HEADER HYDROLASE 16-NOV-12 4I04
TITLE STRUCTURE OF ZYMOGEN OF CATHEPSIN B1 FROM SCHISTOSOMA MANSONI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN B-LIKE PEPTIDASE (C01 FAMILY);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CATHEPSIN B1 ISOTYPE 1;
COMPND 5 EC: 3.4.22.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHISTOSOMA MANSONI;
SOURCE 3 ORGANISM_COMMON: BLOOD FLUKE;
SOURCE 4 ORGANISM_TAXID: 6183;
SOURCE 5 GENE: CB1.1, SMP_103610;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: X33;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PPICZALPHA
KEYWDS PEPTIDASE, DIGESTIVE TRACT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.REZACOVA,A.JILKOVA,J.BRYNDA,M.HORN,M.MARES
REVDAT 3 08-NOV-23 4I04 1 REMARK SEQADV
REVDAT 2 25-MAY-16 4I04 1 JRNL
REVDAT 1 05-FEB-14 4I04 0
JRNL AUTH A.JILKOVA,M.HORN,P.REZACOVA,L.MARESOVA,P.FAJTOVA,J.BRYNDA,
JRNL AUTH 2 J.VONDRASEK,J.H.MCKERROW,C.R.CAFFREY,M.MARES
JRNL TITL ACTIVATION ROUTE OF THE SCHISTOSOMA MANSONI CATHEPSIN B1
JRNL TITL 2 DRUG TARGET: STRUCTURAL MAP WITH A GLYCOSAMINOGLYCAN SWITCH
JRNL REF STRUCTURE V. 22 1786 2014
JRNL REFN ISSN 0969-2126
JRNL PMID 25456815
JRNL DOI 10.1016/J.STR.2014.09.015
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 75.3
REMARK 3 NUMBER OF REFLECTIONS : 71614
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3756
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1585
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 22.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 84
REMARK 3 BIN FREE R VALUE : 0.2850
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 : 24
REMARK 3 SOLVENT ATOMS : 519
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.01000
REMARK 3 B13 (A**2) : 0.01000
REMARK 3 B23 (A**2) : 0.01000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.254
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.209
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.138
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.596
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10117 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13662 ; 1.303 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1234 ; 6.062 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 501 ;34.195 ;23.593
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1742 ;15.521 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 84 ;17.278 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1359 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7842 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5058 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6765 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 723 ; 0.151 ; 0.200
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): 84 ; 0.181 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 32 ; 0.227 ; 0.200
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): 6308 ; 0.565 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9813 ; 0.911 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4506 ; 1.513 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3842 ; 2.260 ; 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 : 20
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 9 A 50
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5600 -39.1120 -42.5370
REMARK 3 T TENSOR
REMARK 3 T11: -0.0085 T22: 0.1650
REMARK 3 T33: 0.0329 T12: 0.1144
REMARK 3 T13: 0.0961 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 1.2831 L22: 4.7832
REMARK 3 L33: 3.9298 L12: -0.3950
REMARK 3 L13: 0.5402 L23: -0.9060
REMARK 3 S TENSOR
REMARK 3 S11: -0.1055 S12: -0.2902 S13: -0.0843
REMARK 3 S21: 0.4985 S22: 0.1815 S23: -0.0004
REMARK 3 S31: 0.1654 S32: 0.0763 S33: -0.0759
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 51 A 117
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8740 -20.3280 -60.5670
REMARK 3 T TENSOR
REMARK 3 T11: -0.0340 T22: -0.0924
REMARK 3 T33: 0.0271 T12: 0.0618
REMARK 3 T13: -0.0083 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 1.4208 L22: 1.5156
REMARK 3 L33: 3.1696 L12: 0.0871
REMARK 3 L13: 0.2783 L23: 0.4670
REMARK 3 S TENSOR
REMARK 3 S11: 0.0847 S12: -0.0456 S13: 0.2263
REMARK 3 S21: 0.1492 S22: 0.0728 S23: 0.1674
REMARK 3 S31: -0.2781 S32: 0.0097 S33: -0.1576
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 118 A 150
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9860 -13.2850 -51.3200
REMARK 3 T TENSOR
REMARK 3 T11: 0.2052 T22: 0.1226
REMARK 3 T33: 0.1229 T12: 0.0317
REMARK 3 T13: -0.0135 T23: -0.1031
REMARK 3 L TENSOR
REMARK 3 L11: 1.5287 L22: 1.3366
REMARK 3 L33: 0.6539 L12: 0.3048
REMARK 3 L13: 0.9940 L23: 0.2961
REMARK 3 S TENSOR
REMARK 3 S11: -0.0002 S12: -0.0399 S13: 0.4013
REMARK 3 S21: 0.2331 S22: 0.1449 S23: 0.0136
REMARK 3 S31: -0.6029 S32: 0.1300 S33: -0.1446
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 : A 151 A 240
REMARK 3 ORIGIN FOR THE GROUP (A): 33.0460 -14.1700 -53.4280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0586 T22: 0.0762
REMARK 3 T33: 0.1119 T12: 0.0372
REMARK 3 T13: -0.0156 T23: -0.0644
REMARK 3 L TENSOR
REMARK 3 L11: 0.9756 L22: 2.1399
REMARK 3 L33: 2.1426 L12: 0.0433
REMARK 3 L13: 0.2067 L23: -0.1793
REMARK 3 S TENSOR
REMARK 3 S11: -0.0618 S12: -0.2829 S13: 0.2505
REMARK 3 S21: 0.3632 S22: 0.0569 S23: -0.2222
REMARK 3 S31: -0.5473 S32: 0.2574 S33: 0.0050
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 241 A 323
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5140 -31.7740 -54.1620
REMARK 3 T TENSOR
REMARK 3 T11: -0.0638 T22: -0.0013
REMARK 3 T33: -0.0273 T12: 0.1246
REMARK 3 T13: 0.0503 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.1395 L22: 2.2268
REMARK 3 L33: 1.8842 L12: -0.2129
REMARK 3 L13: 0.1711 L23: -0.1032
REMARK 3 S TENSOR
REMARK 3 S11: -0.0115 S12: -0.1573 S13: 0.0807
REMARK 3 S21: 0.3128 S22: 0.1427 S23: 0.3112
REMARK 3 S31: -0.1012 S32: -0.1165 S33: -0.1311
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 8 B 42
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8940 8.8560 -31.0580
REMARK 3 T TENSOR
REMARK 3 T11: -0.1145 T22: 0.0342
REMARK 3 T33: -0.1123 T12: -0.0293
REMARK 3 T13: -0.0656 T23: 0.1151
REMARK 3 L TENSOR
REMARK 3 L11: 2.5303 L22: 6.2483
REMARK 3 L33: 7.3971 L12: -0.8886
REMARK 3 L13: -1.4435 L23: 1.1193
REMARK 3 S TENSOR
REMARK 3 S11: 0.0910 S12: 0.3332 S13: 0.2006
REMARK 3 S21: -0.4177 S22: 0.0035 S23: 0.0705
REMARK 3 S31: -0.3014 S32: -0.3420 S33: -0.0946
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 43 B 119
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0570 -12.3530 -13.8940
REMARK 3 T TENSOR
REMARK 3 T11: -0.1373 T22: -0.1674
REMARK 3 T33: -0.1006 T12: -0.0301
REMARK 3 T13: -0.0152 T23: 0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 2.3108 L22: 1.7247
REMARK 3 L33: 2.7064 L12: 0.0474
REMARK 3 L13: -0.9989 L23: 0.1296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0595 S12: 0.0771 S13: -0.1905
REMARK 3 S21: -0.1216 S22: 0.1090 S23: 0.1263
REMARK 3 S31: 0.3256 S32: -0.1626 S33: -0.0495
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 : B 120 B 147
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4930 -20.0930 -21.7950
REMARK 3 T TENSOR
REMARK 3 T11: -0.0403 T22: -0.0593
REMARK 3 T33: -0.0457 T12: -0.0344
REMARK 3 T13: 0.0400 T23: -0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 3.6404 L22: 4.8469
REMARK 3 L33: 2.4697 L12: 0.4563
REMARK 3 L13: -0.4388 L23: 1.9375
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: -0.0142 S13: -0.3560
REMARK 3 S21: -0.1996 S22: 0.0623 S23: -0.1093
REMARK 3 S31: 0.8311 S32: -0.1182 S33: -0.0631
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 : B 148 B 237
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1430 -18.0790 -19.2670
REMARK 3 T TENSOR
REMARK 3 T11: -0.0717 T22: -0.0896
REMARK 3 T33: -0.0669 T12: -0.0135
REMARK 3 T13: -0.0052 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 2.3126 L22: 2.1412
REMARK 3 L33: 2.5484 L12: -0.3205
REMARK 3 L13: -0.8517 L23: 0.0902
REMARK 3 S TENSOR
REMARK 3 S11: -0.0932 S12: 0.1580 S13: -0.2567
REMARK 3 S21: -0.2255 S22: 0.0585 S23: -0.2272
REMARK 3 S31: 0.4126 S32: 0.1963 S33: 0.0346
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 246 B 323
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0800 -0.9980 -19.0220
REMARK 3 T TENSOR
REMARK 3 T11: -0.2040 T22: -0.1025
REMARK 3 T33: -0.1578 T12: -0.0270
REMARK 3 T13: -0.0318 T23: 0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 1.3364 L22: 2.4347
REMARK 3 L33: 2.9600 L12: 0.3641
REMARK 3 L13: -0.3853 L23: 0.0992
REMARK 3 S TENSOR
REMARK 3 S11: -0.0944 S12: 0.1668 S13: 0.0189
REMARK 3 S21: -0.2055 S22: 0.1987 S23: 0.2418
REMARK 3 S31: 0.0222 S32: -0.2709 S33: -0.1044
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 : C 6 C 42
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9390 40.8570 -69.9940
REMARK 3 T TENSOR
REMARK 3 T11: -0.1172 T22: -0.1141
REMARK 3 T33: -0.0221 T12: -0.1147
REMARK 3 T13: 0.0419 T23: -0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 4.7116 L22: 3.8276
REMARK 3 L33: 5.0252 L12: -0.5253
REMARK 3 L13: 0.3089 L23: -2.1538
REMARK 3 S TENSOR
REMARK 3 S11: 0.1144 S12: 0.1093 S13: 0.3049
REMARK 3 S21: 0.0294 S22: -0.1034 S23: -0.3264
REMARK 3 S31: -0.4543 S32: 0.4010 S33: -0.0110
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 : C 43 C 123
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8890 16.7830 -59.7050
REMARK 3 T TENSOR
REMARK 3 T11: -0.1444 T22: -0.1894
REMARK 3 T33: -0.1411 T12: -0.0164
REMARK 3 T13: -0.0329 T23: 0.0719
REMARK 3 L TENSOR
REMARK 3 L11: 2.3373 L22: 2.1185
REMARK 3 L33: 3.0627 L12: -0.3959
REMARK 3 L13: 0.0618 L23: 0.1452
REMARK 3 S TENSOR
REMARK 3 S11: -0.0006 S12: -0.1390 S13: -0.1004
REMARK 3 S21: -0.0568 S22: 0.0887 S23: 0.1645
REMARK 3 S31: 0.1892 S32: -0.0530 S33: -0.0881
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 128 C 209
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2170 15.1240 -50.8030
REMARK 3 T TENSOR
REMARK 3 T11: -0.1607 T22: 0.0394
REMARK 3 T33: -0.0610 T12: 0.0245
REMARK 3 T13: -0.0522 T23: 0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 2.1189 L22: 3.6201
REMARK 3 L33: 3.4804 L12: 0.1461
REMARK 3 L13: 0.0301 L23: -0.8248
REMARK 3 S TENSOR
REMARK 3 S11: 0.0802 S12: -0.2890 S13: 0.0175
REMARK 3 S21: 0.0918 S22: -0.1500 S23: -0.5565
REMARK 3 S31: 0.1961 S32: 0.7097 S33: 0.0698
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 210 C 282
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7390 21.6820 -64.5390
REMARK 3 T TENSOR
REMARK 3 T11: -0.1563 T22: -0.1819
REMARK 3 T33: -0.1577 T12: -0.0381
REMARK 3 T13: -0.0250 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.3372 L22: 2.3886
REMARK 3 L33: 2.3240 L12: -0.6146
REMARK 3 L13: 0.2435 L23: -1.1837
REMARK 3 S TENSOR
REMARK 3 S11: 0.1188 S12: -0.0256 S13: -0.1035
REMARK 3 S21: -0.2449 S22: 0.0863 S23: 0.1835
REMARK 3 S31: 0.1776 S32: -0.0112 S33: -0.2050
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 294 C 323
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5720 24.2640 -64.6840
REMARK 3 T TENSOR
REMARK 3 T11: -0.1891 T22: -0.1929
REMARK 3 T33: -0.1624 T12: -0.0321
REMARK 3 T13: -0.0305 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 2.0084 L22: 4.1783
REMARK 3 L33: 2.6832 L12: -0.3826
REMARK 3 L13: -0.4086 L23: -1.2419
REMARK 3 S TENSOR
REMARK 3 S11: 0.2126 S12: -0.0525 S13: -0.0484
REMARK 3 S21: -0.2955 S22: 0.0900 S23: 0.1557
REMARK 3 S31: 0.0667 S32: -0.1426 S33: -0.3027
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 6 D 46
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6960 7.1390 -3.5280
REMARK 3 T TENSOR
REMARK 3 T11: -0.1595 T22: -0.0206
REMARK 3 T33: 0.0315 T12: 0.0561
REMARK 3 T13: -0.1183 T23: -0.0969
REMARK 3 L TENSOR
REMARK 3 L11: 3.7990 L22: 4.6126
REMARK 3 L33: 4.3648 L12: 0.1366
REMARK 3 L13: 1.1489 L23: -1.1040
REMARK 3 S TENSOR
REMARK 3 S11: 0.1568 S12: -0.1045 S13: -0.4175
REMARK 3 S21: 0.1366 S22: -0.0467 S23: -0.3387
REMARK 3 S31: 0.1356 S32: 0.6987 S33: -0.1101
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 47 D 120
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7720 30.0030 -13.2130
REMARK 3 T TENSOR
REMARK 3 T11: -0.0343 T22: -0.1041
REMARK 3 T33: -0.0781 T12: 0.0147
REMARK 3 T13: 0.0299 T23: 0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 1.5224 L22: 2.5177
REMARK 3 L33: 1.7492 L12: 0.5180
REMARK 3 L13: 0.3234 L23: 0.6599
REMARK 3 S TENSOR
REMARK 3 S11: -0.0467 S12: 0.1703 S13: 0.0683
REMARK 3 S21: -0.2082 S22: 0.1239 S23: 0.2621
REMARK 3 S31: -0.3492 S32: 0.0016 S33: -0.0773
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 121 D 194
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4130 30.3250 -20.2520
REMARK 3 T TENSOR
REMARK 3 T11: -0.0079 T22: 0.0752
REMARK 3 T33: -0.0786 T12: -0.1208
REMARK 3 T13: 0.0535 T23: -0.0338
REMARK 3 L TENSOR
REMARK 3 L11: 2.6007 L22: 4.8007
REMARK 3 L33: 3.3984 L12: -0.5549
REMARK 3 L13: -0.7244 L23: 0.2367
REMARK 3 S TENSOR
REMARK 3 S11: 0.0719 S12: 0.3700 S13: 0.0241
REMARK 3 S21: -0.2552 S22: 0.0740 S23: -0.4117
REMARK 3 S31: -0.3524 S32: 0.4674 S33: -0.1459
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 195 D 295
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2460 25.0790 -12.2700
REMARK 3 T TENSOR
REMARK 3 T11: -0.0713 T22: -0.1031
REMARK 3 T33: -0.1272 T12: 0.0070
REMARK 3 T13: 0.0207 T23: -0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 1.6057 L22: 2.8162
REMARK 3 L33: 1.2701 L12: 0.8400
REMARK 3 L13: 0.0606 L23: -0.6637
REMARK 3 S TENSOR
REMARK 3 S11: 0.0341 S12: 0.2331 S13: 0.1072
REMARK 3 S21: -0.0236 S22: 0.1066 S23: 0.0087
REMARK 3 S31: -0.3006 S32: 0.2017 S33: -0.1408
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 308 D 323
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7950 29.3540 -5.5870
REMARK 3 T TENSOR
REMARK 3 T11: -0.0360 T22: -0.1473
REMARK 3 T33: -0.1221 T12: 0.0451
REMARK 3 T13: 0.1157 T23: -0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 2.7632 L22: 8.2661
REMARK 3 L33: 4.9289 L12: -0.6922
REMARK 3 L13: 2.4303 L23: -3.4797
REMARK 3 S TENSOR
REMARK 3 S11: 0.1368 S12: 0.1241 S13: 0.2621
REMARK 3 S21: 0.5253 S22: -0.0379 S23: 0.2196
REMARK 3 S31: -0.5001 S32: -0.0095 S33: -0.0989
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4I04 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-NOV-12.
REMARK 100 THE DEPOSITION ID IS D_1000076136.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.914
REMARK 200 MONOCHROMATOR : SI(111) CRYSTAL
REMARK 200 OPTICS : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 WITH 2 SETS OF RH-SOATED SILICON
REMARK 200 AND GLASS MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78650
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 78.4
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 42.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.29600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: 3QSD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 0.1M AMMONIUM ACETATE, 0.1M
REMARK 280 BIS-TRIS, 17% PEG 10000. PROTEIN BUFFER AND CONCENTRATION: 5MM
REMARK 280 SODIUM ACETATE, PH 5.5, CPR=5.25MG/ML. RATIO PROTEIN: RESERVOIR=
REMARK 280 2:1. CRYOCOOLED IN MOTHER LIQUOR CONTAINING 20% ETHYLENE GLYCOL.,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K, PH 6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A 1
REMARK 465 ILE A 2
REMARK 465 SER A 3
REMARK 465 VAL A 4
REMARK 465 LYS A 5
REMARK 465 ASN A 6
REMARK 465 GLU A 7
REMARK 465 LYS A 8
REMARK 465 GLU A 179
REMARK 465 HIS A 180
REMARK 465 HIS A 181
REMARK 465 THR A 182
REMARK 465 LYS A 183
REMARK 465 GLY A 184
REMARK 465 LYS A 185
REMARK 465 TYR A 186
REMARK 465 PRO A 187
REMARK 465 PRO A 188
REMARK 465 CYS A 189
REMARK 465 HIS B 1
REMARK 465 ILE B 2
REMARK 465 SER B 3
REMARK 465 VAL B 4
REMARK 465 LYS B 5
REMARK 465 ASN B 6
REMARK 465 GLU B 7
REMARK 465 HIS B 181
REMARK 465 THR B 182
REMARK 465 LYS B 183
REMARK 465 GLY B 184
REMARK 465 LYS B 185
REMARK 465 TYR B 186
REMARK 465 HIS C 1
REMARK 465 ILE C 2
REMARK 465 SER C 3
REMARK 465 VAL C 4
REMARK 465 LYS C 5
REMARK 465 GLU C 179
REMARK 465 HIS C 180
REMARK 465 HIS C 181
REMARK 465 THR C 182
REMARK 465 LYS C 183
REMARK 465 GLY C 184
REMARK 465 LYS C 185
REMARK 465 TYR C 186
REMARK 465 PRO C 187
REMARK 465 PRO C 188
REMARK 465 CYS C 189
REMARK 465 GLY C 190
REMARK 465 HIS D 1
REMARK 465 ILE D 2
REMARK 465 SER D 3
REMARK 465 VAL D 4
REMARK 465 LYS D 5
REMARK 465 HIS D 180
REMARK 465 HIS D 181
REMARK 465 THR D 182
REMARK 465 LYS D 183
REMARK 465 GLY D 184
REMARK 465 LYS D 185
REMARK 465 TYR D 186
REMARK 465 PRO D 187
REMARK 465 PRO D 188
REMARK 465 CYS D 189
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER C 312 O HOH C 562 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 60 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 LEU C 131 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 MET A 46 -127.39 -121.36
REMARK 500 SER A 95 -162.01 56.87
REMARK 500 ASN A 226 81.90 -63.07
REMARK 500 LYS A 282 -1.41 79.27
REMARK 500 ASN A 293 173.87 60.43
REMARK 500 LEU B 12 -0.82 76.60
REMARK 500 MET B 46 -115.61 -111.19
REMARK 500 SER B 95 -155.29 58.56
REMARK 500 ARG B 96 55.95 -92.30
REMARK 500 ASN B 122 80.56 -155.82
REMARK 500 SER B 136 2.55 -68.47
REMARK 500 ILE B 262 -34.76 -132.07
REMARK 500 LYS B 282 -11.82 78.67
REMARK 500 ASN B 293 169.42 65.84
REMARK 500 ASN C 25 50.63 -162.82
REMARK 500 MET C 46 -116.77 -112.62
REMARK 500 SER C 95 -162.89 64.05
REMARK 500 ASN C 226 80.56 -63.53
REMARK 500 LYS C 282 -0.81 76.71
REMARK 500 ASN C 293 172.94 63.22
REMARK 500 ALA C 319 -165.28 -162.91
REMARK 500 ASN D 25 44.44 -173.93
REMARK 500 ARG D 35 -32.36 -132.30
REMARK 500 MET D 46 -107.82 -118.71
REMARK 500 HIS D 65 19.99 53.70
REMARK 500 SER D 95 -155.55 50.90
REMARK 500 GLN D 201 41.99 -82.20
REMARK 500 ASN D 226 72.03 -65.20
REMARK 500 ASN D 293 175.53 64.20
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 EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4I05 RELATED DB: PDB
REMARK 900 RELATED ID: 4I07 RELATED DB: PDB
REMARK 900 RELATED ID: 3QSD RELATED DB: PDB
REMARK 900 MATURE SMCB1 IN COMPLEX WITH INHIBITOR CA074
REMARK 900 RELATED ID: 3S3R RELATED DB: PDB
REMARK 900 MATURE SMCB1 IN COMPLEX WITH INHIBITOR K11777
REMARK 900 RELATED ID: 3S3Q RELATED DB: PDB
REMARK 900 MATURE SMCB1 IN COMPLEX WITH INHIBITOR K11017
DBREF 4I04 A 1 323 UNP Q8MNY2 Q8MNY2_SCHMA 18 340
DBREF 4I04 B 1 323 UNP Q8MNY2 Q8MNY2_SCHMA 18 340
DBREF 4I04 C 1 323 UNP Q8MNY2 Q8MNY2_SCHMA 18 340
DBREF 4I04 D 1 323 UNP Q8MNY2 Q8MNY2_SCHMA 18 340
SEQADV 4I04 SER A 100 UNP Q8MNY2 CYS 117 ENGINEERED MUTATION
SEQADV 4I04 ALA A 168 UNP Q8MNY2 THR 185 ENGINEERED MUTATION
SEQADV 4I04 ALA A 283 UNP Q8MNY2 THR 300 ENGINEERED MUTATION
SEQADV 4I04 SER B 100 UNP Q8MNY2 CYS 117 ENGINEERED MUTATION
SEQADV 4I04 ALA B 168 UNP Q8MNY2 THR 185 ENGINEERED MUTATION
SEQADV 4I04 ALA B 283 UNP Q8MNY2 THR 300 ENGINEERED MUTATION
SEQADV 4I04 SER C 100 UNP Q8MNY2 CYS 117 ENGINEERED MUTATION
SEQADV 4I04 ALA C 168 UNP Q8MNY2 THR 185 ENGINEERED MUTATION
SEQADV 4I04 ALA C 283 UNP Q8MNY2 THR 300 ENGINEERED MUTATION
SEQADV 4I04 SER D 100 UNP Q8MNY2 CYS 117 ENGINEERED MUTATION
SEQADV 4I04 ALA D 168 UNP Q8MNY2 THR 185 ENGINEERED MUTATION
SEQADV 4I04 ALA D 283 UNP Q8MNY2 THR 300 ENGINEERED MUTATION
SEQRES 1 A 323 HIS ILE SER VAL LYS ASN GLU LYS PHE GLU PRO LEU SER
SEQRES 2 A 323 ASP ASP ILE ILE SER TYR ILE ASN GLU HIS PRO ASN ALA
SEQRES 3 A 323 GLY TRP ARG ALA GLU LYS SER ASN ARG PHE HIS SER LEU
SEQRES 4 A 323 ASP ASP ALA ARG ILE GLN MET GLY ALA ARG ARG GLU GLU
SEQRES 5 A 323 PRO ASP LEU ARG ARG THR ARG ARG PRO THR VAL ASP HIS
SEQRES 6 A 323 ASN ASP TRP ASN VAL GLU ILE PRO SER SER PHE ASP SER
SEQRES 7 A 323 ARG LYS LYS TRP PRO ARG CYS LYS SER ILE ALA THR ILE
SEQRES 8 A 323 ARG ASP GLN SER ARG CYS GLY SER SER TRP ALA PHE GLY
SEQRES 9 A 323 ALA VAL GLU ALA MET SER ASP ARG SER CYS ILE GLN SER
SEQRES 10 A 323 GLY GLY LYS GLN ASN VAL GLU LEU SER ALA VAL ASP LEU
SEQRES 11 A 323 LEU SER CYS CYS GLU SER CYS GLY LEU GLY CYS GLU GLY
SEQRES 12 A 323 GLY ILE LEU GLY PRO ALA TRP ASP TYR TRP VAL LYS GLU
SEQRES 13 A 323 GLY ILE VAL THR GLY SER SER LYS GLU ASN HIS ALA GLY
SEQRES 14 A 323 CYS GLU PRO TYR PRO PHE PRO LYS CYS GLU HIS HIS THR
SEQRES 15 A 323 LYS GLY LYS TYR PRO PRO CYS GLY SER LYS ILE TYR LYS
SEQRES 16 A 323 THR PRO ARG CYS LYS GLN THR CYS GLN LYS LYS TYR LYS
SEQRES 17 A 323 THR PRO TYR THR GLN ASP LYS HIS ARG GLY LYS SER SER
SEQRES 18 A 323 TYR ASN VAL LYS ASN ASP GLU LYS ALA ILE GLN LYS GLU
SEQRES 19 A 323 ILE MET LYS TYR GLY PRO VAL GLU ALA GLY PHE THR VAL
SEQRES 20 A 323 TYR GLU ASP PHE LEU ASN TYR LYS SER GLY ILE TYR LYS
SEQRES 21 A 323 HIS ILE THR GLY GLU THR LEU GLY GLY HIS ALA ILE ARG
SEQRES 22 A 323 ILE ILE GLY TRP GLY VAL GLU ASN LYS ALA PRO TYR TRP
SEQRES 23 A 323 LEU ILE ALA ASN SER TRP ASN GLU ASP TRP GLY GLU ASN
SEQRES 24 A 323 GLY TYR PHE ARG ILE VAL ARG GLY ARG ASP GLU CYS SER
SEQRES 25 A 323 ILE GLU SER GLU VAL THR ALA GLY ARG ILE ASN
SEQRES 1 B 323 HIS ILE SER VAL LYS ASN GLU LYS PHE GLU PRO LEU SER
SEQRES 2 B 323 ASP ASP ILE ILE SER TYR ILE ASN GLU HIS PRO ASN ALA
SEQRES 3 B 323 GLY TRP ARG ALA GLU LYS SER ASN ARG PHE HIS SER LEU
SEQRES 4 B 323 ASP ASP ALA ARG ILE GLN MET GLY ALA ARG ARG GLU GLU
SEQRES 5 B 323 PRO ASP LEU ARG ARG THR ARG ARG PRO THR VAL ASP HIS
SEQRES 6 B 323 ASN ASP TRP ASN VAL GLU ILE PRO SER SER PHE ASP SER
SEQRES 7 B 323 ARG LYS LYS TRP PRO ARG CYS LYS SER ILE ALA THR ILE
SEQRES 8 B 323 ARG ASP GLN SER ARG CYS GLY SER SER TRP ALA PHE GLY
SEQRES 9 B 323 ALA VAL GLU ALA MET SER ASP ARG SER CYS ILE GLN SER
SEQRES 10 B 323 GLY GLY LYS GLN ASN VAL GLU LEU SER ALA VAL ASP LEU
SEQRES 11 B 323 LEU SER CYS CYS GLU SER CYS GLY LEU GLY CYS GLU GLY
SEQRES 12 B 323 GLY ILE LEU GLY PRO ALA TRP ASP TYR TRP VAL LYS GLU
SEQRES 13 B 323 GLY ILE VAL THR GLY SER SER LYS GLU ASN HIS ALA GLY
SEQRES 14 B 323 CYS GLU PRO TYR PRO PHE PRO LYS CYS GLU HIS HIS THR
SEQRES 15 B 323 LYS GLY LYS TYR PRO PRO CYS GLY SER LYS ILE TYR LYS
SEQRES 16 B 323 THR PRO ARG CYS LYS GLN THR CYS GLN LYS LYS TYR LYS
SEQRES 17 B 323 THR PRO TYR THR GLN ASP LYS HIS ARG GLY LYS SER SER
SEQRES 18 B 323 TYR ASN VAL LYS ASN ASP GLU LYS ALA ILE GLN LYS GLU
SEQRES 19 B 323 ILE MET LYS TYR GLY PRO VAL GLU ALA GLY PHE THR VAL
SEQRES 20 B 323 TYR GLU ASP PHE LEU ASN TYR LYS SER GLY ILE TYR LYS
SEQRES 21 B 323 HIS ILE THR GLY GLU THR LEU GLY GLY HIS ALA ILE ARG
SEQRES 22 B 323 ILE ILE GLY TRP GLY VAL GLU ASN LYS ALA PRO TYR TRP
SEQRES 23 B 323 LEU ILE ALA ASN SER TRP ASN GLU ASP TRP GLY GLU ASN
SEQRES 24 B 323 GLY TYR PHE ARG ILE VAL ARG GLY ARG ASP GLU CYS SER
SEQRES 25 B 323 ILE GLU SER GLU VAL THR ALA GLY ARG ILE ASN
SEQRES 1 C 323 HIS ILE SER VAL LYS ASN GLU LYS PHE GLU PRO LEU SER
SEQRES 2 C 323 ASP ASP ILE ILE SER TYR ILE ASN GLU HIS PRO ASN ALA
SEQRES 3 C 323 GLY TRP ARG ALA GLU LYS SER ASN ARG PHE HIS SER LEU
SEQRES 4 C 323 ASP ASP ALA ARG ILE GLN MET GLY ALA ARG ARG GLU GLU
SEQRES 5 C 323 PRO ASP LEU ARG ARG THR ARG ARG PRO THR VAL ASP HIS
SEQRES 6 C 323 ASN ASP TRP ASN VAL GLU ILE PRO SER SER PHE ASP SER
SEQRES 7 C 323 ARG LYS LYS TRP PRO ARG CYS LYS SER ILE ALA THR ILE
SEQRES 8 C 323 ARG ASP GLN SER ARG CYS GLY SER SER TRP ALA PHE GLY
SEQRES 9 C 323 ALA VAL GLU ALA MET SER ASP ARG SER CYS ILE GLN SER
SEQRES 10 C 323 GLY GLY LYS GLN ASN VAL GLU LEU SER ALA VAL ASP LEU
SEQRES 11 C 323 LEU SER CYS CYS GLU SER CYS GLY LEU GLY CYS GLU GLY
SEQRES 12 C 323 GLY ILE LEU GLY PRO ALA TRP ASP TYR TRP VAL LYS GLU
SEQRES 13 C 323 GLY ILE VAL THR GLY SER SER LYS GLU ASN HIS ALA GLY
SEQRES 14 C 323 CYS GLU PRO TYR PRO PHE PRO LYS CYS GLU HIS HIS THR
SEQRES 15 C 323 LYS GLY LYS TYR PRO PRO CYS GLY SER LYS ILE TYR LYS
SEQRES 16 C 323 THR PRO ARG CYS LYS GLN THR CYS GLN LYS LYS TYR LYS
SEQRES 17 C 323 THR PRO TYR THR GLN ASP LYS HIS ARG GLY LYS SER SER
SEQRES 18 C 323 TYR ASN VAL LYS ASN ASP GLU LYS ALA ILE GLN LYS GLU
SEQRES 19 C 323 ILE MET LYS TYR GLY PRO VAL GLU ALA GLY PHE THR VAL
SEQRES 20 C 323 TYR GLU ASP PHE LEU ASN TYR LYS SER GLY ILE TYR LYS
SEQRES 21 C 323 HIS ILE THR GLY GLU THR LEU GLY GLY HIS ALA ILE ARG
SEQRES 22 C 323 ILE ILE GLY TRP GLY VAL GLU ASN LYS ALA PRO TYR TRP
SEQRES 23 C 323 LEU ILE ALA ASN SER TRP ASN GLU ASP TRP GLY GLU ASN
SEQRES 24 C 323 GLY TYR PHE ARG ILE VAL ARG GLY ARG ASP GLU CYS SER
SEQRES 25 C 323 ILE GLU SER GLU VAL THR ALA GLY ARG ILE ASN
SEQRES 1 D 323 HIS ILE SER VAL LYS ASN GLU LYS PHE GLU PRO LEU SER
SEQRES 2 D 323 ASP ASP ILE ILE SER TYR ILE ASN GLU HIS PRO ASN ALA
SEQRES 3 D 323 GLY TRP ARG ALA GLU LYS SER ASN ARG PHE HIS SER LEU
SEQRES 4 D 323 ASP ASP ALA ARG ILE GLN MET GLY ALA ARG ARG GLU GLU
SEQRES 5 D 323 PRO ASP LEU ARG ARG THR ARG ARG PRO THR VAL ASP HIS
SEQRES 6 D 323 ASN ASP TRP ASN VAL GLU ILE PRO SER SER PHE ASP SER
SEQRES 7 D 323 ARG LYS LYS TRP PRO ARG CYS LYS SER ILE ALA THR ILE
SEQRES 8 D 323 ARG ASP GLN SER ARG CYS GLY SER SER TRP ALA PHE GLY
SEQRES 9 D 323 ALA VAL GLU ALA MET SER ASP ARG SER CYS ILE GLN SER
SEQRES 10 D 323 GLY GLY LYS GLN ASN VAL GLU LEU SER ALA VAL ASP LEU
SEQRES 11 D 323 LEU SER CYS CYS GLU SER CYS GLY LEU GLY CYS GLU GLY
SEQRES 12 D 323 GLY ILE LEU GLY PRO ALA TRP ASP TYR TRP VAL LYS GLU
SEQRES 13 D 323 GLY ILE VAL THR GLY SER SER LYS GLU ASN HIS ALA GLY
SEQRES 14 D 323 CYS GLU PRO TYR PRO PHE PRO LYS CYS GLU HIS HIS THR
SEQRES 15 D 323 LYS GLY LYS TYR PRO PRO CYS GLY SER LYS ILE TYR LYS
SEQRES 16 D 323 THR PRO ARG CYS LYS GLN THR CYS GLN LYS LYS TYR LYS
SEQRES 17 D 323 THR PRO TYR THR GLN ASP LYS HIS ARG GLY LYS SER SER
SEQRES 18 D 323 TYR ASN VAL LYS ASN ASP GLU LYS ALA ILE GLN LYS GLU
SEQRES 19 D 323 ILE MET LYS TYR GLY PRO VAL GLU ALA GLY PHE THR VAL
SEQRES 20 D 323 TYR GLU ASP PHE LEU ASN TYR LYS SER GLY ILE TYR LYS
SEQRES 21 D 323 HIS ILE THR GLY GLU THR LEU GLY GLY HIS ALA ILE ARG
SEQRES 22 D 323 ILE ILE GLY TRP GLY VAL GLU ASN LYS ALA PRO TYR TRP
SEQRES 23 D 323 LEU ILE ALA ASN SER TRP ASN GLU ASP TRP GLY GLU ASN
SEQRES 24 D 323 GLY TYR PHE ARG ILE VAL ARG GLY ARG ASP GLU CYS SER
SEQRES 25 D 323 ILE GLU SER GLU VAL THR ALA GLY ARG ILE ASN
HET EDO A 401 4
HET EDO A 402 4
HET EDO B 401 4
HET EDO B 402 4
HET EDO B 403 4
HET EDO D 401 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 EDO 6(C2 H6 O2)
FORMUL 11 HOH *519(H2 O)
HELIX 1 1 SER A 13 HIS A 23 1 11
HELIX 2 2 SER A 38 ILE A 44 1 7
HELIX 3 3 GLU A 52 ARG A 60 1 9
HELIX 4 4 SER A 78 TRP A 82 1 5
HELIX 5 5 CYS A 85 THR A 90 5 6
HELIX 6 6 SER A 99 GLN A 116 1 18
HELIX 7 7 SER A 126 CYS A 134 1 9
HELIX 8 8 GLU A 135 GLY A 138 5 4
HELIX 9 9 LEU A 139 GLY A 143 5 5
HELIX 10 10 ILE A 145 GLU A 156 1 12
HELIX 11 11 PRO A 210 LYS A 215 1 6
HELIX 12 12 ASP A 227 GLY A 239 1 13
HELIX 13 13 ASP A 250 LEU A 252 5 3
HELIX 14 14 ASP A 309 ILE A 313 5 5
HELIX 15 15 SER B 13 GLU B 22 1 10
HELIX 16 16 SER B 38 ILE B 44 1 7
HELIX 17 17 GLU B 52 ARG B 60 1 9
HELIX 18 18 SER B 78 TRP B 82 1 5
HELIX 19 19 CYS B 85 THR B 90 5 6
HELIX 20 20 SER B 99 GLN B 116 1 18
HELIX 21 21 SER B 126 CYS B 134 1 9
HELIX 22 22 GLU B 135 GLY B 138 5 4
HELIX 23 23 LEU B 139 GLY B 143 5 5
HELIX 24 24 ILE B 145 GLU B 156 1 12
HELIX 25 25 PRO B 210 LYS B 215 5 6
HELIX 26 26 ASP B 227 GLY B 239 1 13
HELIX 27 27 ASP B 250 LEU B 252 5 3
HELIX 28 28 ASP B 309 ILE B 313 5 5
HELIX 29 29 SER C 13 HIS C 23 1 11
HELIX 30 30 SER C 38 ILE C 44 1 7
HELIX 31 31 GLU C 52 ARG C 60 1 9
HELIX 32 32 SER C 78 TRP C 82 1 5
HELIX 33 33 CYS C 85 THR C 90 5 6
HELIX 34 34 SER C 99 GLN C 116 1 18
HELIX 35 35 SER C 126 CYS C 134 1 9
HELIX 36 36 GLU C 135 GLY C 138 5 4
HELIX 37 37 LEU C 139 GLY C 143 5 5
HELIX 38 38 ILE C 145 GLU C 156 1 12
HELIX 39 39 PRO C 210 LYS C 215 1 6
HELIX 40 40 ASP C 227 GLY C 239 1 13
HELIX 41 41 ASP C 250 LEU C 252 5 3
HELIX 42 42 ASP C 309 ILE C 313 5 5
HELIX 43 43 SER D 13 HIS D 23 1 11
HELIX 44 44 SER D 38 ILE D 44 1 7
HELIX 45 45 GLU D 52 ARG D 60 1 9
HELIX 46 46 SER D 78 TRP D 82 1 5
HELIX 47 47 SER D 99 GLN D 116 1 18
HELIX 48 48 SER D 126 CYS D 134 1 9
HELIX 49 49 LEU D 139 GLY D 143 5 5
HELIX 50 50 ILE D 145 GLU D 156 1 12
HELIX 51 51 PRO D 210 LYS D 215 1 6
HELIX 52 52 ASP D 227 GLY D 239 1 13
HELIX 53 53 ASP D 250 LEU D 252 5 3
HELIX 54 54 ASP D 309 ILE D 313 5 5
SHEET 1 A 6 TRP A 28 ALA A 30 0
SHEET 2 A 6 TYR A 254 TYR A 259 -1 O SER A 256 N ARG A 29
SHEET 3 A 6 TYR A 301 VAL A 305 1 O VAL A 305 N TYR A 259
SHEET 4 A 6 ALA A 283 ALA A 289 -1 N ILE A 288 O PHE A 302
SHEET 5 A 6 THR A 266 GLU A 280 -1 N GLY A 278 O TYR A 285
SHEET 6 A 6 PHE A 76 ASP A 77 -1 N PHE A 76 O TRP A 277
SHEET 1 B 6 TRP A 28 ALA A 30 0
SHEET 2 B 6 TYR A 254 TYR A 259 -1 O SER A 256 N ARG A 29
SHEET 3 B 6 TYR A 301 VAL A 305 1 O VAL A 305 N TYR A 259
SHEET 4 B 6 ALA A 283 ALA A 289 -1 N ILE A 288 O PHE A 302
SHEET 5 B 6 THR A 266 GLU A 280 -1 N GLY A 278 O TYR A 285
SHEET 6 B 6 VAL A 241 TYR A 248 -1 N VAL A 247 O GLY A 268
SHEET 1 C 3 THR A 62 VAL A 63 0
SHEET 2 C 3 SER A 220 VAL A 224 1 O ASN A 223 N VAL A 63
SHEET 3 C 3 THR A 318 ARG A 321 -1 O ALA A 319 N TYR A 222
SHEET 1 D 6 TRP B 28 ALA B 30 0
SHEET 2 D 6 TYR B 254 TYR B 259 -1 O SER B 256 N ARG B 29
SHEET 3 D 6 TYR B 301 VAL B 305 1 O ARG B 303 N TYR B 259
SHEET 4 D 6 ALA B 283 ALA B 289 -1 N ILE B 288 O PHE B 302
SHEET 5 D 6 THR B 266 GLU B 280 -1 N ARG B 273 O ALA B 289
SHEET 6 D 6 PHE B 76 ASP B 77 -1 N PHE B 76 O TRP B 277
SHEET 1 E 6 TRP B 28 ALA B 30 0
SHEET 2 E 6 TYR B 254 TYR B 259 -1 O SER B 256 N ARG B 29
SHEET 3 E 6 TYR B 301 VAL B 305 1 O ARG B 303 N TYR B 259
SHEET 4 E 6 ALA B 283 ALA B 289 -1 N ILE B 288 O PHE B 302
SHEET 5 E 6 THR B 266 GLU B 280 -1 N ARG B 273 O ALA B 289
SHEET 6 E 6 VAL B 241 TYR B 248 -1 N VAL B 247 O GLY B 268
SHEET 1 F 3 THR B 62 VAL B 63 0
SHEET 2 F 3 SER B 220 VAL B 224 1 O ASN B 223 N VAL B 63
SHEET 3 F 3 THR B 318 ARG B 321 -1 O ALA B 319 N TYR B 222
SHEET 1 G 6 TRP C 28 ALA C 30 0
SHEET 2 G 6 TYR C 254 TYR C 259 -1 O SER C 256 N ARG C 29
SHEET 3 G 6 TYR C 301 VAL C 305 1 O ARG C 303 N TYR C 259
SHEET 4 G 6 ALA C 283 ALA C 289 -1 N ILE C 288 O PHE C 302
SHEET 5 G 6 THR C 266 GLU C 280 -1 N GLY C 276 O LEU C 287
SHEET 6 G 6 PHE C 76 ASP C 77 -1 N PHE C 76 O TRP C 277
SHEET 1 H 6 TRP C 28 ALA C 30 0
SHEET 2 H 6 TYR C 254 TYR C 259 -1 O SER C 256 N ARG C 29
SHEET 3 H 6 TYR C 301 VAL C 305 1 O ARG C 303 N TYR C 259
SHEET 4 H 6 ALA C 283 ALA C 289 -1 N ILE C 288 O PHE C 302
SHEET 5 H 6 THR C 266 GLU C 280 -1 N GLY C 276 O LEU C 287
SHEET 6 H 6 VAL C 241 TYR C 248 -1 N VAL C 247 O GLY C 268
SHEET 1 I 3 THR C 62 VAL C 63 0
SHEET 2 I 3 SER C 220 VAL C 224 1 O ASN C 223 N VAL C 63
SHEET 3 I 3 THR C 318 ARG C 321 -1 O ALA C 319 N TYR C 222
SHEET 1 J 6 TRP D 28 ALA D 30 0
SHEET 2 J 6 TYR D 254 TYR D 259 -1 O SER D 256 N ARG D 29
SHEET 3 J 6 TYR D 301 VAL D 305 1 O ARG D 303 N TYR D 259
SHEET 4 J 6 ALA D 283 ALA D 289 -1 N ILE D 288 O PHE D 302
SHEET 5 J 6 THR D 266 GLU D 280 -1 N ARG D 273 O ALA D 289
SHEET 6 J 6 PHE D 76 ASP D 77 -1 N PHE D 76 O TRP D 277
SHEET 1 K 6 TRP D 28 ALA D 30 0
SHEET 2 K 6 TYR D 254 TYR D 259 -1 O SER D 256 N ARG D 29
SHEET 3 K 6 TYR D 301 VAL D 305 1 O ARG D 303 N TYR D 259
SHEET 4 K 6 ALA D 283 ALA D 289 -1 N ILE D 288 O PHE D 302
SHEET 5 K 6 THR D 266 GLU D 280 -1 N ARG D 273 O ALA D 289
SHEET 6 K 6 VAL D 241 TYR D 248 -1 N VAL D 247 O GLY D 268
SHEET 1 L 3 THR D 62 VAL D 63 0
SHEET 2 L 3 SER D 220 VAL D 224 1 O ASN D 223 N VAL D 63
SHEET 3 L 3 THR D 318 ARG D 321 -1 O ALA D 319 N TYR D 222
SSBOND 1 CYS A 85 CYS A 114 1555 1555 2.08
SSBOND 2 CYS A 97 CYS A 141 1555 1555 2.06
SSBOND 3 CYS A 133 CYS A 199 1555 1555 2.06
SSBOND 4 CYS A 134 CYS A 137 1555 1555 2.04
SSBOND 5 CYS A 170 CYS A 203 1555 1555 2.04
SSBOND 6 CYS B 85 CYS B 114 1555 1555 2.07
SSBOND 7 CYS B 97 CYS B 141 1555 1555 2.07
SSBOND 8 CYS B 133 CYS B 199 1555 1555 2.05
SSBOND 9 CYS B 134 CYS B 137 1555 1555 2.04
SSBOND 10 CYS B 170 CYS B 203 1555 1555 2.05
SSBOND 11 CYS B 178 CYS B 189 1555 1555 2.04
SSBOND 12 CYS C 85 CYS C 114 1555 1555 2.07
SSBOND 13 CYS C 97 CYS C 141 1555 1555 2.07
SSBOND 14 CYS C 133 CYS C 199 1555 1555 2.04
SSBOND 15 CYS C 134 CYS C 137 1555 1555 2.05
SSBOND 16 CYS C 170 CYS C 203 1555 1555 2.04
SSBOND 17 CYS D 85 CYS D 114 1555 1555 2.04
SSBOND 18 CYS D 97 CYS D 141 1555 1555 2.07
SSBOND 19 CYS D 133 CYS D 199 1555 1555 2.06
SSBOND 20 CYS D 134 CYS D 137 1555 1555 2.06
SSBOND 21 CYS D 170 CYS D 203 1555 1555 2.04
SITE 1 AC1 4 PHE A 76 ASP A 77 LYS A 80 LYS A 81
SITE 1 AC2 7 VAL A 279 ASN A 281 LYS A 282 VAL C 279
SITE 2 AC2 7 GLU C 280 ASN C 281 LYS C 282
SITE 1 AC3 6 ARG B 79 TRP B 82 CYS B 85 LYS B 86
SITE 2 AC3 6 ILE B 88 ALA B 89
SITE 1 AC4 5 ALA B 89 THR B 90 ILE B 91 GLU B 294
SITE 2 AC4 5 HOH B 548
SITE 1 AC5 5 PHE B 76 ASP B 77 LYS B 81 HOH B 579
SITE 2 AC5 5 HOH B 637
SITE 1 AC6 7 VAL B 279 ASN B 281 LYS B 282 VAL D 279
SITE 2 AC6 7 ASN D 281 LYS D 282 HOH D 592
CRYST1 54.281 83.172 84.569 76.97 86.60 71.11 P 1 4
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 0.018423 -0.006304 0.000288 0.00000
SCALE2 0.000000 0.012708 -0.002843 0.00000
SCALE3 0.000000 0.000000 0.012138 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
