HEADER PROTEIN BINDING 26-MAR-18 6G3W
TITLE CRYSTAL STRUCTURE OF THE BIR3 - SERK2 COMPLEX FROM ARABIDOPSIS
TITLE 2 THALIANA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SOMATIC EMBRYOGENESIS RECEPTOR KINASE 2;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: ATSERK2,SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE 2;
COMPND 5 EC: 2.7.11.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROBABLE INACTIVE RECEPTOR KINASE AT1G27190;
COMPND 9 CHAIN: B, D;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: SERK2, AT1G34210, F23M19.11;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: TNAO38;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 13 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 14 ORGANISM_TAXID: 3702;
SOURCE 15 GENE: AT1G27190, T7N9.25;
SOURCE 16 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: TNAO38;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS LEUCINE RICH REPEAT RECEPTOR, MEMBRANE RECEPTOR, PSEUDOKINASE,
KEYWDS 2 ECTODOMAIN, RECEPTOR COMPLEX, NEGATIVE REGULATOR, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HOTHORN,U.HOHMANN
REVDAT 5 17-JAN-24 6G3W 1 HETSYN
REVDAT 4 29-JUL-20 6G3W 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 05-SEP-18 6G3W 1 JRNL
REVDAT 2 16-MAY-18 6G3W 1 JRNL
REVDAT 1 04-APR-18 6G3W 0
JRNL AUTH U.HOHMANN,J.NICOLET,A.MORETTI,L.A.HOTHORN,M.HOTHORN
JRNL TITL THE SERK3 ELONGATED ALLELE DEFINES A ROLE FOR BIR
JRNL TITL 2 ECTODOMAINS IN BRASSINOSTEROID SIGNALLING.
JRNL REF NAT PLANTS V. 4 345 2018
JRNL REFN ESSN 2055-0278
JRNL PMID 29735985
JRNL DOI 10.1038/S41477-018-0150-9
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0218
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 40314
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2122
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2928
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.3610
REMARK 3 BIN FREE R VALUE SET COUNT : 154
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5634
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 176
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.21000
REMARK 3 B22 (A**2) : 1.96000
REMARK 3 B33 (A**2) : -3.17000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.292
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.214
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.192
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.233
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5934 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5445 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8093 ; 1.434 ; 2.025
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12756 ; 0.808 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 744 ; 5.957 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 234 ;43.427 ;25.641
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 977 ;13.170 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;19.823 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 972 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6481 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1042 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2982 ; 1.214 ; 3.416
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2981 ; 1.214 ; 3.416
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3721 ; 1.977 ; 5.117
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3722 ; 1.976 ; 5.117
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2952 ; 1.668 ; 3.779
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2953 ; 1.668 ; 3.780
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4372 ; 2.785 ; 5.618
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 24038 ; 6.071 ;67.116
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 24012 ; 6.068 ;67.084
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 : 2
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 30 212 C 30 212 5622 0.11 0.05
REMARK 3 2 B 26 212 D 26 212 5266 0.13 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 23
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 26 A 52
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9345 22.0522 119.1556
REMARK 3 T TENSOR
REMARK 3 T11: 0.3073 T22: 0.1766
REMARK 3 T33: 0.1157 T12: -0.0908
REMARK 3 T13: 0.0306 T23: 0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 7.5514 L22: 2.8573
REMARK 3 L33: 6.5146 L12: 0.2361
REMARK 3 L13: 2.8340 L23: -1.1533
REMARK 3 S TENSOR
REMARK 3 S11: 0.0727 S12: 0.5062 S13: 0.2271
REMARK 3 S21: -0.7388 S22: 0.1484 S23: 0.0915
REMARK 3 S31: -0.3131 S32: 0.2643 S33: -0.2211
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 53 A 89
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3432 20.7859 125.6341
REMARK 3 T TENSOR
REMARK 3 T11: 0.2283 T22: 0.1259
REMARK 3 T33: 0.1253 T12: -0.0564
REMARK 3 T13: 0.0828 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 5.9218 L22: 3.1157
REMARK 3 L33: 4.9920 L12: 1.5580
REMARK 3 L13: 2.2965 L23: -0.3838
REMARK 3 S TENSOR
REMARK 3 S11: -0.1142 S12: 0.6724 S13: 0.4622
REMARK 3 S21: -0.3579 S22: 0.1463 S23: -0.2464
REMARK 3 S31: -0.6398 S32: 0.6453 S33: -0.0321
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 90 A 164
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5323 7.6766 127.4160
REMARK 3 T TENSOR
REMARK 3 T11: 0.0480 T22: 0.0375
REMARK 3 T33: 0.0359 T12: 0.0158
REMARK 3 T13: -0.0078 T23: -0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 4.8969 L22: 2.4044
REMARK 3 L33: 3.0749 L12: 1.3493
REMARK 3 L13: 0.7361 L23: 1.0287
REMARK 3 S TENSOR
REMARK 3 S11: 0.0814 S12: 0.3301 S13: -0.2313
REMARK 3 S21: -0.0385 S22: 0.0489 S23: -0.2193
REMARK 3 S31: 0.2249 S32: 0.1204 S33: -0.1304
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 165 A 176
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3403 1.5286 136.5994
REMARK 3 T TENSOR
REMARK 3 T11: 0.2394 T22: 0.1282
REMARK 3 T33: 0.1908 T12: -0.0249
REMARK 3 T13: -0.0782 T23: 0.0395
REMARK 3 L TENSOR
REMARK 3 L11: 8.3370 L22: 2.0770
REMARK 3 L33: 7.3144 L12: 1.4588
REMARK 3 L13: -1.6085 L23: 3.2703
REMARK 3 S TENSOR
REMARK 3 S11: 0.2409 S12: -0.7558 S13: -1.0015
REMARK 3 S21: 0.3338 S22: -0.1507 S23: -0.3564
REMARK 3 S31: 0.4483 S32: 0.0324 S33: -0.0902
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 177 A 213
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8121 -1.1188 133.6574
REMARK 3 T TENSOR
REMARK 3 T11: 0.2255 T22: 0.2010
REMARK 3 T33: 0.1466 T12: -0.1120
REMARK 3 T13: -0.0023 T23: -0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 6.6787 L22: 6.4194
REMARK 3 L33: 5.0106 L12: 1.1409
REMARK 3 L13: -0.3539 L23: -1.7264
REMARK 3 S TENSOR
REMARK 3 S11: 0.0502 S12: -0.2951 S13: -0.6400
REMARK 3 S21: 0.2358 S22: -0.0110 S23: 0.4107
REMARK 3 S31: 0.8771 S32: -0.7241 S33: -0.0393
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 25 B 37
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5744 19.8980 153.2013
REMARK 3 T TENSOR
REMARK 3 T11: 0.0765 T22: 0.1035
REMARK 3 T33: 0.2253 T12: 0.0089
REMARK 3 T13: 0.0192 T23: -0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 3.7143 L22: 2.7789
REMARK 3 L33: 17.4168 L12: 0.2542
REMARK 3 L13: 1.6365 L23: 3.1873
REMARK 3 S TENSOR
REMARK 3 S11: -0.1902 S12: 0.1819 S13: 0.1633
REMARK 3 S21: -0.2620 S22: 0.1852 S23: 0.0640
REMARK 3 S31: -0.3397 S32: -0.0792 S33: 0.0049
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 38 B 76
REMARK 3 ORIGIN FOR THE GROUP (A): -17.3401 19.6451 150.8444
REMARK 3 T TENSOR
REMARK 3 T11: 0.0694 T22: 0.0416
REMARK 3 T33: 0.1397 T12: 0.0202
REMARK 3 T13: -0.0035 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 1.4650 L22: 3.2801
REMARK 3 L33: 6.8695 L12: 0.8622
REMARK 3 L13: -0.2019 L23: 0.7307
REMARK 3 S TENSOR
REMARK 3 S11: -0.0314 S12: 0.0734 S13: 0.2759
REMARK 3 S21: -0.2772 S22: 0.1004 S23: 0.0510
REMARK 3 S31: -0.6054 S32: -0.2458 S33: -0.0690
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 77 B 165
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3416 3.4936 158.4984
REMARK 3 T TENSOR
REMARK 3 T11: 0.0555 T22: 0.0196
REMARK 3 T33: 0.1007 T12: -0.0257
REMARK 3 T13: 0.0271 T23: -0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 1.7815 L22: 2.1189
REMARK 3 L33: 4.4822 L12: 0.1180
REMARK 3 L13: 0.2312 L23: -0.5403
REMARK 3 S TENSOR
REMARK 3 S11: -0.1373 S12: 0.0079 S13: -0.0196
REMARK 3 S21: -0.0886 S22: 0.0765 S23: -0.0038
REMARK 3 S31: 0.4082 S32: -0.1888 S33: 0.0607
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 166 B 173
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8993 -8.7858 150.9260
REMARK 3 T TENSOR
REMARK 3 T11: 0.4304 T22: 0.2118
REMARK 3 T33: 0.3301 T12: -0.0339
REMARK 3 T13: -0.0007 T23: -0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 12.4667 L22: 8.7191
REMARK 3 L33: 4.8508 L12: 7.1675
REMARK 3 L13: -4.6044 L23: -3.8869
REMARK 3 S TENSOR
REMARK 3 S11: 0.1418 S12: -0.2529 S13: -0.9102
REMARK 3 S21: 0.3000 S22: -0.1686 S23: -0.3252
REMARK 3 S31: 0.5079 S32: -0.4722 S33: 0.0269
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 174 B 196
REMARK 3 ORIGIN FOR THE GROUP (A): -17.7231 -12.1033 162.5051
REMARK 3 T TENSOR
REMARK 3 T11: 0.3817 T22: 0.0432
REMARK 3 T33: 0.3663 T12: 0.0685
REMARK 3 T13: -0.0110 T23: -0.0782
REMARK 3 L TENSOR
REMARK 3 L11: 2.7100 L22: 4.6295
REMARK 3 L33: 8.5495 L12: -0.3215
REMARK 3 L13: -2.3258 L23: -2.0445
REMARK 3 S TENSOR
REMARK 3 S11: -0.0241 S12: 0.1532 S13: -0.7020
REMARK 3 S21: -0.5231 S22: -0.0523 S23: -0.1400
REMARK 3 S31: 0.9006 S32: 0.3030 S33: 0.0763
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 : B 197 B 213
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2928 -17.4251 168.6596
REMARK 3 T TENSOR
REMARK 3 T11: 0.3517 T22: 0.0942
REMARK 3 T33: 0.3592 T12: 0.0198
REMARK 3 T13: 0.0166 T23: 0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 9.6290 L22: 11.6808
REMARK 3 L33: 3.9827 L12: 1.1414
REMARK 3 L13: -0.9647 L23: 0.9189
REMARK 3 S TENSOR
REMARK 3 S11: 0.2602 S12: 0.0955 S13: -0.8759
REMARK 3 S21: 0.4307 S22: -0.3963 S23: -0.1429
REMARK 3 S31: 0.4772 S32: -0.3420 S33: 0.1361
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 30 C 39
REMARK 3 ORIGIN FOR THE GROUP (A): -26.5981 -9.4112 112.0342
REMARK 3 T TENSOR
REMARK 3 T11: 0.2452 T22: 0.2904
REMARK 3 T33: 0.2243 T12: -0.0119
REMARK 3 T13: 0.0108 T23: -0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 3.7268 L22: 6.2874
REMARK 3 L33: 2.4562 L12: 0.1051
REMARK 3 L13: 1.3408 L23: -1.1248
REMARK 3 S TENSOR
REMARK 3 S11: -0.0284 S12: -0.0398 S13: -0.3478
REMARK 3 S21: 0.0148 S22: 0.1474 S23: 0.1133
REMARK 3 S31: 0.3539 S32: -0.0727 S33: -0.1190
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 40 C 71
REMARK 3 ORIGIN FOR THE GROUP (A): -34.0106 -5.9488 108.7540
REMARK 3 T TENSOR
REMARK 3 T11: 0.1354 T22: 0.5071
REMARK 3 T33: 0.2873 T12: -0.1203
REMARK 3 T13: -0.0405 T23: -0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 2.4037 L22: 4.7979
REMARK 3 L33: 8.4248 L12: 0.6380
REMARK 3 L13: -1.4135 L23: 3.7150
REMARK 3 S TENSOR
REMARK 3 S11: -0.0835 S12: 0.1375 S13: -0.2370
REMARK 3 S21: 0.1414 S22: -0.0496 S23: 0.5388
REMARK 3 S31: 0.7153 S32: -0.5835 S33: 0.1331
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 72 C 135
REMARK 3 ORIGIN FOR THE GROUP (A): -22.4367 0.3847 105.3405
REMARK 3 T TENSOR
REMARK 3 T11: 0.0657 T22: 0.3592
REMARK 3 T33: 0.0653 T12: -0.0720
REMARK 3 T13: -0.0413 T23: -0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 2.5130 L22: 4.3770
REMARK 3 L33: 6.2063 L12: 1.7283
REMARK 3 L13: 0.3955 L23: 2.1037
REMARK 3 S TENSOR
REMARK 3 S11: -0.1045 S12: 0.4188 S13: -0.0660
REMARK 3 S21: -0.0333 S22: 0.0374 S23: 0.0952
REMARK 3 S31: 0.3500 S32: -0.4487 S33: 0.0671
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 136 C 144
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4236 -0.4257 102.7146
REMARK 3 T TENSOR
REMARK 3 T11: 0.2378 T22: 0.3703
REMARK 3 T33: 0.1610 T12: 0.0357
REMARK 3 T13: -0.0444 T23: -0.0717
REMARK 3 L TENSOR
REMARK 3 L11: 2.9155 L22: 6.0100
REMARK 3 L33: 9.2129 L12: 1.4294
REMARK 3 L13: -3.7121 L23: 3.0362
REMARK 3 S TENSOR
REMARK 3 S11: -0.0668 S12: -0.0104 S13: -0.4780
REMARK 3 S21: 0.4953 S22: 0.0280 S23: -0.8388
REMARK 3 S31: 0.6275 S32: 0.1509 S33: 0.0388
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 : C 145 C 207
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3712 10.0921 97.7121
REMARK 3 T TENSOR
REMARK 3 T11: 0.5586 T22: 0.5366
REMARK 3 T33: 0.1772 T12: -0.2361
REMARK 3 T13: 0.1472 T23: -0.0382
REMARK 3 L TENSOR
REMARK 3 L11: 5.1628 L22: 5.9694
REMARK 3 L33: 6.8231 L12: 3.3012
REMARK 3 L13: -2.3380 L23: -1.6220
REMARK 3 S TENSOR
REMARK 3 S11: -0.2263 S12: 0.9282 S13: 0.0415
REMARK 3 S21: -0.8429 S22: 0.6087 S23: -0.5846
REMARK 3 S31: -1.2995 S32: 0.4960 S33: -0.3824
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 : C 208 C 214
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6319 15.2185 100.5037
REMARK 3 T TENSOR
REMARK 3 T11: 0.8518 T22: 0.7542
REMARK 3 T33: 0.3983 T12: -0.1208
REMARK 3 T13: -0.1402 T23: 0.0657
REMARK 3 L TENSOR
REMARK 3 L11: 6.8986 L22: 10.4216
REMARK 3 L33: 2.4323 L12: 4.6627
REMARK 3 L13: 1.9511 L23: 4.9906
REMARK 3 S TENSOR
REMARK 3 S11: 0.9461 S12: -0.2819 S13: 0.6669
REMARK 3 S21: 0.6465 S22: -0.7699 S23: -0.3527
REMARK 3 S31: 0.1381 S32: -0.3255 S33: -0.1762
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 30 D 38
REMARK 3 ORIGIN FOR THE GROUP (A): -27.9605 20.6114 74.9585
REMARK 3 T TENSOR
REMARK 3 T11: 0.4162 T22: 0.4385
REMARK 3 T33: 0.3697 T12: 0.0260
REMARK 3 T13: -0.0189 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 10.6607 L22: 3.5419
REMARK 3 L33: 8.8023 L12: -0.0530
REMARK 3 L13: 6.8291 L23: 3.9138
REMARK 3 S TENSOR
REMARK 3 S11: 0.1419 S12: -0.1168 S13: -0.1003
REMARK 3 S21: 0.0650 S22: -0.2164 S23: 0.2237
REMARK 3 S31: 0.2479 S32: -0.2215 S33: 0.0745
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 39 D 71
REMARK 3 ORIGIN FOR THE GROUP (A): -30.4673 14.1211 81.1608
REMARK 3 T TENSOR
REMARK 3 T11: 0.5095 T22: 0.7280
REMARK 3 T33: 0.3485 T12: 0.0602
REMARK 3 T13: 0.0162 T23: 0.0813
REMARK 3 L TENSOR
REMARK 3 L11: 6.2726 L22: 0.5168
REMARK 3 L33: 5.9904 L12: -0.4829
REMARK 3 L13: -0.0195 L23: -1.5803
REMARK 3 S TENSOR
REMARK 3 S11: 0.0116 S12: 0.0610 S13: 0.1194
REMARK 3 S21: 0.2353 S22: 0.1250 S23: 0.1466
REMARK 3 S31: -0.5304 S32: -0.5074 S33: -0.1367
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 72 D 91
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3496 15.2648 75.6842
REMARK 3 T TENSOR
REMARK 3 T11: 0.2665 T22: 0.3916
REMARK 3 T33: 0.2850 T12: 0.0901
REMARK 3 T13: -0.0061 T23: 0.1155
REMARK 3 L TENSOR
REMARK 3 L11: 4.2057 L22: 0.4266
REMARK 3 L33: 10.7072 L12: 0.6159
REMARK 3 L13: 1.5571 L23: 0.6555
REMARK 3 S TENSOR
REMARK 3 S11: 0.2093 S12: -0.0720 S13: -0.0920
REMARK 3 S21: 0.3120 S22: 0.0909 S23: -0.0155
REMARK 3 S31: 0.0015 S32: 0.1224 S33: -0.3003
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 92 D 153
REMARK 3 ORIGIN FOR THE GROUP (A): -12.4178 18.3002 74.9467
REMARK 3 T TENSOR
REMARK 3 T11: 0.5737 T22: 0.6411
REMARK 3 T33: 0.2660 T12: -0.1205
REMARK 3 T13: -0.0347 T23: 0.1833
REMARK 3 L TENSOR
REMARK 3 L11: 3.5808 L22: 0.5680
REMARK 3 L33: 4.7415 L12: -0.7884
REMARK 3 L13: 0.0740 L23: -1.0817
REMARK 3 S TENSOR
REMARK 3 S11: 0.1631 S12: -0.1685 S13: 0.4005
REMARK 3 S21: 0.3675 S22: -0.1877 S23: -0.1134
REMARK 3 S31: -0.6367 S32: 0.6307 S33: 0.0246
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 154 D 204
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2953 13.3185 68.7428
REMARK 3 T TENSOR
REMARK 3 T11: 0.5155 T22: 0.8460
REMARK 3 T33: 0.4683 T12: 0.0312
REMARK 3 T13: 0.0069 T23: 0.1900
REMARK 3 L TENSOR
REMARK 3 L11: 2.5966 L22: 1.9148
REMARK 3 L33: 6.4892 L12: 2.0587
REMARK 3 L13: 1.0105 L23: 1.2344
REMARK 3 S TENSOR
REMARK 3 S11: 0.2468 S12: 0.0032 S13: -0.0605
REMARK 3 S21: 0.3443 S22: -0.0978 S23: -0.3708
REMARK 3 S31: 0.4575 S32: 0.8184 S33: -0.1489
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 205 D 213
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3209 9.0128 61.1870
REMARK 3 T TENSOR
REMARK 3 T11: 0.5283 T22: 0.8232
REMARK 3 T33: 0.7509 T12: -0.0057
REMARK 3 T13: 0.0606 T23: 0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 1.8913 L22: 0.9139
REMARK 3 L33: 7.0322 L12: 0.9828
REMARK 3 L13: -2.8866 L23: -2.5287
REMARK 3 S TENSOR
REMARK 3 S11: -0.0657 S12: -0.1230 S13: -0.8271
REMARK 3 S21: 0.1092 S22: -0.2812 S23: -0.0710
REMARK 3 S31: -0.2922 S32: 0.7197 S33: 0.3469
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6G3W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009384.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000027
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42439
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 49.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 13.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 1.60400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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: 6FG8, 4Z61
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) PEG 3,350, 0.2 M MGCL_2 X
REMARK 280 6H_2O, 0.1 M BIS-TRIS PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 25.09200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 154.44600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.07750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 154.44600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.09200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.07750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 28
REMARK 465 SER A 29
REMARK 465 GLY A 215
REMARK 465 SER A 216
REMARK 465 LEU A 217
REMARK 465 GLU A 218
REMARK 465 ASN A 219
REMARK 465 LEU A 220
REMARK 465 TYR A 221
REMARK 465 PHE A 222
REMARK 465 GLN A 223
REMARK 465 GLY A 224
REMARK 465 ALA A 225
REMARK 465 TRP A 226
REMARK 465 SER A 227
REMARK 465 HIS A 228
REMARK 465 PRO A 229
REMARK 465 GLN A 230
REMARK 465 PHE A 231
REMARK 465 GLU A 232
REMARK 465 LYS A 233
REMARK 465 GLY A 234
REMARK 465 SER A 235
REMARK 465 HIS A 236
REMARK 465 HIS A 237
REMARK 465 HIS A 238
REMARK 465 HIS A 239
REMARK 465 HIS A 240
REMARK 465 HIS A 241
REMARK 465 HIS A 242
REMARK 465 HIS A 243
REMARK 465 HIS A 244
REMARK 465 LEU B 214
REMARK 465 GLU B 215
REMARK 465 ASN B 216
REMARK 465 LEU B 217
REMARK 465 TYR B 218
REMARK 465 PHE B 219
REMARK 465 GLN B 220
REMARK 465 SER C 28
REMARK 465 SER C 29
REMARK 465 PRO C 214
REMARK 465 GLY C 215
REMARK 465 SER C 216
REMARK 465 LEU C 217
REMARK 465 GLU C 218
REMARK 465 ASN C 219
REMARK 465 LEU C 220
REMARK 465 TYR C 221
REMARK 465 PHE C 222
REMARK 465 GLN C 223
REMARK 465 GLY C 224
REMARK 465 ALA C 225
REMARK 465 TRP C 226
REMARK 465 SER C 227
REMARK 465 HIS C 228
REMARK 465 PRO C 229
REMARK 465 GLN C 230
REMARK 465 PHE C 231
REMARK 465 GLU C 232
REMARK 465 LYS C 233
REMARK 465 GLY C 234
REMARK 465 SER C 235
REMARK 465 HIS C 236
REMARK 465 HIS C 237
REMARK 465 HIS C 238
REMARK 465 HIS C 239
REMARK 465 HIS C 240
REMARK 465 HIS C 241
REMARK 465 HIS C 242
REMARK 465 HIS C 243
REMARK 465 HIS C 244
REMARK 465 GLU D 25
REMARK 465 LEU D 214
REMARK 465 GLU D 215
REMARK 465 ASN D 216
REMARK 465 LEU D 217
REMARK 465 TYR D 218
REMARK 465 PHE D 219
REMARK 465 GLN D 220
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 211 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 153 62.30 62.50
REMARK 500 ASP A 203 58.93 -160.05
REMARK 500 SER B 53 -131.68 57.81
REMARK 500 ASN B 106 -164.65 -110.07
REMARK 500 ASN B 131 -160.81 -119.43
REMARK 500 ASN B 155 -161.54 -126.42
REMARK 500 ASN B 179 -165.50 -116.36
REMARK 500 ASN C 153 62.35 61.60
REMARK 500 ASP C 203 60.42 -163.08
REMARK 500 SER D 53 -128.15 59.35
REMARK 500 ASN D 106 -165.07 -109.34
REMARK 500 ASN D 131 -162.26 -119.20
REMARK 500 ASN D 155 -162.38 -126.01
REMARK 500 ASN D 179 -165.97 -117.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PEG A 308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6FG8 RELATED DB: PDB
REMARK 900 BIR3 SERK1 COMPLEX
DBREF 6G3W A 28 216 UNP Q9XIC7 SERK2_ARATH 28 216
DBREF 6G3W B 25 214 UNP O04567 Y1719_ARATH 25 214
DBREF 6G3W C 28 216 UNP Q9XIC7 SERK2_ARATH 28 216
DBREF 6G3W D 25 214 UNP O04567 Y1719_ARATH 25 214
SEQADV 6G3W LEU A 217 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLU A 218 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W ASN A 219 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W LEU A 220 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W TYR A 221 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W PHE A 222 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLN A 223 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLY A 224 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W ALA A 225 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W TRP A 226 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W SER A 227 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS A 228 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W PRO A 229 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLN A 230 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W PHE A 231 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLU A 232 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W LYS A 233 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLY A 234 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W SER A 235 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS A 236 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS A 237 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS A 238 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS A 239 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS A 240 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS A 241 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS A 242 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS A 243 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS A 244 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLU B 215 UNP O04567 EXPRESSION TAG
SEQADV 6G3W ASN B 216 UNP O04567 EXPRESSION TAG
SEQADV 6G3W LEU B 217 UNP O04567 EXPRESSION TAG
SEQADV 6G3W TYR B 218 UNP O04567 EXPRESSION TAG
SEQADV 6G3W PHE B 219 UNP O04567 EXPRESSION TAG
SEQADV 6G3W GLN B 220 UNP O04567 EXPRESSION TAG
SEQADV 6G3W LEU C 217 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLU C 218 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W ASN C 219 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W LEU C 220 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W TYR C 221 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W PHE C 222 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLN C 223 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLY C 224 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W ALA C 225 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W TRP C 226 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W SER C 227 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS C 228 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W PRO C 229 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLN C 230 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W PHE C 231 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLU C 232 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W LYS C 233 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLY C 234 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W SER C 235 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS C 236 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS C 237 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS C 238 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS C 239 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS C 240 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS C 241 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS C 242 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS C 243 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W HIS C 244 UNP Q9XIC7 EXPRESSION TAG
SEQADV 6G3W GLU D 215 UNP O04567 EXPRESSION TAG
SEQADV 6G3W ASN D 216 UNP O04567 EXPRESSION TAG
SEQADV 6G3W LEU D 217 UNP O04567 EXPRESSION TAG
SEQADV 6G3W TYR D 218 UNP O04567 EXPRESSION TAG
SEQADV 6G3W PHE D 219 UNP O04567 EXPRESSION TAG
SEQADV 6G3W GLN D 220 UNP O04567 EXPRESSION TAG
SEQRES 1 A 217 SER SER ASN MET GLU GLY ASP ALA LEU HIS SER LEU ARG
SEQRES 2 A 217 ALA ASN LEU VAL ASP PRO ASN ASN VAL LEU GLN SER TRP
SEQRES 3 A 217 ASP PRO THR LEU VAL ASN PRO CYS THR TRP PHE HIS VAL
SEQRES 4 A 217 THR CYS ASN ASN GLU ASN SER VAL ILE ARG VAL ASP LEU
SEQRES 5 A 217 GLY ASN ALA ASP LEU SER GLY GLN LEU VAL PRO GLN LEU
SEQRES 6 A 217 GLY GLN LEU LYS ASN LEU GLN TYR LEU GLU LEU TYR SER
SEQRES 7 A 217 ASN ASN ILE THR GLY PRO VAL PRO SER ASP LEU GLY ASN
SEQRES 8 A 217 LEU THR ASN LEU VAL SER LEU ASP LEU TYR LEU ASN SER
SEQRES 9 A 217 PHE THR GLY PRO ILE PRO ASP SER LEU GLY LYS LEU PHE
SEQRES 10 A 217 LYS LEU ARG PHE LEU ARG LEU ASN ASN ASN SER LEU THR
SEQRES 11 A 217 GLY PRO ILE PRO MET SER LEU THR ASN ILE MET THR LEU
SEQRES 12 A 217 GLN VAL LEU ASP LEU SER ASN ASN ARG LEU SER GLY SER
SEQRES 13 A 217 VAL PRO ASP ASN GLY SER PHE SER LEU PHE THR PRO ILE
SEQRES 14 A 217 SER PHE ALA ASN ASN LEU ASP LEU CYS GLY PRO VAL THR
SEQRES 15 A 217 SER ARG PRO CYS PRO GLY SER LEU GLU ASN LEU TYR PHE
SEQRES 16 A 217 GLN GLY ALA TRP SER HIS PRO GLN PHE GLU LYS GLY SER
SEQRES 17 A 217 HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 196 GLU ASP ASP VAL LEU CYS LEU GLN GLY LEU LYS ASN SER
SEQRES 2 B 196 LEU ILE ASP PRO SER SER ARG LEU SER SER TRP SER PHE
SEQRES 3 B 196 PRO ASN SER SER ALA SER SER ILE CYS LYS LEU THR GLY
SEQRES 4 B 196 VAL SER CYS TRP ASN GLU LYS GLU ASN ARG ILE ILE SER
SEQRES 5 B 196 LEU GLN LEU GLN SER MET GLN LEU ALA GLY GLU ILE PRO
SEQRES 6 B 196 GLU SER LEU LYS LEU CYS ARG SER LEU GLN SER LEU ASP
SEQRES 7 B 196 LEU SER GLY ASN ASP LEU SER GLY SER ILE PRO SER GLN
SEQRES 8 B 196 ILE CYS SER TRP LEU PRO TYR LEU VAL THR LEU ASP LEU
SEQRES 9 B 196 SER GLY ASN LYS LEU GLY GLY SER ILE PRO THR GLN ILE
SEQRES 10 B 196 VAL GLU CYS LYS PHE LEU ASN ALA LEU ILE LEU SER ASP
SEQRES 11 B 196 ASN LYS LEU SER GLY SER ILE PRO SER GLN LEU SER ARG
SEQRES 12 B 196 LEU ASP ARG LEU ARG ARG LEU SER LEU ALA GLY ASN ASP
SEQRES 13 B 196 LEU SER GLY THR ILE PRO SER GLU LEU ALA ARG PHE GLY
SEQRES 14 B 196 GLY ASP ASP PHE SER GLY ASN ASN GLY LEU CYS GLY LYS
SEQRES 15 B 196 PRO LEU SER ARG CYS GLY ALA LEU GLU ASN LEU TYR PHE
SEQRES 16 B 196 GLN
SEQRES 1 C 217 SER SER ASN MET GLU GLY ASP ALA LEU HIS SER LEU ARG
SEQRES 2 C 217 ALA ASN LEU VAL ASP PRO ASN ASN VAL LEU GLN SER TRP
SEQRES 3 C 217 ASP PRO THR LEU VAL ASN PRO CYS THR TRP PHE HIS VAL
SEQRES 4 C 217 THR CYS ASN ASN GLU ASN SER VAL ILE ARG VAL ASP LEU
SEQRES 5 C 217 GLY ASN ALA ASP LEU SER GLY GLN LEU VAL PRO GLN LEU
SEQRES 6 C 217 GLY GLN LEU LYS ASN LEU GLN TYR LEU GLU LEU TYR SER
SEQRES 7 C 217 ASN ASN ILE THR GLY PRO VAL PRO SER ASP LEU GLY ASN
SEQRES 8 C 217 LEU THR ASN LEU VAL SER LEU ASP LEU TYR LEU ASN SER
SEQRES 9 C 217 PHE THR GLY PRO ILE PRO ASP SER LEU GLY LYS LEU PHE
SEQRES 10 C 217 LYS LEU ARG PHE LEU ARG LEU ASN ASN ASN SER LEU THR
SEQRES 11 C 217 GLY PRO ILE PRO MET SER LEU THR ASN ILE MET THR LEU
SEQRES 12 C 217 GLN VAL LEU ASP LEU SER ASN ASN ARG LEU SER GLY SER
SEQRES 13 C 217 VAL PRO ASP ASN GLY SER PHE SER LEU PHE THR PRO ILE
SEQRES 14 C 217 SER PHE ALA ASN ASN LEU ASP LEU CYS GLY PRO VAL THR
SEQRES 15 C 217 SER ARG PRO CYS PRO GLY SER LEU GLU ASN LEU TYR PHE
SEQRES 16 C 217 GLN GLY ALA TRP SER HIS PRO GLN PHE GLU LYS GLY SER
SEQRES 17 C 217 HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 D 196 GLU ASP ASP VAL LEU CYS LEU GLN GLY LEU LYS ASN SER
SEQRES 2 D 196 LEU ILE ASP PRO SER SER ARG LEU SER SER TRP SER PHE
SEQRES 3 D 196 PRO ASN SER SER ALA SER SER ILE CYS LYS LEU THR GLY
SEQRES 4 D 196 VAL SER CYS TRP ASN GLU LYS GLU ASN ARG ILE ILE SER
SEQRES 5 D 196 LEU GLN LEU GLN SER MET GLN LEU ALA GLY GLU ILE PRO
SEQRES 6 D 196 GLU SER LEU LYS LEU CYS ARG SER LEU GLN SER LEU ASP
SEQRES 7 D 196 LEU SER GLY ASN ASP LEU SER GLY SER ILE PRO SER GLN
SEQRES 8 D 196 ILE CYS SER TRP LEU PRO TYR LEU VAL THR LEU ASP LEU
SEQRES 9 D 196 SER GLY ASN LYS LEU GLY GLY SER ILE PRO THR GLN ILE
SEQRES 10 D 196 VAL GLU CYS LYS PHE LEU ASN ALA LEU ILE LEU SER ASP
SEQRES 11 D 196 ASN LYS LEU SER GLY SER ILE PRO SER GLN LEU SER ARG
SEQRES 12 D 196 LEU ASP ARG LEU ARG ARG LEU SER LEU ALA GLY ASN ASP
SEQRES 13 D 196 LEU SER GLY THR ILE PRO SER GLU LEU ALA ARG PHE GLY
SEQRES 14 D 196 GLY ASP ASP PHE SER GLY ASN ASN GLY LEU CYS GLY LYS
SEQRES 15 D 196 PRO LEU SER ARG CYS GLY ALA LEU GLU ASN LEU TYR PHE
SEQRES 16 D 196 GLN
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET NAG A 301 14
HET PEG A 308 6
HET NAG B 301 14
HET EDO B 302 4
HET NAG C 301 14
HET NAG C 302 14
HET NAG C 303 14
HET EDO C 304 4
HET NAG D 301 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 NAG 10(C8 H15 N O6)
FORMUL 5 BMA 2(C6 H12 O6)
FORMUL 8 PEG C4 H10 O3
FORMUL 10 EDO 2(C2 H6 O2)
FORMUL 16 HOH *143(H2 O)
HELIX 1 AA1 ASN A 30 ASN A 42 1 13
HELIX 2 AA2 VAL A 89 LEU A 95 5 7
HELIX 3 AA3 PRO A 113 LEU A 119 5 7
HELIX 4 AA4 PRO A 137 LEU A 143 5 7
HELIX 5 AA5 PRO A 161 ILE A 167 5 7
HELIX 6 AA6 ASN A 187 PHE A 193 5 7
HELIX 7 AA7 THR A 194 PHE A 198 5 5
HELIX 8 AA8 ASP B 26 LEU B 38 1 13
HELIX 9 AA9 ASN B 52 SER B 56 5 5
HELIX 10 AB1 PRO B 89 CYS B 95 5 7
HELIX 11 AB2 GLN B 115 LEU B 120 1 6
HELIX 12 AB3 PRO B 138 CYS B 144 5 7
HELIX 13 AB4 PRO B 162 LEU B 168 5 7
HELIX 14 AB5 PRO B 186 PHE B 192 5 7
HELIX 15 AB6 GLY B 193 PHE B 197 5 5
HELIX 16 AB7 MET C 31 ASN C 42 1 12
HELIX 17 AB8 VAL C 89 LEU C 95 5 7
HELIX 18 AB9 PRO C 113 LEU C 119 5 7
HELIX 19 AC1 PRO C 137 LEU C 143 5 7
HELIX 20 AC2 PRO C 161 ILE C 167 5 7
HELIX 21 AC3 ASN C 187 PHE C 193 5 7
HELIX 22 AC4 THR C 194 ALA C 199 1 6
HELIX 23 AC5 ASP D 27 LEU D 38 1 12
HELIX 24 AC6 ASN D 52 SER D 56 5 5
HELIX 25 AC7 PRO D 89 CYS D 95 5 7
HELIX 26 AC8 GLN D 115 LEU D 120 1 6
HELIX 27 AC9 PRO D 138 CYS D 144 5 7
HELIX 28 AD1 PRO D 162 LEU D 168 5 7
HELIX 29 AD2 PRO D 186 ALA D 190 5 5
SHEET 1 AA1 7 LEU A 43 VAL A 44 0
SHEET 2 AA1 7 SER A 85 GLN A 87 -1 O SER A 85 N VAL A 44
SHEET 3 AA1 7 ASN A 107 GLY A 110 1 O THR A 109 N GLY A 86
SHEET 4 AA1 7 SER A 131 PRO A 135 1 O SER A 131 N ILE A 108
SHEET 5 AA1 7 SER A 155 GLY A 158 1 O SER A 155 N PHE A 132
SHEET 6 AA1 7 ARG A 179 SER A 183 1 O ARG A 179 N LEU A 156
SHEET 7 AA1 7 ASP A 203 CYS A 205 1 O CYS A 205 N GLY A 182
SHEET 1 AA2 6 VAL A 66 CYS A 68 0
SHEET 2 AA2 6 VAL A 74 ASP A 78 -1 O ILE A 75 N THR A 67
SHEET 3 AA2 6 TYR A 100 GLU A 102 1 O GLU A 102 N VAL A 77
SHEET 4 AA2 6 SER A 124 ASP A 126 1 O ASP A 126 N LEU A 101
SHEET 5 AA2 6 PHE A 148 ARG A 150 1 O PHE A 148 N LEU A 125
SHEET 6 AA2 6 VAL A 172 ASP A 174 1 O VAL A 172 N LEU A 149
SHEET 1 AA3 6 VAL B 64 CYS B 66 0
SHEET 2 AA3 6 ILE B 74 GLN B 78 -1 O ILE B 75 N SER B 65
SHEET 3 AA3 6 SER B 100 ASP B 102 1 O ASP B 102 N LEU B 77
SHEET 4 AA3 6 THR B 125 ASP B 127 1 O ASP B 127 N LEU B 101
SHEET 5 AA3 6 ALA B 149 ILE B 151 1 O ILE B 151 N LEU B 126
SHEET 6 AA3 6 ARG B 173 SER B 175 1 O SER B 175 N LEU B 150
SHEET 1 AA4 2 ALA B 85 GLY B 86 0
SHEET 2 AA4 2 ASP B 107 LEU B 108 1 O ASP B 107 N GLY B 86
SHEET 1 AA5 2 SER B 158 GLY B 159 0
SHEET 2 AA5 2 ASP B 180 LEU B 181 1 O ASP B 180 N GLY B 159
SHEET 1 AA6 7 LEU C 43 VAL C 44 0
SHEET 2 AA6 7 SER C 85 GLN C 87 -1 O SER C 85 N VAL C 44
SHEET 3 AA6 7 ASN C 107 GLY C 110 1 O THR C 109 N GLY C 86
SHEET 4 AA6 7 SER C 131 PRO C 135 1 O SER C 131 N ILE C 108
SHEET 5 AA6 7 SER C 155 GLY C 158 1 O SER C 155 N PHE C 132
SHEET 6 AA6 7 ARG C 179 SER C 183 1 O ARG C 179 N LEU C 156
SHEET 7 AA6 7 ASP C 203 CYS C 205 1 O CYS C 205 N GLY C 182
SHEET 1 AA7 6 VAL C 66 CYS C 68 0
SHEET 2 AA7 6 VAL C 74 ASP C 78 -1 O ILE C 75 N THR C 67
SHEET 3 AA7 6 TYR C 100 GLU C 102 1 O GLU C 102 N VAL C 77
SHEET 4 AA7 6 SER C 124 ASP C 126 1 O ASP C 126 N LEU C 101
SHEET 5 AA7 6 PHE C 148 ARG C 150 1 O PHE C 148 N LEU C 125
SHEET 6 AA7 6 VAL C 172 ASP C 174 1 O VAL C 172 N LEU C 149
SHEET 1 AA8 6 VAL D 64 CYS D 66 0
SHEET 2 AA8 6 ILE D 74 GLN D 78 -1 O ILE D 75 N SER D 65
SHEET 3 AA8 6 SER D 100 ASP D 102 1 O ASP D 102 N LEU D 77
SHEET 4 AA8 6 THR D 125 ASP D 127 1 O ASP D 127 N LEU D 101
SHEET 5 AA8 6 ALA D 149 ILE D 151 1 O ILE D 151 N LEU D 126
SHEET 6 AA8 6 ARG D 173 SER D 175 1 O SER D 175 N LEU D 150
SHEET 1 AA9 2 ALA D 85 GLY D 86 0
SHEET 2 AA9 2 ASP D 107 LEU D 108 1 O ASP D 107 N GLY D 86
SHEET 1 AB1 2 SER D 158 GLY D 159 0
SHEET 2 AB1 2 ASP D 180 LEU D 181 1 O ASP D 180 N GLY D 159
SSBOND 1 CYS A 61 CYS A 68 1555 1555 2.05
SSBOND 2 CYS A 205 CYS A 213 1555 1555 2.04
SSBOND 3 CYS B 30 CYS B 95 1555 1555 2.05
SSBOND 4 CYS B 59 CYS B 66 1555 1555 2.05
SSBOND 5 CYS B 117 CYS B 144 1555 1555 2.07
SSBOND 6 CYS B 204 CYS B 211 1555 1555 2.07
SSBOND 7 CYS C 61 CYS C 68 1555 1555 2.07
SSBOND 8 CYS C 205 CYS C 213 1555 1555 2.06
SSBOND 9 CYS D 30 CYS D 95 1555 1555 2.06
SSBOND 10 CYS D 59 CYS D 66 1555 1555 2.07
SSBOND 11 CYS D 117 CYS D 144 1555 1555 2.04
SSBOND 12 CYS D 204 CYS D 211 1555 1555 2.05
LINK ND2 ASN A 118 C1 NAG A 301 1555 1555 1.44
LINK ND2 ASN A 153 C1 NAG E 1 1555 1555 1.43
LINK ND2 ASN A 187 C1 NAG F 1 1555 1555 1.43
LINK ND2 ASN B 52 C1 NAG B 301 1555 1555 1.46
LINK ND2 ASN C 118 C1 NAG C 301 1555 1555 1.44
LINK ND2 ASN C 153 C1 NAG C 303 1555 1555 1.44
LINK ND2 ASN C 187 C1 NAG C 302 1555 1555 1.45
LINK ND2 ASN D 52 C1 NAG D 301 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.43
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.45
CISPEP 1 LYS B 206 PRO B 207 0 4.87
CISPEP 2 LYS D 206 PRO D 207 0 5.58
CRYST1 50.184 52.155 308.892 90.00 90.00 90.00 P 21 21 21 8
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 0.019927 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019174 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003237 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
