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HEADER CELL ADHESION 15-MAR-17 5V5V
TITLE COMPLEX OF NLGN2 WITH MDGA1 IG1-IG2
CAVEAT 5V5V RESIDUE SER 246 AND RESIDUE GLU 247 THAT ARE NEXT TO EACH
CAVEAT 2 5V5V OTHER IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED:
CAVEAT 3 5V5V DISTANCE BETWEEN C AND N ATOMS IS 2.87A.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN-2;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: MAM DOMAIN-CONTAINING GLYCOSYLPHOSPHATIDYLINOSITOL ANCHOR
COMPND 7 PROTEIN 1;
COMPND 8 CHAIN: G, H, I, J, K, L;
COMPND 9 SYNONYM: GPI AND MAM PROTEIN,GPIM,GLYCOSYLPHOSPHATIDYLINOSITOL-MAM,
COMPND 10 MAM DOMAIN-CONTAINING PROTEIN 3;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: NLGN2;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: MDGA1, MAMDC3;
SOURCE 14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE
KEYWDS SYNAPTIC ORGANIZERS, REGULATORY COMPLEX, NEUROLIGINS, MDGAS, CELL
KEYWDS 2 ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.P.GANGWAR,M.MACHIUS,G.RUDENKO
REVDAT 1 05-JUL-17 5V5V 0
JRNL AUTH S.P.GANGWAR,X.ZHONG,S.SESHADRINATHAN,H.CHEN,M.MACHIUS,
JRNL AUTH 2 G.RUDENKO
JRNL TITL MOLECULAR MECHANISM OF MDGA1: REGULATION OF NEUROLIGIN
JRNL TITL 2 2:NEUREXIN TRANS-SYNAPTIC BRIDGES.
JRNL REF NEURON V. 94 1132 2017
JRNL REFN ISSN 1097-4199
JRNL PMID 28641112
JRNL DOI 10.1016/J.NEURON.2017.06.009
REMARK 2
REMARK 2 RESOLUTION. 4.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.3
REMARK 3 NUMBER OF REFLECTIONS : 43940
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) : 0.290
REMARK 3 R VALUE (WORKING SET) : 0.289
REMARK 3 FREE R VALUE : 0.319
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2200
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 4.11
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 4.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1369
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 34.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.3530
REMARK 3 BIN FREE R VALUE SET COUNT : 68
REMARK 3 BIN FREE R VALUE : 0.4070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 33540
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 112.2
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.26000
REMARK 3 B22 (A**2) : 15.66000
REMARK 3 B33 (A**2) : -11.96000
REMARK 3 B12 (A**2) : 0.59000
REMARK 3 B13 (A**2) : 0.79000
REMARK 3 B23 (A**2) : -6.26000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 1.244
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 1.012
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 176.476
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.790
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.741
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 34362 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 31248 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 46680 ; 1.550 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 72408 ; 1.115 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4194 ; 9.001 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1626 ;37.257 ;23.911
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5466 ;20.174 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 228 ;17.476 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5124 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 38178 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 7122 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 30
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 51 609 B 51 609 33738 0.01 0.05
REMARK 3 2 A 51 609 C 51 609 33640 0.01 0.05
REMARK 3 3 A 51 609 D 51 609 33672 0.01 0.05
REMARK 3 4 A 51 609 E 51 609 33646 0.01 0.05
REMARK 3 5 A 51 609 F 51 609 33664 0.01 0.05
REMARK 3 6 G 24 234 H 24 234 10048 0.01 0.05
REMARK 3 7 G 24 234 I 24 234 10030 0.01 0.05
REMARK 3 8 G 24 234 J 24 234 10042 0.01 0.05
REMARK 3 9 G 24 234 K 24 234 10036 0.01 0.05
REMARK 3 10 G 24 234 L 24 234 9992 0.01 0.05
REMARK 3 11 B 51 609 C 51 609 33650 0.01 0.05
REMARK 3 12 B 51 609 D 51 609 33664 0.01 0.05
REMARK 3 13 B 51 609 E 51 609 33662 0.01 0.05
REMARK 3 14 B 51 609 F 51 609 33688 0.01 0.05
REMARK 3 15 C 51 609 D 51 609 33674 0.01 0.05
REMARK 3 16 C 51 609 E 51 609 33738 0.01 0.05
REMARK 3 17 C 51 609 F 51 609 33702 0.01 0.05
REMARK 3 18 D 51 609 E 51 609 33666 0.01 0.05
REMARK 3 19 D 51 609 F 51 609 33754 0.01 0.05
REMARK 3 20 E 51 609 F 51 609 33714 0.01 0.05
REMARK 3 21 H 24 234 I 24 234 10022 0.01 0.05
REMARK 3 22 H 24 234 J 24 234 10042 0.01 0.05
REMARK 3 23 H 24 234 K 24 234 10024 0.01 0.05
REMARK 3 24 H 24 234 L 24 234 9986 0.01 0.05
REMARK 3 25 I 24 234 J 24 234 10066 0.01 0.05
REMARK 3 26 I 24 234 K 24 234 10058 0.02 0.05
REMARK 3 27 I 24 234 L 24 234 10038 0.02 0.05
REMARK 3 28 J 24 234 K 24 234 10090 0.01 0.05
REMARK 3 29 J 24 234 L 24 234 10048 0.01 0.05
REMARK 3 30 K 24 234 L 24 234 10038 0.01 0.05
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 51 A 609
REMARK 3 ORIGIN FOR THE GROUP (A): -58.8092 -23.6378 -23.0024
REMARK 3 T TENSOR
REMARK 3 T11: 0.2962 T22: 0.0993
REMARK 3 T33: 0.7611 T12: 0.0024
REMARK 3 T13: 0.2850 T23: 0.1650
REMARK 3 L TENSOR
REMARK 3 L11: 4.3102 L22: 2.9175
REMARK 3 L33: 4.9227 L12: 1.0117
REMARK 3 L13: -1.9248 L23: -0.2210
REMARK 3 S TENSOR
REMARK 3 S11: -0.8323 S12: 0.2277 S13: -0.6582
REMARK 3 S21: 0.1037 S22: 0.3593 S23: 0.1019
REMARK 3 S31: 0.9804 S32: -0.1963 S33: 0.4730
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 51 B 609
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9930 -21.1977 -55.5335
REMARK 3 T TENSOR
REMARK 3 T11: 0.2283 T22: 0.0736
REMARK 3 T33: 0.7895 T12: 0.0155
REMARK 3 T13: 0.2306 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 5.0015 L22: 3.0219
REMARK 3 L33: 5.2218 L12: -0.4136
REMARK 3 L13: -2.1849 L23: 0.1675
REMARK 3 S TENSOR
REMARK 3 S11: -0.8839 S12: -0.3416 S13: -0.7709
REMARK 3 S21: -0.1138 S22: 0.3808 S23: -0.2802
REMARK 3 S31: 0.8750 S32: -0.0366 S33: 0.5031
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 51 C 609
REMARK 3 ORIGIN FOR THE GROUP (A): -70.8312 -18.6913-102.3132
REMARK 3 T TENSOR
REMARK 3 T11: 0.6220 T22: 0.1803
REMARK 3 T33: 1.0639 T12: -0.0836
REMARK 3 T13: 0.5038 T23: -0.2722
REMARK 3 L TENSOR
REMARK 3 L11: 5.5799 L22: 5.1266
REMARK 3 L33: 3.9823 L12: 1.9046
REMARK 3 L13: -0.1734 L23: -0.6452
REMARK 3 S TENSOR
REMARK 3 S11: -0.8987 S12: 0.8701 S13: -1.0112
REMARK 3 S21: -0.7717 S22: 0.0924 S23: 0.0212
REMARK 3 S31: 0.9291 S32: 0.0287 S33: 0.8063
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 51 D 609
REMARK 3 ORIGIN FOR THE GROUP (A): -43.6756 33.6914 -90.6551
REMARK 3 T TENSOR
REMARK 3 T11: 1.3492 T22: 0.2222
REMARK 3 T33: 1.4489 T12: -0.3505
REMARK 3 T13: 0.0220 T23: 0.3097
REMARK 3 L TENSOR
REMARK 3 L11: 4.4872 L22: 5.2630
REMARK 3 L33: 2.2414 L12: 1.2618
REMARK 3 L13: 0.7936 L23: 0.8957
REMARK 3 S TENSOR
REMARK 3 S11: -0.0477 S12: -0.1772 S13: 1.1111
REMARK 3 S21: -0.7344 S22: -0.0324 S23: -0.0614
REMARK 3 S31: -1.6065 S32: 0.3210 S33: 0.0801
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 51 E 609
REMARK 3 ORIGIN FOR THE GROUP (A): -25.3521 -8.2283-163.1348
REMARK 3 T TENSOR
REMARK 3 T11: 0.6462 T22: 0.5277
REMARK 3 T33: 0.9867 T12: -0.2122
REMARK 3 T13: 0.4166 T23: 0.2500
REMARK 3 L TENSOR
REMARK 3 L11: 4.0221 L22: 6.0572
REMARK 3 L33: 3.8843 L12: -1.9750
REMARK 3 L13: 0.5681 L23: 0.0163
REMARK 3 S TENSOR
REMARK 3 S11: -0.6843 S12: -0.5899 S13: -0.6460
REMARK 3 S21: 0.8324 S22: 0.0891 S23: 0.0172
REMARK 3 S31: 0.8511 S32: -0.2624 S33: 0.5951
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 51 F 609
REMARK 3 ORIGIN FOR THE GROUP (A): -53.3110 44.7928-167.6279
REMARK 3 T TENSOR
REMARK 3 T11: 1.5555 T22: 0.8911
REMARK 3 T33: 1.3211 T12: 0.7295
REMARK 3 T13: -0.0371 T23: -0.3574
REMARK 3 L TENSOR
REMARK 3 L11: 3.0138 L22: 4.8197
REMARK 3 L33: 3.0887 L12: -0.7047
REMARK 3 L13: 0.2363 L23: 0.2129
REMARK 3 S TENSOR
REMARK 3 S11: 0.1100 S12: -0.0588 S13: 0.7965
REMARK 3 S21: 0.4144 S22: -0.1676 S23: 0.1910
REMARK 3 S31: -1.7191 S32: -0.4525 S33: 0.0576
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 24 G 127
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5384 -0.9299 -79.0615
REMARK 3 T TENSOR
REMARK 3 T11: 0.9802 T22: 0.9486
REMARK 3 T33: 1.0704 T12: -0.0460
REMARK 3 T13: 0.1742 T23: 0.1847
REMARK 3 L TENSOR
REMARK 3 L11: 7.1350 L22: 1.2575
REMARK 3 L33: 0.9506 L12: -1.8337
REMARK 3 L13: -1.1834 L23: -0.4034
REMARK 3 S TENSOR
REMARK 3 S11: 0.2283 S12: 0.1945 S13: 0.7582
REMARK 3 S21: -0.4524 S22: -0.2617 S23: -0.6570
REMARK 3 S31: 0.2058 S32: 0.1886 S33: 0.0334
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 128 G 234
REMARK 3 ORIGIN FOR THE GROUP (A): -48.4383 2.2214 -55.3538
REMARK 3 T TENSOR
REMARK 3 T11: 0.3001 T22: 0.8023
REMARK 3 T33: 0.6842 T12: -0.2109
REMARK 3 T13: -0.3447 T23: 0.1072
REMARK 3 L TENSOR
REMARK 3 L11: 7.7906 L22: 4.2323
REMARK 3 L33: 11.6355 L12: -1.8087
REMARK 3 L13: -8.4767 L23: -0.9532
REMARK 3 S TENSOR
REMARK 3 S11: 0.0725 S12: 0.1160 S13: 0.1292
REMARK 3 S21: -0.1753 S22: 0.1911 S23: 0.5432
REMARK 3 S31: -0.1220 S32: -0.3001 S33: -0.2636
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 24 H 127
REMARK 3 ORIGIN FOR THE GROUP (A): -48.3253 -7.0954 3.1039
REMARK 3 T TENSOR
REMARK 3 T11: 1.0614 T22: 0.8757
REMARK 3 T33: 1.0107 T12: 0.0286
REMARK 3 T13: 0.0134 T23: 0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 9.3796 L22: 1.0972
REMARK 3 L33: 3.7541 L12: 2.2995
REMARK 3 L13: -4.0405 L23: -0.6430
REMARK 3 S TENSOR
REMARK 3 S11: -0.0310 S12: -0.6195 S13: 0.3514
REMARK 3 S21: 0.3978 S22: -0.0540 S23: 0.6436
REMARK 3 S31: 0.1544 S32: -0.0668 S33: 0.0850
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 128 H 234
REMARK 3 ORIGIN FOR THE GROUP (A): -18.3926 -0.3606 -19.8017
REMARK 3 T TENSOR
REMARK 3 T11: 0.3903 T22: 0.7584
REMARK 3 T33: 0.5957 T12: 0.2133
REMARK 3 T13: -0.3473 T23: -0.1046
REMARK 3 L TENSOR
REMARK 3 L11: 10.6901 L22: 4.9598
REMARK 3 L33: 12.1541 L12: 1.6191
REMARK 3 L13: -8.6472 L23: -0.2716
REMARK 3 S TENSOR
REMARK 3 S11: 0.1459 S12: -0.1522 S13: -0.0331
REMARK 3 S21: -0.1344 S22: 0.1205 S23: -0.5682
REMARK 3 S31: -0.2346 S32: 0.1931 S33: -0.2665
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 24 I 127
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5065 0.3341-139.9808
REMARK 3 T TENSOR
REMARK 3 T11: 2.0055 T22: 1.0791
REMARK 3 T33: 1.7000 T12: 0.1014
REMARK 3 T13: -0.5869 T23: 0.1813
REMARK 3 L TENSOR
REMARK 3 L11: 1.6367 L22: 10.6923
REMARK 3 L33: 2.3264 L12: -2.8057
REMARK 3 L13: -1.6005 L23: 2.5941
REMARK 3 S TENSOR
REMARK 3 S11: -0.1216 S12: -0.0668 S13: 0.1744
REMARK 3 S21: 0.5018 S22: -0.4179 S23: -0.1003
REMARK 3 S31: 0.7347 S32: 0.4605 S33: 0.5395
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 128 I 234
REMARK 3 ORIGIN FOR THE GROUP (A): -25.0589 31.9440-138.4719
REMARK 3 T TENSOR
REMARK 3 T11: 2.1060 T22: 1.2882
REMARK 3 T33: 1.3376 T12: -0.0266
REMARK 3 T13: -0.6221 T23: -0.2947
REMARK 3 L TENSOR
REMARK 3 L11: 5.1023 L22: 11.0289
REMARK 3 L33: 1.9986 L12: -6.7947
REMARK 3 L13: 0.5671 L23: 0.4846
REMARK 3 S TENSOR
REMARK 3 S11: -0.1374 S12: 0.0697 S13: 0.6103
REMARK 3 S21: 1.0862 S22: -0.7831 S23: -0.7264
REMARK 3 S31: -0.5202 S32: -0.1001 S33: 0.9205
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 24 J 127
REMARK 3 ORIGIN FOR THE GROUP (A): -81.8239 36.2965-154.1402
REMARK 3 T TENSOR
REMARK 3 T11: 1.4242 T22: 1.0397
REMARK 3 T33: 1.7907 T12: 0.0344
REMARK 3 T13: 0.0748 T23: 0.1629
REMARK 3 L TENSOR
REMARK 3 L11: 1.1847 L22: 6.5200
REMARK 3 L33: 0.6306 L12: -2.7680
REMARK 3 L13: 0.2280 L23: -0.6025
REMARK 3 S TENSOR
REMARK 3 S11: 0.0290 S12: 0.0993 S13: 0.1684
REMARK 3 S21: -0.0529 S22: -0.1147 S23: -0.1447
REMARK 3 S31: -0.6014 S32: -0.4490 S33: 0.0858
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 128 J 234
REMARK 3 ORIGIN FOR THE GROUP (A): -62.6185 4.1520-146.1554
REMARK 3 T TENSOR
REMARK 3 T11: 1.1631 T22: 1.4000
REMARK 3 T33: 1.4912 T12: -0.0494
REMARK 3 T13: 0.3662 T23: 0.2601
REMARK 3 L TENSOR
REMARK 3 L11: 6.1081 L22: 9.3174
REMARK 3 L33: 4.0665 L12: -4.2148
REMARK 3 L13: 1.7676 L23: -4.0470
REMARK 3 S TENSOR
REMARK 3 S11: -0.5949 S12: -0.3608 S13: -0.3292
REMARK 3 S21: 0.9192 S22: 0.0359 S23: 0.5823
REMARK 3 S31: 0.1614 S32: -0.3267 S33: 0.5590
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 24 K 127
REMARK 3 ORIGIN FOR THE GROUP (A): -14.9073 27.1822-104.8528
REMARK 3 T TENSOR
REMARK 3 T11: 1.1858 T22: 1.0032
REMARK 3 T33: 1.5657 T12: -0.1671
REMARK 3 T13: 0.1451 T23: 0.0895
REMARK 3 L TENSOR
REMARK 3 L11: 1.6078 L22: 9.4631
REMARK 3 L33: 4.3445 L12: 3.6634
REMARK 3 L13: 1.0706 L23: 4.2848
REMARK 3 S TENSOR
REMARK 3 S11: 0.1241 S12: -0.2489 S13: 0.0731
REMARK 3 S21: 0.0218 S22: -0.2538 S23: -0.0482
REMARK 3 S31: -0.7269 S32: -0.0842 S33: 0.1296
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 128 K 234
REMARK 3 ORIGIN FOR THE GROUP (A): -33.7763 -3.7812-117.1515
REMARK 3 T TENSOR
REMARK 3 T11: 1.0175 T22: 0.9537
REMARK 3 T33: 1.3514 T12: -0.0911
REMARK 3 T13: 0.4191 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 7.7352 L22: 8.7768
REMARK 3 L33: 1.8384 L12: 5.8233
REMARK 3 L13: 1.8923 L23: 1.9910
REMARK 3 S TENSOR
REMARK 3 S11: -0.1435 S12: -0.2674 S13: -0.6001
REMARK 3 S21: -0.7045 S22: -0.2422 S23: -0.7159
REMARK 3 S31: 0.1611 S32: 0.2952 S33: 0.3857
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 24 L 127
REMARK 3 ORIGIN FOR THE GROUP (A): -92.3448 -8.2272-124.7431
REMARK 3 T TENSOR
REMARK 3 T11: 1.4735 T22: 1.1384
REMARK 3 T33: 1.4150 T12: 0.0323
REMARK 3 T13: -0.2738 T23: 0.1607
REMARK 3 L TENSOR
REMARK 3 L11: 1.0886 L22: 13.5373
REMARK 3 L33: 0.6282 L12: 2.6955
REMARK 3 L13: 0.6706 L23: 1.1137
REMARK 3 S TENSOR
REMARK 3 S11: 0.1946 S12: -0.1527 S13: -0.0865
REMARK 3 S21: -0.1159 S22: -0.4730 S23: 0.3182
REMARK 3 S31: 0.4148 S32: -0.0540 S33: 0.2783
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 128 L 234
REMARK 3 ORIGIN FOR THE GROUP (A): -71.6928 23.8737-121.7264
REMARK 3 T TENSOR
REMARK 3 T11: 1.8322 T22: 1.3827
REMARK 3 T33: 1.2886 T12: 0.2398
REMARK 3 T13: -0.4396 T23: 0.7625
REMARK 3 L TENSOR
REMARK 3 L11: 1.4973 L22: 8.9582
REMARK 3 L33: 1.9282 L12: 2.6252
REMARK 3 L13: 0.6703 L23: -1.3589
REMARK 3 S TENSOR
REMARK 3 S11: -0.4317 S12: -0.0971 S13: 0.3308
REMARK 3 S21: -0.2709 S22: -0.0215 S23: -0.0884
REMARK 3 S31: -0.8858 S32: -0.4483 S33: 0.4532
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3
REMARK 3 INDIVIDUAL B-FACTORS WERE NOT REFINED DUE TO THE LOW RESOLUTION OF
REMARK 3 THE DIFFRACTION DATA.
REMARK 3 PLEASE NOTE THAT REFINEMENT OF THE MODEL IS DIFFICULT GIVEN THE
REMARK 3 LOW RESOLUTION OF THE DATA (4.1 A) AND THE LARGE NUMBER OF ATOMS
REMARK 3 IN THE ASYMMETRIC UNIT. THE ELECTRON DENSITY OF MANY SIDE CHAINS
REMARK 3 IS NOT WELL RESOLVED AND THE GEOMETRY OF THE MODEL IS NOT OPTIMAL.
REMARK 4
REMARK 4 5V5V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000226925.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53553
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.110
REMARK 200 RESOLUTION RANGE LOW (A) : 49.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.11
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.58600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3BL8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.03 M NANO3, 0.03 M NA2HPO4, 0.03 M
REMARK 280 (NH4)2SO4, 0.05 M HEPES PH 7.5, 0.05 M MOPS PH 7.5, 12 % (V/V)
REMARK 280 ETHYLENE GLYCOL, 9 % (W/V) PEG 8000, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, B, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 41
REMARK 465 PRO A 42
REMARK 465 VAL A 43
REMARK 465 VAL A 44
REMARK 465 ASN A 45
REMARK 465 THR A 46
REMARK 465 ALA A 47
REMARK 465 TYR A 48
REMARK 465 GLY A 49
REMARK 465 ARG A 50
REMARK 465 ASN A 59
REMARK 465 ASN A 60
REMARK 465 GLU A 61
REMARK 465 LEU A 155
REMARK 465 THR A 156
REMARK 465 LYS A 157
REMARK 465 LYS A 158
REMARK 465 ARG A 159
REMARK 465 ASP A 160
REMARK 465 GLU A 161
REMARK 465 ALA A 162
REMARK 465 THR A 163
REMARK 465 LEU A 164
REMARK 465 ASN A 165
REMARK 465 PRO A 166
REMARK 465 PRO A 167
REMARK 465 ASP A 168
REMARK 465 THR A 169
REMARK 465 ASP A 170
REMARK 465 ILE A 171
REMARK 465 ARG A 172
REMARK 465 ASP A 173
REMARK 465 GLY A 491
REMARK 465 ARG A 492
REMARK 465 PRO A 493
REMARK 465 GLU A 494
REMARK 465 TRP A 495
REMARK 465 ALA A 496
REMARK 465 ILE A 558
REMARK 465 HIS A 559
REMARK 465 THR A 560
REMARK 465 LYS A 561
REMARK 465 ASN A 610
REMARK 465 LEU A 611
REMARK 465 HIS A 612
REMARK 465 ALA A 613
REMARK 465 SER A 614
REMARK 465 THR A 615
REMARK 465 SER A 616
REMARK 465 HIS A 617
REMARK 465 HIS A 618
REMARK 465 HIS A 619
REMARK 465 HIS A 620
REMARK 465 HIS A 621
REMARK 465 HIS A 622
REMARK 465 VAL G 20
REMARK 465 ASP G 21
REMARK 465 TYR G 22
REMARK 465 ALA G 23
REMARK 465 HIS G 65
REMARK 465 PRO G 66
REMARK 465 THR G 75
REMARK 465 ALA G 76
REMARK 465 GLY G 77
REMARK 465 SER G 78
REMARK 465 ALA G 79
REMARK 465 SER G 80
REMARK 465 ASP G 81
REMARK 465 LYS G 82
REMARK 465 PHE G 83
REMARK 465 GLN G 84
REMARK 465 ASN G 90
REMARK 465 SER G 141
REMARK 465 ASP G 142
REMARK 465 VAL G 143
REMARK 465 ARG G 144
REMARK 465 GLY G 145
REMARK 465 ASN G 146
REMARK 465 PHE G 147
REMARK 465 TYR G 148
REMARK 465 GLN G 149
REMARK 465 GLU G 150
REMARK 465 HIS G 178
REMARK 465 SER G 179
REMARK 465 GLN G 180
REMARK 465 ASP G 181
REMARK 465 ASN G 235
REMARK 465 THR G 236
REMARK 465 THR G 237
REMARK 465 GLY G 238
REMARK 465 SER G 239
REMARK 465 ALA G 240
REMARK 465 SER G 241
REMARK 465 THR G 242
REMARK 465 SER G 243
REMARK 465 HIS G 244
REMARK 465 HIS G 245
REMARK 465 HIS G 246
REMARK 465 HIS G 247
REMARK 465 HIS G 248
REMARK 465 HIS G 249
REMARK 465 ALA B 41
REMARK 465 PRO B 42
REMARK 465 VAL B 43
REMARK 465 VAL B 44
REMARK 465 ASN B 45
REMARK 465 THR B 46
REMARK 465 ALA B 47
REMARK 465 TYR B 48
REMARK 465 GLY B 49
REMARK 465 ARG B 50
REMARK 465 ASN B 59
REMARK 465 ASN B 60
REMARK 465 GLU B 61
REMARK 465 LEU B 155
REMARK 465 THR B 156
REMARK 465 LYS B 157
REMARK 465 LYS B 158
REMARK 465 ARG B 159
REMARK 465 ASP B 160
REMARK 465 GLU B 161
REMARK 465 ALA B 162
REMARK 465 THR B 163
REMARK 465 LEU B 164
REMARK 465 ASN B 165
REMARK 465 PRO B 166
REMARK 465 PRO B 167
REMARK 465 ASP B 168
REMARK 465 THR B 169
REMARK 465 ASP B 170
REMARK 465 ILE B 171
REMARK 465 ARG B 172
REMARK 465 ASP B 173
REMARK 465 GLY B 491
REMARK 465 ARG B 492
REMARK 465 PRO B 493
REMARK 465 GLU B 494
REMARK 465 TRP B 495
REMARK 465 ALA B 496
REMARK 465 ILE B 558
REMARK 465 HIS B 559
REMARK 465 THR B 560
REMARK 465 LYS B 561
REMARK 465 ASN B 610
REMARK 465 LEU B 611
REMARK 465 HIS B 612
REMARK 465 ALA B 613
REMARK 465 SER B 614
REMARK 465 THR B 615
REMARK 465 SER B 616
REMARK 465 HIS B 617
REMARK 465 HIS B 618
REMARK 465 HIS B 619
REMARK 465 HIS B 620
REMARK 465 HIS B 621
REMARK 465 HIS B 622
REMARK 465 ALA C 41
REMARK 465 PRO C 42
REMARK 465 VAL C 43
REMARK 465 VAL C 44
REMARK 465 ASN C 45
REMARK 465 THR C 46
REMARK 465 ALA C 47
REMARK 465 TYR C 48
REMARK 465 GLY C 49
REMARK 465 ARG C 50
REMARK 465 ASN C 59
REMARK 465 ASN C 60
REMARK 465 GLU C 61
REMARK 465 LEU C 155
REMARK 465 THR C 156
REMARK 465 LYS C 157
REMARK 465 LYS C 158
REMARK 465 ARG C 159
REMARK 465 ASP C 160
REMARK 465 GLU C 161
REMARK 465 ALA C 162
REMARK 465 THR C 163
REMARK 465 LEU C 164
REMARK 465 ASN C 165
REMARK 465 PRO C 166
REMARK 465 PRO C 167
REMARK 465 ASP C 168
REMARK 465 THR C 169
REMARK 465 ASP C 170
REMARK 465 ILE C 171
REMARK 465 ARG C 172
REMARK 465 ASP C 173
REMARK 465 GLY C 491
REMARK 465 ARG C 492
REMARK 465 PRO C 493
REMARK 465 GLU C 494
REMARK 465 TRP C 495
REMARK 465 ALA C 496
REMARK 465 ILE C 558
REMARK 465 HIS C 559
REMARK 465 THR C 560
REMARK 465 LYS C 561
REMARK 465 ASN C 610
REMARK 465 LEU C 611
REMARK 465 HIS C 612
REMARK 465 ALA C 613
REMARK 465 SER C 614
REMARK 465 THR C 615
REMARK 465 SER C 616
REMARK 465 HIS C 617
REMARK 465 HIS C 618
REMARK 465 HIS C 619
REMARK 465 HIS C 620
REMARK 465 HIS C 621
REMARK 465 HIS C 622
REMARK 465 ALA D 41
REMARK 465 PRO D 42
REMARK 465 VAL D 43
REMARK 465 VAL D 44
REMARK 465 ASN D 45
REMARK 465 THR D 46
REMARK 465 ALA D 47
REMARK 465 TYR D 48
REMARK 465 GLY D 49
REMARK 465 ARG D 50
REMARK 465 ASN D 59
REMARK 465 ASN D 60
REMARK 465 GLU D 61
REMARK 465 LEU D 155
REMARK 465 THR D 156
REMARK 465 LYS D 157
REMARK 465 LYS D 158
REMARK 465 ARG D 159
REMARK 465 ASP D 160
REMARK 465 GLU D 161
REMARK 465 ALA D 162
REMARK 465 THR D 163
REMARK 465 LEU D 164
REMARK 465 ASN D 165
REMARK 465 PRO D 166
REMARK 465 PRO D 167
REMARK 465 ASP D 168
REMARK 465 THR D 169
REMARK 465 ASP D 170
REMARK 465 ILE D 171
REMARK 465 ARG D 172
REMARK 465 ASP D 173
REMARK 465 GLY D 491
REMARK 465 ARG D 492
REMARK 465 PRO D 493
REMARK 465 GLU D 494
REMARK 465 TRP D 495
REMARK 465 ALA D 496
REMARK 465 ILE D 558
REMARK 465 HIS D 559
REMARK 465 THR D 560
REMARK 465 LYS D 561
REMARK 465 ASN D 610
REMARK 465 LEU D 611
REMARK 465 HIS D 612
REMARK 465 ALA D 613
REMARK 465 SER D 614
REMARK 465 THR D 615
REMARK 465 SER D 616
REMARK 465 HIS D 617
REMARK 465 HIS D 618
REMARK 465 HIS D 619
REMARK 465 HIS D 620
REMARK 465 HIS D 621
REMARK 465 HIS D 622
REMARK 465 ALA E 41
REMARK 465 PRO E 42
REMARK 465 VAL E 43
REMARK 465 VAL E 44
REMARK 465 ASN E 45
REMARK 465 THR E 46
REMARK 465 ALA E 47
REMARK 465 TYR E 48
REMARK 465 GLY E 49
REMARK 465 ARG E 50
REMARK 465 ASN E 59
REMARK 465 ASN E 60
REMARK 465 GLU E 61
REMARK 465 LEU E 155
REMARK 465 THR E 156
REMARK 465 LYS E 157
REMARK 465 LYS E 158
REMARK 465 ARG E 159
REMARK 465 ASP E 160
REMARK 465 GLU E 161
REMARK 465 ALA E 162
REMARK 465 THR E 163
REMARK 465 LEU E 164
REMARK 465 ASN E 165
REMARK 465 PRO E 166
REMARK 465 PRO E 167
REMARK 465 ASP E 168
REMARK 465 THR E 169
REMARK 465 ASP E 170
REMARK 465 ILE E 171
REMARK 465 ARG E 172
REMARK 465 ASP E 173
REMARK 465 GLY E 491
REMARK 465 ARG E 492
REMARK 465 PRO E 493
REMARK 465 GLU E 494
REMARK 465 TRP E 495
REMARK 465 ALA E 496
REMARK 465 ILE E 558
REMARK 465 HIS E 559
REMARK 465 THR E 560
REMARK 465 LYS E 561
REMARK 465 ASN E 610
REMARK 465 LEU E 611
REMARK 465 HIS E 612
REMARK 465 ALA E 613
REMARK 465 SER E 614
REMARK 465 THR E 615
REMARK 465 SER E 616
REMARK 465 HIS E 617
REMARK 465 HIS E 618
REMARK 465 HIS E 619
REMARK 465 HIS E 620
REMARK 465 HIS E 621
REMARK 465 HIS E 622
REMARK 465 ALA F 41
REMARK 465 PRO F 42
REMARK 465 VAL F 43
REMARK 465 VAL F 44
REMARK 465 ASN F 45
REMARK 465 THR F 46
REMARK 465 ALA F 47
REMARK 465 TYR F 48
REMARK 465 GLY F 49
REMARK 465 ARG F 50
REMARK 465 ASN F 59
REMARK 465 ASN F 60
REMARK 465 GLU F 61
REMARK 465 LEU F 155
REMARK 465 THR F 156
REMARK 465 LYS F 157
REMARK 465 LYS F 158
REMARK 465 ARG F 159
REMARK 465 ASP F 160
REMARK 465 GLU F 161
REMARK 465 ALA F 162
REMARK 465 THR F 163
REMARK 465 LEU F 164
REMARK 465 ASN F 165
REMARK 465 PRO F 166
REMARK 465 PRO F 167
REMARK 465 ASP F 168
REMARK 465 THR F 169
REMARK 465 ASP F 170
REMARK 465 ILE F 171
REMARK 465 ARG F 172
REMARK 465 ASP F 173
REMARK 465 GLY F 491
REMARK 465 ARG F 492
REMARK 465 PRO F 493
REMARK 465 GLU F 494
REMARK 465 TRP F 495
REMARK 465 ALA F 496
REMARK 465 ILE F 558
REMARK 465 HIS F 559
REMARK 465 THR F 560
REMARK 465 LYS F 561
REMARK 465 ASN F 610
REMARK 465 LEU F 611
REMARK 465 HIS F 612
REMARK 465 ALA F 613
REMARK 465 SER F 614
REMARK 465 THR F 615
REMARK 465 SER F 616
REMARK 465 HIS F 617
REMARK 465 HIS F 618
REMARK 465 HIS F 619
REMARK 465 HIS F 620
REMARK 465 HIS F 621
REMARK 465 HIS F 622
REMARK 465 VAL H 20
REMARK 465 ASP H 21
REMARK 465 TYR H 22
REMARK 465 ALA H 23
REMARK 465 HIS H 65
REMARK 465 PRO H 66
REMARK 465 THR H 75
REMARK 465 ALA H 76
REMARK 465 GLY H 77
REMARK 465 SER H 78
REMARK 465 ALA H 79
REMARK 465 SER H 80
REMARK 465 ASP H 81
REMARK 465 LYS H 82
REMARK 465 PHE H 83
REMARK 465 GLN H 84
REMARK 465 ASN H 90
REMARK 465 SER H 141
REMARK 465 ASP H 142
REMARK 465 VAL H 143
REMARK 465 ARG H 144
REMARK 465 GLY H 145
REMARK 465 ASN H 146
REMARK 465 PHE H 147
REMARK 465 TYR H 148
REMARK 465 GLN H 149
REMARK 465 GLU H 150
REMARK 465 HIS H 178
REMARK 465 SER H 179
REMARK 465 GLN H 180
REMARK 465 ASP H 181
REMARK 465 ASN H 235
REMARK 465 THR H 236
REMARK 465 THR H 237
REMARK 465 GLY H 238
REMARK 465 SER H 239
REMARK 465 ALA H 240
REMARK 465 SER H 241
REMARK 465 THR H 242
REMARK 465 SER H 243
REMARK 465 HIS H 244
REMARK 465 HIS H 245
REMARK 465 HIS H 246
REMARK 465 HIS H 247
REMARK 465 HIS H 248
REMARK 465 HIS H 249
REMARK 465 VAL I 20
REMARK 465 ASP I 21
REMARK 465 TYR I 22
REMARK 465 ALA I 23
REMARK 465 HIS I 65
REMARK 465 PRO I 66
REMARK 465 THR I 75
REMARK 465 ALA I 76
REMARK 465 GLY I 77
REMARK 465 SER I 78
REMARK 465 ALA I 79
REMARK 465 SER I 80
REMARK 465 ASP I 81
REMARK 465 LYS I 82
REMARK 465 PHE I 83
REMARK 465 GLN I 84
REMARK 465 ASN I 90
REMARK 465 SER I 141
REMARK 465 ASP I 142
REMARK 465 VAL I 143
REMARK 465 ARG I 144
REMARK 465 GLY I 145
REMARK 465 ASN I 146
REMARK 465 PHE I 147
REMARK 465 TYR I 148
REMARK 465 GLN I 149
REMARK 465 GLU I 150
REMARK 465 HIS I 178
REMARK 465 SER I 179
REMARK 465 GLN I 180
REMARK 465 ASP I 181
REMARK 465 ASN I 235
REMARK 465 THR I 236
REMARK 465 THR I 237
REMARK 465 GLY I 238
REMARK 465 SER I 239
REMARK 465 ALA I 240
REMARK 465 SER I 241
REMARK 465 THR I 242
REMARK 465 SER I 243
REMARK 465 HIS I 244
REMARK 465 HIS I 245
REMARK 465 HIS I 246
REMARK 465 HIS I 247
REMARK 465 HIS I 248
REMARK 465 HIS I 249
REMARK 465 VAL J 20
REMARK 465 ASP J 21
REMARK 465 TYR J 22
REMARK 465 ALA J 23
REMARK 465 HIS J 65
REMARK 465 PRO J 66
REMARK 465 THR J 75
REMARK 465 ALA J 76
REMARK 465 GLY J 77
REMARK 465 SER J 78
REMARK 465 ALA J 79
REMARK 465 SER J 80
REMARK 465 ASP J 81
REMARK 465 LYS J 82
REMARK 465 PHE J 83
REMARK 465 GLN J 84
REMARK 465 ASN J 90
REMARK 465 SER J 141
REMARK 465 ASP J 142
REMARK 465 VAL J 143
REMARK 465 ARG J 144
REMARK 465 GLY J 145
REMARK 465 ASN J 146
REMARK 465 PHE J 147
REMARK 465 TYR J 148
REMARK 465 GLN J 149
REMARK 465 GLU J 150
REMARK 465 HIS J 178
REMARK 465 SER J 179
REMARK 465 GLN J 180
REMARK 465 ASP J 181
REMARK 465 ASN J 235
REMARK 465 THR J 236
REMARK 465 THR J 237
REMARK 465 GLY J 238
REMARK 465 SER J 239
REMARK 465 ALA J 240
REMARK 465 SER J 241
REMARK 465 THR J 242
REMARK 465 SER J 243
REMARK 465 HIS J 244
REMARK 465 HIS J 245
REMARK 465 HIS J 246
REMARK 465 HIS J 247
REMARK 465 HIS J 248
REMARK 465 HIS J 249
REMARK 465 VAL K 20
REMARK 465 ASP K 21
REMARK 465 TYR K 22
REMARK 465 ALA K 23
REMARK 465 HIS K 65
REMARK 465 PRO K 66
REMARK 465 THR K 75
REMARK 465 ALA K 76
REMARK 465 GLY K 77
REMARK 465 SER K 78
REMARK 465 ALA K 79
REMARK 465 SER K 80
REMARK 465 ASP K 81
REMARK 465 LYS K 82
REMARK 465 PHE K 83
REMARK 465 GLN K 84
REMARK 465 ASN K 90
REMARK 465 SER K 141
REMARK 465 ASP K 142
REMARK 465 VAL K 143
REMARK 465 ARG K 144
REMARK 465 GLY K 145
REMARK 465 ASN K 146
REMARK 465 PHE K 147
REMARK 465 TYR K 148
REMARK 465 GLN K 149
REMARK 465 GLU K 150
REMARK 465 HIS K 178
REMARK 465 SER K 179
REMARK 465 GLN K 180
REMARK 465 ASP K 181
REMARK 465 ASN K 235
REMARK 465 THR K 236
REMARK 465 THR K 237
REMARK 465 GLY K 238
REMARK 465 SER K 239
REMARK 465 ALA K 240
REMARK 465 SER K 241
REMARK 465 THR K 242
REMARK 465 SER K 243
REMARK 465 HIS K 244
REMARK 465 HIS K 245
REMARK 465 HIS K 246
REMARK 465 HIS K 247
REMARK 465 HIS K 248
REMARK 465 HIS K 249
REMARK 465 VAL L 20
REMARK 465 ASP L 21
REMARK 465 TYR L 22
REMARK 465 ALA L 23
REMARK 465 HIS L 65
REMARK 465 PRO L 66
REMARK 465 THR L 75
REMARK 465 ALA L 76
REMARK 465 GLY L 77
REMARK 465 SER L 78
REMARK 465 ALA L 79
REMARK 465 SER L 80
REMARK 465 ASP L 81
REMARK 465 LYS L 82
REMARK 465 PHE L 83
REMARK 465 GLN L 84
REMARK 465 ASN L 90
REMARK 465 SER L 141
REMARK 465 ASP L 142
REMARK 465 VAL L 143
REMARK 465 ARG L 144
REMARK 465 GLY L 145
REMARK 465 ASN L 146
REMARK 465 PHE L 147
REMARK 465 TYR L 148
REMARK 465 GLN L 149
REMARK 465 GLU L 150
REMARK 465 HIS L 178
REMARK 465 SER L 179
REMARK 465 GLN L 180
REMARK 465 ASP L 181
REMARK 465 ASN L 235
REMARK 465 THR L 236
REMARK 465 THR L 237
REMARK 465 GLY L 238
REMARK 465 SER L 239
REMARK 465 ALA L 240
REMARK 465 SER L 241
REMARK 465 THR L 242
REMARK 465 SER L 243
REMARK 465 HIS L 244
REMARK 465 HIS L 245
REMARK 465 HIS L 246
REMARK 465 HIS L 247
REMARK 465 HIS L 248
REMARK 465 HIS L 249
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 CA GLY B 95 O GLY C 153 1655 1.81
REMARK 500 CA GLY A 95 O GLY E 153 1456 2.01
REMARK 500 N VAL B 51 OD1 ASP C 152 1655 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS A 521 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 PRO A 550 C - N - CD ANGL. DEV. = -21.0 DEGREES
REMARK 500 ARG B 52 CA - CB - CG ANGL. DEV. = 19.5 DEGREES
REMARK 500 CYS B 521 CA - CB - SG ANGL. DEV. = 8.6 DEGREES
REMARK 500 PRO B 550 C - N - CD ANGL. DEV. = -21.2 DEGREES
REMARK 500 CYS C 521 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 PRO C 550 C - N - CD ANGL. DEV. = -21.1 DEGREES
REMARK 500 CYS D 521 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 PRO D 550 C - N - CD ANGL. DEV. = -21.1 DEGREES
REMARK 500 CYS E 521 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 PRO E 550 C - N - CD ANGL. DEV. = -21.1 DEGREES
REMARK 500 CYS F 521 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 PRO F 550 C - N - CD ANGL. DEV. = -21.0 DEGREES
REMARK 500 ARG H 166 NE - CZ - NH1 ANGL. DEV. = 3.2 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 ALA A 89 -174.54 -69.39
REMARK 500 VAL A 96 102.79 -56.99
REMARK 500 ASN A 98 81.52 -68.10
REMARK 500 PRO A 107 109.09 -52.16
REMARK 500 HIS A 111 56.97 -93.76
REMARK 500 ALA A 113 98.49 -62.58
REMARK 500 PRO A 115 74.16 -47.72
REMARK 500 LYS A 176 107.99 -47.66
REMARK 500 PHE A 221 16.73 -146.20
REMARK 500 ALA A 229 75.71 -150.73
REMARK 500 ILE A 249 -35.13 -32.75
REMARK 500 HIS A 251 44.27 -85.59
REMARK 500 ARG A 258 52.82 -145.08
REMARK 500 SER A 280 50.17 -103.03
REMARK 500 GLU A 281 -81.19 -66.78
REMARK 500 GLN A 290 96.90 -69.36
REMARK 500 SER A 291 79.95 65.83
REMARK 500 GLN A 303 57.57 -146.96
REMARK 500 ASP A 339 44.23 -79.56
REMARK 500 ASP A 341 101.46 73.47
REMARK 500 PRO A 344 -158.72 -86.27
REMARK 500 ASP A 358 -69.91 -161.38
REMARK 500 ASP A 363 119.74 -34.29
REMARK 500 GLU A 372 59.10 -104.62
REMARK 500 SER A 397 -60.62 -146.19
REMARK 500 LEU A 417 -68.55 -102.79
REMARK 500 MET A 446 31.55 -86.80
REMARK 500 TRP A 460 -60.67 -154.51
REMARK 500 HIS A 485 116.33 -161.63
REMARK 500 ASP A 502 -17.92 -49.62
REMARK 500 ASN A 522 91.96 -60.26
REMARK 500 PRO A 550 -111.46 43.69
REMARK 500 THR A 555 54.74 -155.40
REMARK 500 LYS A 576 -97.48 -73.15
REMARK 500 LYS A 578 66.27 -68.61
REMARK 500 ASN A 592 76.12 56.69
REMARK 500 ALA G 32 -158.93 -153.84
REMARK 500 CYS G 36 -63.32 -139.06
REMARK 500 ILE G 43 -71.90 -97.63
REMARK 500 GLU G 45 103.45 -58.89
REMARK 500 THR G 86 87.51 38.98
REMARK 500 VAL G 88 32.61 -93.82
REMARK 500 LYS G 109 66.89 -104.47
REMARK 500 ASP G 130 -179.98 -64.85
REMARK 500 THR G 139 -179.33 -172.28
REMARK 500 ARG G 171 47.85 -159.18
REMARK 500 LYS G 202 -76.66 -68.09
REMARK 500 LEU G 204 100.56 -53.44
REMARK 500 PRO G 206 -60.90 -22.66
REMARK 500 GLN G 207 51.07 -112.53
REMARK 500
REMARK 500 THIS ENTRY HAS 310 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 398 ASP A 399 134.16
REMARK 500 MET A 446 ARG A 447 145.95
REMARK 500 GLN A 475 SER A 476 149.50
REMARK 500 GLN A 549 PRO A 550 -138.20
REMARK 500 GLN G 207 ASP G 208 149.35
REMARK 500 GLU B 398 ASP B 399 134.76
REMARK 500 MET B 446 ARG B 447 145.82
REMARK 500 GLN B 475 SER B 476 149.90
REMARK 500 GLN B 549 PRO B 550 -138.33
REMARK 500 GLY C 175 LYS C 176 -144.21
REMARK 500 GLU C 398 ASP C 399 135.15
REMARK 500 GLY C 400 VAL C 401 149.79
REMARK 500 MET C 446 ARG C 447 144.63
REMARK 500 GLN C 475 SER C 476 148.89
REMARK 500 GLN C 549 PRO C 550 -137.99
REMARK 500 GLU D 398 ASP D 399 134.83
REMARK 500 MET D 446 ARG D 447 146.33
REMARK 500 GLN D 475 SER D 476 149.37
REMARK 500 GLN D 549 PRO D 550 -139.13
REMARK 500 GLY E 175 LYS E 176 -149.91
REMARK 500 GLU E 398 ASP E 399 134.96
REMARK 500 MET E 446 ARG E 447 144.87
REMARK 500 GLN E 475 SER E 476 148.83
REMARK 500 GLN E 549 PRO E 550 -138.57
REMARK 500 GLU F 398 ASP F 399 134.37
REMARK 500 MET F 446 ARG F 447 145.21
REMARK 500 GLN F 475 SER F 476 148.90
REMARK 500 GLN F 549 PRO F 550 -138.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5V5W RELATED DB: PDB
DBREF 5V5V A 42 612 UNP Q62888 NLGN2_RAT 42 612
DBREF 5V5V G 22 237 UNP Q8NFP4 MDGA1_HUMAN 22 237
DBREF 5V5V B 42 612 UNP Q62888 NLGN2_RAT 42 612
DBREF 5V5V C 42 612 UNP Q62888 NLGN2_RAT 42 612
DBREF 5V5V D 42 612 UNP Q62888 NLGN2_RAT 42 612
DBREF 5V5V E 42 612 UNP Q62888 NLGN2_RAT 42 612
DBREF 5V5V F 42 612 UNP Q62888 NLGN2_RAT 42 612
DBREF 5V5V H 22 237 UNP Q8NFP4 MDGA1_HUMAN 22 237
DBREF 5V5V I 22 237 UNP Q8NFP4 MDGA1_HUMAN 22 237
DBREF 5V5V J 22 237 UNP Q8NFP4 MDGA1_HUMAN 22 237
DBREF 5V5V K 22 237 UNP Q8NFP4 MDGA1_HUMAN 22 237
DBREF 5V5V L 22 237 UNP Q8NFP4 MDGA1_HUMAN 22 237
SEQADV 5V5V ALA A 41 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V ALA A 613 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V SER A 614 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V THR A 615 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V SER A 616 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS A 617 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS A 618 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS A 619 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS A 620 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS A 621 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS A 622 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V VAL G 20 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ASP G 21 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V GLY G 238 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER G 239 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ALA G 240 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER G 241 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V THR G 242 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER G 243 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS G 244 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS G 245 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS G 246 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS G 247 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS G 248 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS G 249 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ALA B 41 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V ALA B 613 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V SER B 614 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V THR B 615 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V SER B 616 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS B 617 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS B 618 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS B 619 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS B 620 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS B 621 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS B 622 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V ALA C 41 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V ALA C 613 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V SER C 614 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V THR C 615 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V SER C 616 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS C 617 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS C 618 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS C 619 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS C 620 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS C 621 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS C 622 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V ALA D 41 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V ALA D 613 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V SER D 614 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V THR D 615 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V SER D 616 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS D 617 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS D 618 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS D 619 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS D 620 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS D 621 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS D 622 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V ALA E 41 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V ALA E 613 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V SER E 614 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V THR E 615 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V SER E 616 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS E 617 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS E 618 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS E 619 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS E 620 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS E 621 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS E 622 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V ALA F 41 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V ALA F 613 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V SER F 614 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V THR F 615 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V SER F 616 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS F 617 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS F 618 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS F 619 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS F 620 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS F 621 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V HIS F 622 UNP Q62888 EXPRESSION TAG
SEQADV 5V5V VAL H 20 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ASP H 21 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V GLY H 238 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER H 239 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ALA H 240 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER H 241 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V THR H 242 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER H 243 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS H 244 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS H 245 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS H 246 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS H 247 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS H 248 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS H 249 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V VAL I 20 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ASP I 21 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V GLY I 238 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER I 239 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ALA I 240 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER I 241 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V THR I 242 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER I 243 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS I 244 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS I 245 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS I 246 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS I 247 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS I 248 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS I 249 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V VAL J 20 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ASP J 21 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V GLY J 238 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER J 239 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ALA J 240 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER J 241 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V THR J 242 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER J 243 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS J 244 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS J 245 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS J 246 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS J 247 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS J 248 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS J 249 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V VAL K 20 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ASP K 21 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V GLY K 238 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER K 239 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ALA K 240 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER K 241 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V THR K 242 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER K 243 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS K 244 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS K 245 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS K 246 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS K 247 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS K 248 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS K 249 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V VAL L 20 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ASP L 21 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V GLY L 238 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER L 239 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V ALA L 240 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER L 241 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V THR L 242 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V SER L 243 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS L 244 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS L 245 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS L 246 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS L 247 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS L 248 UNP Q8NFP4 EXPRESSION TAG
SEQADV 5V5V HIS L 249 UNP Q8NFP4 EXPRESSION TAG
SEQRES 1 A 582 ALA PRO VAL VAL ASN THR ALA TYR GLY ARG VAL ARG GLY
SEQRES 2 A 582 VAL ARG ARG GLU LEU ASN ASN GLU ILE LEU GLY PRO VAL
SEQRES 3 A 582 VAL GLN PHE LEU GLY VAL PRO TYR ALA THR PRO PRO LEU
SEQRES 4 A 582 GLY ALA ARG ARG PHE GLN PRO PRO GLU ALA PRO ALA SER
SEQRES 5 A 582 TRP PRO GLY VAL ARG ASN ALA THR THR LEU PRO PRO ALA
SEQRES 6 A 582 CYS PRO GLN ASN LEU HIS GLY ALA LEU PRO ALA ILE MET
SEQRES 7 A 582 LEU PRO VAL TRP PHE THR ASP ASN LEU GLU ALA ALA ALA
SEQRES 8 A 582 THR TYR VAL GLN ASN GLN SER GLU ASP CYS LEU TYR LEU
SEQRES 9 A 582 ASN LEU TYR VAL PRO THR GLU ASP GLY PRO LEU THR LYS
SEQRES 10 A 582 LYS ARG ASP GLU ALA THR LEU ASN PRO PRO ASP THR ASP
SEQRES 11 A 582 ILE ARG ASP SER GLY LYS LYS PRO VAL MET LEU PHE LEU
SEQRES 12 A 582 HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET PHE
SEQRES 13 A 582 ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE VAL
SEQRES 14 A 582 ALA THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE LEU
SEQRES 15 A 582 SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU
SEQRES 16 A 582 LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU ASN
SEQRES 17 A 582 ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR ILE
SEQRES 18 A 582 PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU LEU
SEQRES 19 A 582 ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS ALA
SEQRES 20 A 582 ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER VAL
SEQRES 21 A 582 ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA ALA
SEQRES 22 A 582 LYS VAL GLY CYS ASP ARG GLU ASP SER THR GLU ALA VAL
SEQRES 23 A 582 GLU CYS LEU ARG ARG LYS SER SER ARG GLU LEU VAL ASP
SEQRES 24 A 582 GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE GLY
SEQRES 25 A 582 PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO GLU
SEQRES 26 A 582 ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP MET
SEQRES 27 A 582 LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL
SEQRES 28 A 582 GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA SER
SEQRES 29 A 582 ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN LEU
SEQRES 30 A 582 TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU THR
SEQRES 31 A 582 ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP ASN
SEQRES 32 A 582 GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE THR
SEQRES 33 A 582 ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA LYS
SEQRES 34 A 582 LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR THR
SEQRES 35 A 582 PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU TRP
SEQRES 36 A 582 ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL PHE
SEQRES 37 A 582 GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO CYS
SEQRES 38 A 582 ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL
SEQRES 39 A 582 MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO
SEQRES 40 A 582 ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR
SEQRES 41 A 582 LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS PHE
SEQRES 42 A 582 ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU LYS
SEQRES 43 A 582 PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL ALA
SEQRES 44 A 582 PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU HIS
SEQRES 45 A 582 ALA SER THR SER HIS HIS HIS HIS HIS HIS
SEQRES 1 G 230 VAL ASP TYR ALA PRO ALA GLN ALA GLN ILE VAL HIS ALA
SEQRES 2 G 230 GLY GLN ALA CYS VAL VAL LYS GLU ASP ASN ILE SER GLU
SEQRES 3 G 230 ARG VAL TYR THR ILE ARG GLU GLY ASP THR LEU MET LEU
SEQRES 4 G 230 GLN CYS LEU VAL THR GLY HIS PRO ARG PRO GLN VAL ARG
SEQRES 5 G 230 TRP THR LYS THR ALA GLY SER ALA SER ASP LYS PHE GLN
SEQRES 6 G 230 GLU THR SER VAL PHE ASN GLU THR LEU ARG ILE GLU ARG
SEQRES 7 G 230 ILE ALA ARG THR GLN GLY GLY ARG TYR TYR CYS LYS ALA
SEQRES 8 G 230 GLU ASN GLY VAL GLY VAL PRO ALA ILE LYS SER ILE ARG
SEQRES 9 G 230 VAL ASP VAL GLN TYR LEU ASP GLU PRO MET LEU THR VAL
SEQRES 10 G 230 HIS GLN THR VAL SER ASP VAL ARG GLY ASN PHE TYR GLN
SEQRES 11 G 230 GLU LYS THR VAL PHE LEU ARG CYS THR VAL ASN SER ASN
SEQRES 12 G 230 PRO PRO ALA ARG PHE ILE TRP LYS ARG GLY SER ASP THR
SEQRES 13 G 230 LEU SER HIS SER GLN ASP ASN GLY VAL ASP ILE TYR GLU
SEQRES 14 G 230 PRO LEU TYR THR GLN GLY GLU THR LYS VAL LEU LYS LEU
SEQRES 15 G 230 LYS ASN LEU ARG PRO GLN ASP TYR ALA SER TYR THR CYS
SEQRES 16 G 230 GLN VAL SER VAL ARG ASN VAL CYS GLY ILE PRO ASP LYS
SEQRES 17 G 230 ALA ILE THR PHE ARG LEU THR ASN THR THR GLY SER ALA
SEQRES 18 G 230 SER THR SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 582 ALA PRO VAL VAL ASN THR ALA TYR GLY ARG VAL ARG GLY
SEQRES 2 B 582 VAL ARG ARG GLU LEU ASN ASN GLU ILE LEU GLY PRO VAL
SEQRES 3 B 582 VAL GLN PHE LEU GLY VAL PRO TYR ALA THR PRO PRO LEU
SEQRES 4 B 582 GLY ALA ARG ARG PHE GLN PRO PRO GLU ALA PRO ALA SER
SEQRES 5 B 582 TRP PRO GLY VAL ARG ASN ALA THR THR LEU PRO PRO ALA
SEQRES 6 B 582 CYS PRO GLN ASN LEU HIS GLY ALA LEU PRO ALA ILE MET
SEQRES 7 B 582 LEU PRO VAL TRP PHE THR ASP ASN LEU GLU ALA ALA ALA
SEQRES 8 B 582 THR TYR VAL GLN ASN GLN SER GLU ASP CYS LEU TYR LEU
SEQRES 9 B 582 ASN LEU TYR VAL PRO THR GLU ASP GLY PRO LEU THR LYS
SEQRES 10 B 582 LYS ARG ASP GLU ALA THR LEU ASN PRO PRO ASP THR ASP
SEQRES 11 B 582 ILE ARG ASP SER GLY LYS LYS PRO VAL MET LEU PHE LEU
SEQRES 12 B 582 HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET PHE
SEQRES 13 B 582 ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE VAL
SEQRES 14 B 582 ALA THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE LEU
SEQRES 15 B 582 SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU
SEQRES 16 B 582 LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU ASN
SEQRES 17 B 582 ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR ILE
SEQRES 18 B 582 PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU LEU
SEQRES 19 B 582 ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS ALA
SEQRES 20 B 582 ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER VAL
SEQRES 21 B 582 ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA ALA
SEQRES 22 B 582 LYS VAL GLY CYS ASP ARG GLU ASP SER THR GLU ALA VAL
SEQRES 23 B 582 GLU CYS LEU ARG ARG LYS SER SER ARG GLU LEU VAL ASP
SEQRES 24 B 582 GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE GLY
SEQRES 25 B 582 PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO GLU
SEQRES 26 B 582 ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP MET
SEQRES 27 B 582 LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL
SEQRES 28 B 582 GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA SER
SEQRES 29 B 582 ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN LEU
SEQRES 30 B 582 TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU THR
SEQRES 31 B 582 ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP ASN
SEQRES 32 B 582 GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE THR
SEQRES 33 B 582 ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA LYS
SEQRES 34 B 582 LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR THR
SEQRES 35 B 582 PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU TRP
SEQRES 36 B 582 ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL PHE
SEQRES 37 B 582 GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO CYS
SEQRES 38 B 582 ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL
SEQRES 39 B 582 MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO
SEQRES 40 B 582 ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR
SEQRES 41 B 582 LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS PHE
SEQRES 42 B 582 ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU LYS
SEQRES 43 B 582 PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL ALA
SEQRES 44 B 582 PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU HIS
SEQRES 45 B 582 ALA SER THR SER HIS HIS HIS HIS HIS HIS
SEQRES 1 C 582 ALA PRO VAL VAL ASN THR ALA TYR GLY ARG VAL ARG GLY
SEQRES 2 C 582 VAL ARG ARG GLU LEU ASN ASN GLU ILE LEU GLY PRO VAL
SEQRES 3 C 582 VAL GLN PHE LEU GLY VAL PRO TYR ALA THR PRO PRO LEU
SEQRES 4 C 582 GLY ALA ARG ARG PHE GLN PRO PRO GLU ALA PRO ALA SER
SEQRES 5 C 582 TRP PRO GLY VAL ARG ASN ALA THR THR LEU PRO PRO ALA
SEQRES 6 C 582 CYS PRO GLN ASN LEU HIS GLY ALA LEU PRO ALA ILE MET
SEQRES 7 C 582 LEU PRO VAL TRP PHE THR ASP ASN LEU GLU ALA ALA ALA
SEQRES 8 C 582 THR TYR VAL GLN ASN GLN SER GLU ASP CYS LEU TYR LEU
SEQRES 9 C 582 ASN LEU TYR VAL PRO THR GLU ASP GLY PRO LEU THR LYS
SEQRES 10 C 582 LYS ARG ASP GLU ALA THR LEU ASN PRO PRO ASP THR ASP
SEQRES 11 C 582 ILE ARG ASP SER GLY LYS LYS PRO VAL MET LEU PHE LEU
SEQRES 12 C 582 HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET PHE
SEQRES 13 C 582 ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE VAL
SEQRES 14 C 582 ALA THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE LEU
SEQRES 15 C 582 SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU
SEQRES 16 C 582 LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU ASN
SEQRES 17 C 582 ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR ILE
SEQRES 18 C 582 PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU LEU
SEQRES 19 C 582 ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS ALA
SEQRES 20 C 582 ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER VAL
SEQRES 21 C 582 ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA ALA
SEQRES 22 C 582 LYS VAL GLY CYS ASP ARG GLU ASP SER THR GLU ALA VAL
SEQRES 23 C 582 GLU CYS LEU ARG ARG LYS SER SER ARG GLU LEU VAL ASP
SEQRES 24 C 582 GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE GLY
SEQRES 25 C 582 PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO GLU
SEQRES 26 C 582 ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP MET
SEQRES 27 C 582 LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL
SEQRES 28 C 582 GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA SER
SEQRES 29 C 582 ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN LEU
SEQRES 30 C 582 TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU THR
SEQRES 31 C 582 ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP ASN
SEQRES 32 C 582 GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE THR
SEQRES 33 C 582 ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA LYS
SEQRES 34 C 582 LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR THR
SEQRES 35 C 582 PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU TRP
SEQRES 36 C 582 ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL PHE
SEQRES 37 C 582 GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO CYS
SEQRES 38 C 582 ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL
SEQRES 39 C 582 MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO
SEQRES 40 C 582 ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR
SEQRES 41 C 582 LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS PHE
SEQRES 42 C 582 ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU LYS
SEQRES 43 C 582 PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL ALA
SEQRES 44 C 582 PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU HIS
SEQRES 45 C 582 ALA SER THR SER HIS HIS HIS HIS HIS HIS
SEQRES 1 D 582 ALA PRO VAL VAL ASN THR ALA TYR GLY ARG VAL ARG GLY
SEQRES 2 D 582 VAL ARG ARG GLU LEU ASN ASN GLU ILE LEU GLY PRO VAL
SEQRES 3 D 582 VAL GLN PHE LEU GLY VAL PRO TYR ALA THR PRO PRO LEU
SEQRES 4 D 582 GLY ALA ARG ARG PHE GLN PRO PRO GLU ALA PRO ALA SER
SEQRES 5 D 582 TRP PRO GLY VAL ARG ASN ALA THR THR LEU PRO PRO ALA
SEQRES 6 D 582 CYS PRO GLN ASN LEU HIS GLY ALA LEU PRO ALA ILE MET
SEQRES 7 D 582 LEU PRO VAL TRP PHE THR ASP ASN LEU GLU ALA ALA ALA
SEQRES 8 D 582 THR TYR VAL GLN ASN GLN SER GLU ASP CYS LEU TYR LEU
SEQRES 9 D 582 ASN LEU TYR VAL PRO THR GLU ASP GLY PRO LEU THR LYS
SEQRES 10 D 582 LYS ARG ASP GLU ALA THR LEU ASN PRO PRO ASP THR ASP
SEQRES 11 D 582 ILE ARG ASP SER GLY LYS LYS PRO VAL MET LEU PHE LEU
SEQRES 12 D 582 HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET PHE
SEQRES 13 D 582 ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE VAL
SEQRES 14 D 582 ALA THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE LEU
SEQRES 15 D 582 SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU
SEQRES 16 D 582 LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU ASN
SEQRES 17 D 582 ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR ILE
SEQRES 18 D 582 PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU LEU
SEQRES 19 D 582 ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS ALA
SEQRES 20 D 582 ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER VAL
SEQRES 21 D 582 ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA ALA
SEQRES 22 D 582 LYS VAL GLY CYS ASP ARG GLU ASP SER THR GLU ALA VAL
SEQRES 23 D 582 GLU CYS LEU ARG ARG LYS SER SER ARG GLU LEU VAL ASP
SEQRES 24 D 582 GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE GLY
SEQRES 25 D 582 PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO GLU
SEQRES 26 D 582 ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP MET
SEQRES 27 D 582 LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL
SEQRES 28 D 582 GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA SER
SEQRES 29 D 582 ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN LEU
SEQRES 30 D 582 TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU THR
SEQRES 31 D 582 ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP ASN
SEQRES 32 D 582 GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE THR
SEQRES 33 D 582 ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA LYS
SEQRES 34 D 582 LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR THR
SEQRES 35 D 582 PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU TRP
SEQRES 36 D 582 ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL PHE
SEQRES 37 D 582 GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO CYS
SEQRES 38 D 582 ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL
SEQRES 39 D 582 MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO
SEQRES 40 D 582 ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR
SEQRES 41 D 582 LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS PHE
SEQRES 42 D 582 ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU LYS
SEQRES 43 D 582 PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL ALA
SEQRES 44 D 582 PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU HIS
SEQRES 45 D 582 ALA SER THR SER HIS HIS HIS HIS HIS HIS
SEQRES 1 E 582 ALA PRO VAL VAL ASN THR ALA TYR GLY ARG VAL ARG GLY
SEQRES 2 E 582 VAL ARG ARG GLU LEU ASN ASN GLU ILE LEU GLY PRO VAL
SEQRES 3 E 582 VAL GLN PHE LEU GLY VAL PRO TYR ALA THR PRO PRO LEU
SEQRES 4 E 582 GLY ALA ARG ARG PHE GLN PRO PRO GLU ALA PRO ALA SER
SEQRES 5 E 582 TRP PRO GLY VAL ARG ASN ALA THR THR LEU PRO PRO ALA
SEQRES 6 E 582 CYS PRO GLN ASN LEU HIS GLY ALA LEU PRO ALA ILE MET
SEQRES 7 E 582 LEU PRO VAL TRP PHE THR ASP ASN LEU GLU ALA ALA ALA
SEQRES 8 E 582 THR TYR VAL GLN ASN GLN SER GLU ASP CYS LEU TYR LEU
SEQRES 9 E 582 ASN LEU TYR VAL PRO THR GLU ASP GLY PRO LEU THR LYS
SEQRES 10 E 582 LYS ARG ASP GLU ALA THR LEU ASN PRO PRO ASP THR ASP
SEQRES 11 E 582 ILE ARG ASP SER GLY LYS LYS PRO VAL MET LEU PHE LEU
SEQRES 12 E 582 HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET PHE
SEQRES 13 E 582 ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE VAL
SEQRES 14 E 582 ALA THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE LEU
SEQRES 15 E 582 SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU
SEQRES 16 E 582 LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU ASN
SEQRES 17 E 582 ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR ILE
SEQRES 18 E 582 PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU LEU
SEQRES 19 E 582 ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS ALA
SEQRES 20 E 582 ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER VAL
SEQRES 21 E 582 ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA ALA
SEQRES 22 E 582 LYS VAL GLY CYS ASP ARG GLU ASP SER THR GLU ALA VAL
SEQRES 23 E 582 GLU CYS LEU ARG ARG LYS SER SER ARG GLU LEU VAL ASP
SEQRES 24 E 582 GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE GLY
SEQRES 25 E 582 PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO GLU
SEQRES 26 E 582 ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP MET
SEQRES 27 E 582 LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL
SEQRES 28 E 582 GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA SER
SEQRES 29 E 582 ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN LEU
SEQRES 30 E 582 TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU THR
SEQRES 31 E 582 ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP ASN
SEQRES 32 E 582 GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE THR
SEQRES 33 E 582 ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA LYS
SEQRES 34 E 582 LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR THR
SEQRES 35 E 582 PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU TRP
SEQRES 36 E 582 ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL PHE
SEQRES 37 E 582 GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO CYS
SEQRES 38 E 582 ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL
SEQRES 39 E 582 MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO
SEQRES 40 E 582 ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR
SEQRES 41 E 582 LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS PHE
SEQRES 42 E 582 ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU LYS
SEQRES 43 E 582 PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL ALA
SEQRES 44 E 582 PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU HIS
SEQRES 45 E 582 ALA SER THR SER HIS HIS HIS HIS HIS HIS
SEQRES 1 F 582 ALA PRO VAL VAL ASN THR ALA TYR GLY ARG VAL ARG GLY
SEQRES 2 F 582 VAL ARG ARG GLU LEU ASN ASN GLU ILE LEU GLY PRO VAL
SEQRES 3 F 582 VAL GLN PHE LEU GLY VAL PRO TYR ALA THR PRO PRO LEU
SEQRES 4 F 582 GLY ALA ARG ARG PHE GLN PRO PRO GLU ALA PRO ALA SER
SEQRES 5 F 582 TRP PRO GLY VAL ARG ASN ALA THR THR LEU PRO PRO ALA
SEQRES 6 F 582 CYS PRO GLN ASN LEU HIS GLY ALA LEU PRO ALA ILE MET
SEQRES 7 F 582 LEU PRO VAL TRP PHE THR ASP ASN LEU GLU ALA ALA ALA
SEQRES 8 F 582 THR TYR VAL GLN ASN GLN SER GLU ASP CYS LEU TYR LEU
SEQRES 9 F 582 ASN LEU TYR VAL PRO THR GLU ASP GLY PRO LEU THR LYS
SEQRES 10 F 582 LYS ARG ASP GLU ALA THR LEU ASN PRO PRO ASP THR ASP
SEQRES 11 F 582 ILE ARG ASP SER GLY LYS LYS PRO VAL MET LEU PHE LEU
SEQRES 12 F 582 HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET PHE
SEQRES 13 F 582 ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE VAL
SEQRES 14 F 582 ALA THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE LEU
SEQRES 15 F 582 SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU
SEQRES 16 F 582 LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU ASN
SEQRES 17 F 582 ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR ILE
SEQRES 18 F 582 PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU LEU
SEQRES 19 F 582 ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS ALA
SEQRES 20 F 582 ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER VAL
SEQRES 21 F 582 ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA ALA
SEQRES 22 F 582 LYS VAL GLY CYS ASP ARG GLU ASP SER THR GLU ALA VAL
SEQRES 23 F 582 GLU CYS LEU ARG ARG LYS SER SER ARG GLU LEU VAL ASP
SEQRES 24 F 582 GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE GLY
SEQRES 25 F 582 PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO GLU
SEQRES 26 F 582 ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP MET
SEQRES 27 F 582 LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL
SEQRES 28 F 582 GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA SER
SEQRES 29 F 582 ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN LEU
SEQRES 30 F 582 TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU THR
SEQRES 31 F 582 ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP ASN
SEQRES 32 F 582 GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE THR
SEQRES 33 F 582 ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA LYS
SEQRES 34 F 582 LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR THR
SEQRES 35 F 582 PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU TRP
SEQRES 36 F 582 ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL PHE
SEQRES 37 F 582 GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO CYS
SEQRES 38 F 582 ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL
SEQRES 39 F 582 MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO
SEQRES 40 F 582 ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR
SEQRES 41 F 582 LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS PHE
SEQRES 42 F 582 ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU LYS
SEQRES 43 F 582 PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL ALA
SEQRES 44 F 582 PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU HIS
SEQRES 45 F 582 ALA SER THR SER HIS HIS HIS HIS HIS HIS
SEQRES 1 H 230 VAL ASP TYR ALA PRO ALA GLN ALA GLN ILE VAL HIS ALA
SEQRES 2 H 230 GLY GLN ALA CYS VAL VAL LYS GLU ASP ASN ILE SER GLU
SEQRES 3 H 230 ARG VAL TYR THR ILE ARG GLU GLY ASP THR LEU MET LEU
SEQRES 4 H 230 GLN CYS LEU VAL THR GLY HIS PRO ARG PRO GLN VAL ARG
SEQRES 5 H 230 TRP THR LYS THR ALA GLY SER ALA SER ASP LYS PHE GLN
SEQRES 6 H 230 GLU THR SER VAL PHE ASN GLU THR LEU ARG ILE GLU ARG
SEQRES 7 H 230 ILE ALA ARG THR GLN GLY GLY ARG TYR TYR CYS LYS ALA
SEQRES 8 H 230 GLU ASN GLY VAL GLY VAL PRO ALA ILE LYS SER ILE ARG
SEQRES 9 H 230 VAL ASP VAL GLN TYR LEU ASP GLU PRO MET LEU THR VAL
SEQRES 10 H 230 HIS GLN THR VAL SER ASP VAL ARG GLY ASN PHE TYR GLN
SEQRES 11 H 230 GLU LYS THR VAL PHE LEU ARG CYS THR VAL ASN SER ASN
SEQRES 12 H 230 PRO PRO ALA ARG PHE ILE TRP LYS ARG GLY SER ASP THR
SEQRES 13 H 230 LEU SER HIS SER GLN ASP ASN GLY VAL ASP ILE TYR GLU
SEQRES 14 H 230 PRO LEU TYR THR GLN GLY GLU THR LYS VAL LEU LYS LEU
SEQRES 15 H 230 LYS ASN LEU ARG PRO GLN ASP TYR ALA SER TYR THR CYS
SEQRES 16 H 230 GLN VAL SER VAL ARG ASN VAL CYS GLY ILE PRO ASP LYS
SEQRES 17 H 230 ALA ILE THR PHE ARG LEU THR ASN THR THR GLY SER ALA
SEQRES 18 H 230 SER THR SER HIS HIS HIS HIS HIS HIS
SEQRES 1 I 230 VAL ASP TYR ALA PRO ALA GLN ALA GLN ILE VAL HIS ALA
SEQRES 2 I 230 GLY GLN ALA CYS VAL VAL LYS GLU ASP ASN ILE SER GLU
SEQRES 3 I 230 ARG VAL TYR THR ILE ARG GLU GLY ASP THR LEU MET LEU
SEQRES 4 I 230 GLN CYS LEU VAL THR GLY HIS PRO ARG PRO GLN VAL ARG
SEQRES 5 I 230 TRP THR LYS THR ALA GLY SER ALA SER ASP LYS PHE GLN
SEQRES 6 I 230 GLU THR SER VAL PHE ASN GLU THR LEU ARG ILE GLU ARG
SEQRES 7 I 230 ILE ALA ARG THR GLN GLY GLY ARG TYR TYR CYS LYS ALA
SEQRES 8 I 230 GLU ASN GLY VAL GLY VAL PRO ALA ILE LYS SER ILE ARG
SEQRES 9 I 230 VAL ASP VAL GLN TYR LEU ASP GLU PRO MET LEU THR VAL
SEQRES 10 I 230 HIS GLN THR VAL SER ASP VAL ARG GLY ASN PHE TYR GLN
SEQRES 11 I 230 GLU LYS THR VAL PHE LEU ARG CYS THR VAL ASN SER ASN
SEQRES 12 I 230 PRO PRO ALA ARG PHE ILE TRP LYS ARG GLY SER ASP THR
SEQRES 13 I 230 LEU SER HIS SER GLN ASP ASN GLY VAL ASP ILE TYR GLU
SEQRES 14 I 230 PRO LEU TYR THR GLN GLY GLU THR LYS VAL LEU LYS LEU
SEQRES 15 I 230 LYS ASN LEU ARG PRO GLN ASP TYR ALA SER TYR THR CYS
SEQRES 16 I 230 GLN VAL SER VAL ARG ASN VAL CYS GLY ILE PRO ASP LYS
SEQRES 17 I 230 ALA ILE THR PHE ARG LEU THR ASN THR THR GLY SER ALA
SEQRES 18 I 230 SER THR SER HIS HIS HIS HIS HIS HIS
SEQRES 1 J 230 VAL ASP TYR ALA PRO ALA GLN ALA GLN ILE VAL HIS ALA
SEQRES 2 J 230 GLY GLN ALA CYS VAL VAL LYS GLU ASP ASN ILE SER GLU
SEQRES 3 J 230 ARG VAL TYR THR ILE ARG GLU GLY ASP THR LEU MET LEU
SEQRES 4 J 230 GLN CYS LEU VAL THR GLY HIS PRO ARG PRO GLN VAL ARG
SEQRES 5 J 230 TRP THR LYS THR ALA GLY SER ALA SER ASP LYS PHE GLN
SEQRES 6 J 230 GLU THR SER VAL PHE ASN GLU THR LEU ARG ILE GLU ARG
SEQRES 7 J 230 ILE ALA ARG THR GLN GLY GLY ARG TYR TYR CYS LYS ALA
SEQRES 8 J 230 GLU ASN GLY VAL GLY VAL PRO ALA ILE LYS SER ILE ARG
SEQRES 9 J 230 VAL ASP VAL GLN TYR LEU ASP GLU PRO MET LEU THR VAL
SEQRES 10 J 230 HIS GLN THR VAL SER ASP VAL ARG GLY ASN PHE TYR GLN
SEQRES 11 J 230 GLU LYS THR VAL PHE LEU ARG CYS THR VAL ASN SER ASN
SEQRES 12 J 230 PRO PRO ALA ARG PHE ILE TRP LYS ARG GLY SER ASP THR
SEQRES 13 J 230 LEU SER HIS SER GLN ASP ASN GLY VAL ASP ILE TYR GLU
SEQRES 14 J 230 PRO LEU TYR THR GLN GLY GLU THR LYS VAL LEU LYS LEU
SEQRES 15 J 230 LYS ASN LEU ARG PRO GLN ASP TYR ALA SER TYR THR CYS
SEQRES 16 J 230 GLN VAL SER VAL ARG ASN VAL CYS GLY ILE PRO ASP LYS
SEQRES 17 J 230 ALA ILE THR PHE ARG LEU THR ASN THR THR GLY SER ALA
SEQRES 18 J 230 SER THR SER HIS HIS HIS HIS HIS HIS
SEQRES 1 K 230 VAL ASP TYR ALA PRO ALA GLN ALA GLN ILE VAL HIS ALA
SEQRES 2 K 230 GLY GLN ALA CYS VAL VAL LYS GLU ASP ASN ILE SER GLU
SEQRES 3 K 230 ARG VAL TYR THR ILE ARG GLU GLY ASP THR LEU MET LEU
SEQRES 4 K 230 GLN CYS LEU VAL THR GLY HIS PRO ARG PRO GLN VAL ARG
SEQRES 5 K 230 TRP THR LYS THR ALA GLY SER ALA SER ASP LYS PHE GLN
SEQRES 6 K 230 GLU THR SER VAL PHE ASN GLU THR LEU ARG ILE GLU ARG
SEQRES 7 K 230 ILE ALA ARG THR GLN GLY GLY ARG TYR TYR CYS LYS ALA
SEQRES 8 K 230 GLU ASN GLY VAL GLY VAL PRO ALA ILE LYS SER ILE ARG
SEQRES 9 K 230 VAL ASP VAL GLN TYR LEU ASP GLU PRO MET LEU THR VAL
SEQRES 10 K 230 HIS GLN THR VAL SER ASP VAL ARG GLY ASN PHE TYR GLN
SEQRES 11 K 230 GLU LYS THR VAL PHE LEU ARG CYS THR VAL ASN SER ASN
SEQRES 12 K 230 PRO PRO ALA ARG PHE ILE TRP LYS ARG GLY SER ASP THR
SEQRES 13 K 230 LEU SER HIS SER GLN ASP ASN GLY VAL ASP ILE TYR GLU
SEQRES 14 K 230 PRO LEU TYR THR GLN GLY GLU THR LYS VAL LEU LYS LEU
SEQRES 15 K 230 LYS ASN LEU ARG PRO GLN ASP TYR ALA SER TYR THR CYS
SEQRES 16 K 230 GLN VAL SER VAL ARG ASN VAL CYS GLY ILE PRO ASP LYS
SEQRES 17 K 230 ALA ILE THR PHE ARG LEU THR ASN THR THR GLY SER ALA
SEQRES 18 K 230 SER THR SER HIS HIS HIS HIS HIS HIS
SEQRES 1 L 230 VAL ASP TYR ALA PRO ALA GLN ALA GLN ILE VAL HIS ALA
SEQRES 2 L 230 GLY GLN ALA CYS VAL VAL LYS GLU ASP ASN ILE SER GLU
SEQRES 3 L 230 ARG VAL TYR THR ILE ARG GLU GLY ASP THR LEU MET LEU
SEQRES 4 L 230 GLN CYS LEU VAL THR GLY HIS PRO ARG PRO GLN VAL ARG
SEQRES 5 L 230 TRP THR LYS THR ALA GLY SER ALA SER ASP LYS PHE GLN
SEQRES 6 L 230 GLU THR SER VAL PHE ASN GLU THR LEU ARG ILE GLU ARG
SEQRES 7 L 230 ILE ALA ARG THR GLN GLY GLY ARG TYR TYR CYS LYS ALA
SEQRES 8 L 230 GLU ASN GLY VAL GLY VAL PRO ALA ILE LYS SER ILE ARG
SEQRES 9 L 230 VAL ASP VAL GLN TYR LEU ASP GLU PRO MET LEU THR VAL
SEQRES 10 L 230 HIS GLN THR VAL SER ASP VAL ARG GLY ASN PHE TYR GLN
SEQRES 11 L 230 GLU LYS THR VAL PHE LEU ARG CYS THR VAL ASN SER ASN
SEQRES 12 L 230 PRO PRO ALA ARG PHE ILE TRP LYS ARG GLY SER ASP THR
SEQRES 13 L 230 LEU SER HIS SER GLN ASP ASN GLY VAL ASP ILE TYR GLU
SEQRES 14 L 230 PRO LEU TYR THR GLN GLY GLU THR LYS VAL LEU LYS LEU
SEQRES 15 L 230 LYS ASN LEU ARG PRO GLN ASP TYR ALA SER TYR THR CYS
SEQRES 16 L 230 GLN VAL SER VAL ARG ASN VAL CYS GLY ILE PRO ASP LYS
SEQRES 17 L 230 ALA ILE THR PHE ARG LEU THR ASN THR THR GLY SER ALA
SEQRES 18 L 230 SER THR SER HIS HIS HIS HIS HIS HIS
HELIX 1 AA1 PRO A 115 LEU A 119 5 5
HELIX 2 AA2 PRO A 120 ASN A 126 1 7
HELIX 3 AA3 ASN A 126 THR A 132 1 7
HELIX 4 AA4 THR A 192 PHE A 196 5 5
HELIX 5 AA5 SER A 199 ASN A 206 1 8
HELIX 6 AA6 LEU A 216 LEU A 222 1 7
HELIX 7 AA7 ASN A 232 SER A 246 1 15
HELIX 8 AA8 ASN A 248 ILE A 249 1 2
HELIX 9 AA9 ALA A 250 PHE A 252 5 3
HELIX 10 AB1 ALA A 266 SER A 277 1 12
HELIX 11 AB2 GLN A 303 VAL A 315 1 13
HELIX 12 AB3 ASP A 321 LYS A 332 1 12
HELIX 13 AB4 SER A 333 ASP A 339 1 7
HELIX 14 AB5 ASP A 363 GLY A 371 1 9
HELIX 15 AB6 GLY A 387 GLU A 392 1 6
HELIX 16 AB7 SER A 402 GLY A 419 1 18
HELIX 17 AB8 GLY A 423 THR A 436 1 14
HELIX 18 AB9 GLY A 444 TRP A 460 1 17
HELIX 19 AC1 TRP A 460 TYR A 474 1 15
HELIX 20 AC2 GLU A 503 PHE A 508 1 6
HELIX 21 AC3 GLY A 509 VAL A 513 5 5
HELIX 22 AC4 SER A 524 GLY A 545 1 22
HELIX 23 AC5 ARG A 594 GLU A 603 1 10
HELIX 24 AC6 LEU A 604 HIS A 609 5 6
HELIX 25 AC7 ALA G 99 GLY G 103 5 5
HELIX 26 AC8 ASN G 220 ILE G 224 5 5
HELIX 27 AC9 PRO B 115 LEU B 119 5 5
HELIX 28 AD1 PRO B 120 ASN B 126 1 7
HELIX 29 AD2 ASN B 126 THR B 132 1 7
HELIX 30 AD3 THR B 192 PHE B 196 5 5
HELIX 31 AD4 SER B 199 ASN B 206 1 8
HELIX 32 AD5 LEU B 216 LEU B 222 1 7
HELIX 33 AD6 ASN B 232 SER B 246 1 15
HELIX 34 AD7 ASN B 248 ILE B 249 1 2
HELIX 35 AD8 ALA B 250 PHE B 252 5 3
HELIX 36 AD9 ALA B 266 SER B 277 1 12
HELIX 37 AE1 GLN B 303 VAL B 315 1 13
HELIX 38 AE2 ASP B 321 LYS B 332 1 12
HELIX 39 AE3 SER B 333 ASP B 339 1 7
HELIX 40 AE4 ASP B 363 GLY B 371 1 9
HELIX 41 AE5 GLY B 387 GLU B 392 1 6
HELIX 42 AE6 SER B 402 GLY B 419 1 18
HELIX 43 AE7 GLY B 423 THR B 436 1 14
HELIX 44 AE8 GLY B 444 TRP B 460 1 17
HELIX 45 AE9 TRP B 460 TYR B 474 1 15
HELIX 46 AF1 GLU B 503 PHE B 508 1 6
HELIX 47 AF2 GLY B 509 VAL B 513 5 5
HELIX 48 AF3 SER B 524 GLY B 545 1 22
HELIX 49 AF4 ARG B 594 GLU B 603 1 10
HELIX 50 AF5 LEU B 604 HIS B 609 5 6
HELIX 51 AF6 PRO C 115 LEU C 119 5 5
HELIX 52 AF7 PRO C 120 ASN C 126 1 7
HELIX 53 AF8 ASN C 126 THR C 132 1 7
HELIX 54 AF9 THR C 192 PHE C 196 5 5
HELIX 55 AG1 SER C 199 ASN C 206 1 8
HELIX 56 AG2 LEU C 216 LEU C 222 1 7
HELIX 57 AG3 ASN C 232 SER C 246 1 15
HELIX 58 AG4 ASN C 248 ILE C 249 1 2
HELIX 59 AG5 ALA C 250 PHE C 252 5 3
HELIX 60 AG6 ALA C 266 SER C 277 1 12
HELIX 61 AG7 GLN C 303 VAL C 315 1 13
HELIX 62 AG8 ASP C 321 LYS C 332 1 12
HELIX 63 AG9 SER C 333 ASP C 339 1 7
HELIX 64 AH1 ASP C 363 GLY C 371 1 9
HELIX 65 AH2 GLY C 387 GLU C 392 1 6
HELIX 66 AH3 SER C 402 GLY C 419 1 18
HELIX 67 AH4 GLY C 423 THR C 436 1 14
HELIX 68 AH5 GLY C 444 TRP C 460 1 17
HELIX 69 AH6 TRP C 460 TYR C 474 1 15
HELIX 70 AH7 GLU C 503 PHE C 508 1 6
HELIX 71 AH8 GLY C 509 VAL C 513 5 5
HELIX 72 AH9 SER C 524 GLY C 545 1 22
HELIX 73 AI1 ARG C 594 GLU C 603 1 10
HELIX 74 AI2 LEU C 604 HIS C 609 5 6
HELIX 75 AI3 PRO D 115 LEU D 119 5 5
HELIX 76 AI4 PRO D 120 ASN D 126 1 7
HELIX 77 AI5 ASN D 126 THR D 132 1 7
HELIX 78 AI6 THR D 192 PHE D 196 5 5
HELIX 79 AI7 SER D 199 ASN D 206 1 8
HELIX 80 AI8 LEU D 216 LEU D 222 1 7
HELIX 81 AI9 ASN D 232 SER D 246 1 15
HELIX 82 AJ1 ASN D 248 ILE D 249 1 2
HELIX 83 AJ2 ALA D 250 PHE D 252 5 3
HELIX 84 AJ3 ALA D 266 SER D 277 1 12
HELIX 85 AJ4 GLN D 303 VAL D 315 1 13
HELIX 86 AJ5 ASP D 321 LYS D 332 1 12
HELIX 87 AJ6 SER D 333 ASP D 339 1 7
HELIX 88 AJ7 ASP D 363 GLY D 371 1 9
HELIX 89 AJ8 GLY D 387 GLU D 392 1 6
HELIX 90 AJ9 SER D 402 GLY D 419 1 18
HELIX 91 AK1 GLY D 423 THR D 436 1 14
HELIX 92 AK2 GLY D 444 TRP D 460 1 17
HELIX 93 AK3 TRP D 460 TYR D 474 1 15
HELIX 94 AK4 GLU D 503 PHE D 508 1 6
HELIX 95 AK5 GLY D 509 VAL D 513 5 5
HELIX 96 AK6 SER D 524 GLY D 545 1 22
HELIX 97 AK7 ARG D 594 GLU D 603 1 10
HELIX 98 AK8 LEU D 604 HIS D 609 5 6
HELIX 99 AK9 PRO E 115 LEU E 119 5 5
HELIX 100 AL1 PRO E 120 ASN E 126 1 7
HELIX 101 AL2 ASN E 126 THR E 132 1 7
HELIX 102 AL3 THR E 192 PHE E 196 5 5
HELIX 103 AL4 SER E 199 ASN E 206 1 8
HELIX 104 AL5 LEU E 216 LEU E 222 1 7
HELIX 105 AL6 ASN E 232 SER E 246 1 15
HELIX 106 AL7 ASN E 248 ILE E 249 1 2
HELIX 107 AL8 ALA E 250 PHE E 252 5 3
HELIX 108 AL9 ALA E 266 SER E 277 1 12
HELIX 109 AM1 GLN E 303 VAL E 315 1 13
HELIX 110 AM2 ASP E 321 LYS E 332 1 12
HELIX 111 AM3 SER E 333 ASP E 339 1 7
HELIX 112 AM4 ASP E 363 GLY E 371 1 9
HELIX 113 AM5 GLY E 387 GLU E 392 1 6
HELIX 114 AM6 SER E 402 GLY E 419 1 18
HELIX 115 AM7 GLY E 423 THR E 436 1 14
HELIX 116 AM8 GLY E 444 TRP E 460 1 17
HELIX 117 AM9 TRP E 460 TYR E 474 1 15
HELIX 118 AN1 GLU E 503 PHE E 508 1 6
HELIX 119 AN2 GLY E 509 VAL E 513 5 5
HELIX 120 AN3 SER E 524 GLY E 545 1 22
HELIX 121 AN4 ARG E 594 GLU E 603 1 10
HELIX 122 AN5 LEU E 604 HIS E 609 5 6
HELIX 123 AN6 PRO F 120 ASN F 126 1 7
HELIX 124 AN7 ASN F 126 THR F 132 1 7
HELIX 125 AN8 THR F 192 PHE F 196 5 5
HELIX 126 AN9 SER F 199 ASN F 206 1 8
HELIX 127 AO1 LEU F 216 LEU F 222 1 7
HELIX 128 AO2 ASN F 232 SER F 246 1 15
HELIX 129 AO3 ASN F 248 ILE F 249 1 2
HELIX 130 AO4 ALA F 250 PHE F 252 5 3
HELIX 131 AO5 ALA F 266 SER F 277 1 12
HELIX 132 AO6 GLN F 303 VAL F 315 1 13
HELIX 133 AO7 ASP F 321 LYS F 332 1 12
HELIX 134 AO8 SER F 333 ASP F 339 1 7
HELIX 135 AO9 ASP F 363 GLY F 371 1 9
HELIX 136 AP1 GLY F 387 GLU F 392 1 6
HELIX 137 AP2 SER F 402 GLY F 419 1 18
HELIX 138 AP3 GLY F 423 THR F 436 1 14
HELIX 139 AP4 GLY F 444 TRP F 460 1 17
HELIX 140 AP5 TRP F 460 TYR F 474 1 15
HELIX 141 AP6 GLU F 503 PHE F 508 1 6
HELIX 142 AP7 GLY F 509 VAL F 513 5 5
HELIX 143 AP8 SER F 524 GLY F 545 1 22
HELIX 144 AP9 ARG F 594 GLU F 603 1 10
HELIX 145 AQ1 LEU F 604 HIS F 609 5 6
HELIX 146 AQ2 ALA H 99 GLY H 103 5 5
HELIX 147 AQ3 ASN H 220 ILE H 224 5 5
HELIX 148 AQ4 ALA I 99 GLY I 103 5 5
HELIX 149 AQ5 ASN I 220 ILE I 224 5 5
HELIX 150 AQ6 ALA J 99 GLY J 103 5 5
HELIX 151 AQ7 ASN J 220 ILE J 224 5 5
HELIX 152 AQ8 ALA K 99 GLY K 103 5 5
HELIX 153 AQ9 ASN K 220 ILE K 224 5 5
HELIX 154 AR1 ALA L 99 GLY L 103 5 5
HELIX 155 AR2 ASN L 220 ILE L 224 5 5
SHEET 1 AA1 4 VAL A 54 ARG A 56 0
SHEET 2 AA1 4 VAL A 66 GLN A 68 -1 O GLN A 68 N VAL A 54
SHEET 3 AA1 4 TYR A 143 PRO A 149 -1 O VAL A 148 N VAL A 67
SHEET 4 AA1 4 VAL A 72 PRO A 73 -1 N VAL A 72 O LEU A 144
SHEET 1 AA211 VAL A 54 ARG A 56 0
SHEET 2 AA211 VAL A 66 GLN A 68 -1 O GLN A 68 N VAL A 54
SHEET 3 AA211 TYR A 143 PRO A 149 -1 O VAL A 148 N VAL A 67
SHEET 4 AA211 ILE A 208 THR A 211 -1 O THR A 211 N ASN A 145
SHEET 5 AA211 LYS A 177 PHE A 182 1 N MET A 180 O ILE A 208
SHEET 6 AA211 GLY A 254 SER A 264 1 O THR A 260 N VAL A 179
SHEET 7 AA211 LYS A 286 GLN A 290 1 O ILE A 288 N GLY A 263
SHEET 8 AA211 ASP A 377 ASN A 383 1 O ASP A 377 N ALA A 287
SHEET 9 AA211 VAL A 478 PHE A 483 1 O PHE A 483 N VAL A 382
SHEET 10 AA211 TYR A 580 HIS A 582 1 O LEU A 581 N PHE A 480
SHEET 11 AA211 ARG A 588 ARG A 590 -1 O ARG A 588 N HIS A 582
SHEET 1 AA3 3 GLN G 26 GLY G 33 0
SHEET 2 AA3 3 THR G 55 THR G 63 -1 O GLN G 59 N VAL G 30
SHEET 3 AA3 3 THR G 92 GLU G 96 -1 O LEU G 93 N LEU G 58
SHEET 1 AA4 4 VAL G 47 ARG G 51 0
SHEET 2 AA4 4 ALA G 118 LEU G 129 1 O GLN G 127 N ILE G 50
SHEET 3 AA4 4 GLY G 104 ALA G 110 -1 N TYR G 106 O ILE G 122
SHEET 4 AA4 4 TRP G 72 THR G 73 -1 N THR G 73 O TYR G 107
SHEET 1 AA5 3 VAL G 47 ARG G 51 0
SHEET 2 AA5 3 ALA G 118 LEU G 129 1 O GLN G 127 N ILE G 50
SHEET 3 AA5 3 SER G 161 ASN G 162 -1 O ASN G 162 N TYR G 128
SHEET 1 AA6 4 MET G 133 THR G 139 0
SHEET 2 AA6 4 THR G 152 THR G 158 -1 O PHE G 154 N HIS G 137
SHEET 3 AA6 4 THR G 196 LEU G 201 -1 O LYS G 197 N CYS G 157
SHEET 4 AA6 4 VAL G 184 TYR G 187 -1 N ASP G 185 O LYS G 200
SHEET 1 AA7 3 ARG G 166 LYS G 170 0
SHEET 2 AA7 3 TYR G 212 SER G 217 -1 O SER G 217 N ARG G 166
SHEET 3 AA7 3 THR G 230 PHE G 231 -1 O PHE G 231 N TYR G 212
SHEET 1 AA8 4 VAL B 54 ARG B 56 0
SHEET 2 AA8 4 VAL B 66 GLN B 68 -1 O GLN B 68 N VAL B 54
SHEET 3 AA8 4 TYR B 143 PRO B 149 -1 O VAL B 148 N VAL B 67
SHEET 4 AA8 4 VAL B 72 PRO B 73 -1 N VAL B 72 O LEU B 144
SHEET 1 AA911 VAL B 54 ARG B 56 0
SHEET 2 AA911 VAL B 66 GLN B 68 -1 O GLN B 68 N VAL B 54
SHEET 3 AA911 TYR B 143 PRO B 149 -1 O VAL B 148 N VAL B 67
SHEET 4 AA911 ILE B 208 THR B 211 -1 O THR B 211 N ASN B 145
SHEET 5 AA911 LYS B 177 PHE B 182 1 N MET B 180 O ILE B 208
SHEET 6 AA911 GLY B 254 SER B 264 1 O THR B 260 N VAL B 179
SHEET 7 AA911 LYS B 286 GLN B 290 1 O ILE B 288 N GLY B 263
SHEET 8 AA911 ASP B 377 ASN B 383 1 O ASP B 377 N ALA B 287
SHEET 9 AA911 VAL B 478 PHE B 483 1 O PHE B 483 N VAL B 382
SHEET 10 AA911 TYR B 580 HIS B 582 1 O LEU B 581 N PHE B 480
SHEET 11 AA911 ARG B 588 ARG B 590 -1 O ARG B 588 N HIS B 582
SHEET 1 AB1 4 VAL C 54 ARG C 56 0
SHEET 2 AB1 4 VAL C 66 GLN C 68 -1 O GLN C 68 N VAL C 54
SHEET 3 AB1 4 TYR C 143 PRO C 149 -1 O VAL C 148 N VAL C 67
SHEET 4 AB1 4 VAL C 72 PRO C 73 -1 N VAL C 72 O LEU C 144
SHEET 1 AB211 VAL C 54 ARG C 56 0
SHEET 2 AB211 VAL C 66 GLN C 68 -1 O GLN C 68 N VAL C 54
SHEET 3 AB211 TYR C 143 PRO C 149 -1 O VAL C 148 N VAL C 67
SHEET 4 AB211 ILE C 208 THR C 211 -1 O THR C 211 N ASN C 145
SHEET 5 AB211 LYS C 177 PHE C 182 1 N MET C 180 O ILE C 208
SHEET 6 AB211 GLY C 254 SER C 264 1 O THR C 260 N VAL C 179
SHEET 7 AB211 LYS C 286 GLN C 290 1 O ILE C 288 N GLY C 263
SHEET 8 AB211 ASP C 377 ASN C 383 1 O ASP C 377 N ALA C 287
SHEET 9 AB211 VAL C 478 PHE C 483 1 O PHE C 483 N VAL C 382
SHEET 10 AB211 TYR C 580 HIS C 582 1 O LEU C 581 N PHE C 480
SHEET 11 AB211 ARG C 588 ARG C 590 -1 O ARG C 588 N HIS C 582
SHEET 1 AB3 4 VAL D 54 ARG D 56 0
SHEET 2 AB3 4 VAL D 66 GLN D 68 -1 O GLN D 68 N VAL D 54
SHEET 3 AB3 4 TYR D 143 PRO D 149 -1 O VAL D 148 N VAL D 67
SHEET 4 AB3 4 VAL D 72 PRO D 73 -1 N VAL D 72 O LEU D 144
SHEET 1 AB411 VAL D 54 ARG D 56 0
SHEET 2 AB411 VAL D 66 GLN D 68 -1 O GLN D 68 N VAL D 54
SHEET 3 AB411 TYR D 143 PRO D 149 -1 O VAL D 148 N VAL D 67
SHEET 4 AB411 ILE D 208 THR D 211 -1 O THR D 211 N ASN D 145
SHEET 5 AB411 LYS D 177 PHE D 182 1 N MET D 180 O ILE D 208
SHEET 6 AB411 GLY D 254 SER D 264 1 O THR D 260 N VAL D 179
SHEET 7 AB411 LYS D 286 GLN D 290 1 O ILE D 288 N GLY D 263
SHEET 8 AB411 ASP D 377 ASN D 383 1 O ASP D 377 N ALA D 287
SHEET 9 AB411 VAL D 478 PHE D 483 1 O PHE D 483 N VAL D 382
SHEET 10 AB411 TYR D 580 HIS D 582 1 O LEU D 581 N PHE D 480
SHEET 11 AB411 ARG D 588 ARG D 590 -1 O ARG D 588 N HIS D 582
SHEET 1 AB5 4 VAL E 54 ARG E 56 0
SHEET 2 AB5 4 VAL E 66 GLN E 68 -1 O GLN E 68 N VAL E 54
SHEET 3 AB5 4 TYR E 143 PRO E 149 -1 O VAL E 148 N VAL E 67
SHEET 4 AB5 4 VAL E 72 PRO E 73 -1 N VAL E 72 O LEU E 144
SHEET 1 AB611 VAL E 54 ARG E 56 0
SHEET 2 AB611 VAL E 66 GLN E 68 -1 O GLN E 68 N VAL E 54
SHEET 3 AB611 TYR E 143 PRO E 149 -1 O VAL E 148 N VAL E 67
SHEET 4 AB611 ILE E 208 THR E 211 -1 O THR E 211 N ASN E 145
SHEET 5 AB611 LYS E 177 PHE E 182 1 N MET E 180 O ILE E 208
SHEET 6 AB611 GLY E 254 SER E 264 1 O THR E 260 N VAL E 179
SHEET 7 AB611 LYS E 286 GLN E 290 1 O ILE E 288 N GLY E 263
SHEET 8 AB611 ASP E 377 ASN E 383 1 O ASP E 377 N ALA E 287
SHEET 9 AB611 VAL E 478 PHE E 483 1 O PHE E 483 N VAL E 382
SHEET 10 AB611 TYR E 580 HIS E 582 1 O LEU E 581 N PHE E 480
SHEET 11 AB611 ARG E 588 ARG E 590 -1 O ARG E 588 N HIS E 582
SHEET 1 AB7 4 VAL F 54 ARG F 56 0
SHEET 2 AB7 4 VAL F 66 GLN F 68 -1 O GLN F 68 N VAL F 54
SHEET 3 AB7 4 TYR F 143 PRO F 149 -1 O VAL F 148 N VAL F 67
SHEET 4 AB7 4 VAL F 72 PRO F 73 -1 N VAL F 72 O LEU F 144
SHEET 1 AB811 VAL F 54 ARG F 56 0
SHEET 2 AB811 VAL F 66 GLN F 68 -1 O GLN F 68 N VAL F 54
SHEET 3 AB811 TYR F 143 PRO F 149 -1 O VAL F 148 N VAL F 67
SHEET 4 AB811 ILE F 208 THR F 211 -1 O THR F 211 N ASN F 145
SHEET 5 AB811 LYS F 177 PHE F 182 1 N MET F 180 O ILE F 208
SHEET 6 AB811 GLY F 254 SER F 264 1 O THR F 260 N VAL F 179
SHEET 7 AB811 LYS F 286 GLN F 290 1 O ILE F 288 N GLY F 263
SHEET 8 AB811 ASP F 377 ASN F 383 1 O ASP F 377 N ALA F 287
SHEET 9 AB811 VAL F 478 PHE F 483 1 O PHE F 483 N VAL F 382
SHEET 10 AB811 TYR F 580 HIS F 582 1 O LEU F 581 N PHE F 480
SHEET 11 AB811 ARG F 588 ARG F 590 -1 O ARG F 588 N HIS F 582
SHEET 1 AB9 3 GLN H 26 GLY H 33 0
SHEET 2 AB9 3 THR H 55 THR H 63 -1 O GLN H 59 N VAL H 30
SHEET 3 AB9 3 THR H 92 GLU H 96 -1 O LEU H 93 N LEU H 58
SHEET 1 AC1 4 VAL H 47 ARG H 51 0
SHEET 2 AC1 4 ALA H 118 LEU H 129 1 O GLN H 127 N ILE H 50
SHEET 3 AC1 4 GLY H 104 ALA H 110 -1 N TYR H 106 O ILE H 122
SHEET 4 AC1 4 TRP H 72 THR H 73 -1 N THR H 73 O TYR H 107
SHEET 1 AC2 3 VAL H 47 ARG H 51 0
SHEET 2 AC2 3 ALA H 118 LEU H 129 1 O GLN H 127 N ILE H 50
SHEET 3 AC2 3 SER H 161 ASN H 162 -1 O ASN H 162 N TYR H 128
SHEET 1 AC3 4 MET H 133 THR H 139 0
SHEET 2 AC3 4 THR H 152 THR H 158 -1 O PHE H 154 N HIS H 137
SHEET 3 AC3 4 THR H 196 LEU H 201 -1 O LYS H 197 N CYS H 157
SHEET 4 AC3 4 VAL H 184 TYR H 187 -1 N ASP H 185 O LYS H 200
SHEET 1 AC4 3 ARG H 166 LYS H 170 0
SHEET 2 AC4 3 TYR H 212 SER H 217 -1 O SER H 217 N ARG H 166
SHEET 3 AC4 3 THR H 230 PHE H 231 -1 O PHE H 231 N TYR H 212
SHEET 1 AC5 3 GLN I 26 GLY I 33 0
SHEET 2 AC5 3 THR I 55 THR I 63 -1 O GLN I 59 N VAL I 30
SHEET 3 AC5 3 THR I 92 GLU I 96 -1 O LEU I 93 N LEU I 58
SHEET 1 AC6 4 VAL I 47 ARG I 51 0
SHEET 2 AC6 4 ALA I 118 LEU I 129 1 O GLN I 127 N ILE I 50
SHEET 3 AC6 4 GLY I 104 ALA I 110 -1 N TYR I 106 O ILE I 122
SHEET 4 AC6 4 TRP I 72 THR I 73 -1 N THR I 73 O TYR I 107
SHEET 1 AC7 3 VAL I 47 ARG I 51 0
SHEET 2 AC7 3 ALA I 118 LEU I 129 1 O GLN I 127 N ILE I 50
SHEET 3 AC7 3 SER I 161 ASN I 162 -1 O ASN I 162 N TYR I 128
SHEET 1 AC8 4 MET I 133 THR I 139 0
SHEET 2 AC8 4 THR I 152 THR I 158 -1 O PHE I 154 N HIS I 137
SHEET 3 AC8 4 THR I 196 LEU I 201 -1 O LYS I 197 N CYS I 157
SHEET 4 AC8 4 VAL I 184 TYR I 187 -1 N ASP I 185 O LYS I 200
SHEET 1 AC9 3 ARG I 166 LYS I 170 0
SHEET 2 AC9 3 TYR I 212 SER I 217 -1 O SER I 217 N ARG I 166
SHEET 3 AC9 3 THR I 230 PHE I 231 -1 O PHE I 231 N TYR I 212
SHEET 1 AD1 3 GLN J 26 GLY J 33 0
SHEET 2 AD1 3 THR J 55 THR J 63 -1 O GLN J 59 N VAL J 30
SHEET 3 AD1 3 THR J 92 GLU J 96 -1 O LEU J 93 N LEU J 58
SHEET 1 AD2 4 VAL J 47 ARG J 51 0
SHEET 2 AD2 4 ALA J 118 LEU J 129 1 O GLN J 127 N ILE J 50
SHEET 3 AD2 4 GLY J 104 ALA J 110 -1 N TYR J 106 O ILE J 122
SHEET 4 AD2 4 TRP J 72 THR J 73 -1 N THR J 73 O TYR J 107
SHEET 1 AD3 3 VAL J 47 ARG J 51 0
SHEET 2 AD3 3 ALA J 118 LEU J 129 1 O GLN J 127 N ILE J 50
SHEET 3 AD3 3 SER J 161 ASN J 162 -1 O ASN J 162 N TYR J 128
SHEET 1 AD4 4 MET J 133 THR J 139 0
SHEET 2 AD4 4 THR J 152 THR J 158 -1 O PHE J 154 N HIS J 137
SHEET 3 AD4 4 THR J 196 LEU J 201 -1 O LYS J 197 N CYS J 157
SHEET 4 AD4 4 VAL J 184 TYR J 187 -1 N ASP J 185 O LYS J 200
SHEET 1 AD5 3 ARG J 166 LYS J 170 0
SHEET 2 AD5 3 TYR J 212 SER J 217 -1 O SER J 217 N ARG J 166
SHEET 3 AD5 3 THR J 230 PHE J 231 -1 O PHE J 231 N TYR J 212
SHEET 1 AD6 3 GLN K 26 GLY K 33 0
SHEET 2 AD6 3 THR K 55 THR K 63 -1 O GLN K 59 N VAL K 30
SHEET 3 AD6 3 THR K 92 GLU K 96 -1 O LEU K 93 N LEU K 58
SHEET 1 AD7 4 VAL K 47 ARG K 51 0
SHEET 2 AD7 4 ALA K 118 LEU K 129 1 O GLN K 127 N ILE K 50
SHEET 3 AD7 4 GLY K 104 ALA K 110 -1 N TYR K 106 O ILE K 122
SHEET 4 AD7 4 TRP K 72 THR K 73 -1 N THR K 73 O TYR K 107
SHEET 1 AD8 3 VAL K 47 ARG K 51 0
SHEET 2 AD8 3 ALA K 118 LEU K 129 1 O GLN K 127 N ILE K 50
SHEET 3 AD8 3 SER K 161 ASN K 162 -1 O ASN K 162 N TYR K 128
SHEET 1 AD9 4 MET K 133 THR K 139 0
SHEET 2 AD9 4 THR K 152 THR K 158 -1 O PHE K 154 N HIS K 137
SHEET 3 AD9 4 THR K 196 LEU K 201 -1 O LYS K 197 N CYS K 157
SHEET 4 AD9 4 VAL K 184 TYR K 187 -1 N ASP K 185 O LYS K 200
SHEET 1 AE1 3 ARG K 166 LYS K 170 0
SHEET 2 AE1 3 TYR K 212 SER K 217 -1 O SER K 217 N ARG K 166
SHEET 3 AE1 3 THR K 230 PHE K 231 -1 O PHE K 231 N TYR K 212
SHEET 1 AE2 3 GLN L 26 GLY L 33 0
SHEET 2 AE2 3 THR L 55 THR L 63 -1 O GLN L 59 N VAL L 30
SHEET 3 AE2 3 THR L 92 GLU L 96 -1 O ILE L 95 N LEU L 56
SHEET 1 AE3 4 VAL L 47 ARG L 51 0
SHEET 2 AE3 4 ALA L 118 LEU L 129 1 O GLN L 127 N ILE L 50
SHEET 3 AE3 4 GLY L 104 ALA L 110 -1 N TYR L 106 O ILE L 122
SHEET 4 AE3 4 TRP L 72 THR L 73 -1 N THR L 73 O TYR L 107
SHEET 1 AE4 3 VAL L 47 ARG L 51 0
SHEET 2 AE4 3 ALA L 118 LEU L 129 1 O GLN L 127 N ILE L 50
SHEET 3 AE4 3 SER L 161 ASN L 162 -1 O ASN L 162 N TYR L 128
SHEET 1 AE5 4 MET L 133 THR L 139 0
SHEET 2 AE5 4 THR L 152 THR L 158 -1 O PHE L 154 N HIS L 137
SHEET 3 AE5 4 THR L 196 LEU L 201 -1 O LYS L 197 N CYS L 157
SHEET 4 AE5 4 VAL L 184 TYR L 187 -1 N ASP L 185 O LYS L 200
SHEET 1 AE6 3 ARG L 166 LYS L 170 0
SHEET 2 AE6 3 TYR L 212 SER L 217 -1 O SER L 217 N ARG L 166
SHEET 3 AE6 3 THR L 230 PHE L 231 -1 O PHE L 231 N TYR L 212
SSBOND 1 CYS A 106 CYS A 141 1555 1555 2.03
SSBOND 2 CYS A 317 CYS A 328 1555 1555 2.05
SSBOND 3 CYS A 487 CYS A 521 1555 1555 2.13
SSBOND 4 CYS G 36 CYS G 222 1555 1555 2.06
SSBOND 5 CYS G 60 CYS G 108 1555 1555 2.02
SSBOND 6 CYS G 157 CYS G 214 1555 1555 2.05
SSBOND 7 CYS B 106 CYS B 141 1555 1555 2.05
SSBOND 8 CYS B 317 CYS B 328 1555 1555 2.06
SSBOND 9 CYS B 487 CYS B 521 1555 1555 2.11
SSBOND 10 CYS C 106 CYS C 141 1555 1555 2.03
SSBOND 11 CYS C 317 CYS C 328 1555 1555 2.05
SSBOND 12 CYS C 487 CYS C 521 1555 1555 2.10
SSBOND 13 CYS D 106 CYS D 141 1555 1555 2.04
SSBOND 14 CYS D 317 CYS D 328 1555 1555 2.04
SSBOND 15 CYS D 487 CYS D 521 1555 1555 2.09
SSBOND 16 CYS E 106 CYS E 141 1555 1555 2.05
SSBOND 17 CYS E 317 CYS E 328 1555 1555 2.05
SSBOND 18 CYS E 487 CYS E 521 1555 1555 2.09
SSBOND 19 CYS F 106 CYS F 141 1555 1555 2.05
SSBOND 20 CYS F 317 CYS F 328 1555 1555 2.04
SSBOND 21 CYS F 487 CYS F 521 1555 1555 2.07
SSBOND 22 CYS H 36 CYS H 222 1555 1555 2.09
SSBOND 23 CYS H 60 CYS H 108 1555 1555 2.02
SSBOND 24 CYS H 157 CYS H 214 1555 1555 2.04
SSBOND 25 CYS I 36 CYS I 222 1555 1555 2.06
SSBOND 26 CYS I 60 CYS I 108 1555 1555 2.04
SSBOND 27 CYS I 157 CYS I 214 1555 1555 2.05
SSBOND 28 CYS J 36 CYS J 222 1555 1555 2.06
SSBOND 29 CYS J 60 CYS J 108 1555 1555 2.04
SSBOND 30 CYS J 157 CYS J 214 1555 1555 2.05
SSBOND 31 CYS K 36 CYS K 222 1555 1555 2.10
SSBOND 32 CYS K 60 CYS K 108 1555 1555 2.03
SSBOND 33 CYS K 157 CYS K 214 1555 1555 2.04
SSBOND 34 CYS L 36 CYS L 222 1555 1555 2.05
SSBOND 35 CYS L 60 CYS L 108 1555 1555 2.03
SSBOND 36 CYS L 157 CYS L 214 1555 1555 2.05
CISPEP 1 TYR A 420 PRO A 421 0 -26.05
CISPEP 2 ASN G 162 PRO G 163 0 1.15
CISPEP 3 GLY G 194 GLU G 195 0 11.51
CISPEP 4 TYR B 420 PRO B 421 0 -25.73
CISPEP 5 TYR C 420 PRO C 421 0 -25.88
CISPEP 6 TYR D 420 PRO D 421 0 -26.06
CISPEP 7 TYR E 420 PRO E 421 0 -25.96
CISPEP 8 TYR F 420 PRO F 421 0 -25.88
CISPEP 9 ASN H 162 PRO H 163 0 0.94
CISPEP 10 GLY H 194 GLU H 195 0 14.93
CISPEP 11 ASN I 162 PRO I 163 0 0.91
CISPEP 12 GLY I 194 GLU I 195 0 12.43
CISPEP 13 ASN J 162 PRO J 163 0 1.23
CISPEP 14 GLY J 194 GLU J 195 0 14.42
CISPEP 15 ASN K 162 PRO K 163 0 1.14
CISPEP 16 GLY K 194 GLU K 195 0 12.16
CISPEP 17 ASN L 162 PRO L 163 0 0.78
CISPEP 18 GLY L 194 GLU L 195 0 13.43
CRYST1 103.118 97.182 190.510 95.52 80.97 88.71 P 1 6
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 0.009698 -0.000218 -0.001571 0.00000
SCALE2 0.000000 0.010293 0.001045 0.00000
SCALE3 0.000000 0.000000 0.005342 0.00000
TER 4131 HIS A 609
TER 5592 THR G 234
TER 9723 HIS B 609
TER 13854 HIS C 609
TER 17985 HIS D 609
TER 22116 HIS E 609
TER 26247 HIS F 609
TER 27708 THR H 234
TER 29169 THR I 234
TER 30630 THR J 234
TER 32091 THR K 234
TER 33552 THR L 234
MASTER 1377 0 0 155 192 0 0 633540 12 72 378
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