HEADER LIGASE 09-SEP-11 3TQI
TITLE STRUCTURE OF THE GMP SYNTHASE (GUAA) FROM COXIELLA BURNETII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GMP SYNTHASE [GLUTAMINE-HYDROLYZING];
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: GMP SYNTHETASE, GLUTAMINE AMIDOTRANSFERASE;
COMPND 5 EC: 6.3.5.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COXIELLA BURNETII;
SOURCE 3 ORGANISM_TAXID: 777;
SOURCE 4 STRAIN: RSA 493 NINE MILE PHASE I;
SOURCE 5 GENE: CBU_1341, GUAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS GMP SYNTHASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.C.FRANKLIN,J.CHEUNG,M.RUDOLPH,M.CASSIDY,E.GARY,F.BURSHTEYN,J.LOVE
REVDAT 4 28-FEB-24 3TQI 1 SEQADV
REVDAT 3 20-JAN-16 3TQI 1 JRNL
REVDAT 2 24-JUN-15 3TQI 1 JRNL
REVDAT 1 28-SEP-11 3TQI 0
JRNL AUTH M.C.FRANKLIN,J.CHEUNG,M.J.RUDOLPH,F.BURSHTEYN,M.CASSIDY,
JRNL AUTH 2 E.GARY,B.HILLERICH,Z.K.YAO,P.R.CARLIER,M.TOTROV,J.D.LOVE
JRNL TITL STRUCTURAL GENOMICS FOR DRUG DESIGN AGAINST THE PATHOGEN
JRNL TITL 2 COXIELLA BURNETII.
JRNL REF PROTEINS V. 83 2124 2015
JRNL REFN ISSN 0887-3585
JRNL PMID 26033498
JRNL DOI 10.1002/PROT.24841
REMARK 2
REMARK 2 RESOLUTION. 2.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 50308
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) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2691
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) : 2.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3411
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.59
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE SET COUNT : 171
REMARK 3 BIN FREE R VALUE : 0.4060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14708
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.24000
REMARK 3 B22 (A**2) : 0.28000
REMARK 3 B33 (A**2) : -1.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.76000
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): 0.441
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.376
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 42.940
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.908
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.879
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15032 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 10300 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20340 ; 1.221 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25160 ; 0.839 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1832 ; 7.403 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 688 ;36.202 ;24.244
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2624 ;18.875 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 84 ;16.496 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2276 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 16484 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2956 ; 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): 9220 ; 0.203 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3744 ; 0.041 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14920 ; 0.423 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5812 ; 0.762 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5420 ; 1.322 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 208 4
REMARK 3 1 B 1 B 208 4
REMARK 3 1 C 1 C 208 4
REMARK 3 1 D 1 D 208 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2534 ; 0.33 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2534 ; 0.35 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 2534 ; 0.36 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 2534 ; 0.34 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2534 ; 0.14 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2534 ; 0.16 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 2534 ; 0.14 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 2534 ; 0.16 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 209 A 416 4
REMARK 3 1 B 209 B 416 4
REMARK 3 1 C 209 C 416 4
REMARK 3 1 D 209 D 416 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 2430 ; 0.39 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 B (A): 2430 ; 0.36 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 C (A): 2430 ; 0.41 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 D (A): 2430 ; 0.38 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 2430 ; 0.15 ; 2.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 2430 ; 0.15 ; 2.00
REMARK 3 MEDIUM THERMAL 2 C (A**2): 2430 ; 0.14 ; 2.00
REMARK 3 MEDIUM THERMAL 2 D (A**2): 2430 ; 0.14 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 417 A 523 4
REMARK 3 1 B 417 B 523 4
REMARK 3 1 C 417 C 523 4
REMARK 3 1 D 417 D 523 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 1288 ; 0.34 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 B (A): 1288 ; 0.38 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 C (A): 1288 ; 0.33 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 D (A): 1288 ; 0.35 ; 0.50
REMARK 3 MEDIUM THERMAL 3 A (A**2): 1288 ; 0.12 ; 2.00
REMARK 3 MEDIUM THERMAL 3 B (A**2): 1288 ; 0.12 ; 2.00
REMARK 3 MEDIUM THERMAL 3 C (A**2): 1288 ; 0.12 ; 2.00
REMARK 3 MEDIUM THERMAL 3 D (A**2): 1288 ; 0.13 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 5 A 208
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0024 47.1582 108.2457
REMARK 3 T TENSOR
REMARK 3 T11: 0.0815 T22: 0.3139
REMARK 3 T33: 0.1978 T12: 0.0364
REMARK 3 T13: 0.0014 T23: 0.1472
REMARK 3 L TENSOR
REMARK 3 L11: 3.6434 L22: 6.7879
REMARK 3 L33: 2.0335 L12: -0.6346
REMARK 3 L13: -0.4264 L23: 0.7709
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: -0.1232 S13: -0.2393
REMARK 3 S21: -0.0825 S22: -0.1149 S23: -0.7797
REMARK 3 S31: 0.0707 S32: 0.3320 S33: 0.1236
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 209 A 416
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0346 81.9948 98.8459
REMARK 3 T TENSOR
REMARK 3 T11: 0.2455 T22: 0.1790
REMARK 3 T33: 0.2525 T12: -0.0640
REMARK 3 T13: 0.0492 T23: -0.0702
REMARK 3 L TENSOR
REMARK 3 L11: 1.8120 L22: 3.6696
REMARK 3 L33: 4.5123 L12: 0.4259
REMARK 3 L13: -1.3180 L23: -1.2365
REMARK 3 S TENSOR
REMARK 3 S11: 0.1596 S12: -0.0741 S13: 0.3479
REMARK 3 S21: -0.0063 S22: -0.0665 S23: -0.1289
REMARK 3 S31: -0.2950 S32: 0.2244 S33: -0.0931
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 417 A 523
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7408 72.1943 74.6411
REMARK 3 T TENSOR
REMARK 3 T11: 0.3678 T22: 0.2579
REMARK 3 T33: 0.1341 T12: -0.0446
REMARK 3 T13: 0.1415 T23: -0.1402
REMARK 3 L TENSOR
REMARK 3 L11: 7.5679 L22: 5.8740
REMARK 3 L33: 10.2964 L12: 0.3558
REMARK 3 L13: -3.4170 L23: -1.1360
REMARK 3 S TENSOR
REMARK 3 S11: 0.0168 S12: 0.4686 S13: 0.0501
REMARK 3 S21: 0.0001 S22: -0.2895 S23: 0.3355
REMARK 3 S31: 0.1197 S32: -1.0258 S33: 0.2727
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 : B 5 B 208
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7452 68.7820 34.7943
REMARK 3 T TENSOR
REMARK 3 T11: 0.1417 T22: 0.1654
REMARK 3 T33: 0.2372 T12: 0.0308
REMARK 3 T13: -0.1086 T23: 0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 8.5715 L22: 4.1042
REMARK 3 L33: 2.6676 L12: -0.3754
REMARK 3 L13: -1.5106 L23: -0.3437
REMARK 3 S TENSOR
REMARK 3 S11: 0.1871 S12: 0.2758 S13: 0.8363
REMARK 3 S21: -0.2708 S22: -0.0127 S23: 0.1569
REMARK 3 S31: -0.1571 S32: 0.0559 S33: -0.1743
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 : B 209 B 416
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1607 62.4201 39.4886
REMARK 3 T TENSOR
REMARK 3 T11: 0.1670 T22: 0.1856
REMARK 3 T33: 0.1508 T12: -0.0095
REMARK 3 T13: 0.0366 T23: 0.0599
REMARK 3 L TENSOR
REMARK 3 L11: 3.0906 L22: 2.3989
REMARK 3 L33: 4.8333 L12: 0.5683
REMARK 3 L13: 0.4207 L23: 1.3004
REMARK 3 S TENSOR
REMARK 3 S11: 0.0514 S12: -0.0680 S13: 0.2817
REMARK 3 S21: 0.2317 S22: -0.0220 S23: 0.1208
REMARK 3 S31: -0.2618 S32: 0.1690 S33: -0.0293
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 417 B 523
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5292 61.5103 64.8742
REMARK 3 T TENSOR
REMARK 3 T11: 0.4445 T22: 0.1899
REMARK 3 T33: 0.1248 T12: -0.0175
REMARK 3 T13: 0.2053 T23: -0.0653
REMARK 3 L TENSOR
REMARK 3 L11: 7.7497 L22: 6.3619
REMARK 3 L33: 8.8048 L12: 1.7884
REMARK 3 L13: 0.7266 L23: 3.0911
REMARK 3 S TENSOR
REMARK 3 S11: -0.0336 S12: -0.0059 S13: -0.2403
REMARK 3 S21: 0.2992 S22: -0.2080 S23: 0.0278
REMARK 3 S31: 0.8296 S32: -0.2788 S33: 0.2416
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 : C 5 C 208
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7921 66.9966 105.1158
REMARK 3 T TENSOR
REMARK 3 T11: 0.1219 T22: 0.1599
REMARK 3 T33: 0.2832 T12: 0.0548
REMARK 3 T13: 0.0304 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 5.3349 L22: 8.4242
REMARK 3 L33: 3.0266 L12: 0.7111
REMARK 3 L13: -0.8461 L23: -2.3753
REMARK 3 S TENSOR
REMARK 3 S11: 0.0798 S12: -0.0780 S13: 0.4011
REMARK 3 S21: 0.0585 S22: 0.2197 S23: 0.7717
REMARK 3 S31: -0.0324 S32: -0.3073 S33: -0.2995
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 209 C 416
REMARK 3 ORIGIN FOR THE GROUP (A): -9.7794 31.0574 105.2486
REMARK 3 T TENSOR
REMARK 3 T11: 0.2777 T22: 0.2218
REMARK 3 T33: 0.1149 T12: -0.0478
REMARK 3 T13: 0.0460 T23: 0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 2.2596 L22: 2.6967
REMARK 3 L33: 5.4075 L12: 0.3583
REMARK 3 L13: 0.7863 L23: -0.1629
REMARK 3 S TENSOR
REMARK 3 S11: -0.0693 S12: 0.1625 S13: -0.0222
REMARK 3 S21: -0.2160 S22: 0.0052 S23: 0.0983
REMARK 3 S31: 0.4996 S32: -0.3980 S33: 0.0641
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 417 C 523
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6396 34.4992 79.6429
REMARK 3 T TENSOR
REMARK 3 T11: 0.3633 T22: 0.2991
REMARK 3 T33: 0.0423 T12: 0.0124
REMARK 3 T13: -0.0701 T23: 0.0687
REMARK 3 L TENSOR
REMARK 3 L11: 5.4799 L22: 7.5822
REMARK 3 L33: 9.1956 L12: 1.5389
REMARK 3 L13: 2.2536 L23: 2.5686
REMARK 3 S TENSOR
REMARK 3 S11: 0.1654 S12: 0.2777 S13: -0.1559
REMARK 3 S21: 0.0466 S22: -0.1403 S23: -0.0548
REMARK 3 S31: -0.1022 S32: 0.7040 S33: -0.0251
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 : D 5 D 208
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8067 28.0070 38.8044
REMARK 3 T TENSOR
REMARK 3 T11: 0.1666 T22: 0.1118
REMARK 3 T33: 0.1630 T12: 0.0320
REMARK 3 T13: 0.1064 T23: 0.0424
REMARK 3 L TENSOR
REMARK 3 L11: 6.8171 L22: 3.1245
REMARK 3 L33: 2.4804 L12: -0.4678
REMARK 3 L13: 1.4329 L23: -0.3979
REMARK 3 S TENSOR
REMARK 3 S11: -0.0679 S12: -0.1003 S13: -0.7189
REMARK 3 S21: 0.0404 S22: -0.1121 S23: -0.1344
REMARK 3 S31: 0.2391 S32: 0.0078 S33: 0.1799
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 : D 209 D 416
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1071 35.3338 42.5403
REMARK 3 T TENSOR
REMARK 3 T11: 0.2133 T22: 0.1953
REMARK 3 T33: 0.1571 T12: -0.0320
REMARK 3 T13: -0.0686 T23: -0.0658
REMARK 3 L TENSOR
REMARK 3 L11: 3.8220 L22: 2.8134
REMARK 3 L33: 3.9293 L12: 0.4179
REMARK 3 L13: -0.6270 L23: -0.3814
REMARK 3 S TENSOR
REMARK 3 S11: 0.0232 S12: -0.0161 S13: -0.2890
REMARK 3 S21: 0.2770 S22: -0.1176 S23: 0.1521
REMARK 3 S31: 0.3045 S32: -0.2916 S33: 0.0944
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 : D 417 D 523
REMARK 3 ORIGIN FOR THE GROUP (A): -14.9396 42.3707 67.1818
REMARK 3 T TENSOR
REMARK 3 T11: 0.5042 T22: 0.2453
REMARK 3 T33: 0.0651 T12: -0.0269
REMARK 3 T13: -0.1402 T23: 0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 6.8264 L22: 4.8946
REMARK 3 L33: 9.8686 L12: 1.4935
REMARK 3 L13: -1.0105 L23: -2.0808
REMARK 3 S TENSOR
REMARK 3 S11: -0.1615 S12: 0.0886 S13: 0.1484
REMARK 3 S21: 0.1944 S22: -0.0667 S23: 0.2398
REMARK 3 S31: -0.7853 S32: 0.1890 S33: 0.2282
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3TQI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1000067796.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53026
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.840
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.44700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE, 0.1 M CALCIUM
REMARK 280 ACETATE, 19% PEG 1000, PH 8.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 71.97650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL UNIT OF THIS PROTEIN IS A DIMER, OF WHICH
REMARK 300 THERE ARE TWO IN THE ASYMMETRIC UNIT: CHAINS A+B, AND CHAINS C+D
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 79610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 LYS A 3
REMARK 465 ASP A 4
REMARK 465 THR A 62
REMARK 465 VAL A 63
REMARK 465 THR A 64
REMARK 465 LEU A 65
REMARK 465 SER A 66
REMARK 465 HIS A 67
REMARK 465 THR A 68
REMARK 465 LEU A 69
REMARK 465 ARG A 70
REMARK 465 ARG A 102
REMARK 465 THR A 103
REMARK 465 ALA A 104
REMARK 465 LYS A 105
REMARK 465 ALA A 106
REMARK 465 ALA A 344
REMARK 465 LYS A 345
REMARK 465 THR A 346
REMARK 465 LYS A 347
REMARK 465 THR A 348
REMARK 465 GLY A 349
REMARK 465 LYS A 350
REMARK 465 GLY A 351
REMARK 465 HIS A 352
REMARK 465 ILE A 353
REMARK 465 ILE A 354
REMARK 465 LYS A 355
REMARK 465 THR A 356
REMARK 465 HIS A 357
REMARK 465 HIS A 358
REMARK 465 ASN A 359
REMARK 465 VAL A 360
REMARK 465 GLY A 361
REMARK 465 GLY A 362
REMARK 465 LEU A 363
REMARK 465 PRO A 364
REMARK 465 LEU A 365
REMARK 465 ASN A 366
REMARK 465 MET A 367
REMARK 465 GLU A 368
REMARK 465 LEU A 369
REMARK 465 GLY A 457
REMARK 465 VAL A 458
REMARK 465 LYS A 459
REMARK 465 GLY A 460
REMARK 465 ASP A 461
REMARK 465 ALA A 462
REMARK 465 ARG A 463
REMARK 465 HIS A 464
REMARK 465 THR A 476
REMARK 465 VAL A 477
REMARK 465 ASP A 478
REMARK 465 PHE A 479
REMARK 465 MET A 480
REMARK 465 THR A 481
REMARK 465 ALA A 482
REMARK 465 GLU A 524
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 LYS B 3
REMARK 465 ASP B 4
REMARK 465 THR B 62
REMARK 465 VAL B 63
REMARK 465 THR B 64
REMARK 465 LEU B 65
REMARK 465 SER B 66
REMARK 465 HIS B 67
REMARK 465 THR B 68
REMARK 465 LEU B 69
REMARK 465 ARG B 70
REMARK 465 ARG B 102
REMARK 465 THR B 103
REMARK 465 ALA B 104
REMARK 465 LYS B 105
REMARK 465 ALA B 106
REMARK 465 ALA B 344
REMARK 465 LYS B 345
REMARK 465 THR B 346
REMARK 465 LYS B 347
REMARK 465 THR B 348
REMARK 465 GLY B 349
REMARK 465 LYS B 350
REMARK 465 GLY B 351
REMARK 465 HIS B 352
REMARK 465 ILE B 353
REMARK 465 ILE B 354
REMARK 465 LYS B 355
REMARK 465 THR B 356
REMARK 465 HIS B 357
REMARK 465 HIS B 358
REMARK 465 ASN B 359
REMARK 465 VAL B 360
REMARK 465 GLY B 361
REMARK 465 GLY B 362
REMARK 465 LEU B 363
REMARK 465 PRO B 364
REMARK 465 LEU B 365
REMARK 465 ASN B 366
REMARK 465 MET B 367
REMARK 465 GLU B 368
REMARK 465 LEU B 369
REMARK 465 GLY B 457
REMARK 465 VAL B 458
REMARK 465 LYS B 459
REMARK 465 GLY B 460
REMARK 465 ASP B 461
REMARK 465 ALA B 462
REMARK 465 ARG B 463
REMARK 465 HIS B 464
REMARK 465 THR B 476
REMARK 465 VAL B 477
REMARK 465 ASP B 478
REMARK 465 PHE B 479
REMARK 465 MET B 480
REMARK 465 THR B 481
REMARK 465 ALA B 482
REMARK 465 GLU B 524
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 ALA C 0
REMARK 465 MET C 1
REMARK 465 LEU C 2
REMARK 465 LYS C 3
REMARK 465 ASP C 4
REMARK 465 THR C 62
REMARK 465 VAL C 63
REMARK 465 THR C 64
REMARK 465 LEU C 65
REMARK 465 SER C 66
REMARK 465 HIS C 67
REMARK 465 THR C 68
REMARK 465 LEU C 69
REMARK 465 ARG C 70
REMARK 465 ARG C 102
REMARK 465 THR C 103
REMARK 465 ALA C 104
REMARK 465 LYS C 105
REMARK 465 ALA C 106
REMARK 465 ALA C 344
REMARK 465 LYS C 345
REMARK 465 THR C 346
REMARK 465 LYS C 347
REMARK 465 THR C 348
REMARK 465 GLY C 349
REMARK 465 LYS C 350
REMARK 465 GLY C 351
REMARK 465 HIS C 352
REMARK 465 ILE C 353
REMARK 465 ILE C 354
REMARK 465 LYS C 355
REMARK 465 THR C 356
REMARK 465 HIS C 357
REMARK 465 HIS C 358
REMARK 465 ASN C 359
REMARK 465 VAL C 360
REMARK 465 GLY C 361
REMARK 465 GLY C 362
REMARK 465 LEU C 363
REMARK 465 PRO C 364
REMARK 465 LEU C 365
REMARK 465 ASN C 366
REMARK 465 MET C 367
REMARK 465 GLU C 368
REMARK 465 LEU C 369
REMARK 465 GLY C 457
REMARK 465 VAL C 458
REMARK 465 LYS C 459
REMARK 465 GLY C 460
REMARK 465 ASP C 461
REMARK 465 ALA C 462
REMARK 465 ARG C 463
REMARK 465 HIS C 464
REMARK 465 THR C 476
REMARK 465 VAL C 477
REMARK 465 ASP C 478
REMARK 465 PHE C 479
REMARK 465 MET C 480
REMARK 465 THR C 481
REMARK 465 ALA C 482
REMARK 465 GLU C 524
REMARK 465 SER D -2
REMARK 465 ASN D -1
REMARK 465 ALA D 0
REMARK 465 MET D 1
REMARK 465 LEU D 2
REMARK 465 LYS D 3
REMARK 465 ASP D 4
REMARK 465 THR D 62
REMARK 465 VAL D 63
REMARK 465 THR D 64
REMARK 465 LEU D 65
REMARK 465 SER D 66
REMARK 465 HIS D 67
REMARK 465 THR D 68
REMARK 465 LEU D 69
REMARK 465 ARG D 70
REMARK 465 ARG D 102
REMARK 465 THR D 103
REMARK 465 ALA D 104
REMARK 465 LYS D 105
REMARK 465 ALA D 106
REMARK 465 ALA D 344
REMARK 465 LYS D 345
REMARK 465 THR D 346
REMARK 465 LYS D 347
REMARK 465 THR D 348
REMARK 465 GLY D 349
REMARK 465 LYS D 350
REMARK 465 GLY D 351
REMARK 465 HIS D 352
REMARK 465 ILE D 353
REMARK 465 ILE D 354
REMARK 465 LYS D 355
REMARK 465 THR D 356
REMARK 465 HIS D 357
REMARK 465 HIS D 358
REMARK 465 ASN D 359
REMARK 465 VAL D 360
REMARK 465 GLY D 361
REMARK 465 GLY D 362
REMARK 465 LEU D 363
REMARK 465 PRO D 364
REMARK 465 LEU D 365
REMARK 465 ASN D 366
REMARK 465 MET D 367
REMARK 465 GLU D 368
REMARK 465 LEU D 369
REMARK 465 GLY D 457
REMARK 465 VAL D 458
REMARK 465 LYS D 459
REMARK 465 GLY D 460
REMARK 465 ASP D 461
REMARK 465 ALA D 462
REMARK 465 ARG D 463
REMARK 465 HIS D 464
REMARK 465 THR D 476
REMARK 465 VAL D 477
REMARK 465 ASP D 478
REMARK 465 PHE D 479
REMARK 465 MET D 480
REMARK 465 THR D 481
REMARK 465 ALA D 482
REMARK 465 GLU D 524
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASP A 261 O ASP A 289 2.11
REMARK 500 O LEU A 407 O ILE A 409 2.16
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 HIS A 6 -13.09 66.73
REMARK 500 SER A 17 120.41 53.94
REMARK 500 LEU A 22 -40.63 124.11
REMARK 500 GLU A 44 110.43 76.46
REMARK 500 THR A 45 132.51 71.75
REMARK 500 ILE A 46 -54.87 80.81
REMARK 500 PRO A 60 -167.66 -74.31
REMARK 500 ALA A 73 -97.35 104.77
REMARK 500 CYS A 86 -113.77 54.24
REMARK 500 LEU A 96 -159.86 -101.26
REMARK 500 ASN A 117 89.54 61.77
REMARK 500 ALA A 119 -153.42 64.57
REMARK 500 ILE A 125 84.57 56.37
REMARK 500 SER A 130 151.53 80.02
REMARK 500 ALA A 158 148.08 -178.68
REMARK 500 PHE A 171 -47.30 88.33
REMARK 500 THR A 210 -59.64 130.36
REMARK 500 SER A 235 117.81 -36.35
REMARK 500 ALA A 283 123.53 61.72
REMARK 500 ALA A 290 -0.30 55.21
REMARK 500 ALA A 297 -29.99 77.19
REMARK 500 ILE A 301 86.29 62.19
REMARK 500 ALA A 323 -47.42 109.55
REMARK 500 LYS A 324 55.47 -91.43
REMARK 500 LYS A 325 -50.86 -177.47
REMARK 500 LEU A 407 0.36 -69.79
REMARK 500 ARG A 410 -11.17 67.72
REMARK 500 SER A 416 -37.89 -135.17
REMARK 500 ALA A 417 -53.99 105.99
REMARK 500 LEU A 434 -59.45 88.28
REMARK 500 ASP A 438 22.04 45.28
REMARK 500 LYS A 454 134.14 75.36
REMARK 500 LYS A 504 -175.60 -63.78
REMARK 500 VAL A 506 -76.96 -114.28
REMARK 500 SER A 507 113.13 62.92
REMARK 500 ARG A 508 127.08 73.27
REMARK 500 SER B 17 124.67 92.58
REMARK 500 LEU B 22 -45.84 114.18
REMARK 500 GLU B 44 112.17 81.97
REMARK 500 THR B 45 126.15 72.54
REMARK 500 ILE B 46 -58.80 92.11
REMARK 500 SER B 57 -145.58 -97.01
REMARK 500 ALA B 73 -77.41 113.90
REMARK 500 CYS B 86 -108.38 50.80
REMARK 500 ASN B 117 97.11 60.96
REMARK 500 ALA B 119 -146.00 61.39
REMARK 500 ILE B 125 82.37 39.47
REMARK 500 VAL B 129 -116.93 -84.96
REMARK 500 SER B 130 150.76 163.40
REMARK 500 ALA B 158 147.22 -174.82
REMARK 500
REMARK 500 THIS ENTRY HAS 140 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 44 THR A 45 -141.22
REMARK 500 SER A 57 GLY A 58 136.11
REMARK 500 GLU B 44 THR B 45 -141.39
REMARK 500 SER B 57 GLY B 58 142.04
REMARK 500 GLU C 44 THR C 45 -140.26
REMARK 500 SER C 57 GLY C 58 142.31
REMARK 500 GLU C 432 GLU C 433 144.60
REMARK 500 GLU D 44 THR D 45 -146.14
REMARK 500 SER D 57 GLY D 58 134.53
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3TQI C 1 524 UNP Q83BZ6 GUAA_COXBU 1 524
DBREF 3TQI A 1 524 UNP Q83BZ6 GUAA_COXBU 1 524
DBREF 3TQI D 1 524 UNP Q83BZ6 GUAA_COXBU 1 524
DBREF 3TQI B 1 524 UNP Q83BZ6 GUAA_COXBU 1 524
SEQADV 3TQI SER C -2 UNP Q83BZ6 EXPRESSION TAG
SEQADV 3TQI ASN C -1 UNP Q83BZ6 EXPRESSION TAG
SEQADV 3TQI ALA C 0 UNP Q83BZ6 EXPRESSION TAG
SEQADV 3TQI SER A -2 UNP Q83BZ6 EXPRESSION TAG
SEQADV 3TQI ASN A -1 UNP Q83BZ6 EXPRESSION TAG
SEQADV 3TQI ALA A 0 UNP Q83BZ6 EXPRESSION TAG
SEQADV 3TQI SER D -2 UNP Q83BZ6 EXPRESSION TAG
SEQADV 3TQI ASN D -1 UNP Q83BZ6 EXPRESSION TAG
SEQADV 3TQI ALA D 0 UNP Q83BZ6 EXPRESSION TAG
SEQADV 3TQI SER B -2 UNP Q83BZ6 EXPRESSION TAG
SEQADV 3TQI ASN B -1 UNP Q83BZ6 EXPRESSION TAG
SEQADV 3TQI ALA B 0 UNP Q83BZ6 EXPRESSION TAG
SEQRES 1 A 527 SER ASN ALA MET LEU LYS ASP ILE HIS GLN HIS ARG ILE
SEQRES 2 A 527 LEU ILE LEU ASP PHE GLY SER GLN TYR ALA GLN LEU ILE
SEQRES 3 A 527 ALA ARG ARG VAL ARG GLU ILE GLY VAL TYR CYS GLU LEU
SEQRES 4 A 527 MET PRO CYS ASP ILE ASP GLU GLU THR ILE ARG ASP PHE
SEQRES 5 A 527 ASN PRO HIS GLY ILE ILE LEU SER GLY GLY PRO GLU THR
SEQRES 6 A 527 VAL THR LEU SER HIS THR LEU ARG ALA PRO ALA PHE ILE
SEQRES 7 A 527 PHE GLU ILE GLY CYS PRO VAL LEU GLY ILE CYS TYR GLY
SEQRES 8 A 527 MET GLN THR MET ALA TYR GLN LEU GLY GLY LYS VAL ASN
SEQRES 9 A 527 ARG THR ALA LYS ALA GLU PHE GLY HIS ALA GLN LEU ARG
SEQRES 10 A 527 VAL LEU ASN PRO ALA PHE LEU PHE ASP GLY ILE GLU ASP
SEQRES 11 A 527 GLN VAL SER PRO GLN GLY GLU PRO LEU LEU ASP VAL TRP
SEQRES 12 A 527 MET SER HIS GLY ASP ILE VAL SER GLU LEU PRO PRO GLY
SEQRES 13 A 527 PHE GLU ALA THR ALA CYS THR ASP ASN SER PRO LEU ALA
SEQRES 14 A 527 ALA MET ALA ASP PHE LYS ARG ARG PHE PHE GLY LEU GLN
SEQRES 15 A 527 PHE HIS PRO GLU VAL THR HIS THR PRO GLN GLY HIS ARG
SEQRES 16 A 527 ILE LEU ALA HIS PHE VAL ILE HIS ILE CYS GLN CYS ILE
SEQRES 17 A 527 PRO ASN TRP THR THR LYS HIS ILE ILE GLU ASP SER ILE
SEQRES 18 A 527 ARG ASP ILE GLN GLU LYS VAL GLY LYS GLU GLN VAL ILE
SEQRES 19 A 527 VAL GLY LEU SER GLY GLY VAL ASP SER ALA VAL THR ALA
SEQRES 20 A 527 THR LEU VAL HIS LYS ALA ILE GLY ASP GLN LEU VAL CYS
SEQRES 21 A 527 VAL LEU VAL ASP THR GLY LEU LEU ARG LEU ASN GLU VAL
SEQRES 22 A 527 ASP GLU VAL LEU ASN VAL PHE GLN LYS HIS LEU GLY ALA
SEQRES 23 A 527 LYS VAL ILE CYS VAL ASP ALA LYS ASP ARG PHE MET LYS
SEQRES 24 A 527 ALA LEU LYS GLY ILE SER ASP PRO GLU GLU LYS ARG LYS
SEQRES 25 A 527 ILE ALA GLY GLU GLN PHE ILE ARG VAL PHE GLU GLU GLN
SEQRES 26 A 527 ALA LYS LYS LEU ASN VAL LYS TRP LEU GLY GLN GLY THR
SEQRES 27 A 527 ILE TYR PRO ASP VAL ILE GLU SER ALA LYS THR LYS THR
SEQRES 28 A 527 GLY LYS GLY HIS ILE ILE LYS THR HIS HIS ASN VAL GLY
SEQRES 29 A 527 GLY LEU PRO LEU ASN MET GLU LEU LYS LEU ILE GLU PRO
SEQRES 30 A 527 LEU ARG GLU LEU PHE LYS ASP GLU VAL ARG LYS LEU GLY
SEQRES 31 A 527 LEU GLU LEU GLY LEU PRO ALA ASP LEU ILE TYR ARG HIS
SEQRES 32 A 527 PRO PHE PRO GLY PRO GLY LEU ALA ILE ARG ILE LEU GLY
SEQRES 33 A 527 GLU VAL SER ALA GLU TYR ILE ASN ILE LEU LYS GLN ALA
SEQRES 34 A 527 ASP ALA ILE PHE ILE GLU GLU LEU LYS LYS SER ASP TYR
SEQRES 35 A 527 TYR HIS GLN VAL SER GLN ALA PHE ALA VAL PHE MET PRO
SEQRES 36 A 527 LEU LYS SER VAL GLY VAL LYS GLY ASP ALA ARG HIS TYR
SEQRES 37 A 527 GLY TYR ILE ILE ALA LEU ARG ALA VAL LYS THR VAL ASP
SEQRES 38 A 527 PHE MET THR ALA GLN TRP ALA ASP LEU PRO HIS GLU PHE
SEQRES 39 A 527 LEU SER LYS VAL SER HIS ARG ILE VAL ASN GLU ILE LYS
SEQRES 40 A 527 GLU VAL SER ARG VAL VAL TYR ASP MET THR ASN LYS PRO
SEQRES 41 A 527 PRO ALA THR ILE GLU TRP GLU
SEQRES 1 B 527 SER ASN ALA MET LEU LYS ASP ILE HIS GLN HIS ARG ILE
SEQRES 2 B 527 LEU ILE LEU ASP PHE GLY SER GLN TYR ALA GLN LEU ILE
SEQRES 3 B 527 ALA ARG ARG VAL ARG GLU ILE GLY VAL TYR CYS GLU LEU
SEQRES 4 B 527 MET PRO CYS ASP ILE ASP GLU GLU THR ILE ARG ASP PHE
SEQRES 5 B 527 ASN PRO HIS GLY ILE ILE LEU SER GLY GLY PRO GLU THR
SEQRES 6 B 527 VAL THR LEU SER HIS THR LEU ARG ALA PRO ALA PHE ILE
SEQRES 7 B 527 PHE GLU ILE GLY CYS PRO VAL LEU GLY ILE CYS TYR GLY
SEQRES 8 B 527 MET GLN THR MET ALA TYR GLN LEU GLY GLY LYS VAL ASN
SEQRES 9 B 527 ARG THR ALA LYS ALA GLU PHE GLY HIS ALA GLN LEU ARG
SEQRES 10 B 527 VAL LEU ASN PRO ALA PHE LEU PHE ASP GLY ILE GLU ASP
SEQRES 11 B 527 GLN VAL SER PRO GLN GLY GLU PRO LEU LEU ASP VAL TRP
SEQRES 12 B 527 MET SER HIS GLY ASP ILE VAL SER GLU LEU PRO PRO GLY
SEQRES 13 B 527 PHE GLU ALA THR ALA CYS THR ASP ASN SER PRO LEU ALA
SEQRES 14 B 527 ALA MET ALA ASP PHE LYS ARG ARG PHE PHE GLY LEU GLN
SEQRES 15 B 527 PHE HIS PRO GLU VAL THR HIS THR PRO GLN GLY HIS ARG
SEQRES 16 B 527 ILE LEU ALA HIS PHE VAL ILE HIS ILE CYS GLN CYS ILE
SEQRES 17 B 527 PRO ASN TRP THR THR LYS HIS ILE ILE GLU ASP SER ILE
SEQRES 18 B 527 ARG ASP ILE GLN GLU LYS VAL GLY LYS GLU GLN VAL ILE
SEQRES 19 B 527 VAL GLY LEU SER GLY GLY VAL ASP SER ALA VAL THR ALA
SEQRES 20 B 527 THR LEU VAL HIS LYS ALA ILE GLY ASP GLN LEU VAL CYS
SEQRES 21 B 527 VAL LEU VAL ASP THR GLY LEU LEU ARG LEU ASN GLU VAL
SEQRES 22 B 527 ASP GLU VAL LEU ASN VAL PHE GLN LYS HIS LEU GLY ALA
SEQRES 23 B 527 LYS VAL ILE CYS VAL ASP ALA LYS ASP ARG PHE MET LYS
SEQRES 24 B 527 ALA LEU LYS GLY ILE SER ASP PRO GLU GLU LYS ARG LYS
SEQRES 25 B 527 ILE ALA GLY GLU GLN PHE ILE ARG VAL PHE GLU GLU GLN
SEQRES 26 B 527 ALA LYS LYS LEU ASN VAL LYS TRP LEU GLY GLN GLY THR
SEQRES 27 B 527 ILE TYR PRO ASP VAL ILE GLU SER ALA LYS THR LYS THR
SEQRES 28 B 527 GLY LYS GLY HIS ILE ILE LYS THR HIS HIS ASN VAL GLY
SEQRES 29 B 527 GLY LEU PRO LEU ASN MET GLU LEU LYS LEU ILE GLU PRO
SEQRES 30 B 527 LEU ARG GLU LEU PHE LYS ASP GLU VAL ARG LYS LEU GLY
SEQRES 31 B 527 LEU GLU LEU GLY LEU PRO ALA ASP LEU ILE TYR ARG HIS
SEQRES 32 B 527 PRO PHE PRO GLY PRO GLY LEU ALA ILE ARG ILE LEU GLY
SEQRES 33 B 527 GLU VAL SER ALA GLU TYR ILE ASN ILE LEU LYS GLN ALA
SEQRES 34 B 527 ASP ALA ILE PHE ILE GLU GLU LEU LYS LYS SER ASP TYR
SEQRES 35 B 527 TYR HIS GLN VAL SER GLN ALA PHE ALA VAL PHE MET PRO
SEQRES 36 B 527 LEU LYS SER VAL GLY VAL LYS GLY ASP ALA ARG HIS TYR
SEQRES 37 B 527 GLY TYR ILE ILE ALA LEU ARG ALA VAL LYS THR VAL ASP
SEQRES 38 B 527 PHE MET THR ALA GLN TRP ALA ASP LEU PRO HIS GLU PHE
SEQRES 39 B 527 LEU SER LYS VAL SER HIS ARG ILE VAL ASN GLU ILE LYS
SEQRES 40 B 527 GLU VAL SER ARG VAL VAL TYR ASP MET THR ASN LYS PRO
SEQRES 41 B 527 PRO ALA THR ILE GLU TRP GLU
SEQRES 1 C 527 SER ASN ALA MET LEU LYS ASP ILE HIS GLN HIS ARG ILE
SEQRES 2 C 527 LEU ILE LEU ASP PHE GLY SER GLN TYR ALA GLN LEU ILE
SEQRES 3 C 527 ALA ARG ARG VAL ARG GLU ILE GLY VAL TYR CYS GLU LEU
SEQRES 4 C 527 MET PRO CYS ASP ILE ASP GLU GLU THR ILE ARG ASP PHE
SEQRES 5 C 527 ASN PRO HIS GLY ILE ILE LEU SER GLY GLY PRO GLU THR
SEQRES 6 C 527 VAL THR LEU SER HIS THR LEU ARG ALA PRO ALA PHE ILE
SEQRES 7 C 527 PHE GLU ILE GLY CYS PRO VAL LEU GLY ILE CYS TYR GLY
SEQRES 8 C 527 MET GLN THR MET ALA TYR GLN LEU GLY GLY LYS VAL ASN
SEQRES 9 C 527 ARG THR ALA LYS ALA GLU PHE GLY HIS ALA GLN LEU ARG
SEQRES 10 C 527 VAL LEU ASN PRO ALA PHE LEU PHE ASP GLY ILE GLU ASP
SEQRES 11 C 527 GLN VAL SER PRO GLN GLY GLU PRO LEU LEU ASP VAL TRP
SEQRES 12 C 527 MET SER HIS GLY ASP ILE VAL SER GLU LEU PRO PRO GLY
SEQRES 13 C 527 PHE GLU ALA THR ALA CYS THR ASP ASN SER PRO LEU ALA
SEQRES 14 C 527 ALA MET ALA ASP PHE LYS ARG ARG PHE PHE GLY LEU GLN
SEQRES 15 C 527 PHE HIS PRO GLU VAL THR HIS THR PRO GLN GLY HIS ARG
SEQRES 16 C 527 ILE LEU ALA HIS PHE VAL ILE HIS ILE CYS GLN CYS ILE
SEQRES 17 C 527 PRO ASN TRP THR THR LYS HIS ILE ILE GLU ASP SER ILE
SEQRES 18 C 527 ARG ASP ILE GLN GLU LYS VAL GLY LYS GLU GLN VAL ILE
SEQRES 19 C 527 VAL GLY LEU SER GLY GLY VAL ASP SER ALA VAL THR ALA
SEQRES 20 C 527 THR LEU VAL HIS LYS ALA ILE GLY ASP GLN LEU VAL CYS
SEQRES 21 C 527 VAL LEU VAL ASP THR GLY LEU LEU ARG LEU ASN GLU VAL
SEQRES 22 C 527 ASP GLU VAL LEU ASN VAL PHE GLN LYS HIS LEU GLY ALA
SEQRES 23 C 527 LYS VAL ILE CYS VAL ASP ALA LYS ASP ARG PHE MET LYS
SEQRES 24 C 527 ALA LEU LYS GLY ILE SER ASP PRO GLU GLU LYS ARG LYS
SEQRES 25 C 527 ILE ALA GLY GLU GLN PHE ILE ARG VAL PHE GLU GLU GLN
SEQRES 26 C 527 ALA LYS LYS LEU ASN VAL LYS TRP LEU GLY GLN GLY THR
SEQRES 27 C 527 ILE TYR PRO ASP VAL ILE GLU SER ALA LYS THR LYS THR
SEQRES 28 C 527 GLY LYS GLY HIS ILE ILE LYS THR HIS HIS ASN VAL GLY
SEQRES 29 C 527 GLY LEU PRO LEU ASN MET GLU LEU LYS LEU ILE GLU PRO
SEQRES 30 C 527 LEU ARG GLU LEU PHE LYS ASP GLU VAL ARG LYS LEU GLY
SEQRES 31 C 527 LEU GLU LEU GLY LEU PRO ALA ASP LEU ILE TYR ARG HIS
SEQRES 32 C 527 PRO PHE PRO GLY PRO GLY LEU ALA ILE ARG ILE LEU GLY
SEQRES 33 C 527 GLU VAL SER ALA GLU TYR ILE ASN ILE LEU LYS GLN ALA
SEQRES 34 C 527 ASP ALA ILE PHE ILE GLU GLU LEU LYS LYS SER ASP TYR
SEQRES 35 C 527 TYR HIS GLN VAL SER GLN ALA PHE ALA VAL PHE MET PRO
SEQRES 36 C 527 LEU LYS SER VAL GLY VAL LYS GLY ASP ALA ARG HIS TYR
SEQRES 37 C 527 GLY TYR ILE ILE ALA LEU ARG ALA VAL LYS THR VAL ASP
SEQRES 38 C 527 PHE MET THR ALA GLN TRP ALA ASP LEU PRO HIS GLU PHE
SEQRES 39 C 527 LEU SER LYS VAL SER HIS ARG ILE VAL ASN GLU ILE LYS
SEQRES 40 C 527 GLU VAL SER ARG VAL VAL TYR ASP MET THR ASN LYS PRO
SEQRES 41 C 527 PRO ALA THR ILE GLU TRP GLU
SEQRES 1 D 527 SER ASN ALA MET LEU LYS ASP ILE HIS GLN HIS ARG ILE
SEQRES 2 D 527 LEU ILE LEU ASP PHE GLY SER GLN TYR ALA GLN LEU ILE
SEQRES 3 D 527 ALA ARG ARG VAL ARG GLU ILE GLY VAL TYR CYS GLU LEU
SEQRES 4 D 527 MET PRO CYS ASP ILE ASP GLU GLU THR ILE ARG ASP PHE
SEQRES 5 D 527 ASN PRO HIS GLY ILE ILE LEU SER GLY GLY PRO GLU THR
SEQRES 6 D 527 VAL THR LEU SER HIS THR LEU ARG ALA PRO ALA PHE ILE
SEQRES 7 D 527 PHE GLU ILE GLY CYS PRO VAL LEU GLY ILE CYS TYR GLY
SEQRES 8 D 527 MET GLN THR MET ALA TYR GLN LEU GLY GLY LYS VAL ASN
SEQRES 9 D 527 ARG THR ALA LYS ALA GLU PHE GLY HIS ALA GLN LEU ARG
SEQRES 10 D 527 VAL LEU ASN PRO ALA PHE LEU PHE ASP GLY ILE GLU ASP
SEQRES 11 D 527 GLN VAL SER PRO GLN GLY GLU PRO LEU LEU ASP VAL TRP
SEQRES 12 D 527 MET SER HIS GLY ASP ILE VAL SER GLU LEU PRO PRO GLY
SEQRES 13 D 527 PHE GLU ALA THR ALA CYS THR ASP ASN SER PRO LEU ALA
SEQRES 14 D 527 ALA MET ALA ASP PHE LYS ARG ARG PHE PHE GLY LEU GLN
SEQRES 15 D 527 PHE HIS PRO GLU VAL THR HIS THR PRO GLN GLY HIS ARG
SEQRES 16 D 527 ILE LEU ALA HIS PHE VAL ILE HIS ILE CYS GLN CYS ILE
SEQRES 17 D 527 PRO ASN TRP THR THR LYS HIS ILE ILE GLU ASP SER ILE
SEQRES 18 D 527 ARG ASP ILE GLN GLU LYS VAL GLY LYS GLU GLN VAL ILE
SEQRES 19 D 527 VAL GLY LEU SER GLY GLY VAL ASP SER ALA VAL THR ALA
SEQRES 20 D 527 THR LEU VAL HIS LYS ALA ILE GLY ASP GLN LEU VAL CYS
SEQRES 21 D 527 VAL LEU VAL ASP THR GLY LEU LEU ARG LEU ASN GLU VAL
SEQRES 22 D 527 ASP GLU VAL LEU ASN VAL PHE GLN LYS HIS LEU GLY ALA
SEQRES 23 D 527 LYS VAL ILE CYS VAL ASP ALA LYS ASP ARG PHE MET LYS
SEQRES 24 D 527 ALA LEU LYS GLY ILE SER ASP PRO GLU GLU LYS ARG LYS
SEQRES 25 D 527 ILE ALA GLY GLU GLN PHE ILE ARG VAL PHE GLU GLU GLN
SEQRES 26 D 527 ALA LYS LYS LEU ASN VAL LYS TRP LEU GLY GLN GLY THR
SEQRES 27 D 527 ILE TYR PRO ASP VAL ILE GLU SER ALA LYS THR LYS THR
SEQRES 28 D 527 GLY LYS GLY HIS ILE ILE LYS THR HIS HIS ASN VAL GLY
SEQRES 29 D 527 GLY LEU PRO LEU ASN MET GLU LEU LYS LEU ILE GLU PRO
SEQRES 30 D 527 LEU ARG GLU LEU PHE LYS ASP GLU VAL ARG LYS LEU GLY
SEQRES 31 D 527 LEU GLU LEU GLY LEU PRO ALA ASP LEU ILE TYR ARG HIS
SEQRES 32 D 527 PRO PHE PRO GLY PRO GLY LEU ALA ILE ARG ILE LEU GLY
SEQRES 33 D 527 GLU VAL SER ALA GLU TYR ILE ASN ILE LEU LYS GLN ALA
SEQRES 34 D 527 ASP ALA ILE PHE ILE GLU GLU LEU LYS LYS SER ASP TYR
SEQRES 35 D 527 TYR HIS GLN VAL SER GLN ALA PHE ALA VAL PHE MET PRO
SEQRES 36 D 527 LEU LYS SER VAL GLY VAL LYS GLY ASP ALA ARG HIS TYR
SEQRES 37 D 527 GLY TYR ILE ILE ALA LEU ARG ALA VAL LYS THR VAL ASP
SEQRES 38 D 527 PHE MET THR ALA GLN TRP ALA ASP LEU PRO HIS GLU PHE
SEQRES 39 D 527 LEU SER LYS VAL SER HIS ARG ILE VAL ASN GLU ILE LYS
SEQRES 40 D 527 GLU VAL SER ARG VAL VAL TYR ASP MET THR ASN LYS PRO
SEQRES 41 D 527 PRO ALA THR ILE GLU TRP GLU
HELIX 1 1 TYR A 19 GLY A 31 1 13
HELIX 2 2 CYS A 86 LEU A 96 1 11
HELIX 3 3 GLN A 189 HIS A 200 1 12
HELIX 4 4 THR A 210 GLY A 226 1 17
HELIX 5 5 GLY A 237 GLY A 252 1 16
HELIX 6 6 ASN A 268 GLN A 278 1 11
HELIX 7 7 ALA A 290 LYS A 296 1 7
HELIX 8 8 ASP A 303 GLN A 322 1 20
HELIX 9 9 ILE A 336 GLU A 342 1 7
HELIX 10 10 PHE A 379 GLY A 391 1 13
HELIX 11 11 PRO A 393 TYR A 398 1 6
HELIX 12 12 PRO A 405 ILE A 409 5 5
HELIX 13 13 ALA A 417 LYS A 436 1 20
HELIX 14 14 TYR A 439 VAL A 443 5 5
HELIX 15 15 PRO A 488 ILE A 503 1 16
HELIX 16 16 TYR B 19 ILE B 30 1 12
HELIX 17 17 CYS B 86 LEU B 96 1 11
HELIX 18 18 GLN B 189 HIS B 200 1 12
HELIX 19 19 THR B 209 GLY B 226 1 18
HELIX 20 20 GLY B 236 GLY B 252 1 17
HELIX 21 21 ASN B 268 GLN B 278 1 11
HELIX 22 22 ALA B 290 LEU B 298 1 9
HELIX 23 23 ASP B 303 GLN B 322 1 20
HELIX 24 24 ILE B 336 GLU B 342 1 7
HELIX 25 25 PHE B 379 LEU B 390 1 12
HELIX 26 26 PRO B 393 TYR B 398 1 6
HELIX 27 27 PRO B 405 ILE B 409 5 5
HELIX 28 28 ALA B 417 LYS B 436 1 20
HELIX 29 29 TYR B 439 VAL B 443 5 5
HELIX 30 30 PRO B 488 ILE B 503 1 16
HELIX 31 31 TYR C 19 GLY C 31 1 13
HELIX 32 32 CYS C 86 LEU C 96 1 11
HELIX 33 33 GLN C 189 HIS C 200 1 12
HELIX 34 34 THR C 209 GLY C 226 1 18
HELIX 35 35 GLY C 236 GLY C 252 1 17
HELIX 36 36 ASN C 268 GLN C 278 1 11
HELIX 37 37 ALA C 290 LYS C 296 1 7
HELIX 38 38 ASP C 303 GLN C 322 1 20
HELIX 39 39 ILE C 336 GLU C 342 1 7
HELIX 40 40 PHE C 379 GLY C 391 1 13
HELIX 41 41 PRO C 393 TYR C 398 1 6
HELIX 42 42 PRO C 405 ILE C 409 5 5
HELIX 43 43 ALA C 417 ILE C 431 1 15
HELIX 44 44 TYR C 439 VAL C 443 5 5
HELIX 45 45 PRO C 488 ILE C 503 1 16
HELIX 46 46 TYR D 19 GLY D 31 1 13
HELIX 47 47 CYS D 86 LEU D 96 1 11
HELIX 48 48 GLN D 189 HIS D 200 1 12
HELIX 49 49 THR D 209 GLY D 226 1 18
HELIX 50 50 GLY D 236 GLY D 252 1 17
HELIX 51 51 ASN D 268 GLN D 278 1 11
HELIX 52 52 ALA D 290 LYS D 296 1 7
HELIX 53 53 ASP D 303 GLN D 322 1 20
HELIX 54 54 ILE D 336 GLU D 342 1 7
HELIX 55 55 PHE D 379 LEU D 390 1 12
HELIX 56 56 PRO D 393 TYR D 398 1 6
HELIX 57 57 PRO D 405 ILE D 409 5 5
HELIX 58 58 ALA D 417 ILE D 431 1 15
HELIX 59 59 TYR D 439 VAL D 443 5 5
HELIX 60 60 PRO D 488 ILE D 503 1 16
SHEET 1 A 9 TYR A 33 PRO A 38 0
SHEET 2 A 9 ARG A 9 ASP A 14 1 N ILE A 12 O GLU A 35
SHEET 3 A 9 GLY A 53 LEU A 56 1 O GLY A 53 N LEU A 11
SHEET 4 A 9 VAL A 82 ILE A 85 1 O LEU A 83 N LEU A 56
SHEET 5 A 9 PHE A 175 LEU A 178 1 O PHE A 176 N GLY A 84
SHEET 6 A 9 SER A 163 ALA A 169 -1 N MET A 168 O GLY A 177
SHEET 7 A 9 GLU A 155 THR A 160 -1 N THR A 157 O ALA A 167
SHEET 8 A 9 PHE A 108 VAL A 115 -1 N ARG A 114 O CYS A 159
SHEET 9 A 9 LEU A 136 SER A 142 -1 O LEU A 137 N LEU A 113
SHEET 1 B 5 LYS A 284 VAL A 288 0
SHEET 2 B 5 LEU A 255 VAL A 260 1 N LEU A 259 O ILE A 286
SHEET 3 B 5 VAL A 230 GLY A 233 1 N VAL A 230 O VAL A 256
SHEET 4 B 5 TRP A 330 GLY A 332 1 O GLY A 332 N ILE A 231
SHEET 5 B 5 LEU A 371 ILE A 372 1 O ILE A 372 N LEU A 331
SHEET 1 C 6 GLN A 445 SER A 455 0
SHEET 2 C 6 GLY A 466 VAL A 474 -1 O ALA A 470 N VAL A 449
SHEET 3 C 6 VAL A 509 ASP A 512 1 O VAL A 510 N LEU A 471
SHEET 4 C 6 VAL B 509 ASP B 512 -1 O TYR B 511 N TYR A 511
SHEET 5 C 6 GLY B 466 VAL B 474 1 N LEU B 471 O ASP B 512
SHEET 6 C 6 GLN B 445 SER B 455 -1 N PHE B 447 O ARG B 472
SHEET 1 D 9 TYR B 33 PRO B 38 0
SHEET 2 D 9 ARG B 9 ASP B 14 1 N ASP B 14 O MET B 37
SHEET 3 D 9 GLY B 53 LEU B 56 1 O ILE B 55 N LEU B 11
SHEET 4 D 9 VAL B 82 ILE B 85 1 O LEU B 83 N LEU B 56
SHEET 5 D 9 PHE B 175 LEU B 178 1 O PHE B 176 N GLY B 84
SHEET 6 D 9 ALA B 167 ALA B 169 -1 N MET B 168 O GLY B 177
SHEET 7 D 9 GLU B 155 CYS B 159 -1 N THR B 157 O ALA B 167
SHEET 8 D 9 PHE B 108 VAL B 115 -1 N ARG B 114 O CYS B 159
SHEET 9 D 9 LEU B 136 SER B 142 -1 O LEU B 137 N LEU B 113
SHEET 1 E 2 LYS B 99 VAL B 100 0
SHEET 2 E 2 VAL B 147 GLU B 149 -1 O GLU B 149 N LYS B 99
SHEET 1 F 5 LYS B 284 VAL B 288 0
SHEET 2 F 5 LEU B 255 VAL B 260 1 N CYS B 257 O LYS B 284
SHEET 3 F 5 VAL B 230 GLY B 233 1 N VAL B 230 O VAL B 256
SHEET 4 F 5 TRP B 330 GLY B 332 1 O GLY B 332 N ILE B 231
SHEET 5 F 5 LEU B 371 ILE B 372 1 O ILE B 372 N LEU B 331
SHEET 1 G 9 TYR C 33 PRO C 38 0
SHEET 2 G 9 ARG C 9 ASP C 14 1 N ASP C 14 O MET C 37
SHEET 3 G 9 GLY C 53 LEU C 56 1 O GLY C 53 N LEU C 11
SHEET 4 G 9 VAL C 82 ILE C 85 1 O LEU C 83 N LEU C 56
SHEET 5 G 9 PHE C 175 LEU C 178 1 O PHE C 176 N VAL C 82
SHEET 6 G 9 ALA C 167 ALA C 169 -1 N MET C 168 O GLY C 177
SHEET 7 G 9 GLU C 155 CYS C 159 -1 N THR C 157 O ALA C 167
SHEET 8 G 9 PHE C 108 VAL C 115 -1 N ARG C 114 O CYS C 159
SHEET 9 G 9 LEU C 136 SER C 142 -1 O LEU C 137 N LEU C 113
SHEET 1 H 2 LYS C 99 VAL C 100 0
SHEET 2 H 2 VAL C 147 GLU C 149 -1 O GLU C 149 N LYS C 99
SHEET 1 I 5 LYS C 284 VAL C 288 0
SHEET 2 I 5 LEU C 255 VAL C 260 1 N LEU C 259 O ILE C 286
SHEET 3 I 5 VAL C 230 GLY C 233 1 N VAL C 230 O VAL C 256
SHEET 4 I 5 TRP C 330 GLY C 332 1 O GLY C 332 N ILE C 231
SHEET 5 I 5 LEU C 371 ILE C 372 1 O ILE C 372 N LEU C 331
SHEET 1 J 6 GLN C 445 SER C 455 0
SHEET 2 J 6 GLY C 466 VAL C 474 -1 O ALA C 470 N VAL C 449
SHEET 3 J 6 VAL C 509 ASP C 512 1 O VAL C 510 N ILE C 469
SHEET 4 J 6 VAL D 509 ASP D 512 -1 O TYR D 511 N TYR C 511
SHEET 5 J 6 GLY D 466 VAL D 474 1 N ILE D 469 O VAL D 510
SHEET 6 J 6 GLN D 445 SER D 455 -1 N PHE D 447 O ARG D 472
SHEET 1 K 9 TYR D 33 PRO D 38 0
SHEET 2 K 9 ARG D 9 ASP D 14 1 N ASP D 14 O MET D 37
SHEET 3 K 9 GLY D 53 LEU D 56 1 O ILE D 55 N LEU D 11
SHEET 4 K 9 VAL D 82 ILE D 85 1 O LEU D 83 N LEU D 56
SHEET 5 K 9 PHE D 175 LEU D 178 1 O PHE D 176 N GLY D 84
SHEET 6 K 9 ALA D 167 ALA D 169 -1 N MET D 168 O GLY D 177
SHEET 7 K 9 GLU D 155 CYS D 159 -1 N THR D 157 O ALA D 167
SHEET 8 K 9 PHE D 108 VAL D 115 -1 N ARG D 114 O CYS D 159
SHEET 9 K 9 LEU D 136 SER D 142 -1 O LEU D 137 N LEU D 113
SHEET 1 L 2 LYS D 99 VAL D 100 0
SHEET 2 L 2 VAL D 147 GLU D 149 -1 O GLU D 149 N LYS D 99
SHEET 1 M 5 LYS D 284 VAL D 288 0
SHEET 2 M 5 LEU D 255 VAL D 260 1 N LEU D 259 O ILE D 286
SHEET 3 M 5 VAL D 230 GLY D 233 1 N VAL D 230 O VAL D 256
SHEET 4 M 5 TRP D 330 GLY D 332 1 O GLY D 332 N ILE D 231
SHEET 5 M 5 LEU D 371 ILE D 372 1 O ILE D 372 N LEU D 331
CRYST1 74.913 143.953 107.885 90.00 97.66 90.00 P 1 21 1 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 0.013349 0.000000 0.001795 0.00000
SCALE2 0.000000 0.006947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009353 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
