HEADER SIGNALING PROTEIN 14-AUG-14 4R38
TITLE LOV DOMAIN FROM ERYTHROBACTER LITORALIS EL346 BLUE-LIGHT ACTIVATED
TITLE 2 HISTIDINE KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BLUE-LIGHT-ACTIVATED HISTIDINE KINASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: N-TERMINAL LOV DOMAIN, UNP RESIDUES 1-134;
COMPND 5 SYNONYM: EL346-LOV-HISTIDINE KINASE, EL346-LOV-HK;
COMPND 6 EC: 2.7.13.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ERYTHROBACTER LITORALIS HTCC2594;
SOURCE 3 ORGANISM_TAXID: 314225;
SOURCE 4 STRAIN: HTCC2594;
SOURCE 5 GENE: ELI_04860;
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
KEYWDS RIBOFLAVIN, LIGHT-ACTIVATED, LOV DOMAIN, PHOTORECEPTOR, SENSORY
KEYWDS 2 TRANSDUCTION, SIGNAL TRANSDUCTION, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.RIVERA-CANCEL,D.R.TOMCHICK,K.H.GARDNER
REVDAT 4 20-SEP-23 4R38 1 REMARK SEQADV
REVDAT 3 22-NOV-17 4R38 1 REMARK
REVDAT 2 31-DEC-14 4R38 1 JRNL
REVDAT 1 03-DEC-14 4R38 0
JRNL AUTH G.RIVERA-CANCEL,W.H.KO,D.R.TOMCHICK,F.CORREA,K.H.GARDNER
JRNL TITL FULL-LENGTH STRUCTURE OF A MONOMERIC HISTIDINE KINASE
JRNL TITL 2 REVEALS BASIS FOR SENSORY REGULATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 17839 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 25468971
JRNL DOI 10.1073/PNAS.1413983111
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 57709
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2941
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 37.1271 - 4.4120 0.99 2919 165 0.1920 0.1889
REMARK 3 2 4.4120 - 3.5028 0.99 2774 155 0.1720 0.1989
REMARK 3 3 3.5028 - 3.0602 1.00 2776 153 0.1893 0.2066
REMARK 3 4 3.0602 - 2.7805 1.00 2775 122 0.1970 0.2417
REMARK 3 5 2.7805 - 2.5813 1.00 2711 154 0.1870 0.2098
REMARK 3 6 2.5813 - 2.4291 1.00 2738 151 0.1815 0.2075
REMARK 3 7 2.4291 - 2.3075 1.00 2721 158 0.1837 0.2186
REMARK 3 8 2.3075 - 2.2071 0.99 2709 136 0.2035 0.2399
REMARK 3 9 2.2071 - 2.1221 1.00 2716 145 0.2103 0.2653
REMARK 3 10 2.1221 - 2.0489 1.00 2681 144 0.2235 0.2476
REMARK 3 11 2.0489 - 1.9848 1.00 2724 145 0.2069 0.2521
REMARK 3 12 1.9848 - 1.9281 1.00 2665 164 0.2218 0.2504
REMARK 3 13 1.9281 - 1.8773 0.99 2693 145 0.2687 0.3200
REMARK 3 14 1.8773 - 1.8315 0.99 2722 128 0.2496 0.2960
REMARK 3 15 1.8315 - 1.7899 0.99 2654 137 0.2633 0.3289
REMARK 3 16 1.7899 - 1.7518 0.97 2678 125 0.2733 0.3079
REMARK 3 17 1.7518 - 1.7168 0.95 2564 121 0.2774 0.3409
REMARK 3 18 1.7168 - 1.6844 0.89 2419 130 0.2745 0.3261
REMARK 3 19 1.6844 - 1.6543 0.86 2265 142 0.2842 0.3260
REMARK 3 20 1.6543 - 1.6262 0.78 2115 113 0.2957 0.3423
REMARK 3 21 1.6262 - 1.6000 0.66 1749 108 0.3144 0.3648
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 3650
REMARK 3 ANGLE : 1.289 4934
REMARK 3 CHIRALITY : 0.075 508
REMARK 3 PLANARITY : 0.006 656
REMARK 3 DIHEDRAL : 13.805 1342
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 15 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1235 1.0222 33.1594
REMARK 3 T TENSOR
REMARK 3 T11: 0.4826 T22: 0.3395
REMARK 3 T33: 0.4008 T12: 0.0416
REMARK 3 T13: -0.0294 T23: -0.0606
REMARK 3 L TENSOR
REMARK 3 L11: 0.1114 L22: 0.0655
REMARK 3 L33: 0.0677 L12: 0.0704
REMARK 3 L13: -0.0106 L23: -0.0542
REMARK 3 S TENSOR
REMARK 3 S11: 0.1317 S12: 0.0587 S13: -0.0953
REMARK 3 S21: 0.0444 S22: -0.3074 S23: 0.3334
REMARK 3 S31: 0.1772 S32: 0.0770 S33: -0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 32 THROUGH 50 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1441 5.0040 29.9969
REMARK 3 T TENSOR
REMARK 3 T11: 0.4036 T22: 0.4220
REMARK 3 T33: 0.3913 T12: 0.0187
REMARK 3 T13: 0.0015 T23: -0.1125
REMARK 3 L TENSOR
REMARK 3 L11: 0.1111 L22: 0.0221
REMARK 3 L33: 0.0517 L12: 0.0518
REMARK 3 L13: 0.0079 L23: 0.0074
REMARK 3 S TENSOR
REMARK 3 S11: -0.0172 S12: 0.0372 S13: 0.0955
REMARK 3 S21: 0.1922 S22: -0.2170 S23: 0.0798
REMARK 3 S31: 0.2104 S32: -0.2090 S33: 0.0002
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 51 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1652 2.4498 19.7542
REMARK 3 T TENSOR
REMARK 3 T11: 0.4723 T22: 0.4404
REMARK 3 T33: 0.3743 T12: 0.0533
REMARK 3 T13: -0.0043 T23: -0.0598
REMARK 3 L TENSOR
REMARK 3 L11: 0.0506 L22: 0.0250
REMARK 3 L33: 0.0544 L12: 0.0534
REMARK 3 L13: 0.0379 L23: 0.0141
REMARK 3 S TENSOR
REMARK 3 S11: -0.0396 S12: 0.3070 S13: -0.0773
REMARK 3 S21: -0.1772 S22: -0.1959 S23: -0.0538
REMARK 3 S31: 0.2869 S32: -0.2151 S33: -0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 65 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9269 2.3824 22.8337
REMARK 3 T TENSOR
REMARK 3 T11: 0.4533 T22: 0.4538
REMARK 3 T33: 0.3923 T12: 0.0757
REMARK 3 T13: 0.0032 T23: -0.0443
REMARK 3 L TENSOR
REMARK 3 L11: 0.0007 L22: 0.0097
REMARK 3 L33: 0.0152 L12: -0.0107
REMARK 3 L13: -0.0126 L23: -0.0014
REMARK 3 S TENSOR
REMARK 3 S11: -0.0249 S12: -0.0509 S13: 0.2139
REMARK 3 S21: -0.0002 S22: -0.0248 S23: -0.3074
REMARK 3 S31: 0.1346 S32: 0.2448 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0022 9.5179 24.1321
REMARK 3 T TENSOR
REMARK 3 T11: 0.4570 T22: 0.3871
REMARK 3 T33: 0.3639 T12: 0.0634
REMARK 3 T13: -0.0173 T23: -0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 0.1696 L22: 0.0044
REMARK 3 L33: 0.1459 L12: -0.1168
REMARK 3 L13: -0.1768 L23: 0.0886
REMARK 3 S TENSOR
REMARK 3 S11: 0.0749 S12: 0.0415 S13: 0.1743
REMARK 3 S21: -0.0995 S22: -0.0424 S23: -0.1688
REMARK 3 S31: -0.2155 S32: 0.1252 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 104 THROUGH 123 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3633 3.6487 34.7701
REMARK 3 T TENSOR
REMARK 3 T11: 0.4223 T22: 0.4041
REMARK 3 T33: 0.3611 T12: 0.0506
REMARK 3 T13: -0.0537 T23: -0.0357
REMARK 3 L TENSOR
REMARK 3 L11: 0.2896 L22: 0.1427
REMARK 3 L33: 0.1061 L12: 0.1711
REMARK 3 L13: -0.0657 L23: 0.0553
REMARK 3 S TENSOR
REMARK 3 S11: 0.1828 S12: -0.2342 S13: 0.1812
REMARK 3 S21: 0.0081 S22: -0.1656 S23: -0.0910
REMARK 3 S31: -0.0391 S32: 0.1044 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 16 THROUGH 49 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2907 -8.7540 45.9241
REMARK 3 T TENSOR
REMARK 3 T11: 0.7382 T22: 0.4119
REMARK 3 T33: 0.3080 T12: -0.0081
REMARK 3 T13: 0.0286 T23: -0.0656
REMARK 3 L TENSOR
REMARK 3 L11: 1.4831 L22: -0.0022
REMARK 3 L33: 0.0770 L12: -0.0699
REMARK 3 L13: 0.1650 L23: 0.0190
REMARK 3 S TENSOR
REMARK 3 S11: -0.3489 S12: 0.1975 S13: 0.3616
REMARK 3 S21: 0.1120 S22: -0.0599 S23: 0.0236
REMARK 3 S31: 1.0452 S32: 0.0586 S33: -0.0892
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 50 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0493 -15.1912 50.2049
REMARK 3 T TENSOR
REMARK 3 T11: 0.8901 T22: 0.6448
REMARK 3 T33: 0.3938 T12: -0.4365
REMARK 3 T13: 0.0765 T23: -0.1419
REMARK 3 L TENSOR
REMARK 3 L11: 0.8402 L22: 0.6243
REMARK 3 L33: 0.0270 L12: -0.3115
REMARK 3 L13: 0.1734 L23: -0.1240
REMARK 3 S TENSOR
REMARK 3 S11: -0.0721 S12: -0.2785 S13: 0.2813
REMARK 3 S21: -0.0889 S22: -0.0945 S23: -0.0192
REMARK 3 S31: 0.6886 S32: -0.3958 S33: -0.3832
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 78 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3906 -7.5700 52.2452
REMARK 3 T TENSOR
REMARK 3 T11: 0.7863 T22: 0.5550
REMARK 3 T33: 0.2342 T12: -0.1594
REMARK 3 T13: 0.1466 T23: -0.1470
REMARK 3 L TENSOR
REMARK 3 L11: 3.1060 L22: 0.2699
REMARK 3 L33: 1.1192 L12: -0.4679
REMARK 3 L13: 1.5177 L23: -0.4410
REMARK 3 S TENSOR
REMARK 3 S11: -0.2030 S12: -0.0441 S13: 0.5570
REMARK 3 S21: 0.4031 S22: -0.4905 S23: 0.0941
REMARK 3 S31: 0.9789 S32: -0.6555 S33: -0.7691
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 16 THROUGH 36 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7771 19.9895 47.3478
REMARK 3 T TENSOR
REMARK 3 T11: 0.3005 T22: 0.3259
REMARK 3 T33: 0.3435 T12: 0.0391
REMARK 3 T13: 0.0063 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 0.1044 L22: 0.0950
REMARK 3 L33: 0.0633 L12: 0.0541
REMARK 3 L13: 0.0102 L23: -0.0716
REMARK 3 S TENSOR
REMARK 3 S11: 0.0679 S12: 0.1685 S13: 0.0825
REMARK 3 S21: -0.0786 S22: -0.0677 S23: -0.0096
REMARK 3 S31: -0.2875 S32: -0.1537 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 37 THROUGH 50 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1908 19.5211 44.4976
REMARK 3 T TENSOR
REMARK 3 T11: 0.2734 T22: 0.4261
REMARK 3 T33: 0.3626 T12: 0.0557
REMARK 3 T13: 0.0029 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.0572 L22: 0.0348
REMARK 3 L33: 0.0219 L12: 0.0297
REMARK 3 L13: -0.0230 L23: 0.0134
REMARK 3 S TENSOR
REMARK 3 S11: -0.0676 S12: -0.0677 S13: -0.0928
REMARK 3 S21: 0.2831 S22: -0.1581 S23: 0.0717
REMARK 3 S31: 0.1576 S32: 0.5032 S33: -0.0001
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 51 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6924 31.3625 41.8069
REMARK 3 T TENSOR
REMARK 3 T11: 0.3506 T22: 0.3399
REMARK 3 T33: 0.3410 T12: 0.0169
REMARK 3 T13: -0.0507 T23: 0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 0.1874 L22: 0.0748
REMARK 3 L33: 0.0355 L12: -0.0107
REMARK 3 L13: 0.0523 L23: 0.0393
REMARK 3 S TENSOR
REMARK 3 S11: -0.0258 S12: 0.0498 S13: 0.0824
REMARK 3 S21: -0.0813 S22: -0.0057 S23: 0.1374
REMARK 3 S31: -0.1749 S32: 0.1092 S33: -0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 65 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3637 32.0298 38.2647
REMARK 3 T TENSOR
REMARK 3 T11: 0.3809 T22: 0.3932
REMARK 3 T33: 0.4358 T12: 0.0697
REMARK 3 T13: -0.1244 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.0115 L22: 0.0017
REMARK 3 L33: 0.0111 L12: 0.0066
REMARK 3 L13: -0.0072 L23: -0.0079
REMARK 3 S TENSOR
REMARK 3 S11: -0.3064 S12: -0.0135 S13: 0.2624
REMARK 3 S21: -0.1041 S22: 0.0472 S23: 0.0844
REMARK 3 S31: -0.3171 S32: -0.0432 S33: 0.0002
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 77 THROUGH 112 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.4311 23.3937 38.9571
REMARK 3 T TENSOR
REMARK 3 T11: 0.2989 T22: 0.4166
REMARK 3 T33: 0.3354 T12: -0.0215
REMARK 3 T13: -0.0300 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.1367 L22: 0.3461
REMARK 3 L33: 0.2767 L12: -0.2111
REMARK 3 L13: 0.1591 L23: -0.0889
REMARK 3 S TENSOR
REMARK 3 S11: -0.0590 S12: 0.0191 S13: -0.0412
REMARK 3 S21: -0.1390 S22: 0.0014 S23: 0.0390
REMARK 3 S31: -0.0537 S32: -0.0902 S33: 0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 113 THROUGH 123 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5536 20.4476 37.1165
REMARK 3 T TENSOR
REMARK 3 T11: 0.3124 T22: 0.4245
REMARK 3 T33: 0.3251 T12: 0.0139
REMARK 3 T13: 0.0354 T23: -0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 0.0177 L22: 0.1009
REMARK 3 L33: 0.0324 L12: 0.0588
REMARK 3 L13: 0.0136 L23: 0.0697
REMARK 3 S TENSOR
REMARK 3 S11: 0.1201 S12: 0.0474 S13: -0.0203
REMARK 3 S21: -0.3024 S22: 0.0129 S23: 0.0889
REMARK 3 S31: -0.0393 S32: -0.0282 S33: -0.0002
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 16 THROUGH 36 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0031 11.9630 58.5812
REMARK 3 T TENSOR
REMARK 3 T11: 0.2501 T22: 0.3133
REMARK 3 T33: 0.3283 T12: -0.0503
REMARK 3 T13: -0.0030 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.1822 L22: 0.0525
REMARK 3 L33: 0.1392 L12: -0.0935
REMARK 3 L13: -0.0967 L23: -0.0437
REMARK 3 S TENSOR
REMARK 3 S11: -0.0493 S12: -0.1444 S13: -0.0647
REMARK 3 S21: -0.0225 S22: -0.0913 S23: -0.0767
REMARK 3 S31: 0.0666 S32: -0.0365 S33: 0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 37 THROUGH 43 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2747 9.0104 60.5354
REMARK 3 T TENSOR
REMARK 3 T11: 0.2773 T22: 0.3681
REMARK 3 T33: 0.3319 T12: 0.0097
REMARK 3 T13: 0.0068 T23: -0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 0.0220 L22: 0.0066
REMARK 3 L33: 0.0239 L12: 0.0069
REMARK 3 L13: -0.0066 L23: 0.0122
REMARK 3 S TENSOR
REMARK 3 S11: 0.0245 S12: 0.2073 S13: -0.4011
REMARK 3 S21: -0.1468 S22: -0.2630 S23: 0.0315
REMARK 3 S31: -0.0482 S32: -0.1402 S33: 0.0002
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 44 THROUGH 50 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7908 16.6269 62.3729
REMARK 3 T TENSOR
REMARK 3 T11: 0.3237 T22: 0.3305
REMARK 3 T33: 0.3824 T12: 0.0359
REMARK 3 T13: 0.0268 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.0079 L22: 0.0008
REMARK 3 L33: 0.0030 L12: 0.0002
REMARK 3 L13: -0.0123 L23: -0.0012
REMARK 3 S TENSOR
REMARK 3 S11: 0.1237 S12: 0.1147 S13: 0.1820
REMARK 3 S21: 0.2736 S22: -0.0732 S23: -0.2464
REMARK 3 S31: 0.1789 S32: -0.0523 S33: 0.0002
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 51 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2889 10.9534 71.6529
REMARK 3 T TENSOR
REMARK 3 T11: 0.3024 T22: 0.3507
REMARK 3 T33: 0.3581 T12: 0.0216
REMARK 3 T13: -0.0044 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 0.0979 L22: 0.0488
REMARK 3 L33: 0.0164 L12: 0.0112
REMARK 3 L13: -0.0161 L23: -0.0151
REMARK 3 S TENSOR
REMARK 3 S11: 0.0510 S12: -0.0815 S13: 0.0380
REMARK 3 S21: 0.0984 S22: 0.0824 S23: 0.1264
REMARK 3 S31: 0.0629 S32: -0.1860 S33: -0.0000
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 65 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5962 4.4819 70.9458
REMARK 3 T TENSOR
REMARK 3 T11: 0.3667 T22: 0.4090
REMARK 3 T33: 0.3823 T12: 0.0532
REMARK 3 T13: 0.0080 T23: 0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 0.0100 L22: 0.0161
REMARK 3 L33: 0.0265 L12: -0.0075
REMARK 3 L13: 0.0052 L23: -0.0146
REMARK 3 S TENSOR
REMARK 3 S11: -0.0750 S12: -0.2691 S13: -0.3239
REMARK 3 S21: 0.3091 S22: -0.0981 S23: -0.2762
REMARK 3 S31: 0.1415 S32: 0.2447 S33: 0.0001
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 77 THROUGH 93 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7654 3.6824 68.6701
REMARK 3 T TENSOR
REMARK 3 T11: 0.3276 T22: 0.2757
REMARK 3 T33: 0.3695 T12: 0.0228
REMARK 3 T13: 0.0261 T23: 0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 0.0260 L22: 0.1263
REMARK 3 L33: 0.2431 L12: -0.0759
REMARK 3 L13: 0.0223 L23: -0.1697
REMARK 3 S TENSOR
REMARK 3 S11: 0.0303 S12: -0.0386 S13: -0.0698
REMARK 3 S21: 0.0715 S22: -0.0309 S23: -0.0550
REMARK 3 S31: 0.1816 S32: 0.0328 S33: -0.0000
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 94 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4217 1.2746 65.9320
REMARK 3 T TENSOR
REMARK 3 T11: 0.3986 T22: 0.3189
REMARK 3 T33: 0.3847 T12: -0.0168
REMARK 3 T13: 0.0281 T23: 0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 0.0172 L22: 0.0284
REMARK 3 L33: 0.0202 L12: -0.0532
REMARK 3 L13: -0.0089 L23: -0.0192
REMARK 3 S TENSOR
REMARK 3 S11: 0.1080 S12: -0.0148 S13: 0.1084
REMARK 3 S21: 0.1294 S22: -0.0144 S23: -0.0938
REMARK 3 S31: 0.0891 S32: -0.0764 S33: -0.0001
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 104 THROUGH 112 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7048 8.9996 52.6271
REMARK 3 T TENSOR
REMARK 3 T11: 0.3388 T22: 0.3549
REMARK 3 T33: 0.4528 T12: 0.0840
REMARK 3 T13: 0.0492 T23: 0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 0.0112 L22: -0.0003
REMARK 3 L33: 0.0142 L12: -0.0032
REMARK 3 L13: 0.0175 L23: -0.0151
REMARK 3 S TENSOR
REMARK 3 S11: -0.2496 S12: 0.0909 S13: -0.1812
REMARK 3 S21: 0.0326 S22: 0.0072 S23: -0.2027
REMARK 3 S31: 0.1554 S32: 0.3103 S33: -0.0002
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 113 THROUGH 123 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5112 3.0824 62.4668
REMARK 3 T TENSOR
REMARK 3 T11: 0.2778 T22: 0.3737
REMARK 3 T33: 0.4140 T12: -0.0155
REMARK 3 T13: -0.0277 T23: 0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 0.0295 L22: 0.0363
REMARK 3 L33: 0.0296 L12: 0.0046
REMARK 3 L13: -0.0322 L23: 0.0244
REMARK 3 S TENSOR
REMARK 3 S11: 0.0965 S12: -0.0486 S13: -0.1533
REMARK 3 S21: -0.1024 S22: -0.1848 S23: -0.0749
REMARK 3 S31: 0.2837 S32: -0.1412 S33: -0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4R38 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000086842.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97901
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58404
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.62400
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2PR5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 0.1 M HEPES, 0.1 M
REMARK 280 MAGNESIUM CHLORIDE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 20.54050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.20200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.69150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.20200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.54050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.69150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 INDIVIDUAL LOV DOMAIN BEHAVES AS A DIMER IN SOLUTION,
REMARK 300 HOWEVER, THE FULL-LENGTH PROTEIN IS A MONOMER.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 GLY A -5
REMARK 465 GLU A -4
REMARK 465 PHE A -3
REMARK 465 LYS A -2
REMARK 465 GLY A -1
REMARK 465 LEU A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 VAL A 3
REMARK 465 GLY A 4
REMARK 465 LEU A 5
REMARK 465 ALA A 6
REMARK 465 GLU A 7
REMARK 465 HIS A 8
REMARK 465 ASP A 9
REMARK 465 LYS A 10
REMARK 465 GLU A 11
REMARK 465 ALA A 12
REMARK 465 TRP A 13
REMARK 465 GLY A 14
REMARK 465 SER A 124
REMARK 465 GLU A 125
REMARK 465 SER A 126
REMARK 465 PRO A 127
REMARK 465 ASP A 128
REMARK 465 ARG A 129
REMARK 465 ALA A 130
REMARK 465 THR A 131
REMARK 465 GLU A 132
REMARK 465 LEU A 133
REMARK 465 ASP A 134
REMARK 465 GLY B -5
REMARK 465 GLU B -4
REMARK 465 PHE B -3
REMARK 465 LYS B -2
REMARK 465 GLY B -1
REMARK 465 LEU B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 VAL B 3
REMARK 465 GLY B 4
REMARK 465 LEU B 5
REMARK 465 ALA B 6
REMARK 465 GLU B 7
REMARK 465 HIS B 8
REMARK 465 ASP B 9
REMARK 465 LYS B 10
REMARK 465 GLU B 11
REMARK 465 ALA B 12
REMARK 465 TRP B 13
REMARK 465 GLY B 14
REMARK 465 ARG B 15
REMARK 465 GLN B 123
REMARK 465 SER B 124
REMARK 465 GLU B 125
REMARK 465 SER B 126
REMARK 465 PRO B 127
REMARK 465 ASP B 128
REMARK 465 ARG B 129
REMARK 465 ALA B 130
REMARK 465 THR B 131
REMARK 465 GLU B 132
REMARK 465 LEU B 133
REMARK 465 ASP B 134
REMARK 465 GLY C -5
REMARK 465 GLU C -4
REMARK 465 PHE C -3
REMARK 465 LYS C -2
REMARK 465 GLY C -1
REMARK 465 LEU C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 VAL C 3
REMARK 465 GLY C 4
REMARK 465 LEU C 5
REMARK 465 ALA C 6
REMARK 465 GLU C 7
REMARK 465 HIS C 8
REMARK 465 ASP C 9
REMARK 465 LYS C 10
REMARK 465 GLU C 11
REMARK 465 ALA C 12
REMARK 465 TRP C 13
REMARK 465 GLY C 14
REMARK 465 ARG C 15
REMARK 465 SER C 124
REMARK 465 GLU C 125
REMARK 465 SER C 126
REMARK 465 PRO C 127
REMARK 465 ASP C 128
REMARK 465 ARG C 129
REMARK 465 ALA C 130
REMARK 465 THR C 131
REMARK 465 GLU C 132
REMARK 465 LEU C 133
REMARK 465 ASP C 134
REMARK 465 GLY D -5
REMARK 465 GLU D -4
REMARK 465 PHE D -3
REMARK 465 LYS D -2
REMARK 465 GLY D -1
REMARK 465 LEU D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 VAL D 3
REMARK 465 GLY D 4
REMARK 465 LEU D 5
REMARK 465 ALA D 6
REMARK 465 GLU D 7
REMARK 465 HIS D 8
REMARK 465 ASP D 9
REMARK 465 LYS D 10
REMARK 465 GLU D 11
REMARK 465 ALA D 12
REMARK 465 TRP D 13
REMARK 465 GLY D 14
REMARK 465 ARG D 15
REMARK 465 SER D 124
REMARK 465 GLU D 125
REMARK 465 SER D 126
REMARK 465 PRO D 127
REMARK 465 ASP D 128
REMARK 465 ARG D 129
REMARK 465 ALA D 130
REMARK 465 THR D 131
REMARK 465 GLU D 132
REMARK 465 LEU D 133
REMARK 465 ASP D 134
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 PRO A 17 36.29 -79.48
REMARK 500 CYS A 55 -6.88 -59.32
REMARK 500 PRO C 17 44.82 -86.08
REMARK 500 PRO D 17 36.25 -89.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RBF A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RBF B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RBF C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RBF D 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4R39 RELATED DB: PDB
REMARK 900 RELATED ID: 4R3A RELATED DB: PDB
DBREF 4R38 A 1 134 UNP Q2NB77 LVHK2_ERYLH 1 134
DBREF 4R38 B 1 134 UNP Q2NB77 LVHK2_ERYLH 1 134
DBREF 4R38 C 1 134 UNP Q2NB77 LVHK2_ERYLH 1 134
DBREF 4R38 D 1 134 UNP Q2NB77 LVHK2_ERYLH 1 134
SEQADV 4R38 GLY A -5 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 GLU A -4 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 PHE A -3 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 LYS A -2 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 GLY A -1 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 LEU A 0 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 GLY B -5 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 GLU B -4 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 PHE B -3 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 LYS B -2 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 GLY B -1 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 LEU B 0 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 GLY C -5 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 GLU C -4 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 PHE C -3 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 LYS C -2 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 GLY C -1 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 LEU C 0 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 GLY D -5 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 GLU D -4 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 PHE D -3 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 LYS D -2 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 GLY D -1 UNP Q2NB77 EXPRESSION TAG
SEQADV 4R38 LEU D 0 UNP Q2NB77 EXPRESSION TAG
SEQRES 1 A 140 GLY GLU PHE LYS GLY LEU MET ALA VAL GLY LEU ALA GLU
SEQRES 2 A 140 HIS ASP LYS GLU ALA TRP GLY ARG LEU PRO PHE SER LEU
SEQRES 3 A 140 THR ILE ALA ASP ILE SER GLN ASP ASP GLU PRO LEU ILE
SEQRES 4 A 140 TYR VAL ASN ARG ALA PHE GLU GLN MET THR GLY TYR SER
SEQRES 5 A 140 ARG SER SER VAL VAL GLY ARG ASN CYS ARG PHE LEU GLN
SEQRES 6 A 140 GLY GLU LYS THR ASP PRO GLY ALA VAL GLU ARG LEU ALA
SEQRES 7 A 140 LYS ALA ILE ARG ASN CYS GLU GLU VAL GLU GLU THR ILE
SEQRES 8 A 140 TYR ASN TYR ARG ALA ASP GLY GLU GLY PHE TRP ASN HIS
SEQRES 9 A 140 LEU LEU MET GLY PRO LEU GLU ASP GLN ASP GLU LYS CYS
SEQRES 10 A 140 ARG TYR PHE VAL GLY ILE GLN VAL ASP MET GLY GLN SER
SEQRES 11 A 140 GLU SER PRO ASP ARG ALA THR GLU LEU ASP
SEQRES 1 B 140 GLY GLU PHE LYS GLY LEU MET ALA VAL GLY LEU ALA GLU
SEQRES 2 B 140 HIS ASP LYS GLU ALA TRP GLY ARG LEU PRO PHE SER LEU
SEQRES 3 B 140 THR ILE ALA ASP ILE SER GLN ASP ASP GLU PRO LEU ILE
SEQRES 4 B 140 TYR VAL ASN ARG ALA PHE GLU GLN MET THR GLY TYR SER
SEQRES 5 B 140 ARG SER SER VAL VAL GLY ARG ASN CYS ARG PHE LEU GLN
SEQRES 6 B 140 GLY GLU LYS THR ASP PRO GLY ALA VAL GLU ARG LEU ALA
SEQRES 7 B 140 LYS ALA ILE ARG ASN CYS GLU GLU VAL GLU GLU THR ILE
SEQRES 8 B 140 TYR ASN TYR ARG ALA ASP GLY GLU GLY PHE TRP ASN HIS
SEQRES 9 B 140 LEU LEU MET GLY PRO LEU GLU ASP GLN ASP GLU LYS CYS
SEQRES 10 B 140 ARG TYR PHE VAL GLY ILE GLN VAL ASP MET GLY GLN SER
SEQRES 11 B 140 GLU SER PRO ASP ARG ALA THR GLU LEU ASP
SEQRES 1 C 140 GLY GLU PHE LYS GLY LEU MET ALA VAL GLY LEU ALA GLU
SEQRES 2 C 140 HIS ASP LYS GLU ALA TRP GLY ARG LEU PRO PHE SER LEU
SEQRES 3 C 140 THR ILE ALA ASP ILE SER GLN ASP ASP GLU PRO LEU ILE
SEQRES 4 C 140 TYR VAL ASN ARG ALA PHE GLU GLN MET THR GLY TYR SER
SEQRES 5 C 140 ARG SER SER VAL VAL GLY ARG ASN CYS ARG PHE LEU GLN
SEQRES 6 C 140 GLY GLU LYS THR ASP PRO GLY ALA VAL GLU ARG LEU ALA
SEQRES 7 C 140 LYS ALA ILE ARG ASN CYS GLU GLU VAL GLU GLU THR ILE
SEQRES 8 C 140 TYR ASN TYR ARG ALA ASP GLY GLU GLY PHE TRP ASN HIS
SEQRES 9 C 140 LEU LEU MET GLY PRO LEU GLU ASP GLN ASP GLU LYS CYS
SEQRES 10 C 140 ARG TYR PHE VAL GLY ILE GLN VAL ASP MET GLY GLN SER
SEQRES 11 C 140 GLU SER PRO ASP ARG ALA THR GLU LEU ASP
SEQRES 1 D 140 GLY GLU PHE LYS GLY LEU MET ALA VAL GLY LEU ALA GLU
SEQRES 2 D 140 HIS ASP LYS GLU ALA TRP GLY ARG LEU PRO PHE SER LEU
SEQRES 3 D 140 THR ILE ALA ASP ILE SER GLN ASP ASP GLU PRO LEU ILE
SEQRES 4 D 140 TYR VAL ASN ARG ALA PHE GLU GLN MET THR GLY TYR SER
SEQRES 5 D 140 ARG SER SER VAL VAL GLY ARG ASN CYS ARG PHE LEU GLN
SEQRES 6 D 140 GLY GLU LYS THR ASP PRO GLY ALA VAL GLU ARG LEU ALA
SEQRES 7 D 140 LYS ALA ILE ARG ASN CYS GLU GLU VAL GLU GLU THR ILE
SEQRES 8 D 140 TYR ASN TYR ARG ALA ASP GLY GLU GLY PHE TRP ASN HIS
SEQRES 9 D 140 LEU LEU MET GLY PRO LEU GLU ASP GLN ASP GLU LYS CYS
SEQRES 10 D 140 ARG TYR PHE VAL GLY ILE GLN VAL ASP MET GLY GLN SER
SEQRES 11 D 140 GLU SER PRO ASP ARG ALA THR GLU LEU ASP
HET RBF A 201 47
HET RBF B 201 47
HET RBF C 201 47
HET RBF D 201 47
HETNAM RBF RIBOFLAVIN
HETSYN RBF RIBOFLAVINE; VITAMIN B2
FORMUL 5 RBF 4(C17 H20 N4 O6)
FORMUL 9 HOH *145(H2 O)
HELIX 1 1 ASN A 36 GLY A 44 1 9
HELIX 2 2 SER A 46 VAL A 51 1 6
HELIX 3 3 ASN A 54 GLN A 59 5 6
HELIX 4 4 ASP A 64 ASN A 77 1 14
HELIX 5 5 ASN B 36 GLY B 44 1 9
HELIX 6 6 SER B 46 VAL B 51 1 6
HELIX 7 7 ASN B 54 GLN B 59 5 6
HELIX 8 8 ASP B 64 CYS B 78 1 15
HELIX 9 9 ASN C 36 GLY C 44 1 9
HELIX 10 10 SER C 46 VAL C 51 1 6
HELIX 11 11 ASN C 54 GLN C 59 5 6
HELIX 12 12 ASP C 64 ASN C 77 1 14
HELIX 13 13 ASN D 36 GLY D 44 1 9
HELIX 14 14 SER D 46 VAL D 51 1 6
HELIX 15 15 ASN D 54 GLN D 59 5 6
HELIX 16 16 ASP D 64 ASN D 77 1 14
SHEET 1 A 5 LEU A 32 VAL A 35 0
SHEET 2 A 5 SER A 19 ASP A 24 -1 N ILE A 22 O ILE A 33
SHEET 3 A 5 TYR A 113 ASP A 120 -1 O PHE A 114 N ALA A 23
SHEET 4 A 5 GLY A 94 PRO A 103 -1 N GLY A 102 O VAL A 115
SHEET 5 A 5 VAL A 81 TYR A 88 -1 N ASN A 87 O PHE A 95
SHEET 1 B 5 LEU B 32 VAL B 35 0
SHEET 2 B 5 SER B 19 ASP B 24 -1 N ILE B 22 O ILE B 33
SHEET 3 B 5 TYR B 113 ASP B 120 -1 O GLY B 116 N THR B 21
SHEET 4 B 5 GLY B 94 PRO B 103 -1 N HIS B 98 O VAL B 119
SHEET 5 B 5 VAL B 81 TYR B 88 -1 N ASN B 87 O PHE B 95
SHEET 1 C 5 LEU C 32 VAL C 35 0
SHEET 2 C 5 SER C 19 ASP C 24 -1 N ILE C 22 O ILE C 33
SHEET 3 C 5 TYR C 113 ASP C 120 -1 O GLY C 116 N THR C 21
SHEET 4 C 5 GLY C 94 PRO C 103 -1 N HIS C 98 O VAL C 119
SHEET 5 C 5 VAL C 81 TYR C 88 -1 N ASN C 87 O PHE C 95
SHEET 1 D 5 LEU D 32 VAL D 35 0
SHEET 2 D 5 SER D 19 ASP D 24 -1 N ILE D 22 O ILE D 33
SHEET 3 D 5 TYR D 113 ASP D 120 -1 O GLY D 116 N THR D 21
SHEET 4 D 5 GLY D 94 PRO D 103 -1 N HIS D 98 O VAL D 119
SHEET 5 D 5 VAL D 81 TYR D 88 -1 N ASN D 87 O PHE D 95
SSBOND 1 CYS A 78 CYS A 111 1555 1555 2.05
SSBOND 2 CYS B 78 CYS B 111 1555 1555 2.03
SSBOND 3 CYS C 78 CYS C 111 1555 1555 2.04
SSBOND 4 CYS D 78 CYS D 111 1555 1555 2.06
SITE 1 AC1 18 THR A 21 ASN A 54 CYS A 55 ARG A 56
SITE 2 AC1 18 LEU A 58 GLN A 59 VAL A 68 ILE A 75
SITE 3 AC1 18 ASN A 87 ASN A 97 LEU A 99 MET A 101
SITE 4 AC1 18 PHE A 114 GLN A 118 HOH A 307 HOH A 327
SITE 5 AC1 18 HOH A 328 HOH A 332
SITE 1 AC2 12 THR B 21 ASN B 54 CYS B 55 ARG B 56
SITE 2 AC2 12 GLN B 59 ILE B 75 ASN B 87 ASN B 97
SITE 3 AC2 12 LEU B 99 MET B 101 PHE B 114 GLN B 118
SITE 1 AC3 16 THR C 21 ASN C 54 CYS C 55 ARG C 56
SITE 2 AC3 16 GLN C 59 VAL C 68 ILE C 75 ASN C 87
SITE 3 AC3 16 ASN C 97 LEU C 99 MET C 101 GLN C 118
SITE 4 AC3 16 HOH C 306 HOH C 315 HOH C 330 HOH C 331
SITE 1 AC4 15 THR D 21 ASN D 54 CYS D 55 ARG D 56
SITE 2 AC4 15 GLN D 59 VAL D 68 ILE D 75 ILE D 85
SITE 3 AC4 15 ASN D 87 ASN D 97 LEU D 99 MET D 101
SITE 4 AC4 15 GLN D 118 HOH D 302 HOH D 350
CRYST1 41.081 89.383 122.404 90.00 90.00 90.00 P 21 21 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 0.024342 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011188 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008170 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
