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HEADER HYDROLASE 04-AUG-07 2QUB
TITLE CRYSTAL STRUCTURE OF EXTRACELLULAR LIPASE LIPA FROM
TITLE 2 SERRATIA MARCESCENS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXTRACELLULAR LIPASE;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SERRATIA MARCESCENS;
SOURCE 3 STRAIN: SM6;
SOURCE 4 GENE: LIPA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS BETA ROLL, ALPHA/BETA HYDROLASE, HELICAL HAIRPIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.MEIER,U.BAUMANN
REVDAT 1 28-AUG-07 2QUB 0
JRNL AUTH R.MEIER,T.DREPPER,V.SVENSSON,K.E.JAEGER,U.BAUMANN
JRNL TITL A CALCIUM-GATED LID AND A LARGE BETA-ROLL SANDWICH
JRNL TITL 2 ARE REVEALED BY THE CRYSTAL STRUCTURE OF
JRNL TITL 3 EXTRACELLULAR LIPASE FROM SERRATIA MARCESCENS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0036
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 428693
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1275
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 24684
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 29575
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.01000
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): 0.096
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.770
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 28510 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 38334 ; 1.098 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3684 ; 5.149 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1350 ;35.224 ;25.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4122 ;10.553 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 84 ;19.564 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4182 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 22164 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 10765 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 18941 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1681 ; 0.143 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 186 ; 0.069 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 192 ; 0.350 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.158 ; 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): 18834 ; 1.543 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 28554 ; 2.031 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11123 ; 3.258 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 9780 ; 4.693 ; 4.500
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 10 A 600
REMARK 3 ORIGIN FOR THE GROUP (A): -70.2396 -29.8629 23.1603
REMARK 3 T TENSOR
REMARK 3 T11: -0.1055 T22: -0.0628
REMARK 3 T33: -0.0534 T12: 0.0239
REMARK 3 T13: 0.0222 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.3478 L22: 1.4181
REMARK 3 L33: 1.2978 L12: -0.1447
REMARK 3 L13: -0.1749 L23: 0.7864
REMARK 3 S TENSOR
REMARK 3 S11: -0.0377 S12: -0.1996 S13: 0.0275
REMARK 3 S21: 0.1132 S22: -0.0219 S23: 0.2614
REMARK 3 S31: 0.0522 S32: -0.1608 S33: 0.0596
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 : C 10 C 600
REMARK 3 ORIGIN FOR THE GROUP (A): -41.8731 -28.5518 17.4648
REMARK 3 T TENSOR
REMARK 3 T11: -0.1029 T22: -0.1127
REMARK 3 T33: -0.1272 T12: 0.0018
REMARK 3 T13: 0.0062 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 2.0080 L22: 0.7174
REMARK 3 L33: 0.5381 L12: -0.4859
REMARK 3 L13: 0.3264 L23: 0.0810
REMARK 3 S TENSOR
REMARK 3 S11: -0.0446 S12: 0.0285 S13: -0.0028
REMARK 3 S21: 0.0020 S22: 0.0197 S23: -0.0105
REMARK 3 S31: -0.0271 S32: 0.0842 S33: 0.0249
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 : E 10 E 600
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9710 -26.0414 37.3747
REMARK 3 T TENSOR
REMARK 3 T11: -0.0601 T22: 0.0449
REMARK 3 T33: -0.0842 T12: 0.0390
REMARK 3 T13: -0.0457 T23: -0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 2.3277 L22: 2.6807
REMARK 3 L33: 2.6446 L12: -0.1996
REMARK 3 L13: 0.5439 L23: 0.8288
REMARK 3 S TENSOR
REMARK 3 S11: -0.1710 S12: -0.3184 S13: 0.1416
REMARK 3 S21: 0.1319 S22: 0.1368 S23: -0.1802
REMARK 3 S31: -0.1601 S32: 0.0842 S33: 0.0341
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 : G 10 G 600
REMARK 3 ORIGIN FOR THE GROUP (A): -40.3624 10.9015 24.9300
REMARK 3 T TENSOR
REMARK 3 T11: -0.0807 T22: -0.1023
REMARK 3 T33: -0.0983 T12: 0.0208
REMARK 3 T13: -0.0181 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 1.0401 L22: 1.3771
REMARK 3 L33: 1.1322 L12: 0.0864
REMARK 3 L13: -0.4070 L23: -0.4017
REMARK 3 S TENSOR
REMARK 3 S11: -0.0426 S12: -0.1196 S13: -0.1401
REMARK 3 S21: 0.1626 S22: 0.0304 S23: -0.1068
REMARK 3 S31: 0.0585 S32: 0.1531 S33: 0.0123
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 : I 10 I 600
REMARK 3 ORIGIN FOR THE GROUP (A): -55.9930 34.4859 18.7758
REMARK 3 T TENSOR
REMARK 3 T11: -0.1085 T22: -0.1181
REMARK 3 T33: -0.1312 T12: -0.0024
REMARK 3 T13: 0.0064 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.5938 L22: 1.6904
REMARK 3 L33: 0.3256 L12: -0.4194
REMARK 3 L13: -0.0591 L23: 0.0729
REMARK 3 S TENSOR
REMARK 3 S11: -0.0082 S12: 0.0188 S13: 0.0347
REMARK 3 S21: -0.0289 S22: -0.0106 S23: -0.0015
REMARK 3 S31: -0.0375 S32: -0.0171 S33: 0.0187
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 : K 10 K 600
REMARK 3 ORIGIN FOR THE GROUP (A): -68.1736 51.3096 38.0383
REMARK 3 T TENSOR
REMARK 3 T11: -0.0613 T22: -0.0736
REMARK 3 T33: -0.0959 T12: 0.0511
REMARK 3 T13: -0.0155 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 1.5223 L22: 1.5291
REMARK 3 L33: 2.9197 L12: -0.0567
REMARK 3 L13: -0.8193 L23: -0.3487
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: -0.0648 S13: 0.0726
REMARK 3 S21: 0.2029 S22: 0.0356 S23: 0.0573
REMARK 3 S31: -0.1069 S32: -0.1762 S33: -0.0269
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -43.2419 18.4226 82.4395
REMARK 3 T TENSOR
REMARK 3 T11: -0.0711 T22: -0.0724
REMARK 3 T33: -0.0913 T12: 0.0216
REMARK 3 T13: 0.0202 T23: 0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 1.7395 L22: 1.4236
REMARK 3 L33: 1.0219 L12: -0.3836
REMARK 3 L13: 0.5206 L23: 0.3590
REMARK 3 S TENSOR
REMARK 3 S11: 0.0694 S12: 0.2409 S13: 0.1953
REMARK 3 S21: -0.2463 S22: -0.0764 S23: 0.0109
REMARK 3 S31: -0.1994 S32: 0.0080 S33: 0.0070
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -30.4784 -6.9267 88.6137
REMARK 3 T TENSOR
REMARK 3 T11: -0.1246 T22: -0.1119
REMARK 3 T33: -0.1101 T12: 0.0000
REMARK 3 T13: -0.0114 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 2.3604 L22: 1.4798
REMARK 3 L33: 0.3775 L12: -1.2249
REMARK 3 L13: -0.2296 L23: 0.1891
REMARK 3 S TENSOR
REMARK 3 S11: -0.0181 S12: 0.0757 S13: -0.1358
REMARK 3 S21: 0.0649 S22: -0.0092 S23: 0.0341
REMARK 3 S31: 0.0428 S32: 0.0341 S33: 0.0274
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3636 -25.8604 69.3142
REMARK 3 T TENSOR
REMARK 3 T11: -0.0020 T22: 0.1577
REMARK 3 T33: 0.0587 T12: 0.0991
REMARK 3 T13: -0.0217 T23: -0.1900
REMARK 3 L TENSOR
REMARK 3 L11: 2.8085 L22: 2.2973
REMARK 3 L33: 2.7333 L12: 0.2149
REMARK 3 L13: 0.7264 L23: 1.1793
REMARK 3 S TENSOR
REMARK 3 S11: 0.1731 S12: 0.5316 S13: -0.4911
REMARK 3 S21: -0.2223 S22: -0.2602 S23: 0.1454
REMARK 3 S31: 0.1332 S32: -0.1385 S33: 0.0871
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -93.1315 11.6992 84.0175
REMARK 3 T TENSOR
REMARK 3 T11: -0.0812 T22: -0.1050
REMARK 3 T33: -0.0911 T12: 0.0171
REMARK 3 T13: -0.0014 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 1.2239 L22: 1.3308
REMARK 3 L33: 1.1662 L12: -0.0205
REMARK 3 L13: -0.5383 L23: 0.3958
REMARK 3 S TENSOR
REMARK 3 S11: -0.0296 S12: 0.1249 S13: -0.1841
REMARK 3 S21: -0.1466 S22: 0.0096 S23: 0.0549
REMARK 3 S31: 0.0470 S32: -0.1214 S33: 0.0200
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -78.7042 36.1915 90.0420
REMARK 3 T TENSOR
REMARK 3 T11: -0.0997 T22: -0.1097
REMARK 3 T33: -0.1289 T12: 0.0140
REMARK 3 T13: 0.0122 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.5443 L22: 1.9555
REMARK 3 L33: 0.4804 L12: 0.4253
REMARK 3 L13: -0.1319 L23: -0.2324
REMARK 3 S TENSOR
REMARK 3 S11: 0.0175 S12: -0.0294 S13: 0.0224
REMARK 3 S21: 0.0687 S22: -0.0507 S23: -0.0045
REMARK 3 S31: -0.0900 S32: 0.0518 S33: 0.0331
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -67.0936 52.6784 70.3210
REMARK 3 T TENSOR
REMARK 3 T11: -0.0089 T22: -0.0878
REMARK 3 T33: -0.1145 T12: -0.0426
REMARK 3 T13: -0.0111 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 2.3079 L22: 2.0434
REMARK 3 L33: 2.5414 L12: -0.0742
REMARK 3 L13: -0.9388 L23: 0.1133
REMARK 3 S TENSOR
REMARK 3 S11: -0.0293 S12: 0.0016 S13: 0.1372
REMARK 3 S21: -0.1937 S22: 0.0472 S23: -0.0932
REMARK 3 S31: -0.1207 S32: 0.1680 S33: -0.0179
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -91.3226 19.5005 22.5688
REMARK 3 T TENSOR
REMARK 3 T11: -0.1094 T22: -0.0797
REMARK 3 T33: -0.1089 T12: -0.0310
REMARK 3 T13: -0.0061 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.5188 L22: 0.7844
REMARK 3 L33: 1.0907 L12: 0.2050
REMARK 3 L13: 0.7809 L23: 0.0534
REMARK 3 S TENSOR
REMARK 3 S11: 0.0691 S12: -0.1677 S13: 0.0525
REMARK 3 S21: 0.0969 S22: -0.0824 S23: -0.0686
REMARK 3 S31: -0.0541 S32: -0.0279 S33: 0.0133
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -104.5924 -5.5957 16.2833
REMARK 3 T TENSOR
REMARK 3 T11: -0.0975 T22: -0.0921
REMARK 3 T33: -0.1063 T12: -0.0098
REMARK 3 T13: -0.0287 T23: 0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 1.3733 L22: 1.5698
REMARK 3 L33: 0.4711 L12: 0.8892
REMARK 3 L13: -0.1042 L23: -0.0981
REMARK 3 S TENSOR
REMARK 3 S11: 0.0270 S12: -0.0321 S13: -0.0819
REMARK 3 S21: 0.0215 S22: -0.0448 S23: -0.0341
REMARK 3 S31: 0.0548 S32: -0.0288 S33: 0.0178
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -111.5409 -24.8008 35.8930
REMARK 3 T TENSOR
REMARK 3 T11: 0.0504 T22: -0.0406
REMARK 3 T33: -0.0331 T12: -0.0645
REMARK 3 T13: 0.0246 T23: 0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 2.2347 L22: 2.5881
REMARK 3 L33: 3.7590 L12: -0.6429
REMARK 3 L13: 1.1416 L23: -1.5236
REMARK 3 S TENSOR
REMARK 3 S11: 0.0080 S12: -0.2970 S13: -0.2367
REMARK 3 S21: 0.3241 S22: -0.0376 S23: 0.0210
REMARK 3 S31: 0.0103 S32: 0.0483 S33: 0.0295
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -61.7274 -32.0956 81.3605
REMARK 3 T TENSOR
REMARK 3 T11: -0.1110 T22: -0.0852
REMARK 3 T33: -0.0839 T12: -0.0216
REMARK 3 T13: 0.0340 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 1.2874 L22: 1.2034
REMARK 3 L33: 1.2336 L12: 0.4279
REMARK 3 L13: -0.4914 L23: -0.5838
REMARK 3 S TENSOR
REMARK 3 S11: -0.0435 S12: 0.2043 S13: -0.0235
REMARK 3 S21: -0.1226 S22: 0.0551 S23: -0.1550
REMARK 3 S31: 0.0440 S32: 0.0442 S33: -0.0116
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -89.8179 -28.7833 87.4828
REMARK 3 T TENSOR
REMARK 3 T11: -0.0989 T22: -0.0608
REMARK 3 T33: -0.1041 T12: 0.0132
REMARK 3 T13: 0.0186 T23: 0.0490
REMARK 3 L TENSOR
REMARK 3 L11: 2.3861 L22: 0.5521
REMARK 3 L33: 0.4260 L12: 0.5042
REMARK 3 L13: -0.5254 L23: -0.0648
REMARK 3 S TENSOR
REMARK 3 S11: 0.0144 S12: 0.2218 S13: 0.1096
REMARK 3 S21: -0.0098 S22: 0.0264 S23: 0.0545
REMARK 3 S31: -0.0471 S32: -0.1413 S33: -0.0408
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -109.8998 -24.1661 68.0974
REMARK 3 T TENSOR
REMARK 3 T11: 0.0047 T22: 0.3196
REMARK 3 T33: 0.0382 T12: 0.0710
REMARK 3 T13: -0.0473 T23: 0.0839
REMARK 3 L TENSOR
REMARK 3 L11: 1.3367 L22: 1.6371
REMARK 3 L33: 3.5039 L12: -0.0061
REMARK 3 L13: -0.5184 L23: -0.8895
REMARK 3 S TENSOR
REMARK 3 S11: 0.0132 S12: 0.5456 S13: 0.1669
REMARK 3 S21: -0.3020 S22: 0.1272 S23: 0.1873
REMARK 3 S31: -0.2087 S32: -0.5159 S33: -0.1404
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QUB COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB044064.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 430068
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 24.000
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : 0.06600
REMARK 200 FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33500
REMARK 200 R SYM FOR SHELL (I) : 0.33500
REMARK 200 FOR SHELL : 2.600
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% MPD, 0.1M NA-ACETATE, PH 4.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 281K, PH 4.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 2/3+X,1/3+Y,1/3+Z
REMARK 290 5555 2/3-Y,1/3+X-Y,1/3+Z
REMARK 290 6555 2/3-X+Y,1/3-X,1/3+Z
REMARK 290 7555 1/3+X,2/3+Y,2/3+Z
REMARK 290 8555 1/3-Y,2/3+X-Y,2/3+Z
REMARK 290 9555 1/3-X+Y,2/3-X,2/3+Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 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 101.20050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 58.42814
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 105.91033
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 101.20050
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 58.42814
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 105.91033
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 101.20050
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 58.42814
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 105.91033
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 116.85627
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 211.82067
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 116.85627
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 211.82067
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 116.85627
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 211.82067
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: MONOMER
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: MONOMER
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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
REMARK 500 NE2 GLN G 420 O HOH G 916 1.97
REMARK 500 OE2 GLU G 364 O HOH G 924 2.03
REMARK 500 O HOH G 821 O HOH G 967 2.03
REMARK 500 O HOH I 785 O HOH I 926 2.04
REMARK 500 O HOH A 796 O HOH A 908 2.06
REMARK 500 OE1 GLN C 420 O HOH C 899 2.12
REMARK 500 O HOH K 826 O HOH K 842 2.12
REMARK 500 OE1 GLN E 420 O HOH E 853 2.14
REMARK 500 NH2 ARG K 438 OG1 THR K 524 2.15
REMARK 500 CE LYS C 424 O HOH C 839 2.16
REMARK 500 OH TYR E 555 O HOH E 857 2.16
REMARK 500 OE2 GLU A 364 O HOH A 942 2.18
REMARK 500 O HOH G 714 O HOH G 736 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CD1 LEU C 461 O HOH K 768 9444 1.05
REMARK 500 CG LEU C 461 O HOH K 768 9444 2.07
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 NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 157 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP C 157 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP E 157 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP E 397 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP G 157 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP I 157 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP K 157 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP K 397 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 7 -130.58 44.99
REMARK 500 SER A 144 177.48 126.37
REMARK 500 SER A 207 -120.65 68.95
REMARK 500 ARG A 393 -156.86 56.98
REMARK 500 ASN A 433 -43.96 -138.44
REMARK 500 ASN A 509 -153.30 59.47
REMARK 500 ASN A 583 -127.18 59.77
REMARK 500 LYS C 7 -130.48 45.97
REMARK 500 SER C 60 -164.87 -160.75
REMARK 500 GLU C 130 -14.37 157.39
REMARK 500 SER C 144 176.86 124.56
REMARK 500 SER C 207 -121.46 68.74
REMARK 500 ARG C 393 -157.43 56.53
REMARK 500 ASN C 433 -43.44 -137.44
REMARK 500 LEU C 461 -47.32 71.57
REMARK 500 ASN C 509 -157.05 59.25
REMARK 500 ASN C 583 -128.81 54.04
REMARK 500 LYS E 7 -125.13 45.34
REMARK 500 GLU E 130 -9.48 178.82
REMARK 500 SER E 144 175.77 119.19
REMARK 500 SER E 207 -120.02 67.68
REMARK 500 SER E 304 146.49 -170.29
REMARK 500 ARG E 393 -156.13 58.18
REMARK 500 ASN E 433 -40.91 -138.11
REMARK 500 LEU E 461 -58.70 82.83
REMARK 500 ASN E 509 -153.86 58.63
REMARK 500 ASN E 583 -134.57 53.95
REMARK 500 LYS G 7 -126.52 46.61
REMARK 500 GLU G 130 -13.62 131.99
REMARK 500 SER G 144 176.48 121.05
REMARK 500 SER G 207 -121.94 67.29
REMARK 500 SER G 304 142.87 -170.59
REMARK 500 ARG G 393 -155.44 59.01
REMARK 500 ASN G 433 -43.35 -137.35
REMARK 500 ASN G 509 -152.64 57.64
REMARK 500 ASN G 583 -128.79 54.91
REMARK 500 LYS I 7 -124.52 49.46
REMARK 500 SER I 60 -159.09 -161.27
REMARK 500 SER I 144 176.84 129.80
REMARK 500 SER I 207 -119.71 70.36
REMARK 500 ARG I 393 -156.17 58.56
REMARK 500 ASN I 433 -38.74 -140.14
REMARK 500 LEU I 461 18.88 1.98
REMARK 500 ASN I 509 -151.21 57.80
REMARK 500 ASN I 583 -123.97 58.53
REMARK 500 LYS K 7 -128.02 46.47
REMARK 500 GLU K 130 -5.40 142.85
REMARK 500 SER K 144 176.53 121.10
REMARK 500 SER K 207 -121.43 67.71
REMARK 500 ARG K 393 -159.19 58.31
REMARK 500 GLN K 420 19.99 58.80
REMARK 500 ASN K 433 -44.66 -134.38
REMARK 500 LEU K 461 -49.37 75.42
REMARK 500 ASN K 509 -154.18 59.64
REMARK 500 ALA K 510 -177.51 -57.84
REMARK 500 SER K 529 -176.55 -61.82
REMARK 500 ALA K 559 -18.10 -49.88
REMARK 500 GLN K 582 77.18 -115.89
REMARK 500 ASN K 583 -118.60 72.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 621 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 118 O
REMARK 620 2 GLN A 120 OE1 76.4
REMARK 620 3 SER A 144 O 161.0 86.1
REMARK 620 4 ASP A 153 OD2 90.6 91.2 82.3
REMARK 620 5 ASP A 157 OD1 75.7 150.0 122.8 100.0
REMARK 620 6 ASP A 157 OD2 128.2 155.3 69.8 90.8 53.1
REMARK 620 7 HOH A 678 O 98.6 86.2 87.4 169.5 87.1 87.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 620 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 254 OE1
REMARK 620 2 ASP A 276 OD1 99.0
REMARK 620 3 ASP A 276 OD2 97.8 54.3
REMARK 620 4 ASN A 284 O 85.1 84.6 138.8
REMARK 620 5 ASN A 285 OD1 97.4 152.5 144.0 74.9
REMARK 620 6 HOH A 625 O 173.3 75.7 82.4 90.3 86.1
REMARK 620 7 HOH A 638 O 94.6 128.2 74.5 146.5 71.9 91.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 619 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 375 O
REMARK 620 2 GLY A 377 O 89.9
REMARK 620 3 ASP A 379 OD2 78.3 89.6
REMARK 620 4 GLY A 392 O 81.5 171.0 90.9
REMARK 620 5 ASP A 394 O 85.8 81.2 161.7 95.8
REMARK 620 6 ASP A 397 OD1 157.0 81.4 80.4 107.5 113.5
REMARK 620 7 ASP A 397 OD2 147.8 118.1 114.9 69.6 83.4 51.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 617 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 384 O
REMARK 620 2 GLY A 386 O 90.9
REMARK 620 3 ASP A 388 OD2 84.8 74.9
REMARK 620 4 ASP A 401 OD1 95.6 157.6 84.4
REMARK 620 5 ASP A 401 OD2 88.9 148.2 136.6 53.6
REMARK 620 6 GLY A 403 O 91.1 78.8 153.3 122.4 69.5
REMARK 620 7 ASN A 406 OD1 177.7 91.3 95.1 82.1 89.6 90.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 618 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 393 O
REMARK 620 2 GLY A 395 O 110.9
REMARK 620 3 ASP A 397 OD2 80.8 82.1
REMARK 620 4 GLY A 410 O 85.2 163.9 101.8
REMARK 620 5 LYS A 412 O 93.3 80.4 158.2 98.5
REMARK 620 6 ASN A 415 OD1 165.1 83.3 97.4 80.7 93.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 614 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 491 O
REMARK 620 2 GLY A 493 O 96.7
REMARK 620 3 ASP A 495 OD2 84.3 83.4
REMARK 620 4 GLY A 508 O 89.0 171.2 90.6
REMARK 620 5 ALA A 510 O 78.9 86.8 159.4 100.8
REMARK 620 6 ASP A 513 OD1 170.8 79.6 87.0 93.7 109.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 616 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 509 O
REMARK 620 2 GLY A 511 O 108.1
REMARK 620 3 ASP A 513 OD2 83.0 81.4
REMARK 620 4 GLY A 527 O 81.4 169.3 95.3
REMARK 620 5 SER A 529 O 86.0 85.5 159.2 100.4
REMARK 620 6 ASP A 532 OD1 159.3 81.3 80.2 88.1 113.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 615 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 528 O
REMARK 620 2 GLY A 530 O 101.3
REMARK 620 3 ASP A 532 OD2 85.9 82.9
REMARK 620 4 PHE A 549 O 87.2 87.4 166.7
REMARK 620 5 ASP A 552 OD1 166.7 91.1 91.1 98.2
REMARK 620 6 HOH A 705 O 80.8 176.8 94.9 95.1 86.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 621 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 118 O
REMARK 620 2 GLN C 120 OE1 75.1
REMARK 620 3 SER C 144 O 161.4 87.5
REMARK 620 4 ASP C 153 OD2 89.4 88.3 83.5
REMARK 620 5 ASP C 157 OD1 74.1 147.7 124.1 100.7
REMARK 620 6 ASP C 157 OD2 127.1 157.8 70.7 93.4 53.4
REMARK 620 7 HOH C 633 O 97.6 89.0 88.4 171.6 85.7 86.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 620 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 254 OE1
REMARK 620 2 ASP C 276 OD1 98.3
REMARK 620 3 ASP C 276 OD2 95.8 53.9
REMARK 620 4 ASN C 284 O 85.5 84.8 138.5
REMARK 620 5 ASN C 285 OD1 99.2 152.0 144.5 75.0
REMARK 620 6 HOH C 654 O 93.5 127.8 74.4 147.1 72.7
REMARK 620 7 HOH C 643 O 173.8 76.8 84.4 90.3 84.0 92.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 619 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 375 O
REMARK 620 2 GLY C 377 O 90.1
REMARK 620 3 ASP C 379 OD2 80.2 88.4
REMARK 620 4 GLY C 392 O 81.7 171.8 90.7
REMARK 620 5 ASP C 394 O 83.5 83.0 161.5 95.5
REMARK 620 6 ASP C 397 OD1 160.2 81.7 81.6 106.3 113.1
REMARK 620 7 ASP C 397 OD2 145.8 119.7 114.4 68.0 84.0 51.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 617 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 384 O
REMARK 620 2 GLY C 386 O 90.5
REMARK 620 3 ASP C 388 OD2 85.7 75.5
REMARK 620 4 ASP C 401 OD1 97.6 158.8 85.7
REMARK 620 5 ASP C 401 OD2 90.0 146.8 137.7 53.2
REMARK 620 6 GLY C 403 O 90.8 77.5 152.6 121.7 69.3
REMARK 620 7 ASN C 406 OD1 178.8 90.5 94.0 81.2 89.5 90.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 618 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG C 393 O
REMARK 620 2 GLY C 395 O 109.4
REMARK 620 3 ASP C 397 OD2 81.2 80.5
REMARK 620 4 GLY C 410 O 85.8 164.8 101.4
REMARK 620 5 LYS C 412 O 94.3 82.4 159.7 98.0
REMARK 620 6 ASN C 415 OD1 165.4 84.4 97.2 80.3 92.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 614 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 491 O
REMARK 620 2 GLY C 493 O 95.4
REMARK 620 3 ASP C 495 OD2 84.6 83.2
REMARK 620 4 GLY C 508 O 88.4 174.1 92.7
REMARK 620 5 ALA C 510 O 82.7 86.9 163.1 98.0
REMARK 620 6 ASP C 513 OD1 170.2 82.7 85.6 92.8 106.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 616 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 509 O
REMARK 620 2 GLY C 511 O 106.7
REMARK 620 3 ASP C 513 OD2 80.6 84.2
REMARK 620 4 GLY C 527 O 82.9 170.3 96.5
REMARK 620 5 SER C 529 O 87.5 82.0 158.4 99.8
REMARK 620 6 ASP C 532 OD1 156.3 82.9 78.9 87.8 115.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 615 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 528 O
REMARK 620 2 GLY C 530 O 101.1
REMARK 620 3 ASP C 532 OD2 87.7 83.6
REMARK 620 4 PHE C 549 O 89.0 86.6 168.9
REMARK 620 5 ASP C 552 OD1 163.1 94.7 88.2 97.9
REMARK 620 6 HOH C 751 O 80.2 178.6 95.8 94.0 83.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 621 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 118 O
REMARK 620 2 GLN E 120 OE1 74.9
REMARK 620 3 SER E 144 O 161.5 87.3
REMARK 620 4 ASP E 153 OD2 92.8 92.3 82.7
REMARK 620 5 ASP E 157 OD1 75.0 148.0 123.4 100.0
REMARK 620 6 ASP E 157 OD2 128.1 156.7 70.1 90.6 53.4
REMARK 620 7 HOH E 653 O 95.7 83.7 87.1 169.3 88.5 89.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 620 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 254 OE1
REMARK 620 2 ASP E 276 OD1 97.1
REMARK 620 3 ASP E 276 OD2 96.3 54.5
REMARK 620 4 ASN E 284 O 86.2 84.5 138.9
REMARK 620 5 ASN E 285 OD1 98.8 151.7 145.2 73.5
REMARK 620 6 HOH E 624 O 173.1 77.0 83.3 89.6 85.2
REMARK 620 7 HOH E 625 O 93.8 128.6 74.5 146.5 73.4 92.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 619 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER E 375 O
REMARK 620 2 GLY E 377 O 90.0
REMARK 620 3 ASP E 379 OD2 80.1 89.9
REMARK 620 4 GLY E 392 O 81.0 171.0 89.8
REMARK 620 5 ASP E 394 O 84.9 82.0 162.9 95.8
REMARK 620 6 ASP E 397 OD1 160.4 82.6 81.8 106.3 111.7
REMARK 620 7 ASP E 397 OD2 145.2 119.8 114.8 68.3 82.3 51.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 617 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY E 384 O
REMARK 620 2 GLY E 386 O 90.4
REMARK 620 3 ASP E 388 OD2 85.4 80.2
REMARK 620 4 ASP E 401 OD1 99.1 159.0 82.0
REMARK 620 5 ASP E 401 OD2 91.6 145.6 134.2 53.3
REMARK 620 6 GLY E 403 O 91.3 77.0 156.9 121.0 68.6
REMARK 620 7 ASN E 406 OD1 179.0 90.1 95.5 80.6 87.5 88.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 618 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG E 393 O
REMARK 620 2 GLY E 395 O 110.4
REMARK 620 3 ASP E 397 OD2 80.8 82.7
REMARK 620 4 GLY E 410 O 84.7 164.8 102.0
REMARK 620 5 LYS E 412 O 93.3 79.4 157.8 98.7
REMARK 620 6 ASN E 415 OD1 162.9 86.5 99.8 78.5 92.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 614 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY E 491 O
REMARK 620 2 GLY E 493 O 94.2
REMARK 620 3 ASP E 495 OD2 83.0 78.6
REMARK 620 4 GLY E 508 O 92.0 172.4 97.7
REMARK 620 5 ALA E 510 O 75.5 85.5 152.2 100.4
REMARK 620 6 ASP E 513 OD1 169.6 77.3 89.5 96.1 109.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 616 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN E 509 O
REMARK 620 2 GLY E 511 O 110.1
REMARK 620 3 ASP E 513 OD2 80.8 82.3
REMARK 620 4 GLY E 527 O 80.1 169.7 98.5
REMARK 620 5 SER E 529 O 85.0 82.0 153.7 100.8
REMARK 620 6 ASP E 532 OD1 161.0 77.9 83.4 91.9 113.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 615 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY E 528 O
REMARK 620 2 GLY E 530 O 95.3
REMARK 620 3 ASP E 532 OD2 86.5 80.3
REMARK 620 4 PHE E 549 O 86.7 80.4 158.9
REMARK 620 5 ASP E 552 OD1 174.9 88.7 91.1 97.1
REMARK 620 6 HOH E 756 O 80.4 175.8 99.0 99.5 95.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 621 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 118 O
REMARK 620 2 GLN G 120 OE1 77.2
REMARK 620 3 SER G 144 O 162.2 85.9
REMARK 620 4 ASP G 153 OD2 92.9 90.7 81.9
REMARK 620 5 ASP G 157 OD1 72.8 148.0 124.8 101.5
REMARK 620 6 ASP G 157 OD2 125.0 157.4 72.4 92.4 52.5
REMARK 620 7 HOH G 630 O 95.4 85.9 88.6 170.2 86.0 87.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 620 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 254 OE1
REMARK 620 2 ASP G 276 OD1 98.4
REMARK 620 3 ASP G 276 OD2 96.6 53.8
REMARK 620 4 ASN G 284 O 85.9 85.0 138.8
REMARK 620 5 ASN G 285 OD1 98.5 151.4 145.5 73.4
REMARK 620 6 HOH G 624 O 174.5 77.5 84.1 90.0 83.8
REMARK 620 7 HOH G 650 O 92.3 128.1 74.6 146.6 74.0 93.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 619 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER G 375 O
REMARK 620 2 GLY G 377 O 89.9
REMARK 620 3 ASP G 379 OD2 77.0 88.5
REMARK 620 4 GLY G 392 O 79.2 169.0 87.7
REMARK 620 5 ASP G 394 O 84.6 82.6 159.5 97.6
REMARK 620 6 ASP G 397 OD1 156.6 81.2 81.2 108.3 115.3
REMARK 620 7 ASP G 397 OD2 147.2 119.1 115.9 71.7 84.4 52.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 617 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY G 384 O
REMARK 620 2 GLY G 386 O 90.7
REMARK 620 3 ASP G 388 OD2 82.9 78.7
REMARK 620 4 ASP G 401 OD1 96.2 158.8 82.2
REMARK 620 5 ASP G 401 OD2 90.3 146.5 134.5 53.8
REMARK 620 6 GLY G 403 O 90.7 77.8 155.6 122.0 68.7
REMARK 620 7 ASN G 406 OD1 177.8 90.9 95.9 81.9 89.3 91.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 618 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG G 393 O
REMARK 620 2 GLY G 395 O 110.5
REMARK 620 3 ASP G 397 OD2 81.9 81.4
REMARK 620 4 GLY G 410 O 84.8 164.7 101.9
REMARK 620 5 LYS G 412 O 92.5 78.8 156.1 100.7
REMARK 620 6 ASN G 415 OD1 164.5 84.3 96.5 80.5 94.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 614 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY G 491 O
REMARK 620 2 GLY G 493 O 98.0
REMARK 620 3 ASP G 495 OD2 84.6 81.1
REMARK 620 4 GLY G 508 O 89.7 171.3 95.6
REMARK 620 5 ALA G 510 O 82.1 87.6 161.1 97.6
REMARK 620 6 ASP G 513 OD1 172.1 81.5 87.5 90.3 105.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 616 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN G 509 O
REMARK 620 2 GLY G 511 O 105.1
REMARK 620 3 ASP G 513 OD2 80.9 80.7
REMARK 620 4 GLY G 527 O 81.7 172.1 96.7
REMARK 620 5 SER G 529 O 82.4 83.7 153.3 101.4
REMARK 620 6 ASP G 532 OD1 159.6 79.1 80.1 93.1 118.0
REMARK 620 7 ASP G 532 OD2 138.7 110.2 125.0 65.1 80.8 52.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 615 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY G 528 O
REMARK 620 2 GLY G 530 O 101.5
REMARK 620 3 ASP G 532 OD2 79.8 84.7
REMARK 620 4 PHE G 549 O 88.9 84.0 162.1
REMARK 620 5 ASP G 552 OD1 164.1 94.4 101.6 93.1
REMARK 620 6 HOH G 642 O 78.9 176.0 99.3 92.1 85.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 621 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR I 118 O
REMARK 620 2 GLN I 120 OE1 78.9
REMARK 620 3 SER I 144 O 162.6 84.7
REMARK 620 4 ASP I 153 OD2 93.4 95.0 82.2
REMARK 620 5 ASP I 157 OD1 72.4 149.5 124.7 96.9
REMARK 620 6 ASP I 157 OD2 124.8 156.2 71.9 86.0 53.0
REMARK 620 7 HOH I 631 O 98.0 88.6 87.2 168.5 85.2 86.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 620 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU I 254 OE1
REMARK 620 2 ASP I 276 OD1 99.0
REMARK 620 3 ASP I 276 OD2 94.8 54.8
REMARK 620 4 ASN I 284 O 86.8 83.2 137.8
REMARK 620 5 ASN I 285 OD1 100.6 151.2 142.9 77.0
REMARK 620 6 HOH I 622 O 95.1 128.5 74.9 147.1 70.4
REMARK 620 7 HOH I 624 O 173.7 75.4 84.3 89.7 83.7 90.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 619 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER I 375 O
REMARK 620 2 GLY I 377 O 89.3
REMARK 620 3 ASP I 379 OD2 77.9 89.7
REMARK 620 4 GLY I 392 O 79.6 168.8 89.5
REMARK 620 5 ASP I 394 O 87.4 82.9 163.6 94.8
REMARK 620 6 ASP I 397 OD1 156.9 81.5 80.9 109.4 112.3
REMARK 620 7 ASP I 397 OD2 148.3 117.4 116.4 72.7 80.0 52.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 617 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY I 384 O
REMARK 620 2 GLY I 386 O 89.6
REMARK 620 3 ASP I 388 OD2 83.7 74.9
REMARK 620 4 ASP I 401 OD1 93.8 157.6 83.5
REMARK 620 5 ASP I 401 OD2 89.2 148.4 136.2 53.9
REMARK 620 6 GLY I 403 O 91.6 78.0 152.5 124.0 70.5
REMARK 620 7 ASN I 406 OD1 176.8 91.0 93.4 84.5 91.9 91.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 618 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG I 393 O
REMARK 620 2 GLY I 395 O 110.8
REMARK 620 3 ASP I 397 OD2 82.4 79.0
REMARK 620 4 GLY I 410 O 83.8 165.4 105.6
REMARK 620 5 LYS I 412 O 94.1 80.4 156.4 97.2
REMARK 620 6 ASN I 415 OD1 164.2 84.8 98.7 80.8 91.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 614 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY I 491 O
REMARK 620 2 GLY I 493 O 91.6
REMARK 620 3 ASP I 495 OD2 84.6 84.9
REMARK 620 4 GLY I 508 O 92.9 175.4 94.7
REMARK 620 5 ALA I 510 O 82.3 85.5 163.5 96.0
REMARK 620 6 ASP I 513 OD1 172.1 81.0 92.0 94.4 99.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 616 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN I 509 O
REMARK 620 2 GLY I 511 O 103.3
REMARK 620 3 ASP I 513 OD2 80.3 81.0
REMARK 620 4 GLY I 527 O 82.6 172.7 96.0
REMARK 620 5 SER I 529 O 83.8 83.5 154.6 101.6
REMARK 620 6 ASP I 532 OD1 156.2 80.1 77.0 92.7 120.0
REMARK 620 7 ASP I 532 OD2 139.5 111.3 124.7 65.0 79.8 54.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 615 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY I 528 O
REMARK 620 2 GLY I 530 O 103.8
REMARK 620 3 ASP I 532 OD2 79.9 81.1
REMARK 620 4 PHE I 549 O 86.0 86.2 158.1
REMARK 620 5 ASP I 552 OD1 164.7 91.5 102.8 95.3
REMARK 620 6 HOH I 847 O 80.5 175.6 101.0 93.0 84.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA K 621 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR K 118 O
REMARK 620 2 GLN K 120 OE1 75.9
REMARK 620 3 SER K 144 O 160.3 85.1
REMARK 620 4 ASP K 153 OD2 93.3 92.5 82.3
REMARK 620 5 ASP K 157 OD1 73.3 147.1 126.3 100.4
REMARK 620 6 ASP K 157 OD2 126.2 157.6 73.2 90.3 53.3
REMARK 620 7 HOH K 641 O 96.2 85.8 87.3 169.6 86.4 87.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA K 620 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU K 254 OE1
REMARK 620 2 ASP K 276 OD1 98.0
REMARK 620 3 ASP K 276 OD2 94.9 54.7
REMARK 620 4 ASN K 284 O 86.5 83.7 138.2
REMARK 620 5 ASN K 285 OD1 97.6 152.5 145.5 74.8
REMARK 620 6 HOH K 662 O 175.6 78.5 85.2 90.5 84.6
REMARK 620 7 HOH K 637 O 92.6 130.1 76.0 145.8 71.5 91.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA K 619 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER K 375 O
REMARK 620 2 GLY K 377 O 89.6
REMARK 620 3 ASP K 379 OD2 79.4 88.2
REMARK 620 4 GLY K 392 O 80.8 170.3 91.8
REMARK 620 5 ASP K 394 O 82.9 83.2 160.4 93.8
REMARK 620 6 ASP K 397 OD1 158.4 81.8 80.6 107.8 115.4
REMARK 620 7 ASP K 397 OD2 147.2 117.4 117.1 71.1 82.5 52.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA K 617 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY K 384 O
REMARK 620 2 GLY K 386 O 93.3
REMARK 620 3 ASP K 388 OD2 84.9 77.2
REMARK 620 4 ASP K 401 OD1 96.7 157.1 83.2
REMARK 620 5 ASP K 401 OD2 89.0 147.5 135.3 53.6
REMARK 620 6 GLY K 403 O 92.2 79.3 156.1 120.7 68.2
REMARK 620 7 ASN K 406 OD1 176.5 89.3 93.3 80.0 90.1 90.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA K 618 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG K 393 O
REMARK 620 2 GLY K 395 O 109.4
REMARK 620 3 ASP K 397 OD2 80.7 78.7
REMARK 620 4 GLY K 410 O 84.8 165.8 105.7
REMARK 620 5 LYS K 412 O 93.6 80.1 154.7 98.2
REMARK 620 6 ASN K 415 OD1 164.8 85.1 98.4 80.9 93.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA K 614 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY K 491 O
REMARK 620 2 GLY K 493 O 75.3
REMARK 620 3 ASP K 495 OD2 68.8 73.0
REMARK 620 4 GLY K 508 O 97.7 165.0 92.2
REMARK 620 5 ALA K 510 O 100.0 101.4 168.3 92.8
REMARK 620 6 ASP K 513 OD1 149.0 82.1 84.6 98.9 105.1
REMARK 620 7 ASP K 513 OD2 155.1 118.3 133.4 73.3 58.3 55.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA K 616 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN K 509 O
REMARK 620 2 GLY K 511 O 106.6
REMARK 620 3 ASP K 513 OD2 69.3 71.3
REMARK 620 4 GLY K 527 O 73.3 169.5 99.3
REMARK 620 5 SER K 529 O 98.0 94.1 155.8 96.3
REMARK 620 6 ASP K 532 OD1 151.4 76.6 85.6 98.4 110.3
REMARK 620 7 ASP K 532 OD2 139.6 110.9 137.4 72.5 65.3 55.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA K 615 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY K 528 O
REMARK 620 2 GLY K 530 O 101.5
REMARK 620 3 ASP K 532 OD2 78.4 76.3
REMARK 620 4 PHE K 549 O 89.1 89.0 158.2
REMARK 620 5 ASP K 552 OD1 164.8 92.5 99.5 97.1
REMARK 620 6 HOH K 781 O 78.6 178.1 101.9 92.9 87.2
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QUA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LIPA FROM SERRATIA MARCESCENS. SPACE
REMARK 900 GROUP P321
DBREF 2QUB A 1 613 UNP Q59933 Q59933_SERMA 1 613
DBREF 2QUB C 1 613 UNP Q59933 Q59933_SERMA 1 613
DBREF 2QUB E 1 613 UNP Q59933 Q59933_SERMA 1 613
DBREF 2QUB G 1 613 UNP Q59933 Q59933_SERMA 1 613
DBREF 2QUB I 1 613 UNP Q59933 Q59933_SERMA 1 613
DBREF 2QUB K 1 613 UNP Q59933 Q59933_SERMA 1 613
SEQADV 2QUB SER A -1 UNP Q59933 EXPRESSION TAG
SEQADV 2QUB HIS A 0 UNP Q59933 EXPRESSION TAG
SEQADV 2QUB SER C -1 UNP Q59933 EXPRESSION TAG
SEQADV 2QUB HIS C 0 UNP Q59933 EXPRESSION TAG
SEQADV 2QUB SER E -1 UNP Q59933 EXPRESSION TAG
SEQADV 2QUB HIS E 0 UNP Q59933 EXPRESSION TAG
SEQADV 2QUB SER G -1 UNP Q59933 EXPRESSION TAG
SEQADV 2QUB HIS G 0 UNP Q59933 EXPRESSION TAG
SEQADV 2QUB SER I -1 UNP Q59933 EXPRESSION TAG
SEQADV 2QUB HIS I 0 UNP Q59933 EXPRESSION TAG
SEQADV 2QUB SER K -1 UNP Q59933 EXPRESSION TAG
SEQADV 2QUB HIS K 0 UNP Q59933 EXPRESSION TAG
SEQRES 1 A 615 SER HIS MET GLY ILE PHE SER TYR LYS ASP LEU ASP GLU
SEQRES 2 A 615 ASN ALA SER LYS ALA LEU PHE SER ASP ALA LEU ALA ILE
SEQRES 3 A 615 SER THR TYR ALA TYR HIS ASN ILE ASP ASN GLY PHE ASP
SEQRES 4 A 615 GLU GLY TYR HIS GLN THR GLY PHE GLY LEU GLY LEU PRO
SEQRES 5 A 615 LEU THR LEU ILE THR ALA LEU ILE GLY SER THR GLN SER
SEQRES 6 A 615 GLN GLY GLY LEU PRO GLY LEU PRO TRP ASN PRO ASP SER
SEQRES 7 A 615 GLU GLN ALA ALA GLN GLU ALA VAL ASN ASN ALA GLY TRP
SEQRES 8 A 615 SER VAL ILE SER ALA THR GLN LEU GLY TYR ALA GLY LYS
SEQRES 9 A 615 THR ASP ALA ARG GLY THR TYR TYR GLY GLU THR ALA GLY
SEQRES 10 A 615 TYR THR THR ALA GLN ALA GLU VAL LEU GLY LYS TYR ASP
SEQRES 11 A 615 SER GLU GLY ASN LEU THR ALA ILE GLY ILE SER PHE ARG
SEQRES 12 A 615 GLY THR SER GLY PRO ARG GLU SER LEU ILE GLY ASP THR
SEQRES 13 A 615 ILE GLY ASP VAL ILE ASN ASP LEU LEU ALA GLY PHE GLY
SEQRES 14 A 615 PRO LYS GLY TYR ALA ASP GLY TYR THR LEU LYS ALA PHE
SEQRES 15 A 615 GLY ASN LEU LEU GLY ASP VAL ALA LYS PHE ALA GLN ALA
SEQRES 16 A 615 HIS GLY LEU SER GLY GLU ASP VAL VAL VAL SER GLY HIS
SEQRES 17 A 615 SER LEU GLY GLY LEU ALA VAL ASN SER MET ALA ALA GLN
SEQRES 18 A 615 SER ASP ALA ASN TRP GLY GLY PHE TYR ALA GLN SER ASN
SEQRES 19 A 615 TYR VAL ALA PHE ALA SER PRO THR GLN TYR GLU ALA GLY
SEQRES 20 A 615 GLY LYS VAL ILE ASN ILE GLY TYR GLU ASN ASP PRO VAL
SEQRES 21 A 615 PHE ARG ALA LEU ASP GLY THR SER LEU THR LEU PRO SER
SEQRES 22 A 615 LEU GLY VAL HIS ASP ALA PRO HIS THR SER ALA THR ASN
SEQRES 23 A 615 ASN ILE VAL ASN PHE ASN ASP HIS TYR ALA SER ASP ALA
SEQRES 24 A 615 TRP ASN LEU LEU PRO PHE SER ILE LEU ASN ILE PRO THR
SEQRES 25 A 615 TRP LEU SER HIS LEU PRO PHE PHE TYR GLN ASP GLY LEU
SEQRES 26 A 615 MET ARG VAL LEU ASN SER GLU PHE TYR SER LEU THR ASP
SEQRES 27 A 615 LYS ASP SER THR ILE ILE VAL SER ASN LEU SER ASN VAL
SEQRES 28 A 615 THR ARG GLY ASN THR TRP VAL GLU ASP LEU ASN ARG ASN
SEQRES 29 A 615 ALA GLU THR HIS SER GLY PRO THR PHE ILE ILE GLY SER
SEQRES 30 A 615 ASP GLY ASN ASP LEU ILE LYS GLY GLY LYS GLY ASN ASP
SEQRES 31 A 615 TYR LEU GLU GLY ARG ASP GLY ASP ASP ILE PHE ARG ASP
SEQRES 32 A 615 ALA GLY GLY TYR ASN LEU ILE ALA GLY GLY LYS GLY HIS
SEQRES 33 A 615 ASN ILE PHE ASP THR GLN GLN ALA LEU LYS ASN THR GLU
SEQRES 34 A 615 VAL ALA TYR ASP GLY ASN THR LEU TYR LEU ARG ASP ALA
SEQRES 35 A 615 LYS GLY GLY ILE THR LEU ALA ASP ASP ILE SER THR LEU
SEQRES 36 A 615 ARG SER LYS GLU THR SER TRP LEU ILE PHE ASN LYS GLU
SEQRES 37 A 615 VAL ASP HIS GLN VAL THR ALA ALA GLY LEU LYS SER ASP
SEQRES 38 A 615 SER GLY LEU LYS ALA TYR ALA ALA ALA THR GLY GLY ASP
SEQRES 39 A 615 GLY ASP ASP VAL LEU GLN ALA ARG SER HIS ASP ALA TRP
SEQRES 40 A 615 LEU PHE GLY ASN ALA GLY ASN ASP THR LEU ILE GLY HIS
SEQRES 41 A 615 ALA GLY GLY ASN LEU THR PHE VAL GLY GLY SER GLY ASP
SEQRES 42 A 615 ASP ILE LEU LYS GLY VAL GLY ASN GLY ASN THR PHE LEU
SEQRES 43 A 615 PHE SER GLY ASP PHE GLY ARG ASP GLN LEU TYR GLY PHE
SEQRES 44 A 615 ASN ALA SER ASP LYS LEU VAL PHE ILE GLY THR GLU GLY
SEQRES 45 A 615 ALA SER GLY ASN ILE ARG ASP TYR ALA THR GLN GLN ASN
SEQRES 46 A 615 ASP ASP LEU VAL LEU ALA PHE GLY HIS SER GLN VAL THR
SEQRES 47 A 615 LEU ILE GLY VAL SER LEU ASP HIS ILE SER THR ASP GLN
SEQRES 48 A 615 VAL VAL LEU ALA
SEQRES 1 C 615 SER HIS MET GLY ILE PHE SER TYR LYS ASP LEU ASP GLU
SEQRES 2 C 615 ASN ALA SER LYS ALA LEU PHE SER ASP ALA LEU ALA ILE
SEQRES 3 C 615 SER THR TYR ALA TYR HIS ASN ILE ASP ASN GLY PHE ASP
SEQRES 4 C 615 GLU GLY TYR HIS GLN THR GLY PHE GLY LEU GLY LEU PRO
SEQRES 5 C 615 LEU THR LEU ILE THR ALA LEU ILE GLY SER THR GLN SER
SEQRES 6 C 615 GLN GLY GLY LEU PRO GLY LEU PRO TRP ASN PRO ASP SER
SEQRES 7 C 615 GLU GLN ALA ALA GLN GLU ALA VAL ASN ASN ALA GLY TRP
SEQRES 8 C 615 SER VAL ILE SER ALA THR GLN LEU GLY TYR ALA GLY LYS
SEQRES 9 C 615 THR ASP ALA ARG GLY THR TYR TYR GLY GLU THR ALA GLY
SEQRES 10 C 615 TYR THR THR ALA GLN ALA GLU VAL LEU GLY LYS TYR ASP
SEQRES 11 C 615 SER GLU GLY ASN LEU THR ALA ILE GLY ILE SER PHE ARG
SEQRES 12 C 615 GLY THR SER GLY PRO ARG GLU SER LEU ILE GLY ASP THR
SEQRES 13 C 615 ILE GLY ASP VAL ILE ASN ASP LEU LEU ALA GLY PHE GLY
SEQRES 14 C 615 PRO LYS GLY TYR ALA ASP GLY TYR THR LEU LYS ALA PHE
SEQRES 15 C 615 GLY ASN LEU LEU GLY ASP VAL ALA LYS PHE ALA GLN ALA
SEQRES 16 C 615 HIS GLY LEU SER GLY GLU ASP VAL VAL VAL SER GLY HIS
SEQRES 17 C 615 SER LEU GLY GLY LEU ALA VAL ASN SER MET ALA ALA GLN
SEQRES 18 C 615 SER ASP ALA ASN TRP GLY GLY PHE TYR ALA GLN SER ASN
SEQRES 19 C 615 TYR VAL ALA PHE ALA SER PRO THR GLN TYR GLU ALA GLY
SEQRES 20 C 615 GLY LYS VAL ILE ASN ILE GLY TYR GLU ASN ASP PRO VAL
SEQRES 21 C 615 PHE ARG ALA LEU ASP GLY THR SER LEU THR LEU PRO SER
SEQRES 22 C 615 LEU GLY VAL HIS ASP ALA PRO HIS THR SER ALA THR ASN
SEQRES 23 C 615 ASN ILE VAL ASN PHE ASN ASP HIS TYR ALA SER ASP ALA
SEQRES 24 C 615 TRP ASN LEU LEU PRO PHE SER ILE LEU ASN ILE PRO THR
SEQRES 25 C 615 TRP LEU SER HIS LEU PRO PHE PHE TYR GLN ASP GLY LEU
SEQRES 26 C 615 MET ARG VAL LEU ASN SER GLU PHE TYR SER LEU THR ASP
SEQRES 27 C 615 LYS ASP SER THR ILE ILE VAL SER ASN LEU SER ASN VAL
SEQRES 28 C 615 THR ARG GLY ASN THR TRP VAL GLU ASP LEU ASN ARG ASN
SEQRES 29 C 615 ALA GLU THR HIS SER GLY PRO THR PHE ILE ILE GLY SER
SEQRES 30 C 615 ASP GLY ASN ASP LEU ILE LYS GLY GLY LYS GLY ASN ASP
SEQRES 31 C 615 TYR LEU GLU GLY ARG ASP GLY ASP ASP ILE PHE ARG ASP
SEQRES 32 C 615 ALA GLY GLY TYR ASN LEU ILE ALA GLY GLY LYS GLY HIS
SEQRES 33 C 615 ASN ILE PHE ASP THR GLN GLN ALA LEU LYS ASN THR GLU
SEQRES 34 C 615 VAL ALA TYR ASP GLY ASN THR LEU TYR LEU ARG ASP ALA
SEQRES 35 C 615 LYS GLY GLY ILE THR LEU ALA ASP ASP ILE SER THR LEU
SEQRES 36 C 615 ARG SER LYS GLU THR SER TRP LEU ILE PHE ASN LYS GLU
SEQRES 37 C 615 VAL ASP HIS GLN VAL THR ALA ALA GLY LEU LYS SER ASP
SEQRES 38 C 615 SER GLY LEU LYS ALA TYR ALA ALA ALA THR GLY GLY ASP
SEQRES 39 C 615 GLY ASP ASP VAL LEU GLN ALA ARG SER HIS ASP ALA TRP
SEQRES 40 C 615 LEU PHE GLY ASN ALA GLY ASN ASP THR LEU ILE GLY HIS
SEQRES 41 C 615 ALA GLY GLY ASN LEU THR PHE VAL GLY GLY SER GLY ASP
SEQRES 42 C 615 ASP ILE LEU LYS GLY VAL GLY ASN GLY ASN THR PHE LEU
SEQRES 43 C 615 PHE SER GLY ASP PHE GLY ARG ASP GLN LEU TYR GLY PHE
SEQRES 44 C 615 ASN ALA SER ASP LYS LEU VAL PHE ILE GLY THR GLU GLY
SEQRES 45 C 615 ALA SER GLY ASN ILE ARG ASP TYR ALA THR GLN GLN ASN
SEQRES 46 C 615 ASP ASP LEU VAL LEU ALA PHE GLY HIS SER GLN VAL THR
SEQRES 47 C 615 LEU ILE GLY VAL SER LEU ASP HIS ILE SER THR ASP GLN
SEQRES 48 C 615 VAL VAL LEU ALA
SEQRES 1 E 615 SER HIS MET GLY ILE PHE SER TYR LYS ASP LEU ASP GLU
SEQRES 2 E 615 ASN ALA SER LYS ALA LEU PHE SER ASP ALA LEU ALA ILE
SEQRES 3 E 615 SER THR TYR ALA TYR HIS ASN ILE ASP ASN GLY PHE ASP
SEQRES 4 E 615 GLU GLY TYR HIS GLN THR GLY PHE GLY LEU GLY LEU PRO
SEQRES 5 E 615 LEU THR LEU ILE THR ALA LEU ILE GLY SER THR GLN SER
SEQRES 6 E 615 GLN GLY GLY LEU PRO GLY LEU PRO TRP ASN PRO ASP SER
SEQRES 7 E 615 GLU GLN ALA ALA GLN GLU ALA VAL ASN ASN ALA GLY TRP
SEQRES 8 E 615 SER VAL ILE SER ALA THR GLN LEU GLY TYR ALA GLY LYS
SEQRES 9 E 615 THR ASP ALA ARG GLY THR TYR TYR GLY GLU THR ALA GLY
SEQRES 10 E 615 TYR THR THR ALA GLN ALA GLU VAL LEU GLY LYS TYR ASP
SEQRES 11 E 615 SER GLU GLY ASN LEU THR ALA ILE GLY ILE SER PHE ARG
SEQRES 12 E 615 GLY THR SER GLY PRO ARG GLU SER LEU ILE GLY ASP THR
SEQRES 13 E 615 ILE GLY ASP VAL ILE ASN ASP LEU LEU ALA GLY PHE GLY
SEQRES 14 E 615 PRO LYS GLY TYR ALA ASP GLY TYR THR LEU LYS ALA PHE
SEQRES 15 E 615 GLY ASN LEU LEU GLY ASP VAL ALA LYS PHE ALA GLN ALA
SEQRES 16 E 615 HIS GLY LEU SER GLY GLU ASP VAL VAL VAL SER GLY HIS
SEQRES 17 E 615 SER LEU GLY GLY LEU ALA VAL ASN SER MET ALA ALA GLN
SEQRES 18 E 615 SER ASP ALA ASN TRP GLY GLY PHE TYR ALA GLN SER ASN
SEQRES 19 E 615 TYR VAL ALA PHE ALA SER PRO THR GLN TYR GLU ALA GLY
SEQRES 20 E 615 GLY LYS VAL ILE ASN ILE GLY TYR GLU ASN ASP PRO VAL
SEQRES 21 E 615 PHE ARG ALA LEU ASP GLY THR SER LEU THR LEU PRO SER
SEQRES 22 E 615 LEU GLY VAL HIS ASP ALA PRO HIS THR SER ALA THR ASN
SEQRES 23 E 615 ASN ILE VAL ASN PHE ASN ASP HIS TYR ALA SER ASP ALA
SEQRES 24 E 615 TRP ASN LEU LEU PRO PHE SER ILE LEU ASN ILE PRO THR
SEQRES 25 E 615 TRP LEU SER HIS LEU PRO PHE PHE TYR GLN ASP GLY LEU
SEQRES 26 E 615 MET ARG VAL LEU ASN SER GLU PHE TYR SER LEU THR ASP
SEQRES 27 E 615 LYS ASP SER THR ILE ILE VAL SER ASN LEU SER ASN VAL
SEQRES 28 E 615 THR ARG GLY ASN THR TRP VAL GLU ASP LEU ASN ARG ASN
SEQRES 29 E 615 ALA GLU THR HIS SER GLY PRO THR PHE ILE ILE GLY SER
SEQRES 30 E 615 ASP GLY ASN ASP LEU ILE LYS GLY GLY LYS GLY ASN ASP
SEQRES 31 E 615 TYR LEU GLU GLY ARG ASP GLY ASP ASP ILE PHE ARG ASP
SEQRES 32 E 615 ALA GLY GLY TYR ASN LEU ILE ALA GLY GLY LYS GLY HIS
SEQRES 33 E 615 ASN ILE PHE ASP THR GLN GLN ALA LEU LYS ASN THR GLU
SEQRES 34 E 615 VAL ALA TYR ASP GLY ASN THR LEU TYR LEU ARG ASP ALA
SEQRES 35 E 615 LYS GLY GLY ILE THR LEU ALA ASP ASP ILE SER THR LEU
SEQRES 36 E 615 ARG SER LYS GLU THR SER TRP LEU ILE PHE ASN LYS GLU
SEQRES 37 E 615 VAL ASP HIS GLN VAL THR ALA ALA GLY LEU LYS SER ASP
SEQRES 38 E 615 SER GLY LEU LYS ALA TYR ALA ALA ALA THR GLY GLY ASP
SEQRES 39 E 615 GLY ASP ASP VAL LEU GLN ALA ARG SER HIS ASP ALA TRP
SEQRES 40 E 615 LEU PHE GLY ASN ALA GLY ASN ASP THR LEU ILE GLY HIS
SEQRES 41 E 615 ALA GLY GLY ASN LEU THR PHE VAL GLY GLY SER GLY ASP
SEQRES 42 E 615 ASP ILE LEU LYS GLY VAL GLY ASN GLY ASN THR PHE LEU
SEQRES 43 E 615 PHE SER GLY ASP PHE GLY ARG ASP GLN LEU TYR GLY PHE
SEQRES 44 E 615 ASN ALA SER ASP LYS LEU VAL PHE ILE GLY THR GLU GLY
SEQRES 45 E 615 ALA SER GLY ASN ILE ARG ASP TYR ALA THR GLN GLN ASN
SEQRES 46 E 615 ASP ASP LEU VAL LEU ALA PHE GLY HIS SER GLN VAL THR
SEQRES 47 E 615 LEU ILE GLY VAL SER LEU ASP HIS ILE SER THR ASP GLN
SEQRES 48 E 615 VAL VAL LEU ALA
SEQRES 1 G 615 SER HIS MET GLY ILE PHE SER TYR LYS ASP LEU ASP GLU
SEQRES 2 G 615 ASN ALA SER LYS ALA LEU PHE SER ASP ALA LEU ALA ILE
SEQRES 3 G 615 SER THR TYR ALA TYR HIS ASN ILE ASP ASN GLY PHE ASP
SEQRES 4 G 615 GLU GLY TYR HIS GLN THR GLY PHE GLY LEU GLY LEU PRO
SEQRES 5 G 615 LEU THR LEU ILE THR ALA LEU ILE GLY SER THR GLN SER
SEQRES 6 G 615 GLN GLY GLY LEU PRO GLY LEU PRO TRP ASN PRO ASP SER
SEQRES 7 G 615 GLU GLN ALA ALA GLN GLU ALA VAL ASN ASN ALA GLY TRP
SEQRES 8 G 615 SER VAL ILE SER ALA THR GLN LEU GLY TYR ALA GLY LYS
SEQRES 9 G 615 THR ASP ALA ARG GLY THR TYR TYR GLY GLU THR ALA GLY
SEQRES 10 G 615 TYR THR THR ALA GLN ALA GLU VAL LEU GLY LYS TYR ASP
SEQRES 11 G 615 SER GLU GLY ASN LEU THR ALA ILE GLY ILE SER PHE ARG
SEQRES 12 G 615 GLY THR SER GLY PRO ARG GLU SER LEU ILE GLY ASP THR
SEQRES 13 G 615 ILE GLY ASP VAL ILE ASN ASP LEU LEU ALA GLY PHE GLY
SEQRES 14 G 615 PRO LYS GLY TYR ALA ASP GLY TYR THR LEU LYS ALA PHE
SEQRES 15 G 615 GLY ASN LEU LEU GLY ASP VAL ALA LYS PHE ALA GLN ALA
SEQRES 16 G 615 HIS GLY LEU SER GLY GLU ASP VAL VAL VAL SER GLY HIS
SEQRES 17 G 615 SER LEU GLY GLY LEU ALA VAL ASN SER MET ALA ALA GLN
SEQRES 18 G 615 SER ASP ALA ASN TRP GLY GLY PHE TYR ALA GLN SER ASN
SEQRES 19 G 615 TYR VAL ALA PHE ALA SER PRO THR GLN TYR GLU ALA GLY
SEQRES 20 G 615 GLY LYS VAL ILE ASN ILE GLY TYR GLU ASN ASP PRO VAL
SEQRES 21 G 615 PHE ARG ALA LEU ASP GLY THR SER LEU THR LEU PRO SER
SEQRES 22 G 615 LEU GLY VAL HIS ASP ALA PRO HIS THR SER ALA THR ASN
SEQRES 23 G 615 ASN ILE VAL ASN PHE ASN ASP HIS TYR ALA SER ASP ALA
SEQRES 24 G 615 TRP ASN LEU LEU PRO PHE SER ILE LEU ASN ILE PRO THR
SEQRES 25 G 615 TRP LEU SER HIS LEU PRO PHE PHE TYR GLN ASP GLY LEU
SEQRES 26 G 615 MET ARG VAL LEU ASN SER GLU PHE TYR SER LEU THR ASP
SEQRES 27 G 615 LYS ASP SER THR ILE ILE VAL SER ASN LEU SER ASN VAL
SEQRES 28 G 615 THR ARG GLY ASN THR TRP VAL GLU ASP LEU ASN ARG ASN
SEQRES 29 G 615 ALA GLU THR HIS SER GLY PRO THR PHE ILE ILE GLY SER
SEQRES 30 G 615 ASP GLY ASN ASP LEU ILE LYS GLY GLY LYS GLY ASN ASP
SEQRES 31 G 615 TYR LEU GLU GLY ARG ASP GLY ASP ASP ILE PHE ARG ASP
SEQRES 32 G 615 ALA GLY GLY TYR ASN LEU ILE ALA GLY GLY LYS GLY HIS
SEQRES 33 G 615 ASN ILE PHE ASP THR GLN GLN ALA LEU LYS ASN THR GLU
SEQRES 34 G 615 VAL ALA TYR ASP GLY ASN THR LEU TYR LEU ARG ASP ALA
SEQRES 35 G 615 LYS GLY GLY ILE THR LEU ALA ASP ASP ILE SER THR LEU
SEQRES 36 G 615 ARG SER LYS GLU THR SER TRP LEU ILE PHE ASN LYS GLU
SEQRES 37 G 615 VAL ASP HIS GLN VAL THR ALA ALA GLY LEU LYS SER ASP
SEQRES 38 G 615 SER GLY LEU LYS ALA TYR ALA ALA ALA THR GLY GLY ASP
SEQRES 39 G 615 GLY ASP ASP VAL LEU GLN ALA ARG SER HIS ASP ALA TRP
SEQRES 40 G 615 LEU PHE GLY ASN ALA GLY ASN ASP THR LEU ILE GLY HIS
SEQRES 41 G 615 ALA GLY GLY ASN LEU THR PHE VAL GLY GLY SER GLY ASP
SEQRES 42 G 615 ASP ILE LEU LYS GLY VAL GLY ASN GLY ASN THR PHE LEU
SEQRES 43 G 615 PHE SER GLY ASP PHE GLY ARG ASP GLN LEU TYR GLY PHE
SEQRES 44 G 615 ASN ALA SER ASP LYS LEU VAL PHE ILE GLY THR GLU GLY
SEQRES 45 G 615 ALA SER GLY ASN ILE ARG ASP TYR ALA THR GLN GLN ASN
SEQRES 46 G 615 ASP ASP LEU VAL LEU ALA PHE GLY HIS SER GLN VAL THR
SEQRES 47 G 615 LEU ILE GLY VAL SER LEU ASP HIS ILE SER THR ASP GLN
SEQRES 48 G 615 VAL VAL LEU ALA
SEQRES 1 I 615 SER HIS MET GLY ILE PHE SER TYR LYS ASP LEU ASP GLU
SEQRES 2 I 615 ASN ALA SER LYS ALA LEU PHE SER ASP ALA LEU ALA ILE
SEQRES 3 I 615 SER THR TYR ALA TYR HIS ASN ILE ASP ASN GLY PHE ASP
SEQRES 4 I 615 GLU GLY TYR HIS GLN THR GLY PHE GLY LEU GLY LEU PRO
SEQRES 5 I 615 LEU THR LEU ILE THR ALA LEU ILE GLY SER THR GLN SER
SEQRES 6 I 615 GLN GLY GLY LEU PRO GLY LEU PRO TRP ASN PRO ASP SER
SEQRES 7 I 615 GLU GLN ALA ALA GLN GLU ALA VAL ASN ASN ALA GLY TRP
SEQRES 8 I 615 SER VAL ILE SER ALA THR GLN LEU GLY TYR ALA GLY LYS
SEQRES 9 I 615 THR ASP ALA ARG GLY THR TYR TYR GLY GLU THR ALA GLY
SEQRES 10 I 615 TYR THR THR ALA GLN ALA GLU VAL LEU GLY LYS TYR ASP
SEQRES 11 I 615 SER GLU GLY ASN LEU THR ALA ILE GLY ILE SER PHE ARG
SEQRES 12 I 615 GLY THR SER GLY PRO ARG GLU SER LEU ILE GLY ASP THR
SEQRES 13 I 615 ILE GLY ASP VAL ILE ASN ASP LEU LEU ALA GLY PHE GLY
SEQRES 14 I 615 PRO LYS GLY TYR ALA ASP GLY TYR THR LEU LYS ALA PHE
SEQRES 15 I 615 GLY ASN LEU LEU GLY ASP VAL ALA LYS PHE ALA GLN ALA
SEQRES 16 I 615 HIS GLY LEU SER GLY GLU ASP VAL VAL VAL SER GLY HIS
SEQRES 17 I 615 SER LEU GLY GLY LEU ALA VAL ASN SER MET ALA ALA GLN
SEQRES 18 I 615 SER ASP ALA ASN TRP GLY GLY PHE TYR ALA GLN SER ASN
SEQRES 19 I 615 TYR VAL ALA PHE ALA SER PRO THR GLN TYR GLU ALA GLY
SEQRES 20 I 615 GLY LYS VAL ILE ASN ILE GLY TYR GLU ASN ASP PRO VAL
SEQRES 21 I 615 PHE ARG ALA LEU ASP GLY THR SER LEU THR LEU PRO SER
SEQRES 22 I 615 LEU GLY VAL HIS ASP ALA PRO HIS THR SER ALA THR ASN
SEQRES 23 I 615 ASN ILE VAL ASN PHE ASN ASP HIS TYR ALA SER ASP ALA
SEQRES 24 I 615 TRP ASN LEU LEU PRO PHE SER ILE LEU ASN ILE PRO THR
SEQRES 25 I 615 TRP LEU SER HIS LEU PRO PHE PHE TYR GLN ASP GLY LEU
SEQRES 26 I 615 MET ARG VAL LEU ASN SER GLU PHE TYR SER LEU THR ASP
SEQRES 27 I 615 LYS ASP SER THR ILE ILE VAL SER ASN LEU SER ASN VAL
SEQRES 28 I 615 THR ARG GLY ASN THR TRP VAL GLU ASP LEU ASN ARG ASN
SEQRES 29 I 615 ALA GLU THR HIS SER GLY PRO THR PHE ILE ILE GLY SER
SEQRES 30 I 615 ASP GLY ASN ASP LEU ILE LYS GLY GLY LYS GLY ASN ASP
SEQRES 31 I 615 TYR LEU GLU GLY ARG ASP GLY ASP ASP ILE PHE ARG ASP
SEQRES 32 I 615 ALA GLY GLY TYR ASN LEU ILE ALA GLY GLY LYS GLY HIS
SEQRES 33 I 615 ASN ILE PHE ASP THR GLN GLN ALA LEU LYS ASN THR GLU
SEQRES 34 I 615 VAL ALA TYR ASP GLY ASN THR LEU TYR LEU ARG ASP ALA
SEQRES 35 I 615 LYS GLY GLY ILE THR LEU ALA ASP ASP ILE SER THR LEU
SEQRES 36 I 615 ARG SER LYS GLU THR SER TRP LEU ILE PHE ASN LYS GLU
SEQRES 37 I 615 VAL ASP HIS GLN VAL THR ALA ALA GLY LEU LYS SER ASP
SEQRES 38 I 615 SER GLY LEU LYS ALA TYR ALA ALA ALA THR GLY GLY ASP
SEQRES 39 I 615 GLY ASP ASP VAL LEU GLN ALA ARG SER HIS ASP ALA TRP
SEQRES 40 I 615 LEU PHE GLY ASN ALA GLY ASN ASP THR LEU ILE GLY HIS
SEQRES 41 I 615 ALA GLY GLY ASN LEU THR PHE VAL GLY GLY SER GLY ASP
SEQRES 42 I 615 ASP ILE LEU LYS GLY VAL GLY ASN GLY ASN THR PHE LEU
SEQRES 43 I 615 PHE SER GLY ASP PHE GLY ARG ASP GLN LEU TYR GLY PHE
SEQRES 44 I 615 ASN ALA SER ASP LYS LEU VAL PHE ILE GLY THR GLU GLY
SEQRES 45 I 615 ALA SER GLY ASN ILE ARG ASP TYR ALA THR GLN GLN ASN
SEQRES 46 I 615 ASP ASP LEU VAL LEU ALA PHE GLY HIS SER GLN VAL THR
SEQRES 47 I 615 LEU ILE GLY VAL SER LEU ASP HIS ILE SER THR ASP GLN
SEQRES 48 I 615 VAL VAL LEU ALA
SEQRES 1 K 615 SER HIS MET GLY ILE PHE SER TYR LYS ASP LEU ASP GLU
SEQRES 2 K 615 ASN ALA SER LYS ALA LEU PHE SER ASP ALA LEU ALA ILE
SEQRES 3 K 615 SER THR TYR ALA TYR HIS ASN ILE ASP ASN GLY PHE ASP
SEQRES 4 K 615 GLU GLY TYR HIS GLN THR GLY PHE GLY LEU GLY LEU PRO
SEQRES 5 K 615 LEU THR LEU ILE THR ALA LEU ILE GLY SER THR GLN SER
SEQRES 6 K 615 GLN GLY GLY LEU PRO GLY LEU PRO TRP ASN PRO ASP SER
SEQRES 7 K 615 GLU GLN ALA ALA GLN GLU ALA VAL ASN ASN ALA GLY TRP
SEQRES 8 K 615 SER VAL ILE SER ALA THR GLN LEU GLY TYR ALA GLY LYS
SEQRES 9 K 615 THR ASP ALA ARG GLY THR TYR TYR GLY GLU THR ALA GLY
SEQRES 10 K 615 TYR THR THR ALA GLN ALA GLU VAL LEU GLY LYS TYR ASP
SEQRES 11 K 615 SER GLU GLY ASN LEU THR ALA ILE GLY ILE SER PHE ARG
SEQRES 12 K 615 GLY THR SER GLY PRO ARG GLU SER LEU ILE GLY ASP THR
SEQRES 13 K 615 ILE GLY ASP VAL ILE ASN ASP LEU LEU ALA GLY PHE GLY
SEQRES 14 K 615 PRO LYS GLY TYR ALA ASP GLY TYR THR LEU LYS ALA PHE
SEQRES 15 K 615 GLY ASN LEU LEU GLY ASP VAL ALA LYS PHE ALA GLN ALA
SEQRES 16 K 615 HIS GLY LEU SER GLY GLU ASP VAL VAL VAL SER GLY HIS
SEQRES 17 K 615 SER LEU GLY GLY LEU ALA VAL ASN SER MET ALA ALA GLN
SEQRES 18 K 615 SER ASP ALA ASN TRP GLY GLY PHE TYR ALA GLN SER ASN
SEQRES 19 K 615 TYR VAL ALA PHE ALA SER PRO THR GLN TYR GLU ALA GLY
SEQRES 20 K 615 GLY LYS VAL ILE ASN ILE GLY TYR GLU ASN ASP PRO VAL
SEQRES 21 K 615 PHE ARG ALA LEU ASP GLY THR SER LEU THR LEU PRO SER
SEQRES 22 K 615 LEU GLY VAL HIS ASP ALA PRO HIS THR SER ALA THR ASN
SEQRES 23 K 615 ASN ILE VAL ASN PHE ASN ASP HIS TYR ALA SER ASP ALA
SEQRES 24 K 615 TRP ASN LEU LEU PRO PHE SER ILE LEU ASN ILE PRO THR
SEQRES 25 K 615 TRP LEU SER HIS LEU PRO PHE PHE TYR GLN ASP GLY LEU
SEQRES 26 K 615 MET ARG VAL LEU ASN SER GLU PHE TYR SER LEU THR ASP
SEQRES 27 K 615 LYS ASP SER THR ILE ILE VAL SER ASN LEU SER ASN VAL
SEQRES 28 K 615 THR ARG GLY ASN THR TRP VAL GLU ASP LEU ASN ARG ASN
SEQRES 29 K 615 ALA GLU THR HIS SER GLY PRO THR PHE ILE ILE GLY SER
SEQRES 30 K 615 ASP GLY ASN ASP LEU ILE LYS GLY GLY LYS GLY ASN ASP
SEQRES 31 K 615 TYR LEU GLU GLY ARG ASP GLY ASP ASP ILE PHE ARG ASP
SEQRES 32 K 615 ALA GLY GLY TYR ASN LEU ILE ALA GLY GLY LYS GLY HIS
SEQRES 33 K 615 ASN ILE PHE ASP THR GLN GLN ALA LEU LYS ASN THR GLU
SEQRES 34 K 615 VAL ALA TYR ASP GLY ASN THR LEU TYR LEU ARG ASP ALA
SEQRES 35 K 615 LYS GLY GLY ILE THR LEU ALA ASP ASP ILE SER THR LEU
SEQRES 36 K 615 ARG SER LYS GLU THR SER TRP LEU ILE PHE ASN LYS GLU
SEQRES 37 K 615 VAL ASP HIS GLN VAL THR ALA ALA GLY LEU LYS SER ASP
SEQRES 38 K 615 SER GLY LEU LYS ALA TYR ALA ALA ALA THR GLY GLY ASP
SEQRES 39 K 615 GLY ASP ASP VAL LEU GLN ALA ARG SER HIS ASP ALA TRP
SEQRES 40 K 615 LEU PHE GLY ASN ALA GLY ASN ASP THR LEU ILE GLY HIS
SEQRES 41 K 615 ALA GLY GLY ASN LEU THR PHE VAL GLY GLY SER GLY ASP
SEQRES 42 K 615 ASP ILE LEU LYS GLY VAL GLY ASN GLY ASN THR PHE LEU
SEQRES 43 K 615 PHE SER GLY ASP PHE GLY ARG ASP GLN LEU TYR GLY PHE
SEQRES 44 K 615 ASN ALA SER ASP LYS LEU VAL PHE ILE GLY THR GLU GLY
SEQRES 45 K 615 ALA SER GLY ASN ILE ARG ASP TYR ALA THR GLN GLN ASN
SEQRES 46 K 615 ASP ASP LEU VAL LEU ALA PHE GLY HIS SER GLN VAL THR
SEQRES 47 K 615 LEU ILE GLY VAL SER LEU ASP HIS ILE SER THR ASP GLN
SEQRES 48 K 615 VAL VAL LEU ALA
HET CA A 614 1
HET CA A 615 1
HET CA A 616 1
HET CA A 617 1
HET CA A 618 1
HET CA A 619 1
HET CA A 620 1
HET CA A 621 1
HET CA C 614 1
HET CA C 615 1
HET CA C 616 1
HET CA C 617 1
HET CA C 618 1
HET CA C 619 1
HET CA C 620 1
HET CA C 621 1
HET CA E 614 1
HET CA E 615 1
HET CA E 616 1
HET CA E 617 1
HET CA E 618 1
HET CA E 619 1
HET CA E 620 1
HET CA E 621 1
HET CA G 614 1
HET CA G 615 1
HET CA G 616 1
HET CA G 617 1
HET CA G 618 1
HET CA G 619 1
HET CA G 620 1
HET CA G 621 1
HET CA I 614 1
HET CA I 615 1
HET CA I 616 1
HET CA I 617 1
HET CA I 618 1
HET CA I 619 1
HET CA I 620 1
HET CA I 621 1
HET CA K 614 1
HET CA K 615 1
HET CA K 616 1
HET CA K 617 1
HET CA K 618 1
HET CA K 619 1
HET CA K 620 1
HET CA K 621 1
HETNAM CA CALCIUM ION
FORMUL 7 CA 48(CA 2+)
FORMUL 55 HOH *1921(H2 O)
HELIX 1 1 ASP A 10 ALA A 28 1 19
HELIX 2 2 ASP A 33 GLY A 44 1 12
HELIX 3 3 GLY A 48 GLY A 59 1 12
HELIX 4 4 ASP A 75 ALA A 87 1 13
HELIX 5 5 SER A 93 GLY A 98 1 6
HELIX 6 6 PRO A 146 GLU A 148 5 3
HELIX 7 7 SER A 149 GLY A 167 1 19
HELIX 8 8 GLY A 170 HIS A 194 1 25
HELIX 9 9 SER A 197 GLU A 199 5 3
HELIX 10 10 SER A 207 SER A 220 1 14
HELIX 11 11 ASN A 223 PHE A 227 5 5
HELIX 12 12 THR A 268 GLY A 273 5 6
HELIX 13 13 ASN A 290 SER A 295 1 6
HELIX 14 14 ALA A 297 LEU A 301 5 5
HELIX 15 15 ASN A 307 HIS A 314 5 8
HELIX 16 16 LEU A 315 ASN A 328 1 14
HELIX 17 17 PHE A 331 THR A 335 5 5
HELIX 18 18 ALA A 422 THR A 426 5 5
HELIX 19 19 ASN A 574 ASP A 577 5 4
HELIX 20 20 SER A 601 ILE A 605 5 5
HELIX 21 21 SER A 606 ASP A 608 5 3
HELIX 22 22 ASP C 10 ALA C 28 1 19
HELIX 23 23 ASP C 33 GLY C 44 1 12
HELIX 24 24 GLY C 48 GLY C 59 1 12
HELIX 25 25 ASP C 75 ALA C 87 1 13
HELIX 26 26 SER C 93 GLY C 98 1 6
HELIX 27 27 PRO C 146 GLU C 148 5 3
HELIX 28 28 SER C 149 GLY C 167 1 19
HELIX 29 29 GLY C 170 HIS C 194 1 25
HELIX 30 30 SER C 197 GLU C 199 5 3
HELIX 31 31 SER C 207 SER C 220 1 14
HELIX 32 32 ASN C 223 PHE C 227 5 5
HELIX 33 33 THR C 268 GLY C 273 5 6
HELIX 34 34 ASN C 290 SER C 295 1 6
HELIX 35 35 ALA C 297 LEU C 301 5 5
HELIX 36 36 ASN C 307 HIS C 314 5 8
HELIX 37 37 LEU C 315 ASN C 328 1 14
HELIX 38 38 PHE C 331 THR C 335 5 5
HELIX 39 39 ALA C 422 THR C 426 5 5
HELIX 40 40 ASN C 574 ASP C 577 5 4
HELIX 41 41 SER C 601 ILE C 605 5 5
HELIX 42 42 SER C 606 ASP C 608 5 3
HELIX 43 43 ASP E 10 ALA E 28 1 19
HELIX 44 44 ASP E 33 GLY E 44 1 12
HELIX 45 45 GLY E 48 GLY E 59 1 12
HELIX 46 46 ASP E 75 ALA E 87 1 13
HELIX 47 47 SER E 93 GLY E 98 1 6
HELIX 48 48 PRO E 146 GLU E 148 5 3
HELIX 49 49 SER E 149 GLY E 167 1 19
HELIX 50 50 GLY E 170 HIS E 194 1 25
HELIX 51 51 SER E 197 GLU E 199 5 3
HELIX 52 52 SER E 207 SER E 220 1 14
HELIX 53 53 ASN E 223 PHE E 227 5 5
HELIX 54 54 THR E 268 GLY E 273 5 6
HELIX 55 55 ASN E 290 SER E 295 1 6
HELIX 56 56 ALA E 297 LEU E 301 5 5
HELIX 57 57 ASN E 307 HIS E 314 5 8
HELIX 58 58 LEU E 315 ASN E 328 1 14
HELIX 59 59 PHE E 331 THR E 335 5 5
HELIX 60 60 ALA E 422 THR E 426 5 5
HELIX 61 61 ASN E 574 ASP E 577 5 4
HELIX 62 62 SER E 601 ILE E 605 5 5
HELIX 63 63 SER E 606 ASP E 608 5 3
HELIX 64 64 ASP G 10 ALA G 28 1 19
HELIX 65 65 ASP G 33 GLY G 44 1 12
HELIX 66 66 GLY G 48 GLY G 59 1 12
HELIX 67 67 ASP G 75 ALA G 87 1 13
HELIX 68 68 SER G 93 GLY G 98 1 6
HELIX 69 69 PRO G 146 GLU G 148 5 3
HELIX 70 70 SER G 149 GLY G 167 1 19
HELIX 71 71 GLY G 170 HIS G 194 1 25
HELIX 72 72 SER G 197 GLU G 199 5 3
HELIX 73 73 SER G 207 SER G 220 1 14
HELIX 74 74 ASN G 223 PHE G 227 5 5
HELIX 75 75 THR G 268 GLY G 273 5 6
HELIX 76 76 ASN G 290 SER G 295 1 6
HELIX 77 77 ALA G 297 LEU G 301 5 5
HELIX 78 78 ASN G 307 HIS G 314 5 8
HELIX 79 79 LEU G 315 ASN G 328 1 14
HELIX 80 80 PHE G 331 THR G 335 5 5
HELIX 81 81 ALA G 422 THR G 426 5 5
HELIX 82 82 ASN G 574 ASP G 577 5 4
HELIX 83 83 SER G 601 ILE G 605 5 5
HELIX 84 84 SER G 606 ASP G 608 5 3
HELIX 85 85 ASP I 10 ALA I 28 1 19
HELIX 86 86 ASP I 33 GLY I 44 1 12
HELIX 87 87 GLY I 48 GLY I 59 1 12
HELIX 88 88 ASP I 75 ALA I 87 1 13
HELIX 89 89 SER I 93 GLY I 98 1 6
HELIX 90 90 PRO I 146 GLU I 148 5 3
HELIX 91 91 SER I 149 GLY I 167 1 19
HELIX 92 92 GLY I 170 HIS I 194 1 25
HELIX 93 93 SER I 197 GLU I 199 5 3
HELIX 94 94 SER I 207 SER I 220 1 14
HELIX 95 95 ASN I 223 PHE I 227 5 5
HELIX 96 96 THR I 268 GLY I 273 5 6
HELIX 97 97 ASN I 290 SER I 295 1 6
HELIX 98 98 ALA I 297 LEU I 301 5 5
HELIX 99 99 ASN I 307 HIS I 314 5 8
HELIX 100 100 LEU I 315 ASN I 328 1 14
HELIX 101 101 PHE I 331 THR I 335 5 5
HELIX 102 102 ALA I 422 THR I 426 5 5
HELIX 103 103 ASN I 574 ASP I 577 5 4
HELIX 104 104 SER I 601 ILE I 605 5 5
HELIX 105 105 SER I 606 ASP I 608 5 3
HELIX 106 106 ASP K 10 ALA K 28 1 19
HELIX 107 107 ASP K 33 GLY K 44 1 12
HELIX 108 108 GLY K 48 GLY K 59 1 12
HELIX 109 109 ASP K 75 ALA K 87 1 13
HELIX 110 110 SER K 93 GLY K 98 1 6
HELIX 111 111 PRO K 146 GLU K 148 5 3
HELIX 112 112 SER K 149 GLY K 167 1 19
HELIX 113 113 GLY K 170 HIS K 194 1 25
HELIX 114 114 SER K 197 GLU K 199 5 3
HELIX 115 115 SER K 207 SER K 220 1 14
HELIX 116 116 ASN K 223 PHE K 227 5 5
HELIX 117 117 THR K 268 GLY K 273 5 6
HELIX 118 118 ASN K 290 SER K 295 1 6
HELIX 119 119 ALA K 297 LEU K 301 5 5
HELIX 120 120 ASN K 307 HIS K 314 5 8
HELIX 121 121 LEU K 315 ASN K 328 1 14
HELIX 122 122 PHE K 331 THR K 335 5 5
HELIX 123 123 ALA K 422 THR K 426 5 5
HELIX 124 124 ASN K 574 ASP K 577 5 4
HELIX 125 125 SER K 601 ILE K 605 5 5
HELIX 126 126 SER K 606 ASP K 608 5 3
SHEET 1 A 3 SER A 90 VAL A 91 0
SHEET 2 A 3 GLN A 120 TYR A 127 -1 O GLY A 125 N SER A 90
SHEET 3 A 3 TYR A 109 TYR A 110 -1 N TYR A 109 O ALA A 121
SHEET 1 B 6 SER A 90 VAL A 91 0
SHEET 2 B 6 GLN A 120 TYR A 127 -1 O GLY A 125 N SER A 90
SHEET 3 B 6 LEU A 133 PHE A 140 -1 O THR A 134 N LYS A 126
SHEET 4 B 6 VAL A 201 HIS A 206 1 O VAL A 202 N ILE A 138
SHEET 5 B 6 ASN A 232 PHE A 236 1 O ASN A 232 N VAL A 203
SHEET 6 B 6 VAL A 248 ILE A 251 1 O ILE A 251 N ALA A 235
SHEET 1 C 8 ILE A 286 PHE A 289 0
SHEET 2 C 8 THR A 340 SER A 344 1 O ILE A 341 N VAL A 287
SHEET 3 C 8 THR A 370 ILE A 373 1 O PHE A 371 N ILE A 342
SHEET 4 C 8 ASP A 388 GLU A 391 1 O TYR A 389 N THR A 370
SHEET 5 C 8 ASN A 406 ALA A 409 1 O ALA A 409 N LEU A 390
SHEET 6 C 8 ILE A 444 ASP A 448 1 O ASP A 448 N ILE A 408
SHEET 7 C 8 THR A 434 ARG A 438 -1 N LEU A 435 O ALA A 447
SHEET 8 C 8 GLU A 427 TYR A 430 -1 N ALA A 429 O TYR A 436
SHEET 1 D 7 LEU A 380 GLY A 383 0
SHEET 2 D 7 ILE A 398 ASP A 401 1 O ARG A 400 N GLY A 383
SHEET 3 D 7 ILE A 416 ASP A 418 1 O ASP A 418 N PHE A 399
SHEET 4 D 7 THR A 452 GLU A 457 1 O ARG A 454 N PHE A 417
SHEET 5 D 7 LYS A 465 THR A 472 -1 O HIS A 469 N LEU A 453
SHEET 6 D 7 GLY A 475 SER A 478 -1 O LYS A 477 N GLN A 470
SHEET 7 D 7 GLY A 481 LYS A 483 -1 O LYS A 483 N LEU A 476
SHEET 1 E 6 ALA A 487 THR A 489 0
SHEET 2 E 6 TRP A 505 PHE A 507 1 O PHE A 507 N ALA A 488
SHEET 3 E 6 THR A 524 VAL A 526 1 O VAL A 526 N LEU A 506
SHEET 4 E 6 THR A 542 SER A 546 1 O THR A 542 N PHE A 525
SHEET 5 E 6 LYS A 562 ILE A 566 1 O LYS A 562 N PHE A 543
SHEET 6 E 6 VAL A 610 ALA A 613 1 O ALA A 613 N PHE A 565
SHEET 1 F 7 VAL A 496 GLN A 498 0
SHEET 2 F 7 THR A 514 ILE A 516 1 O ILE A 516 N LEU A 497
SHEET 3 F 7 ILE A 533 LYS A 535 1 O LYS A 535 N LEU A 515
SHEET 4 F 7 ARG A 551 TYR A 555 1 O TYR A 555 N LEU A 534
SHEET 5 F 7 SER A 593 LEU A 597 1 O THR A 596 N LEU A 554
SHEET 6 F 7 ASP A 585 PHE A 590 -1 N LEU A 586 O LEU A 597
SHEET 7 F 7 ALA A 579 GLN A 582 -1 N GLN A 582 O ASP A 585
SHEET 1 G 3 SER C 90 VAL C 91 0
SHEET 2 G 3 GLN C 120 TYR C 127 -1 O GLY C 125 N SER C 90
SHEET 3 G 3 TYR C 109 TYR C 110 -1 N TYR C 109 O ALA C 121
SHEET 1 H 6 SER C 90 VAL C 91 0
SHEET 2 H 6 GLN C 120 TYR C 127 -1 O GLY C 125 N SER C 90
SHEET 3 H 6 LEU C 133 PHE C 140 -1 O THR C 134 N LYS C 126
SHEET 4 H 6 VAL C 201 HIS C 206 1 O VAL C 202 N ILE C 138
SHEET 5 H 6 ASN C 232 PHE C 236 1 O ASN C 232 N VAL C 203
SHEET 6 H 6 VAL C 248 ILE C 251 1 O ILE C 251 N ALA C 235
SHEET 1 I 8 ILE C 286 PHE C 289 0
SHEET 2 I 8 THR C 340 SER C 344 1 O ILE C 341 N VAL C 287
SHEET 3 I 8 THR C 370 ILE C 373 1 O PHE C 371 N ILE C 342
SHEET 4 I 8 ASP C 388 GLU C 391 1 O GLU C 391 N ILE C 372
SHEET 5 I 8 ASN C 406 ALA C 409 1 O ALA C 409 N LEU C 390
SHEET 6 I 8 ILE C 444 ASP C 448 1 O ASP C 448 N ILE C 408
SHEET 7 I 8 THR C 434 ARG C 438 -1 N LEU C 435 O ALA C 447
SHEET 8 I 8 GLU C 427 TYR C 430 -1 N ALA C 429 O TYR C 436
SHEET 1 J 7 LEU C 380 GLY C 383 0
SHEET 2 J 7 ILE C 398 ASP C 401 1 O ILE C 398 N ILE C 381
SHEET 3 J 7 ILE C 416 ASP C 418 1 O ASP C 418 N PHE C 399
SHEET 4 J 7 THR C 452 SER C 459 1 O ARG C 454 N PHE C 417
SHEET 5 J 7 PHE C 463 THR C 472 -1 O HIS C 469 N LEU C 453
SHEET 6 J 7 GLY C 475 SER C 478 -1 O LYS C 477 N GLN C 470
SHEET 7 J 7 GLY C 481 LYS C 483 -1 O LYS C 483 N LEU C 476
SHEET 1 K 6 ALA C 487 THR C 489 0
SHEET 2 K 6 TRP C 505 PHE C 507 1 O PHE C 507 N ALA C 488
SHEET 3 K 6 THR C 524 VAL C 526 1 O THR C 524 N LEU C 506
SHEET 4 K 6 THR C 542 SER C 546 1 O THR C 542 N PHE C 525
SHEET 5 K 6 LYS C 562 ILE C 566 1 O VAL C 564 N PHE C 543
SHEET 6 K 6 VAL C 610 ALA C 613 1 O ALA C 613 N PHE C 565
SHEET 1 L 7 VAL C 496 GLN C 498 0
SHEET 2 L 7 THR C 514 ILE C 516 1 O ILE C 516 N LEU C 497
SHEET 3 L 7 ILE C 533 LYS C 535 1 O ILE C 533 N LEU C 515
SHEET 4 L 7 ARG C 551 TYR C 555 1 O TYR C 555 N LEU C 534
SHEET 5 L 7 SER C 593 LEU C 597 1 O THR C 596 N LEU C 554
SHEET 6 L 7 ASP C 585 PHE C 590 -1 N LEU C 586 O LEU C 597
SHEET 7 L 7 ALA C 579 GLN C 582 -1 N GLN C 582 O ASP C 585
SHEET 1 M 3 SER E 90 VAL E 91 0
SHEET 2 M 3 GLN E 120 TYR E 127 -1 O GLY E 125 N SER E 90
SHEET 3 M 3 TYR E 109 TYR E 110 -1 N TYR E 109 O ALA E 121
SHEET 1 N 6 SER E 90 VAL E 91 0
SHEET 2 N 6 GLN E 120 TYR E 127 -1 O GLY E 125 N SER E 90
SHEET 3 N 6 LEU E 133 PHE E 140 -1 O THR E 134 N LYS E 126
SHEET 4 N 6 VAL E 201 HIS E 206 1 O VAL E 202 N ILE E 138
SHEET 5 N 6 ASN E 232 PHE E 236 1 O PHE E 236 N GLY E 205
SHEET 6 N 6 VAL E 248 ILE E 251 1 O ILE E 251 N ALA E 235
SHEET 1 O 8 ILE E 286 PHE E 289 0
SHEET 2 O 8 THR E 340 SER E 344 1 O ILE E 341 N VAL E 287
SHEET 3 O 8 THR E 370 ILE E 373 1 O PHE E 371 N ILE E 342
SHEET 4 O 8 ASP E 388 GLU E 391 1 O GLU E 391 N ILE E 372
SHEET 5 O 8 ASN E 406 ALA E 409 1 O ALA E 409 N LEU E 390
SHEET 6 O 8 ILE E 444 ASP E 448 1 O ASP E 448 N ILE E 408
SHEET 7 O 8 THR E 434 ARG E 438 -1 N LEU E 437 O THR E 445
SHEET 8 O 8 GLU E 427 TYR E 430 -1 N ALA E 429 O TYR E 436
SHEET 1 P 7 LEU E 380 GLY E 383 0
SHEET 2 P 7 ILE E 398 ASP E 401 1 O ILE E 398 N ILE E 381
SHEET 3 P 7 ASN E 415 ASP E 418 1 O ASP E 418 N PHE E 399
SHEET 4 P 7 ILE E 450 SER E 459 1 O ARG E 454 N PHE E 417
SHEET 5 P 7 PHE E 463 THR E 472 -1 O LYS E 465 N GLU E 457
SHEET 6 P 7 GLY E 475 SER E 478 -1 O LYS E 477 N GLN E 470
SHEET 7 P 7 GLY E 481 LYS E 483 -1 O GLY E 481 N SER E 478
SHEET 1 Q 6 ALA E 487 THR E 489 0
SHEET 2 Q 6 TRP E 505 PHE E 507 1 O PHE E 507 N ALA E 488
SHEET 3 Q 6 THR E 524 VAL E 526 1 O THR E 524 N LEU E 506
SHEET 4 Q 6 THR E 542 SER E 546 1 O THR E 542 N PHE E 525
SHEET 5 Q 6 LYS E 562 ILE E 566 1 O VAL E 564 N PHE E 543
SHEET 6 Q 6 VAL E 610 ALA E 613 1 O ALA E 613 N PHE E 565
SHEET 1 R 7 VAL E 496 GLN E 498 0
SHEET 2 R 7 THR E 514 ILE E 516 1 O ILE E 516 N LEU E 497
SHEET 3 R 7 ILE E 533 LYS E 535 1 O ILE E 533 N LEU E 515
SHEET 4 R 7 ARG E 551 TYR E 555 1 O TYR E 555 N LEU E 534
SHEET 5 R 7 SER E 593 LEU E 597 1 O THR E 596 N LEU E 554
SHEET 6 R 7 ASP E 585 PHE E 590 -1 N LEU E 586 O LEU E 597
SHEET 7 R 7 ALA E 579 GLN E 582 -1 N GLN E 582 O ASP E 585
SHEET 1 S 3 SER G 90 VAL G 91 0
SHEET 2 S 3 GLN G 120 TYR G 127 -1 O GLY G 125 N SER G 90
SHEET 3 S 3 TYR G 109 TYR G 110 -1 N TYR G 109 O ALA G 121
SHEET 1 T 6 SER G 90 VAL G 91 0
SHEET 2 T 6 GLN G 120 TYR G 127 -1 O GLY G 125 N SER G 90
SHEET 3 T 6 LEU G 133 PHE G 140 -1 O THR G 134 N LYS G 126
SHEET 4 T 6 VAL G 201 HIS G 206 1 O VAL G 202 N ILE G 138
SHEET 5 T 6 ASN G 232 PHE G 236 1 O ASN G 232 N VAL G 203
SHEET 6 T 6 VAL G 248 ILE G 251 1 O ILE G 251 N ALA G 235
SHEET 1 U 8 ILE G 286 PHE G 289 0
SHEET 2 U 8 THR G 340 SER G 344 1 O ILE G 341 N VAL G 287
SHEET 3 U 8 THR G 370 ILE G 373 1 O PHE G 371 N ILE G 342
SHEET 4 U 8 ASP G 388 GLU G 391 1 O GLU G 391 N ILE G 372
SHEET 5 U 8 ASN G 406 ALA G 409 1 O ALA G 409 N LEU G 390
SHEET 6 U 8 ILE G 444 ASP G 448 1 O ASP G 448 N ILE G 408
SHEET 7 U 8 THR G 434 ARG G 438 -1 N LEU G 435 O ALA G 447
SHEET 8 U 8 GLU G 427 TYR G 430 -1 N ALA G 429 O TYR G 436
SHEET 1 V 7 LEU G 380 GLY G 383 0
SHEET 2 V 7 ILE G 398 ASP G 401 1 O ARG G 400 N GLY G 383
SHEET 3 V 7 ILE G 416 ASP G 418 1 O ASP G 418 N PHE G 399
SHEET 4 V 7 THR G 452 GLU G 457 1 O ARG G 454 N PHE G 417
SHEET 5 V 7 LYS G 465 THR G 472 -1 O HIS G 469 N LEU G 453
SHEET 6 V 7 GLY G 475 SER G 478 -1 O LYS G 477 N GLN G 470
SHEET 7 V 7 GLY G 481 LYS G 483 -1 O LYS G 483 N LEU G 476
SHEET 1 W 6 ALA G 487 THR G 489 0
SHEET 2 W 6 TRP G 505 PHE G 507 1 O PHE G 507 N ALA G 488
SHEET 3 W 6 THR G 524 VAL G 526 1 O THR G 524 N LEU G 506
SHEET 4 W 6 THR G 542 SER G 546 1 O THR G 542 N PHE G 525
SHEET 5 W 6 LYS G 562 ILE G 566 1 O LYS G 562 N PHE G 543
SHEET 6 W 6 VAL G 610 ALA G 613 1 O ALA G 613 N PHE G 565
SHEET 1 X 7 VAL G 496 GLN G 498 0
SHEET 2 X 7 THR G 514 ILE G 516 1 O ILE G 516 N LEU G 497
SHEET 3 X 7 ILE G 533 LYS G 535 1 O ILE G 533 N LEU G 515
SHEET 4 X 7 ARG G 551 TYR G 555 1 O GLN G 553 N LEU G 534
SHEET 5 X 7 SER G 593 LEU G 597 1 O THR G 596 N LEU G 554
SHEET 6 X 7 ASP G 585 PHE G 590 -1 N LEU G 586 O LEU G 597
SHEET 7 X 7 ALA G 579 GLN G 582 -1 N GLN G 582 O ASP G 585
SHEET 1 Y 3 SER I 90 VAL I 91 0
SHEET 2 Y 3 GLN I 120 TYR I 127 -1 O GLY I 125 N SER I 90
SHEET 3 Y 3 TYR I 109 TYR I 110 -1 N TYR I 109 O ALA I 121
SHEET 1 Z 6 SER I 90 VAL I 91 0
SHEET 2 Z 6 GLN I 120 TYR I 127 -1 O GLY I 125 N SER I 90
SHEET 3 Z 6 LEU I 133 PHE I 140 -1 O THR I 134 N LYS I 126
SHEET 4 Z 6 VAL I 201 HIS I 206 1 O VAL I 202 N ILE I 138
SHEET 5 Z 6 ASN I 232 PHE I 236 1 O PHE I 236 N GLY I 205
SHEET 6 Z 6 VAL I 248 ILE I 251 1 O ILE I 251 N ALA I 235
SHEET 1 AA 8 ILE I 286 PHE I 289 0
SHEET 2 AA 8 THR I 340 SER I 344 1 O ILE I 341 N VAL I 287
SHEET 3 AA 8 THR I 370 ILE I 373 1 O PHE I 371 N ILE I 342
SHEET 4 AA 8 ASP I 388 GLU I 391 1 O GLU I 391 N ILE I 372
SHEET 5 AA 8 ASN I 406 ALA I 409 1 O ALA I 409 N LEU I 390
SHEET 6 AA 8 ILE I 444 ASP I 448 1 O ASP I 448 N ILE I 408
SHEET 7 AA 8 THR I 434 ARG I 438 -1 N LEU I 435 O ALA I 447
SHEET 8 AA 8 GLU I 427 TYR I 430 -1 N ALA I 429 O TYR I 436
SHEET 1 AB 7 LEU I 380 GLY I 383 0
SHEET 2 AB 7 ILE I 398 ASP I 401 1 O ILE I 398 N ILE I 381
SHEET 3 AB 7 ILE I 416 ASP I 418 1 O ASP I 418 N PHE I 399
SHEET 4 AB 7 THR I 452 SER I 459 1 O ARG I 454 N PHE I 417
SHEET 5 AB 7 PHE I 463 THR I 472 -1 O HIS I 469 N LEU I 453
SHEET 6 AB 7 GLY I 475 SER I 478 -1 O LYS I 477 N GLN I 470
SHEET 7 AB 7 GLY I 481 LYS I 483 -1 O LYS I 483 N LEU I 476
SHEET 1 AC 6 ALA I 487 THR I 489 0
SHEET 2 AC 6 TRP I 505 PHE I 507 1 O PHE I 507 N ALA I 488
SHEET 3 AC 6 THR I 524 VAL I 526 1 O VAL I 526 N LEU I 506
SHEET 4 AC 6 THR I 542 SER I 546 1 O THR I 542 N PHE I 525
SHEET 5 AC 6 LYS I 562 ILE I 566 1 O LYS I 562 N PHE I 543
SHEET 6 AC 6 VAL I 610 ALA I 613 1 O VAL I 611 N PHE I 565
SHEET 1 AD 7 VAL I 496 GLN I 498 0
SHEET 2 AD 7 THR I 514 ILE I 516 1 O ILE I 516 N LEU I 497
SHEET 3 AD 7 ILE I 533 LYS I 535 1 O ILE I 533 N LEU I 515
SHEET 4 AD 7 ARG I 551 TYR I 555 1 O TYR I 555 N LEU I 534
SHEET 5 AD 7 SER I 593 LEU I 597 1 O THR I 596 N LEU I 554
SHEET 6 AD 7 ASP I 585 PHE I 590 -1 N PHE I 590 O SER I 593
SHEET 7 AD 7 ALA I 579 GLN I 582 -1 N THR I 580 O VAL I 587
SHEET 1 AE 3 SER K 90 VAL K 91 0
SHEET 2 AE 3 GLN K 120 TYR K 127 -1 O GLY K 125 N SER K 90
SHEET 3 AE 3 TYR K 109 TYR K 110 -1 N TYR K 109 O ALA K 121
SHEET 1 AF 6 SER K 90 VAL K 91 0
SHEET 2 AF 6 GLN K 120 TYR K 127 -1 O GLY K 125 N SER K 90
SHEET 3 AF 6 LEU K 133 PHE K 140 -1 O THR K 134 N LYS K 126
SHEET 4 AF 6 VAL K 201 HIS K 206 1 O VAL K 202 N ILE K 136
SHEET 5 AF 6 ASN K 232 PHE K 236 1 O ASN K 232 N VAL K 203
SHEET 6 AF 6 VAL K 248 ILE K 251 1 O ILE K 251 N ALA K 235
SHEET 1 AG 8 ILE K 286 PHE K 289 0
SHEET 2 AG 8 THR K 340 SER K 344 1 O ILE K 341 N VAL K 287
SHEET 3 AG 8 THR K 370 ILE K 373 1 O PHE K 371 N ILE K 342
SHEET 4 AG 8 ASP K 388 GLU K 391 1 O GLU K 391 N ILE K 372
SHEET 5 AG 8 ASN K 406 ALA K 409 1 O ALA K 409 N LEU K 390
SHEET 6 AG 8 ILE K 444 ASP K 448 1 O ASP K 448 N ILE K 408
SHEET 7 AG 8 THR K 434 ARG K 438 -1 N LEU K 435 O ALA K 447
SHEET 8 AG 8 GLU K 427 TYR K 430 -1 N ALA K 429 O TYR K 436
SHEET 1 AH 7 LEU K 380 GLY K 383 0
SHEET 2 AH 7 ILE K 398 ASP K 401 1 O ILE K 398 N ILE K 381
SHEET 3 AH 7 ILE K 416 ASP K 418 1 O ASP K 418 N PHE K 399
SHEET 4 AH 7 THR K 452 SER K 459 1 O ARG K 454 N PHE K 417
SHEET 5 AH 7 PHE K 463 THR K 472 -1 O PHE K 463 N SER K 459
SHEET 6 AH 7 GLY K 475 SER K 478 -1 O LYS K 477 N GLN K 470
SHEET 7 AH 7 GLY K 481 LYS K 483 -1 O LYS K 483 N LEU K 476
SHEET 1 AI 6 ALA K 487 THR K 489 0
SHEET 2 AI 6 TRP K 505 PHE K 507 1 O PHE K 507 N ALA K 488
SHEET 3 AI 6 THR K 524 VAL K 526 1 O THR K 524 N LEU K 506
SHEET 4 AI 6 THR K 542 SER K 546 1 O THR K 542 N PHE K 525
SHEET 5 AI 6 LYS K 562 ILE K 566 1 O VAL K 564 N PHE K 545
SHEET 6 AI 6 VAL K 610 ALA K 613 1 O ALA K 613 N PHE K 565
SHEET 1 AJ 7 VAL K 496 GLN K 498 0
SHEET 2 AJ 7 THR K 514 ILE K 516 1 O ILE K 516 N LEU K 497
SHEET 3 AJ 7 ILE K 533 LYS K 535 1 O LYS K 535 N LEU K 515
SHEET 4 AJ 7 ARG K 551 TYR K 555 1 O TYR K 555 N LEU K 534
SHEET 5 AJ 7 SER K 593 ILE K 598 1 O THR K 596 N LEU K 554
SHEET 6 AJ 7 ASP K 585 PHE K 590 -1 N PHE K 590 O SER K 593
SHEET 7 AJ 7 ALA K 579 GLN K 582 -1 N GLN K 582 O ASP K 585
LINK O THR A 118 CA CA A 621 1555 1555 2.32
LINK OE1 GLN A 120 CA CA A 621 1555 1555 2.35
LINK O SER A 144 CA CA A 621 1555 1555 2.41
LINK OD2 ASP A 153 CA CA A 621 1555 1555 2.34
LINK OD1 ASP A 157 CA CA A 621 1555 1555 2.45
LINK OD2 ASP A 157 CA CA A 621 1555 1555 2.37
LINK OE1 GLU A 254 CA CA A 620 1555 1555 2.36
LINK OD1 ASP A 276 CA CA A 620 1555 1555 2.40
LINK OD2 ASP A 276 CA CA A 620 1555 1555 2.37
LINK O ASN A 284 CA CA A 620 1555 1555 2.38
LINK OD1 ASN A 285 CA CA A 620 1555 1555 2.34
LINK O SER A 375 CA CA A 619 1555 1555 2.40
LINK O GLY A 377 CA CA A 619 1555 1555 2.38
LINK OD2 ASP A 379 CA CA A 619 1555 1555 2.35
LINK O GLY A 384 CA CA A 617 1555 1555 2.35
LINK O GLY A 386 CA CA A 617 1555 1555 2.37
LINK OD2 ASP A 388 CA CA A 617 1555 1555 2.36
LINK O GLY A 392 CA CA A 619 1555 1555 2.32
LINK O ARG A 393 CA CA A 618 1555 1555 2.38
LINK O ASP A 394 CA CA A 619 1555 1555 2.35
LINK O GLY A 395 CA CA A 618 1555 1555 2.37
LINK OD1 ASP A 397 CA CA A 619 1555 1555 2.37
LINK OD2 ASP A 397 CA CA A 618 1555 1555 2.43
LINK OD2 ASP A 397 CA CA A 619 1555 1555 2.59
LINK OD1 ASP A 401 CA CA A 617 1555 1555 2.39
LINK OD2 ASP A 401 CA CA A 617 1555 1555 2.38
LINK O GLY A 403 CA CA A 617 1555 1555 2.35
LINK OD1 ASN A 406 CA CA A 617 1555 1555 2.36
LINK O GLY A 410 CA CA A 618 1555 1555 2.34
LINK O LYS A 412 CA CA A 618 1555 1555 2.35
LINK OD1 ASN A 415 CA CA A 618 1555 1555 2.39
LINK O GLY A 491 CA CA A 614 1555 1555 2.31
LINK O GLY A 493 CA CA A 614 1555 1555 2.35
LINK OD2 ASP A 495 CA CA A 614 1555 1555 2.33
LINK O GLY A 508 CA CA A 614 1555 1555 2.32
LINK O ASN A 509 CA CA A 616 1555 1555 2.34
LINK O ALA A 510 CA CA A 614 1555 1555 2.30
LINK O GLY A 511 CA CA A 616 1555 1555 2.37
LINK OD1 ASP A 513 CA CA A 614 1555 1555 2.32
LINK OD2 ASP A 513 CA CA A 616 1555 1555 2.33
LINK O GLY A 527 CA CA A 616 1555 1555 2.36
LINK O GLY A 528 CA CA A 615 1555 1555 2.36
LINK O SER A 529 CA CA A 616 1555 1555 2.35
LINK O GLY A 530 CA CA A 615 1555 1555 2.36
LINK OD1 ASP A 532 CA CA A 616 1555 1555 2.35
LINK OD2 ASP A 532 CA CA A 615 1555 1555 2.32
LINK O PHE A 549 CA CA A 615 1555 1555 2.32
LINK OD1 ASP A 552 CA CA A 615 1555 1555 2.36
LINK O THR C 118 CA CA C 621 1555 1555 2.34
LINK OE1 GLN C 120 CA CA C 621 1555 1555 2.36
LINK O SER C 144 CA CA C 621 1555 1555 2.38
LINK OD2 ASP C 153 CA CA C 621 1555 1555 2.31
LINK OD1 ASP C 157 CA CA C 621 1555 1555 2.46
LINK OD2 ASP C 157 CA CA C 621 1555 1555 2.34
LINK OE1 GLU C 254 CA CA C 620 1555 1555 2.37
LINK OD1 ASP C 276 CA CA C 620 1555 1555 2.40
LINK OD2 ASP C 276 CA CA C 620 1555 1555 2.39
LINK O ASN C 284 CA CA C 620 1555 1555 2.36
LINK OD1 ASN C 285 CA CA C 620 1555 1555 2.35
LINK O SER C 375 CA CA C 619 1555 1555 2.39
LINK O GLY C 377 CA CA C 619 1555 1555 2.40
LINK OD2 ASP C 379 CA CA C 619 1555 1555 2.36
LINK O GLY C 384 CA CA C 617 1555 1555 2.37
LINK O GLY C 386 CA CA C 617 1555 1555 2.37
LINK OD2 ASP C 388 CA CA C 617 1555 1555 2.39
LINK O GLY C 392 CA CA C 619 1555 1555 2.31
LINK O ARG C 393 CA CA C 618 1555 1555 2.38
LINK O ASP C 394 CA CA C 619 1555 1555 2.35
LINK O GLY C 395 CA CA C 618 1555 1555 2.37
LINK OD1 ASP C 397 CA CA C 619 1555 1555 2.36
LINK OD2 ASP C 397 CA CA C 619 1555 1555 2.63
LINK OD2 ASP C 397 CA CA C 618 1555 1555 2.44
LINK OD1 ASP C 401 CA CA C 617 1555 1555 2.42
LINK OD2 ASP C 401 CA CA C 617 1555 1555 2.41
LINK O GLY C 403 CA CA C 617 1555 1555 2.38
LINK OD1 ASN C 406 CA CA C 617 1555 1555 2.37
LINK O GLY C 410 CA CA C 618 1555 1555 2.35
LINK O LYS C 412 CA CA C 618 1555 1555 2.37
LINK OD1 ASN C 415 CA CA C 618 1555 1555 2.39
LINK O GLY C 491 CA CA C 614 1555 1555 2.33
LINK O GLY C 493 CA CA C 614 1555 1555 2.35
LINK OD2 ASP C 495 CA CA C 614 1555 1555 2.32
LINK O GLY C 508 CA CA C 614 1555 1555 2.35
LINK O ASN C 509 CA CA C 616 1555 1555 2.33
LINK O ALA C 510 CA CA C 614 1555 1555 2.33
LINK O GLY C 511 CA CA C 616 1555 1555 2.39
LINK OD1 ASP C 513 CA CA C 614 1555 1555 2.31
LINK OD2 ASP C 513 CA CA C 616 1555 1555 2.34
LINK O GLY C 527 CA CA C 616 1555 1555 2.38
LINK O GLY C 528 CA CA C 615 1555 1555 2.36
LINK O SER C 529 CA CA C 616 1555 1555 2.36
LINK O GLY C 530 CA CA C 615 1555 1555 2.34
LINK OD1 ASP C 532 CA CA C 616 1555 1555 2.34
LINK OD2 ASP C 532 CA CA C 615 1555 1555 2.33
LINK O PHE C 549 CA CA C 615 1555 1555 2.31
LINK OD1 ASP C 552 CA CA C 615 1555 1555 2.38
LINK O THR E 118 CA CA E 621 1555 1555 2.35
LINK OE1 GLN E 120 CA CA E 621 1555 1555 2.38
LINK O SER E 144 CA CA E 621 1555 1555 2.42
LINK OD2 ASP E 153 CA CA E 621 1555 1555 2.32
LINK OD1 ASP E 157 CA CA E 621 1555 1555 2.46
LINK OD2 ASP E 157 CA CA E 621 1555 1555 2.33
LINK OE1 GLU E 254 CA CA E 620 1555 1555 2.35
LINK OD1 ASP E 276 CA CA E 620 1555 1555 2.39
LINK OD2 ASP E 276 CA CA E 620 1555 1555 2.39
LINK O ASN E 284 CA CA E 620 1555 1555 2.38
LINK OD1 ASN E 285 CA CA E 620 1555 1555 2.34
LINK O SER E 375 CA CA E 619 1555 1555 2.39
LINK O GLY E 377 CA CA E 619 1555 1555 2.38
LINK OD2 ASP E 379 CA CA E 619 1555 1555 2.37
LINK O GLY E 384 CA CA E 617 1555 1555 2.35
LINK O GLY E 386 CA CA E 617 1555 1555 2.36
LINK OD2 ASP E 388 CA CA E 617 1555 1555 2.37
LINK O GLY E 392 CA CA E 619 1555 1555 2.33
LINK O ARG E 393 CA CA E 618 1555 1555 2.39
LINK O ASP E 394 CA CA E 619 1555 1555 2.35
LINK O GLY E 395 CA CA E 618 1555 1555 2.35
LINK OD1 ASP E 397 CA CA E 619 1555 1555 2.37
LINK OD2 ASP E 397 CA CA E 618 1555 1555 2.42
LINK OD2 ASP E 397 CA CA E 619 1555 1555 2.58
LINK OD1 ASP E 401 CA CA E 617 1555 1555 2.41
LINK OD2 ASP E 401 CA CA E 617 1555 1555 2.39
LINK O GLY E 403 CA CA E 617 1555 1555 2.35
LINK OD1 ASN E 406 CA CA E 617 1555 1555 2.35
LINK O GLY E 410 CA CA E 618 1555 1555 2.37
LINK O LYS E 412 CA CA E 618 1555 1555 2.36
LINK OD1 ASN E 415 CA CA E 618 1555 1555 2.40
LINK O GLY E 491 CA CA E 614 1555 1555 2.32
LINK O GLY E 493 CA CA E 614 1555 1555 2.35
LINK OD2 ASP E 495 CA CA E 614 1555 1555 2.33
LINK O GLY E 508 CA CA E 614 1555 1555 2.34
LINK O ASN E 509 CA CA E 616 1555 1555 2.35
LINK O ALA E 510 CA CA E 614 1555 1555 2.33
LINK O GLY E 511 CA CA E 616 1555 1555 2.35
LINK OD1 ASP E 513 CA CA E 614 1555 1555 2.32
LINK OD2 ASP E 513 CA CA E 616 1555 1555 2.33
LINK O GLY E 527 CA CA E 616 1555 1555 2.33
LINK O GLY E 528 CA CA E 615 1555 1555 2.37
LINK O SER E 529 CA CA E 616 1555 1555 2.36
LINK O GLY E 530 CA CA E 615 1555 1555 2.34
LINK OD1 ASP E 532 CA CA E 616 1555 1555 2.35
LINK OD2 ASP E 532 CA CA E 615 1555 1555 2.32
LINK O PHE E 549 CA CA E 615 1555 1555 2.33
LINK OD1 ASP E 552 CA CA E 615 1555 1555 2.37
LINK O THR G 118 CA CA G 621 1555 1555 2.35
LINK OE1 GLN G 120 CA CA G 621 1555 1555 2.38
LINK O SER G 144 CA CA G 621 1555 1555 2.41
LINK OD2 ASP G 153 CA CA G 621 1555 1555 2.32
LINK OD1 ASP G 157 CA CA G 621 1555 1555 2.51
LINK OD2 ASP G 157 CA CA G 621 1555 1555 2.33
LINK OE1 GLU G 254 CA CA G 620 1555 1555 2.36
LINK OD1 ASP G 276 CA CA G 620 1555 1555 2.41
LINK OD2 ASP G 276 CA CA G 620 1555 1555 2.39
LINK O ASN G 284 CA CA G 620 1555 1555 2.37
LINK OD1 ASN G 285 CA CA G 620 1555 1555 2.35
LINK O SER G 375 CA CA G 619 1555 1555 2.39
LINK O GLY G 377 CA CA G 619 1555 1555 2.37
LINK OD2 ASP G 379 CA CA G 619 1555 1555 2.38
LINK O GLY G 384 CA CA G 617 1555 1555 2.35
LINK O GLY G 386 CA CA G 617 1555 1555 2.38
LINK OD2 ASP G 388 CA CA G 617 1555 1555 2.37
LINK O GLY G 392 CA CA G 619 1555 1555 2.34
LINK O ARG G 393 CA CA G 618 1555 1555 2.37
LINK O ASP G 394 CA CA G 619 1555 1555 2.34
LINK O GLY G 395 CA CA G 618 1555 1555 2.36
LINK OD1 ASP G 397 CA CA G 619 1555 1555 2.35
LINK OD2 ASP G 397 CA CA G 619 1555 1555 2.56
LINK OD2 ASP G 397 CA CA G 618 1555 1555 2.43
LINK OD1 ASP G 401 CA CA G 617 1555 1555 2.40
LINK OD2 ASP G 401 CA CA G 617 1555 1555 2.39
LINK O GLY G 403 CA CA G 617 1555 1555 2.35
LINK OD1 ASN G 406 CA CA G 617 1555 1555 2.36
LINK O GLY G 410 CA CA G 618 1555 1555 2.36
LINK O LYS G 412 CA CA G 618 1555 1555 2.37
LINK OD1 ASN G 415 CA CA G 618 1555 1555 2.39
LINK O GLY G 491 CA CA G 614 1555 1555 2.34
LINK O GLY G 493 CA CA G 614 1555 1555 2.36
LINK OD2 ASP G 495 CA CA G 614 1555 1555 2.33
LINK O GLY G 508 CA CA G 614 1555 1555 2.35
LINK O ASN G 509 CA CA G 616 1555 1555 2.36
LINK O ALA G 510 CA CA G 614 1555 1555 2.31
LINK O GLY G 511 CA CA G 616 1555 1555 2.40
LINK OD1 ASP G 513 CA CA G 614 1555 1555 2.32
LINK OD2 ASP G 513 CA CA G 616 1555 1555 2.35
LINK O GLY G 527 CA CA G 616 1555 1555 2.34
LINK O GLY G 528 CA CA G 615 1555 1555 2.36
LINK O SER G 529 CA CA G 616 1555 1555 2.35
LINK O GLY G 530 CA CA G 615 1555 1555 2.35
LINK OD1 ASP G 532 CA CA G 616 1555 1555 2.33
LINK OD2 ASP G 532 CA CA G 615 1555 1555 2.44
LINK OD2 ASP G 532 CA CA G 616 1555 1555 2.56
LINK O PHE G 549 CA CA G 615 1555 1555 2.35
LINK OD1 ASP G 552 CA CA G 615 1555 1555 2.38
LINK O THR I 118 CA CA I 621 1555 1555 2.33
LINK OE1 GLN I 120 CA CA I 621 1555 1555 2.37
LINK O SER I 144 CA CA I 621 1555 1555 2.38
LINK OD2 ASP I 153 CA CA I 621 1555 1555 2.35
LINK OD1 ASP I 157 CA CA I 621 1555 1555 2.47
LINK OD2 ASP I 157 CA CA I 621 1555 1555 2.37
LINK OE1 GLU I 254 CA CA I 620 1555 1555 2.35
LINK OD1 ASP I 276 CA CA I 620 1555 1555 2.39
LINK OD2 ASP I 276 CA CA I 620 1555 1555 2.33
LINK O ASN I 284 CA CA I 620 1555 1555 2.39
LINK OD1 ASN I 285 CA CA I 620 1555 1555 2.35
LINK O SER I 375 CA CA I 619 1555 1555 2.39
LINK O GLY I 377 CA CA I 619 1555 1555 2.38
LINK OD2 ASP I 379 CA CA I 619 1555 1555 2.34
LINK O GLY I 384 CA CA I 617 1555 1555 2.35
LINK O GLY I 386 CA CA I 617 1555 1555 2.36
LINK OD2 ASP I 388 CA CA I 617 1555 1555 2.36
LINK O GLY I 392 CA CA I 619 1555 1555 2.34
LINK O ARG I 393 CA CA I 618 1555 1555 2.38
LINK O ASP I 394 CA CA I 619 1555 1555 2.35
LINK O GLY I 395 CA CA I 618 1555 1555 2.38
LINK OD1 ASP I 397 CA CA I 619 1555 1555 2.37
LINK OD2 ASP I 397 CA CA I 618 1555 1555 2.43
LINK OD2 ASP I 397 CA CA I 619 1555 1555 2.54
LINK OD1 ASP I 401 CA CA I 617 1555 1555 2.41
LINK OD2 ASP I 401 CA CA I 617 1555 1555 2.38
LINK O GLY I 403 CA CA I 617 1555 1555 2.34
LINK OD1 ASN I 406 CA CA I 617 1555 1555 2.36
LINK O GLY I 410 CA CA I 618 1555 1555 2.37
LINK O LYS I 412 CA CA I 618 1555 1555 2.33
LINK OD1 ASN I 415 CA CA I 618 1555 1555 2.40
LINK O GLY I 491 CA CA I 614 1555 1555 2.34
LINK O GLY I 493 CA CA I 614 1555 1555 2.34
LINK OD2 ASP I 495 CA CA I 614 1555 1555 2.32
LINK O GLY I 508 CA CA I 614 1555 1555 2.35
LINK O ASN I 509 CA CA I 616 1555 1555 2.38
LINK O ALA I 510 CA CA I 614 1555 1555 2.31
LINK O GLY I 511 CA CA I 616 1555 1555 2.39
LINK OD1 ASP I 513 CA CA I 614 1555 1555 2.32
LINK OD2 ASP I 513 CA CA I 616 1555 1555 2.33
LINK O GLY I 527 CA CA I 616 1555 1555 2.34
LINK O GLY I 528 CA CA I 615 1555 1555 2.35
LINK O SER I 529 CA CA I 616 1555 1555 2.32
LINK O GLY I 530 CA CA I 615 1555 1555 2.36
LINK OD1 ASP I 532 CA CA I 616 1555 1555 2.32
LINK OD2 ASP I 532 CA CA I 616 1555 1555 2.48
LINK OD2 ASP I 532 CA CA I 615 1555 1555 2.44
LINK O PHE I 549 CA CA I 615 1555 1555 2.33
LINK OD1 ASP I 552 CA CA I 615 1555 1555 2.39
LINK O THR K 118 CA CA K 621 1555 1555 2.35
LINK OE1 GLN K 120 CA CA K 621 1555 1555 2.37
LINK O SER K 144 CA CA K 621 1555 1555 2.42
LINK OD2 ASP K 153 CA CA K 621 1555 1555 2.33
LINK OD1 ASP K 157 CA CA K 621 1555 1555 2.48
LINK OD2 ASP K 157 CA CA K 621 1555 1555 2.32
LINK OE1 GLU K 254 CA CA K 620 1555 1555 2.35
LINK OD1 ASP K 276 CA CA K 620 1555 1555 2.39
LINK OD2 ASP K 276 CA CA K 620 1555 1555 2.36
LINK O ASN K 284 CA CA K 620 1555 1555 2.36
LINK OD1 ASN K 285 CA CA K 620 1555 1555 2.35
LINK O SER K 375 CA CA K 619 1555 1555 2.39
LINK O GLY K 377 CA CA K 619 1555 1555 2.33
LINK OD2 ASP K 379 CA CA K 619 1555 1555 2.37
LINK O GLY K 384 CA CA K 617 1555 1555 2.34
LINK O GLY K 386 CA CA K 617 1555 1555 2.36
LINK OD2 ASP K 388 CA CA K 617 1555 1555 2.36
LINK O GLY K 392 CA CA K 619 1555 1555 2.30
LINK O ARG K 393 CA CA K 618 1555 1555 2.38
LINK O ASP K 394 CA CA K 619 1555 1555 2.33
LINK O GLY K 395 CA CA K 618 1555 1555 2.37
LINK OD1 ASP K 397 CA CA K 619 1555 1555 2.36
LINK OD2 ASP K 397 CA CA K 618 1555 1555 2.41
LINK OD2 ASP K 397 CA CA K 619 1555 1555 2.56
LINK OD1 ASP K 401 CA CA K 617 1555 1555 2.42
LINK OD2 ASP K 401 CA CA K 617 1555 1555 2.39
LINK O GLY K 403 CA CA K 617 1555 1555 2.34
LINK OD1 ASN K 406 CA CA K 617 1555 1555 2.35
LINK O GLY K 410 CA CA K 618 1555 1555 2.34
LINK O LYS K 412 CA CA K 618 1555 1555 2.34
LINK OD1 ASN K 415 CA CA K 618 1555 1555 2.39
LINK O GLY K 491 CA CA K 614 1555 1555 2.34
LINK O GLY K 493 CA CA K 614 1555 1555 2.35
LINK OD2 ASP K 495 CA CA K 614 1555 1555 2.34
LINK O GLY K 508 CA CA K 614 1555 1555 2.34
LINK O ASN K 509 CA CA K 616 1555 1555 2.35
LINK O ALA K 510 CA CA K 614 1555 1555 2.31
LINK O GLY K 511 CA CA K 616 1555 1555 2.37
LINK OD1 ASP K 513 CA CA K 614 1555 1555 2.28
LINK OD2 ASP K 513 CA CA K 614 1555 1555 2.48
LINK OD2 ASP K 513 CA CA K 616 1555 1555 2.48
LINK O GLY K 527 CA CA K 616 1555 1555 2.35
LINK O GLY K 528 CA CA K 615 1555 1555 2.34
LINK O SER K 529 CA CA K 616 1555 1555 2.34
LINK O GLY K 530 CA CA K 615 1555 1555 2.37
LINK OD1 ASP K 532 CA CA K 616 1555 1555 2.29
LINK OD2 ASP K 532 CA CA K 616 1555 1555 2.44
LINK OD2 ASP K 532 CA CA K 615 1555 1555 2.44
LINK O PHE K 549 CA CA K 615 1555 1555 2.34
LINK OD1 ASP K 552 CA CA K 615 1555 1555 2.37
LINK CA CA A 615 O HOH A 705 1555 1555 2.31
LINK CA CA A 620 O HOH A 625 1555 1555 2.36
LINK CA CA A 620 O HOH A 638 1555 1555 2.36
LINK CA CA A 621 O HOH A 678 1555 1555 2.31
LINK CA CA C 615 O HOH C 751 1555 1555 2.33
LINK CA CA C 620 O HOH C 654 1555 1555 2.37
LINK CA CA C 620 O HOH C 643 1555 1555 2.34
LINK CA CA C 621 O HOH C 633 1555 1555 2.35
LINK CA CA E 615 O HOH E 756 1555 1555 2.31
LINK CA CA E 620 O HOH E 624 1555 1555 2.36
LINK CA CA E 620 O HOH E 625 1555 1555 2.39
LINK CA CA E 621 O HOH E 653 1555 1555 2.33
LINK CA CA G 615 O HOH G 642 1555 1555 2.33
LINK CA CA G 620 O HOH G 624 1555 1555 2.35
LINK CA CA G 620 O HOH G 650 1555 1555 2.36
LINK CA CA G 621 O HOH G 630 1555 1555 2.35
LINK CA CA I 615 O HOH I 847 1555 1555 2.33
LINK CA CA I 620 O HOH I 622 1555 1555 2.37
LINK CA CA I 620 O HOH I 624 1555 1555 2.36
LINK CA CA I 621 O HOH I 631 1555 1555 2.33
LINK CA CA K 615 O HOH K 781 1555 1555 2.34
LINK CA CA K 620 O HOH K 662 1555 1555 2.35
LINK CA CA K 620 O HOH K 637 1555 1555 2.35
LINK CA CA K 621 O HOH K 641 1555 1555 2.33
CRYST1 202.401 202.401 317.731 90.00 90.00 120.00 H 3 54
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 0.004941 0.002853 0.000000 0.00000
SCALE2 0.000000 0.005705 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003147 0.00000
TER 4602 ALA A 613
TER 9204 ALA C 613
TER 13806 ALA E 613
TER 18408 ALA G 613
TER 23010 ALA I 613
TER 27612 ALA K 613
MASTER 1301 0 48 126 222 0 0 629575 6 0 288
END |