HEADER SIGNALING PROTEIN 24-MAR-16 5IYX
TITLE CRYSTAL STRUCTURE OF THE ARABIDOPSIS RECEPTOR KINASE HAESA IN COMPLEX
TITLE 2 WITH THE PEPTIDE HORMONE IDA AND THE CO-RECEPTOR SERK1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR-LIKE PROTEIN KINASE 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ECTODOMAIN, RESIDUES 20-620;
COMPND 5 SYNONYM: PROTEIN HAESA;
COMPND 6 EC: 2.7.10.1,2.7.11.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTEIN IDA;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 56-69;
COMPND 12 SYNONYM: PROTEIN INFLORESCENCE DEFICIENT IN ABSCISSION;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1;
COMPND 16 CHAIN: C;
COMPND 17 SYNONYM: ATSERK1,SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE 1;
COMPND 18 EC: 2.7.10.1,2.7.11.1;
COMPND 19 ENGINEERED: YES;
COMPND 20 OTHER_DETAILS: N115D AND N163Q
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 ORGAN: FLOWER;
SOURCE 6 TISSUE: ABCSISSION;
SOURCE 7 GENE: RLK5, HAE, AT4G28490, F21O9.180;
SOURCE 8 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 9 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 11 EXPRESSION_SYSTEM_CELL_LINE: BTI38;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PBAC3MOD;
SOURCE 14 MOL_ID: 2;
SOURCE 15 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 16 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 17 ORGANISM_TAXID: 3702;
SOURCE 18 ORGAN: FLOWER;
SOURCE 19 TISSUE: ABSCISSION ZONE;
SOURCE 20 GENE: IDA, AT1G68765, F14K14;
SOURCE 21 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 22 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 24 EXPRESSION_SYSTEM_STRAIN: BTI38;
SOURCE 25 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 26 EXPRESSION_SYSTEM_PLASMID: PBAC3MOD;
SOURCE 27 MOL_ID: 3;
SOURCE 28 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 29 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 30 ORGANISM_TAXID: 3702;
SOURCE 31 ORGAN: FLOWER;
SOURCE 32 TISSUE: ABSCISSION ZONE;
SOURCE 33 GENE: SERK1, AT1G71830, F14O23.21, F14O23_24;
SOURCE 34 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 35 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 36 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 37 EXPRESSION_SYSTEM_STRAIN: BTI38;
SOURCE 38 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 39 EXPRESSION_SYSTEM_PLASMID: PBAC3MOD
KEYWDS MEMBRANE RECEPTOR KINASE, PEPTIDE HORMONE RECEPTOR, SIGNALING
KEYWDS 2 COMPLEX, PLANT DEVELOPMENT, ORGAN SHEDDING, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SANTIAGO,M.HOTHORN
REVDAT 4 10-JAN-24 5IYX 1 HETSYN
REVDAT 3 29-JUL-20 5IYX 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 28-SEP-16 5IYX 1
REVDAT 1 20-APR-16 5IYX 0
JRNL AUTH J.SANTIAGO,B.BRANDT,M.WILDHAGEN,U.HOHMANN,L.A.HOTHORN,
JRNL AUTH 2 M.A.BUTENKO,M.HOTHORN
JRNL TITL MECHANISTIC INSIGHT INTO A PEPTIDE HORMONE SIGNALING COMPLEX
JRNL TITL 2 MEDIATING FLORAL ORGAN ABSCISSION.
JRNL REF ELIFE V. 5 2016
JRNL REFN ESSN 2050-084X
JRNL PMID 27058169
JRNL DOI 10.7554/ELIFE.15075
REMARK 2
REMARK 2 RESOLUTION. 2.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 38969
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2051
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) : 2.43
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2631
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.4100
REMARK 3 BIN FREE R VALUE SET COUNT : 138
REMARK 3 BIN FREE R VALUE : 0.3930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6066
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 176
REMARK 3 SOLVENT ATOMS : 135
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.74000
REMARK 3 B22 (A**2) : -2.10000
REMARK 3 B33 (A**2) : 4.84000
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): 0.329
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.235
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.212
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.027
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6389 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6099 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8718 ; 1.410 ; 2.022
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14104 ; 1.038 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 797 ; 6.066 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 255 ;43.695 ;25.882
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1049 ;13.116 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;16.808 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1049 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7162 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1332 ; 0.002 ; 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): 3185 ; 0.918 ; 3.554
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3184 ; 0.917 ; 3.554
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3977 ; 1.514 ; 5.330
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3978 ; 1.514 ; 5.330
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3204 ; 1.557 ; 3.906
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3205 ; 1.556 ; 3.907
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4740 ; 2.564 ; 5.795
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 27302 ; 6.024 ;34.900
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 27298 ; 6.025 ;34.898
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
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 21 A 55
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1168 2.9681 17.8478
REMARK 3 T TENSOR
REMARK 3 T11: 0.5697 T22: 0.9539
REMARK 3 T33: 0.3232 T12: -0.2930
REMARK 3 T13: 0.2194 T23: -0.1087
REMARK 3 L TENSOR
REMARK 3 L11: 0.9468 L22: 7.4793
REMARK 3 L33: 4.9175 L12: -1.3398
REMARK 3 L13: -0.8832 L23: 0.3371
REMARK 3 S TENSOR
REMARK 3 S11: 0.2727 S12: -0.5732 S13: 0.2526
REMARK 3 S21: 1.0344 S22: -0.1948 S23: -0.2353
REMARK 3 S31: -0.4650 S32: -0.4167 S33: -0.0779
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 56 A 124
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7838 7.1376 8.6142
REMARK 3 T TENSOR
REMARK 3 T11: 0.3607 T22: 0.4893
REMARK 3 T33: 0.1307 T12: -0.0250
REMARK 3 T13: 0.0823 T23: -0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 4.5674 L22: 1.9246
REMARK 3 L33: 5.5906 L12: 0.8178
REMARK 3 L13: 0.8725 L23: 0.4824
REMARK 3 S TENSOR
REMARK 3 S11: 0.0714 S12: -0.7826 S13: 0.5071
REMARK 3 S21: 0.5883 S22: 0.0399 S23: 0.1402
REMARK 3 S31: -0.5582 S32: 0.0156 S33: -0.1114
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 125 A 270
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9534 8.0868 -11.5663
REMARK 3 T TENSOR
REMARK 3 T11: 0.1795 T22: 0.2797
REMARK 3 T33: 0.0936 T12: -0.0740
REMARK 3 T13: 0.0051 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 2.4141 L22: 2.7602
REMARK 3 L33: 2.8576 L12: -0.2124
REMARK 3 L13: -0.5309 L23: 1.0426
REMARK 3 S TENSOR
REMARK 3 S11: 0.1730 S12: -0.2523 S13: 0.3690
REMARK 3 S21: 0.1649 S22: 0.0215 S23: -0.3425
REMARK 3 S31: -0.5502 S32: 0.2819 S33: -0.1945
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 271 A 337
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2763 -11.2472 -21.5957
REMARK 3 T TENSOR
REMARK 3 T11: 0.0134 T22: 0.3037
REMARK 3 T33: 0.1380 T12: -0.0352
REMARK 3 T13: -0.0144 T23: -0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 2.6650 L22: 4.2457
REMARK 3 L33: 3.1429 L12: -0.2679
REMARK 3 L13: 0.4078 L23: -0.0797
REMARK 3 S TENSOR
REMARK 3 S11: 0.0812 S12: 0.0431 S13: 0.0281
REMARK 3 S21: 0.0816 S22: 0.0095 S23: -0.7342
REMARK 3 S31: -0.1227 S32: 0.5861 S33: -0.0907
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 338 A 520
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8479 -36.5669 -25.0747
REMARK 3 T TENSOR
REMARK 3 T11: 0.1533 T22: 0.2593
REMARK 3 T33: 0.1708 T12: 0.0839
REMARK 3 T13: -0.0207 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 2.9543 L22: 3.2065
REMARK 3 L33: 1.2773 L12: 1.4861
REMARK 3 L13: 1.1242 L23: 0.4466
REMARK 3 S TENSOR
REMARK 3 S11: 0.2078 S12: -0.0331 S13: -0.6855
REMARK 3 S21: 0.1138 S22: -0.0262 S23: -0.3142
REMARK 3 S31: 0.4134 S32: 0.1115 S33: -0.1816
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 : A 521 A 616
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1699 -45.9696 -40.2739
REMARK 3 T TENSOR
REMARK 3 T11: 0.2325 T22: 0.2082
REMARK 3 T33: 0.1470 T12: -0.0578
REMARK 3 T13: -0.0810 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 3.2501 L22: 1.8725
REMARK 3 L33: 3.7911 L12: 0.6744
REMARK 3 L13: 1.6815 L23: 1.5914
REMARK 3 S TENSOR
REMARK 3 S11: 0.2673 S12: 0.0780 S13: -0.4925
REMARK 3 S21: -0.0709 S22: 0.0213 S23: -0.0279
REMARK 3 S31: 0.6085 S32: -0.3670 S33: -0.2887
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 56 B 69
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8615 -10.2218 -14.8246
REMARK 3 T TENSOR
REMARK 3 T11: 0.0842 T22: 0.2465
REMARK 3 T33: 0.0760 T12: -0.0720
REMARK 3 T13: 0.0001 T23: 0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 1.6377 L22: 7.9647
REMARK 3 L33: 5.8629 L12: -3.4215
REMARK 3 L13: -0.7841 L23: 3.7320
REMARK 3 S TENSOR
REMARK 3 S11: -0.1454 S12: 0.0536 S13: -0.3180
REMARK 3 S21: 0.1060 S22: -0.1305 S23: 0.7264
REMARK 3 S31: -0.3717 S32: -0.2353 S33: 0.2758
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 : C 26 C 39
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5884 -15.8520 -25.1108
REMARK 3 T TENSOR
REMARK 3 T11: 0.1329 T22: 0.2024
REMARK 3 T33: 0.1973 T12: -0.0320
REMARK 3 T13: -0.0117 T23: -0.0382
REMARK 3 L TENSOR
REMARK 3 L11: 2.5104 L22: 8.6416
REMARK 3 L33: 9.8666 L12: 0.4931
REMARK 3 L13: -1.7915 L23: -1.5189
REMARK 3 S TENSOR
REMARK 3 S11: 0.2903 S12: -0.0856 S13: 0.5196
REMARK 3 S21: -0.0257 S22: -0.1018 S23: -0.1942
REMARK 3 S31: -0.7374 S32: 0.1423 S33: -0.1885
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 : C 40 C 59
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9235 -23.0650 -20.3612
REMARK 3 T TENSOR
REMARK 3 T11: 0.1122 T22: 0.2574
REMARK 3 T33: 0.0803 T12: -0.0273
REMARK 3 T13: -0.0128 T23: -0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 12.4037 L22: 2.6915
REMARK 3 L33: 0.1780 L12: 2.6396
REMARK 3 L13: -1.4322 L23: -0.1505
REMARK 3 S TENSOR
REMARK 3 S11: 0.3001 S12: -0.3434 S13: -0.1971
REMARK 3 S21: 0.4927 S22: -0.3117 S23: 0.0900
REMARK 3 S31: -0.0025 S32: 0.0134 S33: 0.0115
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 : C 60 C 75
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2604 -26.0975 -31.7889
REMARK 3 T TENSOR
REMARK 3 T11: 0.0182 T22: 0.1135
REMARK 3 T33: 0.0671 T12: 0.0105
REMARK 3 T13: 0.0250 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 5.1035 L22: 6.6776
REMARK 3 L33: 9.9285 L12: 2.8891
REMARK 3 L13: 0.1755 L23: -1.9785
REMARK 3 S TENSOR
REMARK 3 S11: -0.1590 S12: 0.3087 S13: -0.5541
REMARK 3 S21: -0.1079 S22: -0.0762 S23: -0.4088
REMARK 3 S31: 0.3122 S32: 0.2572 S33: 0.2352
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 76 C 171
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5181 -21.8675 -34.4000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0379 T22: 0.1512
REMARK 3 T33: 0.0934 T12: 0.0041
REMARK 3 T13: -0.0097 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 5.3045 L22: 1.6424
REMARK 3 L33: 2.9560 L12: 0.9835
REMARK 3 L13: 0.3623 L23: 0.3453
REMARK 3 S TENSOR
REMARK 3 S11: -0.0829 S12: 0.0468 S13: 0.6606
REMARK 3 S21: 0.0076 S22: -0.0011 S23: 0.2461
REMARK 3 S31: -0.3233 S32: -0.0953 S33: 0.0839
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 172 C 194
REMARK 3 ORIGIN FOR THE GROUP (A): -17.5050 -26.2090 -40.9522
REMARK 3 T TENSOR
REMARK 3 T11: 0.1011 T22: 0.3093
REMARK 3 T33: 0.0937 T12: -0.0371
REMARK 3 T13: -0.0423 T23: -0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 5.8133 L22: 4.1224
REMARK 3 L33: 7.1812 L12: 1.3641
REMARK 3 L13: -2.0525 L23: -0.2749
REMARK 3 S TENSOR
REMARK 3 S11: 0.0244 S12: 0.5156 S13: 0.1795
REMARK 3 S21: -0.5240 S22: 0.1885 S23: 0.2693
REMARK 3 S31: 0.3805 S32: -0.5815 S33: -0.2129
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 195 C 211
REMARK 3 ORIGIN FOR THE GROUP (A): -25.3148 -25.2580 -39.2838
REMARK 3 T TENSOR
REMARK 3 T11: 0.4031 T22: 0.4731
REMARK 3 T33: 0.6024 T12: -0.1131
REMARK 3 T13: -0.3991 T23: 0.0617
REMARK 3 L TENSOR
REMARK 3 L11: 8.6444 L22: 0.1986
REMARK 3 L33: 4.7740 L12: -0.8075
REMARK 3 L13: -3.3924 L23: 0.0566
REMARK 3 S TENSOR
REMARK 3 S11: 0.3608 S12: 0.1987 S13: -0.1888
REMARK 3 S21: -0.2442 S22: 0.0410 S23: 0.2723
REMARK 3 S31: 0.2568 S32: -1.2047 S33: -0.4018
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5IYX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219673.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000020
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41023
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.430
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.960
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: 5IXO, 4LSC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 8,000, 0.2 M MGCL2, 0.1 M
REMARK 280 CITRIC ACID PH 4.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 37.25350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.37950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.22800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.37950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.25350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.22800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLY A 15
REMARK 465 SER A 16
REMARK 465 SER A 17
REMARK 465 MET A 18
REMARK 465 GLY A 19
REMARK 465 SER A 20
REMARK 465 THR A 617
REMARK 465 ARG A 618
REMARK 465 SER A 619
REMARK 465 LYS A 620
REMARK 465 LEU A 621
REMARK 465 GLU A 622
REMARK 465 GLY A 623
REMARK 465 SER A 624
REMARK 465 GLU A 625
REMARK 465 ASN A 626
REMARK 465 LEU A 627
REMARK 465 TYR A 628
REMARK 465 PHE A 629
REMARK 465 GLN A 630
REMARK 465 GLY A 631
REMARK 465 SER A 632
REMARK 465 ALA A 633
REMARK 465 TRP A 634
REMARK 465 SER A 635
REMARK 465 HIS A 636
REMARK 465 PRO A 637
REMARK 465 GLN A 638
REMARK 465 PHE A 639
REMARK 465 GLU A 640
REMARK 465 LYS A 641
REMARK 465 GLY A 642
REMARK 465 GLY A 643
REMARK 465 GLY A 644
REMARK 465 SER A 645
REMARK 465 GLY A 646
REMARK 465 GLY A 647
REMARK 465 GLY A 648
REMARK 465 SER A 649
REMARK 465 GLY A 650
REMARK 465 GLY A 651
REMARK 465 SER A 652
REMARK 465 ALA A 653
REMARK 465 TRP A 654
REMARK 465 SER A 655
REMARK 465 HIS A 656
REMARK 465 PRO A 657
REMARK 465 GLN A 658
REMARK 465 PHE A 659
REMARK 465 GLU A 660
REMARK 465 LYS A 661
REMARK 465 GLY A 662
REMARK 465 ALA A 663
REMARK 465 HIS A 664
REMARK 465 HIS A 665
REMARK 465 HIS A 666
REMARK 465 HIS A 667
REMARK 465 HIS A 668
REMARK 465 HIS A 669
REMARK 465 HIS A 670
REMARK 465 HIS A 671
REMARK 465 HIS A 672
REMARK 465 GLY C 20
REMARK 465 SER C 21
REMARK 465 SER C 22
REMARK 465 MET C 23
REMARK 465 ALA C 24
REMARK 465 SER C 25
REMARK 465 GLY C 212
REMARK 465 SER C 213
REMARK 465 LEU C 214
REMARK 465 GLU C 215
REMARK 465 ASN C 216
REMARK 465 LEU C 217
REMARK 465 TYR C 218
REMARK 465 PHE C 219
REMARK 465 GLN C 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 LEU A 21 CG CD1 CD2
REMARK 470 ASN A 22 CG OD1 ND2
REMARK 470 SER A 46 CB OG
REMARK 470 ASP A 47 CB CG OD1 OD2
REMARK 470 ASP A 50 CG OD1 OD2
REMARK 470 PHE A 136 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 451 CG CD CE NZ
REMARK 470 LYS A 497 CG CD CE NZ
REMARK 470 GLU A 562 CG CD OE1 OE2
REMARK 470 ILE A 616 CG1 CG2 CD1
REMARK 470 PRO C 211 CG CD
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 PRO C 211 C - N - CA ANGL. DEV. = 16.6 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 ASN A 22 174.71 65.40
REMARK 500 ASP A 47 101.14 -167.79
REMARK 500 ASN A 48 -93.00 -67.47
REMARK 500 ASN A 98 62.33 61.47
REMARK 500 LEU A 138 63.62 -118.00
REMARK 500 ASN A 149 -169.22 -114.28
REMARK 500 ASP A 153 -177.03 72.33
REMARK 500 LEU A 198 47.21 -99.05
REMARK 500 SER A 231 -38.75 -37.42
REMARK 500 ASN A 269 66.03 63.23
REMARK 500 MET A 280 -35.23 -38.59
REMARK 500 ASN A 294 -157.55 -130.64
REMARK 500 ASN A 305 54.07 -143.68
REMARK 500 SER A 326 -9.69 -57.74
REMARK 500 GLN A 358 -56.56 -122.26
REMARK 500 CYS A 376 42.06 -101.16
REMARK 500 ASN A 389 -160.82 -123.94
REMARK 500 ASN A 413 -168.19 -129.45
REMARK 500 ASP A 436 61.21 62.34
REMARK 500 ASN A 437 -155.43 -138.01
REMARK 500 LYS A 508 60.13 65.92
REMARK 500 LYS A 571 71.88 -107.58
REMARK 500 ASN A 580 -169.08 -128.42
REMARK 500 ASP A 610 83.91 66.39
REMARK 500 ASN C 103 -167.06 -126.58
REMARK 500 LEU C 126 60.22 60.10
REMARK 500 ASP C 200 60.36 -153.86
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5IYX A 20 620 UNP P47735 RLK5_ARATH 20 620
DBREF 5IYX B 56 69 UNP Q8LAD7 IDA_ARATH 56 69
DBREF 5IYX C 24 213 UNP Q94AG2 SERK1_ARATH 24 213
SEQADV 5IYX GLY A 15 UNP P47735 EXPRESSION TAG
SEQADV 5IYX SER A 16 UNP P47735 EXPRESSION TAG
SEQADV 5IYX SER A 17 UNP P47735 EXPRESSION TAG
SEQADV 5IYX MET A 18 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLY A 19 UNP P47735 EXPRESSION TAG
SEQADV 5IYX LEU A 621 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLU A 622 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLY A 623 UNP P47735 EXPRESSION TAG
SEQADV 5IYX SER A 624 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLU A 625 UNP P47735 EXPRESSION TAG
SEQADV 5IYX ASN A 626 UNP P47735 EXPRESSION TAG
SEQADV 5IYX LEU A 627 UNP P47735 EXPRESSION TAG
SEQADV 5IYX TYR A 628 UNP P47735 EXPRESSION TAG
SEQADV 5IYX PHE A 629 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLN A 630 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLY A 631 UNP P47735 EXPRESSION TAG
SEQADV 5IYX SER A 632 UNP P47735 EXPRESSION TAG
SEQADV 5IYX ALA A 633 UNP P47735 EXPRESSION TAG
SEQADV 5IYX TRP A 634 UNP P47735 EXPRESSION TAG
SEQADV 5IYX SER A 635 UNP P47735 EXPRESSION TAG
SEQADV 5IYX HIS A 636 UNP P47735 EXPRESSION TAG
SEQADV 5IYX PRO A 637 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLN A 638 UNP P47735 EXPRESSION TAG
SEQADV 5IYX PHE A 639 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLU A 640 UNP P47735 EXPRESSION TAG
SEQADV 5IYX LYS A 641 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLY A 642 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLY A 643 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLY A 644 UNP P47735 EXPRESSION TAG
SEQADV 5IYX SER A 645 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLY A 646 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLY A 647 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLY A 648 UNP P47735 EXPRESSION TAG
SEQADV 5IYX SER A 649 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLY A 650 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLY A 651 UNP P47735 EXPRESSION TAG
SEQADV 5IYX SER A 652 UNP P47735 EXPRESSION TAG
SEQADV 5IYX ALA A 653 UNP P47735 EXPRESSION TAG
SEQADV 5IYX TRP A 654 UNP P47735 EXPRESSION TAG
SEQADV 5IYX SER A 655 UNP P47735 EXPRESSION TAG
SEQADV 5IYX HIS A 656 UNP P47735 EXPRESSION TAG
SEQADV 5IYX PRO A 657 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLN A 658 UNP P47735 EXPRESSION TAG
SEQADV 5IYX PHE A 659 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLU A 660 UNP P47735 EXPRESSION TAG
SEQADV 5IYX LYS A 661 UNP P47735 EXPRESSION TAG
SEQADV 5IYX GLY A 662 UNP P47735 EXPRESSION TAG
SEQADV 5IYX ALA A 663 UNP P47735 EXPRESSION TAG
SEQADV 5IYX HIS A 664 UNP P47735 EXPRESSION TAG
SEQADV 5IYX HIS A 665 UNP P47735 EXPRESSION TAG
SEQADV 5IYX HIS A 666 UNP P47735 EXPRESSION TAG
SEQADV 5IYX HIS A 667 UNP P47735 EXPRESSION TAG
SEQADV 5IYX HIS A 668 UNP P47735 EXPRESSION TAG
SEQADV 5IYX HIS A 669 UNP P47735 EXPRESSION TAG
SEQADV 5IYX HIS A 670 UNP P47735 EXPRESSION TAG
SEQADV 5IYX HIS A 671 UNP P47735 EXPRESSION TAG
SEQADV 5IYX HIS A 672 UNP P47735 EXPRESSION TAG
SEQADV 5IYX TYR B 56 UNP Q8LAD7 GLY 56 ENGINEERED MUTATION
SEQADV 5IYX GLY C 20 UNP Q94AG2 EXPRESSION TAG
SEQADV 5IYX SER C 21 UNP Q94AG2 EXPRESSION TAG
SEQADV 5IYX SER C 22 UNP Q94AG2 EXPRESSION TAG
SEQADV 5IYX MET C 23 UNP Q94AG2 EXPRESSION TAG
SEQADV 5IYX ASP C 115 UNP Q94AG2 ASN 115 ENGINEERED MUTATION
SEQADV 5IYX GLN C 163 UNP Q94AG2 ASN 163 ENGINEERED MUTATION
SEQADV 5IYX LEU C 214 UNP Q94AG2 EXPRESSION TAG
SEQADV 5IYX GLU C 215 UNP Q94AG2 EXPRESSION TAG
SEQADV 5IYX ASN C 216 UNP Q94AG2 EXPRESSION TAG
SEQADV 5IYX LEU C 217 UNP Q94AG2 EXPRESSION TAG
SEQADV 5IYX TYR C 218 UNP Q94AG2 EXPRESSION TAG
SEQADV 5IYX PHE C 219 UNP Q94AG2 EXPRESSION TAG
SEQADV 5IYX GLN C 220 UNP Q94AG2 EXPRESSION TAG
SEQRES 1 A 658 GLY SER SER MET GLY SER LEU ASN GLN ASP ALA THR ILE
SEQRES 2 A 658 LEU ARG GLN ALA LYS LEU GLY LEU SER ASP PRO ALA GLN
SEQRES 3 A 658 SER LEU SER SER TRP SER ASP ASN ASN ASP VAL THR PRO
SEQRES 4 A 658 CYS LYS TRP LEU GLY VAL SER CYS ASP ALA THR SER ASN
SEQRES 5 A 658 VAL VAL SER VAL ASP LEU SER SER PHE MET LEU VAL GLY
SEQRES 6 A 658 PRO PHE PRO SER ILE LEU CYS HIS LEU PRO SER LEU HIS
SEQRES 7 A 658 SER LEU SER LEU TYR ASN ASN SER ILE ASN GLY SER LEU
SEQRES 8 A 658 SER ALA ASP ASP PHE ASP THR CYS HIS ASN LEU ILE SER
SEQRES 9 A 658 LEU ASP LEU SER GLU ASN LEU LEU VAL GLY SER ILE PRO
SEQRES 10 A 658 LYS SER LEU PRO PHE ASN LEU PRO ASN LEU LYS PHE LEU
SEQRES 11 A 658 GLU ILE SER GLY ASN ASN LEU SER ASP THR ILE PRO SER
SEQRES 12 A 658 SER PHE GLY GLU PHE ARG LYS LEU GLU SER LEU ASN LEU
SEQRES 13 A 658 ALA GLY ASN PHE LEU SER GLY THR ILE PRO ALA SER LEU
SEQRES 14 A 658 GLY ASN VAL THR THR LEU LYS GLU LEU LYS LEU ALA TYR
SEQRES 15 A 658 ASN LEU PHE SER PRO SER GLN ILE PRO SER GLN LEU GLY
SEQRES 16 A 658 ASN LEU THR GLU LEU GLN VAL LEU TRP LEU ALA GLY CYS
SEQRES 17 A 658 ASN LEU VAL GLY PRO ILE PRO PRO SER LEU SER ARG LEU
SEQRES 18 A 658 THR SER LEU VAL ASN LEU ASP LEU THR PHE ASN GLN LEU
SEQRES 19 A 658 THR GLY SER ILE PRO SER TRP ILE THR GLN LEU LYS THR
SEQRES 20 A 658 VAL GLU GLN ILE GLU LEU PHE ASN ASN SER PHE SER GLY
SEQRES 21 A 658 GLU LEU PRO GLU SER MET GLY ASN MET THR THR LEU LYS
SEQRES 22 A 658 ARG PHE ASP ALA SER MET ASN LYS LEU THR GLY LYS ILE
SEQRES 23 A 658 PRO ASP ASN LEU ASN LEU LEU ASN LEU GLU SER LEU ASN
SEQRES 24 A 658 LEU PHE GLU ASN MET LEU GLU GLY PRO LEU PRO GLU SER
SEQRES 25 A 658 ILE THR ARG SER LYS THR LEU SER GLU LEU LYS LEU PHE
SEQRES 26 A 658 ASN ASN ARG LEU THR GLY VAL LEU PRO SER GLN LEU GLY
SEQRES 27 A 658 ALA ASN SER PRO LEU GLN TYR VAL ASP LEU SER TYR ASN
SEQRES 28 A 658 ARG PHE SER GLY GLU ILE PRO ALA ASN VAL CYS GLY GLU
SEQRES 29 A 658 GLY LYS LEU GLU TYR LEU ILE LEU ILE ASP ASN SER PHE
SEQRES 30 A 658 SER GLY GLU ILE SER ASN ASN LEU GLY LYS CYS LYS SER
SEQRES 31 A 658 LEU THR ARG VAL ARG LEU SER ASN ASN LYS LEU SER GLY
SEQRES 32 A 658 GLN ILE PRO HIS GLY PHE TRP GLY LEU PRO ARG LEU SER
SEQRES 33 A 658 LEU LEU GLU LEU SER ASP ASN SER PHE THR GLY SER ILE
SEQRES 34 A 658 PRO LYS THR ILE ILE GLY ALA LYS ASN LEU SER ASN LEU
SEQRES 35 A 658 ARG ILE SER LYS ASN ARG PHE SER GLY SER ILE PRO ASN
SEQRES 36 A 658 GLU ILE GLY SER LEU ASN GLY ILE ILE GLU ILE SER GLY
SEQRES 37 A 658 ALA GLU ASN ASP PHE SER GLY GLU ILE PRO GLU SER LEU
SEQRES 38 A 658 VAL LYS LEU LYS GLN LEU SER ARG LEU ASP LEU SER LYS
SEQRES 39 A 658 ASN GLN LEU SER GLY GLU ILE PRO ARG GLU LEU ARG GLY
SEQRES 40 A 658 TRP LYS ASN LEU ASN GLU LEU ASN LEU ALA ASN ASN HIS
SEQRES 41 A 658 LEU SER GLY GLU ILE PRO LYS GLU VAL GLY ILE LEU PRO
SEQRES 42 A 658 VAL LEU ASN TYR LEU ASP LEU SER SER ASN GLN PHE SER
SEQRES 43 A 658 GLY GLU ILE PRO LEU GLU LEU GLN ASN LEU LYS LEU ASN
SEQRES 44 A 658 VAL LEU ASN LEU SER TYR ASN HIS LEU SER GLY LYS ILE
SEQRES 45 A 658 PRO PRO LEU TYR ALA ASN LYS ILE TYR ALA HIS ASP PHE
SEQRES 46 A 658 ILE GLY ASN PRO GLY LEU CYS VAL ASP LEU ASP GLY LEU
SEQRES 47 A 658 CYS ARG LYS ILE THR ARG SER LYS LEU GLU GLY SER GLU
SEQRES 48 A 658 ASN LEU TYR PHE GLN GLY SER ALA TRP SER HIS PRO GLN
SEQRES 49 A 658 PHE GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY
SEQRES 50 A 658 SER ALA TRP SER HIS PRO GLN PHE GLU LYS GLY ALA HIS
SEQRES 51 A 658 HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 14 TYR VAL PRO ILE PRO PRO SER ALA HYP SER LYS ARG HIS
SEQRES 2 B 14 ASN
SEQRES 1 C 201 GLY SER SER MET ALA SER ALA ASN LEU GLU GLY ASP ALA
SEQRES 2 C 201 LEU HIS THR LEU ARG VAL THR LEU VAL ASP PRO ASN ASN
SEQRES 3 C 201 VAL LEU GLN SER TRP ASP PRO THR LEU VAL ASN PRO CYS
SEQRES 4 C 201 THR TRP PHE HIS VAL THR CYS ASN ASN GLU ASN SER VAL
SEQRES 5 C 201 ILE ARG VAL ASP LEU GLY ASN ALA GLU LEU SER GLY HIS
SEQRES 6 C 201 LEU VAL PRO GLU LEU GLY VAL LEU LYS ASN LEU GLN TYR
SEQRES 7 C 201 LEU GLU LEU TYR SER ASN ASN ILE THR GLY PRO ILE PRO
SEQRES 8 C 201 SER ASN LEU GLY ASP LEU THR ASN LEU VAL SER LEU ASP
SEQRES 9 C 201 LEU TYR LEU ASN SER PHE SER GLY PRO ILE PRO GLU SER
SEQRES 10 C 201 LEU GLY LYS LEU SER LYS LEU ARG PHE LEU ARG LEU ASN
SEQRES 11 C 201 ASN ASN SER LEU THR GLY SER ILE PRO MET SER LEU THR
SEQRES 12 C 201 GLN ILE THR THR LEU GLN VAL LEU ASP LEU SER ASN ASN
SEQRES 13 C 201 ARG LEU SER GLY SER VAL PRO ASP ASN GLY SER PHE SER
SEQRES 14 C 201 LEU PHE THR PRO ILE SER PHE ALA ASN ASN LEU ASP LEU
SEQRES 15 C 201 CYS GLY PRO VAL THR SER HIS PRO CYS PRO GLY SER LEU
SEQRES 16 C 201 GLU ASN LEU TYR PHE GLN
MODRES 5IYX HYP B 64 PRO MODIFIED RESIDUE
HET HYP B 64 8
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG A 703 14
HET NAG A 708 14
HET EDO A 711 4
HET EDO A 712 4
HET NAG C 301 14
HET NAG C 302 14
HETNAM HYP 4-HYDROXYPROLINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN HYP HYDROXYPROLINE
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 EDO ETHYLENE GLYCOL
FORMUL 2 HYP C5 H9 N O3
FORMUL 4 NAG 12(C8 H15 N O6)
FORMUL 10 EDO 2(C2 H6 O2)
FORMUL 14 HOH *135(H2 O)
HELIX 1 AA1 LEU A 21 GLY A 34 1 14
HELIX 2 AA2 THR A 52 TRP A 56 5 5
HELIX 3 AA3 PRO A 82 LEU A 88 5 7
HELIX 4 AA4 SER A 106 ASP A 111 5 6
HELIX 5 AA5 SER A 133 LEU A 138 1 6
HELIX 6 AA6 PRO A 156 PHE A 162 5 7
HELIX 7 AA7 PRO A 180 VAL A 186 5 7
HELIX 8 AA8 PRO A 205 LEU A 211 5 7
HELIX 9 AA9 PRO A 229 LEU A 235 5 7
HELIX 10 AB1 PRO A 253 LEU A 259 5 7
HELIX 11 AB2 PRO A 277 MET A 283 5 7
HELIX 12 AB3 PRO A 324 SER A 330 5 7
HELIX 13 AB4 SER A 396 CYS A 402 5 7
HELIX 14 AB5 PRO A 420 GLY A 425 1 6
HELIX 15 AB6 PRO A 444 ALA A 450 5 7
HELIX 16 AB7 PRO A 468 LEU A 474 5 7
HELIX 17 AB8 PRO A 492 LEU A 498 5 7
HELIX 18 AB9 PRO A 540 LEU A 546 5 7
HELIX 19 AC1 PRO A 564 LEU A 570 5 7
HELIX 20 AC2 ASN A 592 ILE A 600 5 9
HELIX 21 AC3 ASN C 27 THR C 39 1 13
HELIX 22 AC4 ASN C 56 TRP C 60 5 5
HELIX 23 AC5 VAL C 86 LEU C 92 5 7
HELIX 24 AC6 PRO C 110 LEU C 116 5 7
HELIX 25 AC7 PRO C 134 LEU C 140 5 7
HELIX 26 AC8 PRO C 158 ILE C 164 5 7
HELIX 27 AC9 ASN C 184 PHE C 190 5 7
HELIX 28 AD1 THR C 191 PHE C 195 5 5
SHEET 1 AA123 VAL A 59 CYS A 61 0
SHEET 2 AA123 VAL A 67 ASP A 71 -1 O SER A 69 N SER A 60
SHEET 3 AA123 SER A 93 SER A 95 1 O SER A 95 N VAL A 70
SHEET 4 AA123 SER A 118 ASP A 120 1 O ASP A 120 N LEU A 94
SHEET 5 AA123 PHE A 143 GLU A 145 1 O GLU A 145 N LEU A 119
SHEET 6 AA123 SER A 167 ASN A 169 1 O ASN A 169 N LEU A 144
SHEET 7 AA123 GLU A 191 LYS A 193 1 O LYS A 193 N LEU A 168
SHEET 8 AA123 VAL A 216 TRP A 218 1 O TRP A 218 N LEU A 192
SHEET 9 AA123 ASN A 240 ASP A 242 1 O ASP A 242 N LEU A 217
SHEET 10 AA123 GLN A 264 GLU A 266 1 O GLU A 266 N LEU A 241
SHEET 11 AA123 ARG A 288 ASP A 290 1 O ARG A 288 N ILE A 265
SHEET 12 AA123 SER A 311 ASN A 313 1 O SER A 311 N PHE A 289
SHEET 13 AA123 GLU A 335 LYS A 337 1 O GLU A 335 N LEU A 312
SHEET 14 AA123 TYR A 359 ASP A 361 1 O TYR A 359 N LEU A 336
SHEET 15 AA123 TYR A 383 ILE A 385 1 O ILE A 385 N VAL A 360
SHEET 16 AA123 ARG A 407 ARG A 409 1 O ARG A 409 N LEU A 384
SHEET 17 AA123 LEU A 431 GLU A 433 1 O LEU A 431 N VAL A 408
SHEET 18 AA123 ASN A 455 ARG A 457 1 O ARG A 457 N LEU A 432
SHEET 19 AA123 GLU A 479 SER A 481 1 O SER A 481 N LEU A 456
SHEET 20 AA123 ARG A 503 ASP A 505 1 O ASP A 505 N ILE A 480
SHEET 21 AA123 GLU A 527 ASN A 529 1 O ASN A 529 N LEU A 504
SHEET 22 AA123 TYR A 551 ASP A 553 1 O TYR A 551 N LEU A 528
SHEET 23 AA123 VAL A 574 ASN A 576 1 O VAL A 574 N LEU A 552
SHEET 1 AA2 2 VAL A 78 GLY A 79 0
SHEET 2 AA2 2 SER A 100 ILE A 101 1 O SER A 100 N GLY A 79
SHEET 1 AA3 2 VAL A 127 GLY A 128 0
SHEET 2 AA3 2 ASN A 150 LEU A 151 1 O ASN A 150 N GLY A 128
SHEET 1 AA4 2 VAL A 225 GLY A 226 0
SHEET 2 AA4 2 GLN A 247 LEU A 248 1 O GLN A 247 N GLY A 226
SHEET 1 AA5 8 GLU A 320 GLY A 321 0
SHEET 2 AA5 8 ARG A 342 VAL A 346 1 O THR A 344 N GLY A 321
SHEET 3 AA5 8 ARG A 366 GLY A 369 1 O ARG A 366 N LEU A 343
SHEET 4 AA5 8 SER A 390 GLY A 393 1 O SER A 390 N PHE A 367
SHEET 5 AA5 8 LYS A 414 GLN A 418 1 O SER A 416 N GLY A 393
SHEET 6 AA5 8 SER A 438 GLY A 441 1 O SER A 438 N LEU A 415
SHEET 7 AA5 8 ARG A 462 SER A 466 1 O SER A 464 N GLY A 441
SHEET 8 AA5 8 ASP A 486 SER A 488 1 O ASP A 486 N PHE A 463
SHEET 1 AA6 6 SER A 512 GLY A 513 0
SHEET 2 AA6 6 HIS A 534 GLY A 537 1 O SER A 536 N GLY A 513
SHEET 3 AA6 6 GLN A 558 GLY A 561 1 O GLN A 558 N LEU A 535
SHEET 4 AA6 6 HIS A 581 LYS A 585 1 O SER A 583 N GLY A 561
SHEET 5 AA6 6 GLY A 604 ASP A 608 1 O CYS A 606 N GLY A 584
SHEET 6 AA6 6 CYS A 613 ARG A 614 -1 O ARG A 614 N VAL A 607
SHEET 1 AA7 7 LEU C 40 VAL C 41 0
SHEET 2 AA7 7 SER C 82 GLY C 83 -1 O SER C 82 N VAL C 41
SHEET 3 AA7 7 ASN C 104 PRO C 108 1 O THR C 106 N GLY C 83
SHEET 4 AA7 7 SER C 128 GLY C 131 1 O SER C 128 N ILE C 105
SHEET 5 AA7 7 SER C 152 GLY C 155 1 O SER C 152 N PHE C 129
SHEET 6 AA7 7 ARG C 176 SER C 180 1 O ARG C 176 N LEU C 153
SHEET 7 AA7 7 ASP C 200 CYS C 202 1 O ASP C 200 N GLY C 179
SHEET 1 AA8 6 VAL C 63 CYS C 65 0
SHEET 2 AA8 6 VAL C 71 ASP C 75 -1 O ILE C 72 N THR C 64
SHEET 3 AA8 6 TYR C 97 GLU C 99 1 O GLU C 99 N VAL C 74
SHEET 4 AA8 6 SER C 121 ASP C 123 1 O ASP C 123 N LEU C 98
SHEET 5 AA8 6 PHE C 145 ARG C 147 1 O PHE C 145 N LEU C 122
SHEET 6 AA8 6 VAL C 169 ASP C 171 1 O VAL C 169 N LEU C 146
SSBOND 1 CYS A 54 CYS A 61 1555 1555 2.06
SSBOND 2 CYS A 86 CYS A 113 1555 1555 2.03
SSBOND 3 CYS A 376 CYS A 402 1555 1555 2.05
SSBOND 4 CYS A 606 CYS A 613 1555 1555 2.06
SSBOND 5 CYS C 58 CYS C 65 1555 1555 2.11
SSBOND 6 CYS C 202 CYS C 210 1555 1555 2.08
LINK ND2 ASN A 98 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 102 C1 NAG A 703 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN A 269 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN A 282 C1 NAG A 708 1555 1555 1.45
LINK ND2 ASN A 576 C1 NAG G 1 1555 1555 1.44
LINK C ALA B 63 N HYP B 64 1555 1555 1.34
LINK C HYP B 64 N SER B 65 1555 1555 1.33
LINK ND2 ASN C 150 C1 NAG C 301 1555 1555 1.48
LINK ND2 ASN C 184 C1 NAG C 302 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
CRYST1 74.507 100.456 142.759 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013422 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009955 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007005 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
