HEADER SIGNALING PROTEIN 28-JUL-17 5Y39
TITLE CRYSTAL STRUCTURE OF RAGULATOR COMPLEX (P18 76-145)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAGULATOR COMPLEX PROTEIN LAMTOR1;
COMPND 3 CHAIN: A, F;
COMPND 4 FRAGMENT: COILED COIL, UNP RESIDUES 76-145;
COMPND 5 SYNONYM: LATE ENDOSOMAL/LYSOSOMAL ADAPTOR AND MAPK AND MTOR ACTIVATOR
COMPND 6 1,LIPID RAFT ADAPTOR PROTEIN P18,PROTEIN ASSOCIATED WITH DRMS AND
COMPND 7 ENDOSOMES,P27KIP1-RELEASING FACTOR FROM RHOA,P27RF-RHO;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: RAGULATOR COMPLEX PROTEIN LAMTOR2;
COMPND 11 CHAIN: B, G;
COMPND 12 FRAGMENT: ROADBLOCK DOMAIN;
COMPND 13 SYNONYM: ENDOSOMAL ADAPTOR PROTEIN P14,LATE ENDOSOMAL/LYSOSOMAL MP1-
COMPND 14 INTERACTING PROTEIN,LATE ENDOSOMAL/LYSOSOMAL ADAPTOR AND MAPK AND
COMPND 15 MTOR ACTIVATOR 2,MITOGEN-ACTIVATED PROTEIN-BINDING PROTEIN-
COMPND 16 INTERACTING PROTEIN,MAPBP-INTERACTING PROTEIN,ROADBLOCK DOMAIN-
COMPND 17 CONTAINING PROTEIN 3;
COMPND 18 ENGINEERED: YES;
COMPND 19 MOL_ID: 3;
COMPND 20 MOLECULE: RAGULATOR COMPLEX PROTEIN LAMTOR3;
COMPND 21 CHAIN: C, H;
COMPND 22 FRAGMENT: ROADBLOCK DOMAIN;
COMPND 23 SYNONYM: LATE ENDOSOMAL/LYSOSOMAL ADAPTOR AND MAPK AND MTOR ACTIVATOR
COMPND 24 3,MEK-BINDING PARTNER 1,MP1,MITOGEN-ACTIVATED PROTEIN KINASE KINASE
COMPND 25 1-INTERACTING PROTEIN 1,MITOGEN-ACTIVATED PROTEIN KINASE SCAFFOLD
COMPND 26 PROTEIN 1;
COMPND 27 ENGINEERED: YES;
COMPND 28 MOL_ID: 4;
COMPND 29 MOLECULE: RAGULATOR COMPLEX PROTEIN LAMTOR4;
COMPND 30 CHAIN: D, I;
COMPND 31 FRAGMENT: ROADBLOCK DOMAIN;
COMPND 32 SYNONYM: LATE ENDOSOMAL/LYSOSOMAL ADAPTOR AND MAPK AND MTOR ACTIVATOR
COMPND 33 4;
COMPND 34 ENGINEERED: YES;
COMPND 35 MOL_ID: 5;
COMPND 36 MOLECULE: RAGULATOR COMPLEX PROTEIN LAMTOR5;
COMPND 37 CHAIN: E, J;
COMPND 38 FRAGMENT: ROADBLOCK DOMAIN, UNP RESIDUES 1-90;
COMPND 39 SYNONYM: HEPATITIS B VIRUS X-INTERACTING PROTEIN,HBX-INTERACTING
COMPND 40 PROTEIN,LATE ENDOSOMAL/LYSOSOMAL ADAPTOR AND MAPK AND MTOR ACTIVATOR
COMPND 41 5;
COMPND 42 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LAMTOR1, C11ORF59, PDRO, PP7157;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28SUMO;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: LAMTOR2, MAPBPIP, ROBLD3, HSPC003;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PETDUET;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 GENE: LAMTOR3, MAP2K1IP1, MAPKSP1, PRO2783;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 31 MOL_ID: 4;
SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 33 ORGANISM_COMMON: HUMAN;
SOURCE 34 ORGANISM_TAXID: 9606;
SOURCE 35 GENE: LAMTOR4, C7ORF59;
SOURCE 36 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 37 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 38 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 39 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 40 EXPRESSION_SYSTEM_PLASMID: PETDUET;
SOURCE 41 MOL_ID: 5;
SOURCE 42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 43 ORGANISM_COMMON: HUMAN;
SOURCE 44 ORGANISM_TAXID: 9606;
SOURCE 45 GENE: LAMTOR5, HBXIP, XIP;
SOURCE 46 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 47 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 48 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 49 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 50 EXPRESSION_SYSTEM_PLASMID: PETDUET
KEYWDS RAGULATOR COMPLEX, LAMTOR, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.ZHANG,J.DING
REVDAT 2 27-MAR-24 5Y39 1 REMARK
REVDAT 1 06-DEC-17 5Y39 0
JRNL AUTH T.ZHANG,R.WANG,Z.WANG,X.WANG,F.WANG,J.DING
JRNL TITL STRUCTURAL BASIS FOR RAGULATOR FUNCTIONING AS A SCAFFOLD IN
JRNL TITL 2 MEMBRANE-ANCHORING OF RAG GTPASES AND MTORC1
JRNL REF NAT COMMUN V. 8 1394 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 29123114
JRNL DOI 10.1038/S41467-017-01567-4
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0123
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) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.1
REMARK 3 NUMBER OF REFLECTIONS : 25354
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1365
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) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1126
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 53.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.2840
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6750
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 58
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.08000
REMARK 3 B22 (A**2) : -4.26000
REMARK 3 B33 (A**2) : 3.18000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.383
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.314
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.870
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6836 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9265 ; 1.167 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 885 ; 5.683 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 273 ;39.644 ;24.945
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1143 ;19.255 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;17.500 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1123 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5016 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3594 ; 1.991 ; 4.103
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4461 ; 2.446 ; 6.098
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3241 ; 2.213 ; 4.323
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): 10066 ; 4.206 ;91.019
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): 6835 ; 4.077 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 6749 ;52.543 ; 5.000
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 : 10
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 79 A 145
REMARK 3 ORIGIN FOR THE GROUP (A): -17.6970 -26.0235 -5.9171
REMARK 3 T TENSOR
REMARK 3 T11: 0.1487 T22: 0.2640
REMARK 3 T33: 0.0747 T12: 0.0282
REMARK 3 T13: 0.0069 T23: 0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 0.3416 L22: 0.7806
REMARK 3 L33: 0.3071 L12: 0.3437
REMARK 3 L13: 0.1158 L23: 0.1366
REMARK 3 S TENSOR
REMARK 3 S11: 0.0259 S12: -0.0294 S13: -0.0299
REMARK 3 S21: 0.0756 S22: -0.0334 S23: 0.0416
REMARK 3 S31: 0.0545 S32: -0.0308 S33: 0.0075
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 5 B 120
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3641 -15.8763 -16.5813
REMARK 3 T TENSOR
REMARK 3 T11: 0.1743 T22: 0.2841
REMARK 3 T33: 0.1551 T12: 0.0035
REMARK 3 T13: 0.0073 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.0257 L22: 0.2682
REMARK 3 L33: 0.5111 L12: 0.0627
REMARK 3 L13: -0.0801 L23: -0.3632
REMARK 3 S TENSOR
REMARK 3 S11: -0.0106 S12: -0.0072 S13: -0.0454
REMARK 3 S21: 0.0006 S22: -0.0046 S23: -0.0236
REMARK 3 S31: -0.0505 S32: 0.0369 S33: 0.0152
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 3 C 123
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4100 -15.5435 0.6644
REMARK 3 T TENSOR
REMARK 3 T11: 0.1768 T22: 0.2902
REMARK 3 T33: 0.1247 T12: 0.0039
REMARK 3 T13: 0.0066 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.2340 L22: 0.6383
REMARK 3 L33: 0.6684 L12: 0.0964
REMARK 3 L13: 0.0569 L23: 0.1165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0051 S12: -0.0032 S13: -0.0378
REMARK 3 S21: 0.0757 S22: -0.0421 S23: 0.0006
REMARK 3 S31: -0.0492 S32: -0.0650 S33: 0.0370
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 0 D 98
REMARK 3 ORIGIN FOR THE GROUP (A): -25.0750 -44.0338 -8.5930
REMARK 3 T TENSOR
REMARK 3 T11: 0.1741 T22: 0.2921
REMARK 3 T33: 0.1477 T12: -0.0094
REMARK 3 T13: 0.0062 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.4322 L22: 0.3607
REMARK 3 L33: 0.4508 L12: -0.0872
REMARK 3 L13: -0.1248 L23: -0.0346
REMARK 3 S TENSOR
REMARK 3 S11: -0.0199 S12: 0.0076 S13: -0.0185
REMARK 3 S21: -0.0870 S22: 0.0236 S23: -0.0103
REMARK 3 S31: 0.0398 S32: -0.0183 S33: -0.0038
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 83 E 172
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2990 -32.0563 -21.2133
REMARK 3 T TENSOR
REMARK 3 T11: 0.1914 T22: 0.2796
REMARK 3 T33: 0.1448 T12: 0.0145
REMARK 3 T13: 0.0180 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.8978 L22: 0.2335
REMARK 3 L33: 0.8927 L12: 0.2732
REMARK 3 L13: 0.2969 L23: -0.2503
REMARK 3 S TENSOR
REMARK 3 S11: -0.0173 S12: 0.0325 S13: -0.0124
REMARK 3 S21: -0.0537 S22: -0.0181 S23: -0.0385
REMARK 3 S31: 0.0666 S32: 0.0421 S33: 0.0354
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 114 F 145
REMARK 3 ORIGIN FOR THE GROUP (A): -42.2666 -22.0320 -21.4745
REMARK 3 T TENSOR
REMARK 3 T11: 0.1937 T22: 0.3593
REMARK 3 T33: 0.2165 T12: -0.0882
REMARK 3 T13: 0.0927 T23: -0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 6.8278 L22: 0.5251
REMARK 3 L33: 0.2541 L12: -1.8407
REMARK 3 L13: -1.2725 L23: 0.3393
REMARK 3 S TENSOR
REMARK 3 S11: 0.0885 S12: -0.3141 S13: 0.1179
REMARK 3 S21: 0.0194 S22: -0.0156 S23: -0.0269
REMARK 3 S31: -0.0146 S32: 0.0883 S33: -0.0729
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 6 G 122
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8514 -2.5504 -39.5333
REMARK 3 T TENSOR
REMARK 3 T11: 0.2065 T22: 0.3179
REMARK 3 T33: 0.0938 T12: -0.0001
REMARK 3 T13: 0.0162 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.6021 L22: 0.5611
REMARK 3 L33: 0.0810 L12: -0.2744
REMARK 3 L13: -0.1784 L23: 0.1356
REMARK 3 S TENSOR
REMARK 3 S11: 0.0109 S12: -0.0620 S13: -0.0672
REMARK 3 S21: 0.0039 S22: -0.0217 S23: 0.0374
REMARK 3 S31: -0.0671 S32: 0.0295 S33: 0.0108
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 : H 3 H 119
REMARK 3 ORIGIN FOR THE GROUP (A): -33.3847 10.7360 -30.6216
REMARK 3 T TENSOR
REMARK 3 T11: 0.2180 T22: 0.3302
REMARK 3 T33: 0.0871 T12: -0.0033
REMARK 3 T13: 0.0327 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.8518 L22: 1.5569
REMARK 3 L33: 0.3528 L12: -0.3734
REMARK 3 L13: -0.3226 L23: 0.5205
REMARK 3 S TENSOR
REMARK 3 S11: -0.0403 S12: -0.0525 S13: -0.0224
REMARK 3 S21: -0.1055 S22: 0.0246 S23: 0.2220
REMARK 3 S31: -0.1754 S32: 0.0689 S33: 0.0157
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 : I 4 I 88
REMARK 3 ORIGIN FOR THE GROUP (A): -50.4314 -10.0743 -10.7071
REMARK 3 T TENSOR
REMARK 3 T11: 0.2797 T22: 0.4295
REMARK 3 T33: 0.4306 T12: -0.1625
REMARK 3 T13: 0.2954 T23: -0.1852
REMARK 3 L TENSOR
REMARK 3 L11: 2.9805 L22: 2.0767
REMARK 3 L33: 3.0505 L12: -2.3944
REMARK 3 L13: -0.2868 L23: -0.2052
REMARK 3 S TENSOR
REMARK 3 S11: -0.2882 S12: 0.2383 S13: -0.0857
REMARK 3 S21: 0.3679 S22: -0.3392 S23: 0.1433
REMARK 3 S31: 0.1019 S32: 0.0925 S33: 0.6273
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 : J 83 J 171
REMARK 3 ORIGIN FOR THE GROUP (A): -37.5878 -15.5910 -26.7027
REMARK 3 T TENSOR
REMARK 3 T11: 0.1428 T22: 0.3235
REMARK 3 T33: 0.1530 T12: 0.0212
REMARK 3 T13: 0.0551 T23: 0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 0.3658 L22: 1.8516
REMARK 3 L33: 0.9385 L12: 0.6998
REMARK 3 L13: -0.4325 L23: -0.3713
REMARK 3 S TENSOR
REMARK 3 S11: 0.0433 S12: 0.0392 S13: 0.0879
REMARK 3 S21: 0.1605 S22: 0.0448 S23: 0.1540
REMARK 3 S31: 0.0242 S32: -0.0040 S33: -0.0881
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: NULL
REMARK 4
REMARK 4 5Y39 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1300004600.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29802
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.50900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS (PH 5.5), AND 25% (W/V)
REMARK 280 PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.90250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.90250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 55.32950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.92700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 55.32950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.92700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.90250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 55.32950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 58.92700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 78.90250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 55.32950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 58.92700
REMARK 290 SMTRY3 8 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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H, 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 MET A 76
REMARK 465 GLU A 77
REMARK 465 GLN A 78
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 4
REMARK 465 GLN B 121
REMARK 465 VAL B 122
REMARK 465 ALA B 123
REMARK 465 ALA B 124
REMARK 465 SER B 125
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 SER C 124
REMARK 465 MET D -1
REMARK 465 VAL D 99
REMARK 465 MET F 76
REMARK 465 GLU F 77
REMARK 465 GLN F 78
REMARK 465 HIS F 79
REMARK 465 GLU F 80
REMARK 465 TYR F 81
REMARK 465 MET F 82
REMARK 465 ASP F 83
REMARK 465 ARG F 84
REMARK 465 ALA F 85
REMARK 465 ARG F 86
REMARK 465 GLN F 87
REMARK 465 TYR F 88
REMARK 465 SER F 89
REMARK 465 THR F 90
REMARK 465 ARG F 91
REMARK 465 LEU F 92
REMARK 465 ALA F 93
REMARK 465 VAL F 94
REMARK 465 LEU F 95
REMARK 465 SER F 96
REMARK 465 SER F 97
REMARK 465 SER F 98
REMARK 465 LEU F 99
REMARK 465 THR F 100
REMARK 465 HIS F 101
REMARK 465 TRP F 102
REMARK 465 LYS F 103
REMARK 465 LYS F 104
REMARK 465 LEU F 105
REMARK 465 PRO F 106
REMARK 465 PRO F 107
REMARK 465 LEU F 108
REMARK 465 PRO F 109
REMARK 465 SER F 110
REMARK 465 LEU F 111
REMARK 465 THR F 112
REMARK 465 SER F 113
REMARK 465 MET G 1
REMARK 465 LEU G 2
REMARK 465 ARG G 3
REMARK 465 PRO G 4
REMARK 465 LYS G 5
REMARK 465 ALA G 123
REMARK 465 ALA G 124
REMARK 465 SER G 125
REMARK 465 MET H 1
REMARK 465 ALA H 2
REMARK 465 VAL H 120
REMARK 465 VAL H 121
REMARK 465 GLU H 122
REMARK 465 VAL H 123
REMARK 465 SER H 124
REMARK 465 MET I -1
REMARK 465 GLY I 0
REMARK 465 MET I 1
REMARK 465 THR I 2
REMARK 465 SER I 3
REMARK 465 ILE I 12
REMARK 465 PRO I 13
REMARK 465 ASP I 14
REMARK 465 GLN I 15
REMARK 465 GLY I 24
REMARK 465 ALA I 25
REMARK 465 VAL I 26
REMARK 465 GLY I 31
REMARK 465 ASP I 32
REMARK 465 LEU I 33
REMARK 465 GLU I 34
REMARK 465 ASN I 35
REMARK 465 ASP I 36
REMARK 465 GLU I 37
REMARK 465 LEU I 55
REMARK 465 HIS I 56
REMARK 465 ARG I 57
REMARK 465 GLY I 58
REMARK 465 MET I 59
REMARK 465 ASN I 60
REMARK 465 VAL I 61
REMARK 465 PRO I 62
REMARK 465 PHE I 63
REMARK 465 GLY I 71
REMARK 465 SER I 80
REMARK 465 ARG I 89
REMARK 465 GLN I 90
REMARK 465 ASN I 91
REMARK 465 ARG I 92
REMARK 465 GLY I 93
REMARK 465 ARG I 94
REMARK 465 GLU I 95
REMARK 465 PRO I 96
REMARK 465 ILE I 97
REMARK 465 ASP I 98
REMARK 465 VAL I 99
REMARK 465 PRO J 98
REMARK 465 SER J 99
REMARK 465 ASP J 152
REMARK 465 ASN J 153
REMARK 465 GLY J 154
REMARK 465 ALA J 172
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 ASN D 60 CG OD1 ND2
REMARK 470 GLN F 114 CG CD OE1 NE2
REMARK 470 GLN F 117 CG CD OE1 NE2
REMARK 470 LEU F 119 CG CD1 CD2
REMARK 470 GLU F 122 CG CD OE1 OE2
REMARK 470 ARG F 134 CG CD NE CZ NH1 NH2
REMARK 470 PHE G 64 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN G 65 CG OD1 ND2
REMARK 470 GLU G 66 CG CD OE1 OE2
REMARK 470 ARG H 7 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 11 CG CD CE NZ
REMARK 470 LYS H 67 CG CD CE NZ
REMARK 470 GLU H 116 CG CD OE1 OE2
REMARK 470 LEU I 5 CG CD1 CD2
REMARK 470 THR I 6 OG1 CG2
REMARK 470 GLN I 7 CG CD OE1 NE2
REMARK 470 LEU I 9 CG CD1 CD2
REMARK 470 GLU I 10 CG CD OE1 OE2
REMARK 470 LEU I 16 CG CD1 CD2
REMARK 470 TYR I 18 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL I 20 CG1 CG2
REMARK 470 LEU I 21 CG CD1 CD2
REMARK 470 SER I 22 OG
REMARK 470 GLU I 23 CG CD OE1 OE2
REMARK 470 SER I 29 OG
REMARK 470 GLN I 38 CG CD OE1 NE2
REMARK 470 VAL I 47 CG1 CG2
REMARK 470 ARG I 54 CG CD NE CZ NH1 NH2
REMARK 470 GLU I 72 CG CD OE1 OE2
REMARK 470 GLN I 82 CG CD OE1 NE2
REMARK 470 ARG I 83 CG CD NE CZ NH1 NH2
REMARK 470 PHE I 85 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL I 86 CG1 CG2
REMARK 470 VAL I 87 CG1 CG2
REMARK 470 LYS J 170 CG CD CE NZ
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 LEU A 99 78.65 -110.72
REMARK 500 THR A 100 79.74 -109.66
REMARK 500 LYS A 103 -28.40 -140.86
REMARK 500 ALA B 87 -126.37 48.89
REMARK 500 PRO B 118 39.41 -81.76
REMARK 500 LEU B 119 23.18 -148.90
REMARK 500 SER C 66 -137.73 53.24
REMARK 500 GLU E 122 1.55 -62.45
REMARK 500 HIS E 161 -151.96 -106.62
REMARK 500 LEU F 119 0.51 -66.76
REMARK 500 SER F 121 -164.90 -76.76
REMARK 500 SER F 144 21.78 -77.62
REMARK 500 GLU G 66 8.00 55.59
REMARK 500 ALA G 87 -130.41 49.61
REMARK 500 LYS H 11 21.20 -77.48
REMARK 500 SER H 66 -174.38 -64.72
REMARK 500 LYS H 67 131.73 -36.40
REMARK 500 SER I 29 45.02 -101.26
REMARK 500 LYS J 96 3.55 -63.79
REMARK 500 HIS J 161 -72.36 -81.06
REMARK 500 ASP J 162 -85.33 -129.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5Y38 RELATED DB: PDB
DBREF 5Y39 A 76 145 UNP Q6IAA8 LTOR1_HUMAN 76 145
DBREF 5Y39 B 1 125 UNP Q9Y2Q5 LTOR2_HUMAN 1 125
DBREF 5Y39 C 1 124 UNP Q9UHA4 LTOR3_HUMAN 1 124
DBREF 5Y39 D 1 99 UNP Q0VGL1 LTOR4_HUMAN 1 99
DBREF 5Y39 E 83 172 UNP O43504 LTOR5_HUMAN 1 90
DBREF 5Y39 F 76 145 UNP Q6IAA8 LTOR1_HUMAN 76 145
DBREF 5Y39 G 1 125 UNP Q9Y2Q5 LTOR2_HUMAN 1 125
DBREF 5Y39 H 1 124 UNP Q9UHA4 LTOR3_HUMAN 1 124
DBREF 5Y39 I 1 99 UNP Q0VGL1 LTOR4_HUMAN 1 99
DBREF 5Y39 J 83 172 UNP O43504 LTOR5_HUMAN 1 90
SEQADV 5Y39 MET D -1 UNP Q0VGL1 EXPRESSION TAG
SEQADV 5Y39 GLY D 0 UNP Q0VGL1 EXPRESSION TAG
SEQADV 5Y39 MET I -1 UNP Q0VGL1 EXPRESSION TAG
SEQADV 5Y39 GLY I 0 UNP Q0VGL1 EXPRESSION TAG
SEQRES 1 A 70 MET GLU GLN HIS GLU TYR MET ASP ARG ALA ARG GLN TYR
SEQRES 2 A 70 SER THR ARG LEU ALA VAL LEU SER SER SER LEU THR HIS
SEQRES 3 A 70 TRP LYS LYS LEU PRO PRO LEU PRO SER LEU THR SER GLN
SEQRES 4 A 70 PRO HIS GLN VAL LEU ALA SER GLU PRO ILE PRO PHE SER
SEQRES 5 A 70 ASP LEU GLN GLN VAL SER ARG ILE ALA ALA TYR ALA TYR
SEQRES 6 A 70 SER ALA LEU SER GLN
SEQRES 1 B 125 MET LEU ARG PRO LYS ALA LEU THR GLN VAL LEU SER GLN
SEQRES 2 B 125 ALA ASN THR GLY GLY VAL GLN SER THR LEU LEU LEU ASN
SEQRES 3 B 125 ASN GLU GLY SER LEU LEU ALA TYR SER GLY TYR GLY ASP
SEQRES 4 B 125 THR ASP ALA ARG VAL THR ALA ALA ILE ALA SER ASN ILE
SEQRES 5 B 125 TRP ALA ALA TYR ASP ARG ASN GLY ASN GLN ALA PHE ASN
SEQRES 6 B 125 GLU ASP ASN LEU LYS PHE ILE LEU MET ASP CYS MET GLU
SEQRES 7 B 125 GLY ARG VAL ALA ILE THR ARG VAL ALA ASN LEU LEU LEU
SEQRES 8 B 125 CYS MET TYR ALA LYS GLU THR VAL GLY PHE GLY MET LEU
SEQRES 9 B 125 LYS ALA LYS ALA GLN ALA LEU VAL GLN TYR LEU GLU GLU
SEQRES 10 B 125 PRO LEU THR GLN VAL ALA ALA SER
SEQRES 1 C 124 MET ALA ASP ASP LEU LYS ARG PHE LEU TYR LYS LYS LEU
SEQRES 2 C 124 PRO SER VAL GLU GLY LEU HIS ALA ILE VAL VAL SER ASP
SEQRES 3 C 124 ARG ASP GLY VAL PRO VAL ILE LYS VAL ALA ASN ASP ASN
SEQRES 4 C 124 ALA PRO GLU HIS ALA LEU ARG PRO GLY PHE LEU SER THR
SEQRES 5 C 124 PHE ALA LEU ALA THR ASP GLN GLY SER LYS LEU GLY LEU
SEQRES 6 C 124 SER LYS ASN LYS SER ILE ILE CYS TYR TYR ASN THR TYR
SEQRES 7 C 124 GLN VAL VAL GLN PHE ASN ARG LEU PRO LEU VAL VAL SER
SEQRES 8 C 124 PHE ILE ALA SER SER SER ALA ASN THR GLY LEU ILE VAL
SEQRES 9 C 124 SER LEU GLU LYS GLU LEU ALA PRO LEU PHE GLU GLU LEU
SEQRES 10 C 124 ARG GLN VAL VAL GLU VAL SER
SEQRES 1 D 101 MET GLY MET THR SER ALA LEU THR GLN GLY LEU GLU ARG
SEQRES 2 D 101 ILE PRO ASP GLN LEU GLY TYR LEU VAL LEU SER GLU GLY
SEQRES 3 D 101 ALA VAL LEU ALA SER SER GLY ASP LEU GLU ASN ASP GLU
SEQRES 4 D 101 GLN ALA ALA SER ALA ILE SER GLU LEU VAL SER THR ALA
SEQRES 5 D 101 CYS GLY PHE ARG LEU HIS ARG GLY MET ASN VAL PRO PHE
SEQRES 6 D 101 LYS ARG LEU SER VAL VAL PHE GLY GLU HIS THR LEU LEU
SEQRES 7 D 101 VAL THR VAL SER GLY GLN ARG VAL PHE VAL VAL LYS ARG
SEQRES 8 D 101 GLN ASN ARG GLY ARG GLU PRO ILE ASP VAL
SEQRES 1 E 90 MET GLU ALA THR LEU GLU GLN HIS LEU GLU ASP THR MET
SEQRES 2 E 90 LYS ASN PRO SER ILE VAL GLY VAL LEU CYS THR ASP SER
SEQRES 3 E 90 GLN GLY LEU ASN LEU GLY CYS ARG GLY THR LEU SER ASP
SEQRES 4 E 90 GLU HIS ALA GLY VAL ILE SER VAL LEU ALA GLN GLN ALA
SEQRES 5 E 90 ALA LYS LEU THR SER ASP PRO THR ASP ILE PRO VAL VAL
SEQRES 6 E 90 CYS LEU GLU SER ASP ASN GLY ASN ILE MET ILE GLN LYS
SEQRES 7 E 90 HIS ASP GLY ILE THR VAL ALA VAL HIS LYS MET ALA
SEQRES 1 F 70 MET GLU GLN HIS GLU TYR MET ASP ARG ALA ARG GLN TYR
SEQRES 2 F 70 SER THR ARG LEU ALA VAL LEU SER SER SER LEU THR HIS
SEQRES 3 F 70 TRP LYS LYS LEU PRO PRO LEU PRO SER LEU THR SER GLN
SEQRES 4 F 70 PRO HIS GLN VAL LEU ALA SER GLU PRO ILE PRO PHE SER
SEQRES 5 F 70 ASP LEU GLN GLN VAL SER ARG ILE ALA ALA TYR ALA TYR
SEQRES 6 F 70 SER ALA LEU SER GLN
SEQRES 1 G 125 MET LEU ARG PRO LYS ALA LEU THR GLN VAL LEU SER GLN
SEQRES 2 G 125 ALA ASN THR GLY GLY VAL GLN SER THR LEU LEU LEU ASN
SEQRES 3 G 125 ASN GLU GLY SER LEU LEU ALA TYR SER GLY TYR GLY ASP
SEQRES 4 G 125 THR ASP ALA ARG VAL THR ALA ALA ILE ALA SER ASN ILE
SEQRES 5 G 125 TRP ALA ALA TYR ASP ARG ASN GLY ASN GLN ALA PHE ASN
SEQRES 6 G 125 GLU ASP ASN LEU LYS PHE ILE LEU MET ASP CYS MET GLU
SEQRES 7 G 125 GLY ARG VAL ALA ILE THR ARG VAL ALA ASN LEU LEU LEU
SEQRES 8 G 125 CYS MET TYR ALA LYS GLU THR VAL GLY PHE GLY MET LEU
SEQRES 9 G 125 LYS ALA LYS ALA GLN ALA LEU VAL GLN TYR LEU GLU GLU
SEQRES 10 G 125 PRO LEU THR GLN VAL ALA ALA SER
SEQRES 1 H 124 MET ALA ASP ASP LEU LYS ARG PHE LEU TYR LYS LYS LEU
SEQRES 2 H 124 PRO SER VAL GLU GLY LEU HIS ALA ILE VAL VAL SER ASP
SEQRES 3 H 124 ARG ASP GLY VAL PRO VAL ILE LYS VAL ALA ASN ASP ASN
SEQRES 4 H 124 ALA PRO GLU HIS ALA LEU ARG PRO GLY PHE LEU SER THR
SEQRES 5 H 124 PHE ALA LEU ALA THR ASP GLN GLY SER LYS LEU GLY LEU
SEQRES 6 H 124 SER LYS ASN LYS SER ILE ILE CYS TYR TYR ASN THR TYR
SEQRES 7 H 124 GLN VAL VAL GLN PHE ASN ARG LEU PRO LEU VAL VAL SER
SEQRES 8 H 124 PHE ILE ALA SER SER SER ALA ASN THR GLY LEU ILE VAL
SEQRES 9 H 124 SER LEU GLU LYS GLU LEU ALA PRO LEU PHE GLU GLU LEU
SEQRES 10 H 124 ARG GLN VAL VAL GLU VAL SER
SEQRES 1 I 101 MET GLY MET THR SER ALA LEU THR GLN GLY LEU GLU ARG
SEQRES 2 I 101 ILE PRO ASP GLN LEU GLY TYR LEU VAL LEU SER GLU GLY
SEQRES 3 I 101 ALA VAL LEU ALA SER SER GLY ASP LEU GLU ASN ASP GLU
SEQRES 4 I 101 GLN ALA ALA SER ALA ILE SER GLU LEU VAL SER THR ALA
SEQRES 5 I 101 CYS GLY PHE ARG LEU HIS ARG GLY MET ASN VAL PRO PHE
SEQRES 6 I 101 LYS ARG LEU SER VAL VAL PHE GLY GLU HIS THR LEU LEU
SEQRES 7 I 101 VAL THR VAL SER GLY GLN ARG VAL PHE VAL VAL LYS ARG
SEQRES 8 I 101 GLN ASN ARG GLY ARG GLU PRO ILE ASP VAL
SEQRES 1 J 90 MET GLU ALA THR LEU GLU GLN HIS LEU GLU ASP THR MET
SEQRES 2 J 90 LYS ASN PRO SER ILE VAL GLY VAL LEU CYS THR ASP SER
SEQRES 3 J 90 GLN GLY LEU ASN LEU GLY CYS ARG GLY THR LEU SER ASP
SEQRES 4 J 90 GLU HIS ALA GLY VAL ILE SER VAL LEU ALA GLN GLN ALA
SEQRES 5 J 90 ALA LYS LEU THR SER ASP PRO THR ASP ILE PRO VAL VAL
SEQRES 6 J 90 CYS LEU GLU SER ASP ASN GLY ASN ILE MET ILE GLN LYS
SEQRES 7 J 90 HIS ASP GLY ILE THR VAL ALA VAL HIS LYS MET ALA
FORMUL 11 HOH *58(H2 O)
HELIX 1 AA1 TYR A 81 SER A 97 1 17
HELIX 2 AA2 GLN A 114 SER A 121 1 8
HELIX 3 AA3 PRO A 125 GLN A 145 1 21
HELIX 4 AA4 ALA B 6 GLN B 13 1 8
HELIX 5 AA5 ASP B 41 GLN B 62 1 22
HELIX 6 AA6 GLY B 100 GLU B 117 1 18
HELIX 7 AA7 PRO B 118 THR B 120 5 3
HELIX 8 AA8 ASP C 4 LEU C 13 1 10
HELIX 9 AA9 PRO C 14 VAL C 16 5 3
HELIX 10 AB1 PRO C 41 LEU C 45 5 5
HELIX 11 AB2 ARG C 46 SER C 51 1 6
HELIX 12 AB3 SER C 51 SER C 61 1 11
HELIX 13 AB4 ASN C 99 GLU C 116 1 18
HELIX 14 AB5 LEU C 117 VAL C 121 5 5
HELIX 15 AB6 MET D 1 ARG D 11 1 11
HELIX 16 AB7 ASP D 36 GLY D 52 1 17
HELIX 17 AB8 GLU E 84 ASN E 97 1 14
HELIX 18 AB9 SER E 120 GLU E 122 5 3
HELIX 19 AC1 HIS E 123 LYS E 136 1 14
HELIX 20 AC2 PRO F 115 LEU F 119 1 5
HELIX 21 AC3 PRO F 125 LEU F 143 1 19
HELIX 22 AC4 LEU G 7 GLN G 13 1 7
HELIX 23 AC5 ASP G 41 ASN G 59 1 19
HELIX 24 AC6 ASN G 59 PHE G 64 1 6
HELIX 25 AC7 GLY G 100 VAL G 122 1 23
HELIX 26 AC8 ASP H 4 LYS H 11 1 8
HELIX 27 AC9 LYS H 12 VAL H 16 5 5
HELIX 28 AD1 PRO H 41 LEU H 45 5 5
HELIX 29 AD2 ARG H 46 SER H 51 1 6
HELIX 30 AD3 SER H 51 SER H 61 1 11
HELIX 31 AD4 ASN H 99 GLU H 116 1 18
HELIX 32 AD5 THR I 6 ARG I 11 1 6
HELIX 33 AD6 ALA I 39 PHE I 53 1 15
HELIX 34 AD7 GLU J 84 MET J 95 1 12
HELIX 35 AD8 HIS J 123 ALA J 135 1 13
HELIX 36 AD9 LYS J 136 THR J 138 5 3
SHEET 1 AA110 LEU B 31 GLY B 36 0
SHEET 2 AA110 VAL B 19 LEU B 25 -1 N LEU B 24 O LEU B 32
SHEET 3 AA110 LEU B 89 ALA B 95 -1 O LEU B 90 N LEU B 25
SHEET 4 AA110 GLY B 79 VAL B 86 -1 N THR B 84 O LEU B 91
SHEET 5 AA110 LEU B 69 CYS B 76 -1 N CYS B 76 O GLY B 79
SHEET 6 AA110 ASN C 68 TYR C 75 -1 O LYS C 69 N ASP B 75
SHEET 7 AA110 TYR C 78 ARG C 85 -1 O ASN C 84 N LYS C 69
SHEET 8 AA110 LEU C 88 SER C 95 -1 O ALA C 94 N GLN C 79
SHEET 9 AA110 LEU C 19 SER C 25 -1 N VAL C 23 O SER C 91
SHEET 10 AA110 PRO C 31 ALA C 36 -1 O VAL C 32 N VAL C 24
SHEET 1 AA210 ALA D 25 GLY D 31 0
SHEET 2 AA210 GLN D 15 SER D 22 -1 N VAL D 20 O ALA D 28
SHEET 3 AA210 ARG D 83 GLN D 90 -1 O LYS D 88 N LEU D 16
SHEET 4 AA210 HIS D 73 SER D 80 -1 N THR D 78 O PHE D 85
SHEET 5 AA210 ARG D 65 VAL D 69 -1 N LEU D 66 O VAL D 77
SHEET 6 AA210 VAL E 146 GLU E 150 -1 O GLU E 150 N ARG D 65
SHEET 7 AA210 GLY E 154 LYS E 160 -1 O ILE E 158 N VAL E 147
SHEET 8 AA210 ILE E 164 MET E 171 -1 O LYS E 170 N ASN E 155
SHEET 9 AA210 ILE E 100 ASP E 107 -1 N THR E 106 O THR E 165
SHEET 10 AA210 ASN E 112 GLY E 117 -1 O GLY E 114 N CYS E 105
SHEET 1 AA310 LEU G 31 GLY G 36 0
SHEET 2 AA310 VAL G 19 ASN G 26 -1 N LEU G 24 O ALA G 33
SHEET 3 AA310 LEU G 89 ALA G 95 -1 O CYS G 92 N LEU G 23
SHEET 4 AA310 GLY G 79 VAL G 86 -1 N THR G 84 O LEU G 91
SHEET 5 AA310 LEU G 69 CYS G 76 -1 N CYS G 76 O GLY G 79
SHEET 6 AA310 ASN H 68 TYR H 75 -1 O ILE H 72 N LEU G 73
SHEET 7 AA310 TYR H 78 ARG H 85 -1 O ASN H 84 N LYS H 69
SHEET 8 AA310 LEU H 88 SER H 95 -1 O VAL H 90 N PHE H 83
SHEET 9 AA310 LEU H 19 SER H 25 -1 N VAL H 23 O SER H 91
SHEET 10 AA310 PRO H 31 ALA H 36 -1 O VAL H 35 N ILE H 22
SHEET 1 AA4 4 VAL I 20 LEU I 21 0
SHEET 2 AA4 4 VAL I 84 VAL I 87 -1 O VAL I 84 N LEU I 21
SHEET 3 AA4 4 LEU I 76 THR I 78 -1 N THR I 78 O PHE I 85
SHEET 4 AA4 4 LEU I 66 SER I 67 -1 N LEU I 66 O VAL I 77
SHEET 1 AA5 5 ASN J 112 GLY J 117 0
SHEET 2 AA5 5 GLY J 102 THR J 106 -1 N CYS J 105 O LEU J 113
SHEET 3 AA5 5 THR J 165 HIS J 169 -1 O THR J 165 N THR J 106
SHEET 4 AA5 5 ILE J 156 LYS J 160 -1 N MET J 157 O VAL J 168
SHEET 5 AA5 5 VAL J 147 LEU J 149 -1 N VAL J 147 O ILE J 158
CISPEP 1 LEU C 86 PRO C 87 0 15.71
CISPEP 2 LEU H 86 PRO H 87 0 9.73
CRYST1 110.659 117.854 157.805 90.00 90.00 90.00 C 2 2 21 16
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 0.009037 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008485 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006337 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
