARG A 333 ALA A 339 -1 O GLY A 335 N GLU A 326
SHEET 9 AA1 9 TYR A 186 ASN A 194 -1 N ILE A 193 O ILE A 334
SHEET 1 AA213 LYS A 73 TYR A 83 0
SHEET 2 AA213 GLY A 86 VAL A 99 -1 O LEU A 92 N GLY A 76
SHEET 3 AA213 ILE A 102 GLU A 113 -1 O GLU A 110 N PHE A 91
SHEET 4 AA213 VAL A 44 PRO A 47 1 N VAL A 44 O GLY A 109
SHEET 5 AA213 GLY A 126 GLY A 129 -1 O VAL A 127 N TRP A 45
SHEET 6 AA213 GLN A 31 ASP A 38 1 N VAL A 36 O VAL A 128
SHEET 7 AA213 GLN A 19 ILE A 26 -1 N GLY A 22 O VAL A 35
SHEET 8 AA213 SER A 8 TYR A 15 -1 N TYR A 15 O GLN A 19
SHEET 9 AA213 GLY A 174 LEU A 178 -1 O LEU A 178 N SER A 8
SHEET 10 AA213 VAL A 157 TYR A 162 -1 N TYR A 161 O GLN A 175
SHEET 11 AA213 PHE A 323 ASP A 328 -1 O PHE A 327 N PHE A 158
SHEET 12 AA213 ARG A 333 ALA A 339 -1 O GLY A 335 N GLU A 326
SHEET 13 AA213 TYR A 186 ASN A 194 -1 N ILE A 193 O ILE A 334
SHEET 1 AA3 4 SER A 213 LEU A 216 0
SHEET 2 AA3 4 GLN A 202 VAL A 210 -1 N VAL A 208 O LEU A 216
SHEET 3 AA3 4 ILE A 268 LEU A 272 -1 O HIS A 271 N GLY A 207
SHEET 4 AA3 4 LYS A 275 LEU A 279 -1 O LEU A 279 N ILE A 268
SHEET 1 AA4 6 SER A 213 LEU A 216 0
SHEET 2 AA4 6 GLN A 202 VAL A 210 -1 N VAL A 208 O LEU A 216
SHEET 3 AA4 6 CYS A 221 VAL A 225 -1 O ALA A 223 N ILE A 203
SHEET 4 AA4 6 TRP A 313 LEU A 315 1 O LEU A 315 N LEU A 224
SHEET 5 AA4 6 ILE A 232 GLY A 234 -1 N SER A 233 O ALA A 314
SHEET 6 AA4 6 ILE A 300 ALA A 302 1 O HIS A 301 N ILE A 232
SHEET 1 AA5 3 LYS A 249 LYS A 250 0
SHEET 2 AA5 3 TYR A 255 LYS A 258 -1 O VAL A 256 N LYS A 249
SHEET 3 AA5 3 LEU A 295 THR A 297 -1 O CYS A 296 N VAL A 257
SHEET 1 AA6 9 LYS B 73 TYR B 83 0
SHEET 2 AA6 9 GLY B 86 VAL B 99 -1 O LEU B 92 N GLY B 76
SHEET 3 AA6 9 GLN B 19 ILE B 26 -1 N GLY B 25 O THR B 98
SHEET 4 AA6 9 SER B 8 TYR B 15 -1 N THR B 13 O TYR B 21
SHEET 5 AA6 9 GLY B 174 LEU B 178 -1 O LEU B 178 N SER B 8
SHEET 6 AA6 9 VAL B 157 TYR B 162 -1 N SER B 159 O VAL B 177
SHEET 7 AA6 9 PHE B 323 ASP B 328 -1 O PHE B 327 N PHE B 158
SHEET 8 AA6 9 ARG B 333 ALA B 339 -1 O GLY B 335 N GLU B 326
SHEET 9 AA6 9 TYR B 186 ASN B 194 -1 N ILE B 193 O ILE B 334
SHEET 1 AA713 LYS B 73 TYR B 83 0
SHEET 2 AA713 GLY B 86 VAL B 99 -1 O LEU B 92 N GLY B 76
SHEET 3 AA713 ILE B 102 GLU B 113 -1 O VAL B 104 N ILE B 97
SHEET 4 AA713 VAL B 44 PRO B 47 1 N VAL B 44 O GLY B 109
SHEET 5 AA713 GLY B 126 GLY B 129 -1 O VAL B 127 N TRP B 45
SHEET 6 AA713 GLN B 31 ASP B 38 1 N VAL B 36 O VAL B 128
SHEET 7 AA713 GLN B 19 ILE B 26 -1 N GLY B 22 O VAL B 35
SHEET 8 AA713 SER B 8 TYR B 15 -1 N THR B 13 O TYR B 21
SHEET 9 AA713 GLY B 174 LEU B 178 -1 O LEU B 178 N SER B 8
SHEET 10 AA713 VAL B 157 TYR B 162 -1 N SER B 159 O VAL B 177
SHEET 11 AA713 PHE B 323 ASP B 328 -1 O PHE B 327 N PHE B 158
SHEET 12 AA713 ARG B 333 ALA B 339 -1 O GLY B 335 N GLU B 326
SHEET 13 AA713 TYR B 186 ASN B 194 -1 N ILE B 193 O ILE B 334
SHEET 1 AA8 4 SER B 213 LEU B 216 0
SHEET 2 AA8 4 GLN B 202 VAL B 210 -1 N VAL B 208 O LEU B 216
SHEET 3 AA8 4 ILE B 268 LEU B 272 -1 O HIS B 271 N GLY B 207
SHEET 4 AA8 4 LYS B 275 LEU B 279 -1 O LEU B 279 N ILE B 268
SHEET 1 AA9 6 SER B 213 LEU B 216 0
SHEET 2 AA9 6 GLN B 202 VAL B 210 -1 N VAL B 208 O LEU B 216
SHEET 3 AA9 6 CYS B 221 VAL B 225 -1 O CYS B 221 N MET B 205
SHEET 4 AA9 6 TRP B 313 LEU B 315 1 O LEU B 315 N LEU B 224
SHEET 5 AA9 6 ILE B 232 GLY B 234 -1 N SER B 233 O ALA B 314
SHEET 6 AA9 6 ILE B 300 ALA B 302 1 O HIS B 301 N ILE B 232
SHEET 1 AB1 3 LYS B 249 LYS B 250 0
SHEET 2 AB1 3 TYR B 255 LYS B 258 -1 O VAL B 256 N LYS B 249
SHEET 3 AB1 3 LEU B 295 THR B 297 -1 O CYS B 296 N VAL B 257
SSBOND 1 CYS A 51 CYS A 58 1555 1555 2.01
SSBOND 2 CYS A 217 CYS A 221 1555 1555 2.04
SSBOND 3 CYS A 259 CYS A 296 1555 1555 2.06
SSBOND 4 CYS B 51 CYS B 58 1555 1555 2.00
SSBOND 5 CYS B 217 CYS B 221 1555 1555 2.04
SSBOND 6 CYS B 259 CYS B 296 1555 1555 2.06
LINK ND2 ASN A 75 C1 NAG A 401 1555 1555 1.45
LINK ND2 ASN B 75 C1 NAG B 401 1555 1555 1.45
CISPEP 1 THR A 28 PRO A 29 0 -7.10
CISPEP 2 LEU A 117 PRO A 118 0 10.84
CISPEP 3 PRO A 307 PRO A 308 0 2.98
CISPEP 4 GLY A 310 PRO A 311 0 -1.82
CISPEP 5 THR B 28 PRO B 29 0 -5.00
CISPEP 6 LEU B 117 PRO B 118 0 9.31
CISPEP 7 PRO B 307 PRO B 308 0 0.98
CISPEP 8 GLY B 310 PRO B 311 0 5.64
CRYST1 139.317 139.317 139.317 90.00 90.00 90.00 P 21 3 24
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 0.007178 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007178 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007178 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
