HEADER SIGNALING PROTEIN 19-JAN-11 3QE0
TITLE A GALPHA-I1 P-LOOP MUTATION PREVENTS TRANSITION TO THE ACTIVATED STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: ALPHA-I1 SUBUNIT, RESIDUES 33-354;
COMPND 5 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN;
COMPND 6 EC: 3.6.5.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: KB752 PEPTIDE;
COMPND 11 CHAIN: G, F;
COMPND 12 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: GNAI1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PLIC-HIS;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: SYNTHETIC PHAGE DISPLAY PEPTIDE
KEYWDS KB752, RAS-LIKE DOMAIN, ALL-HELICAL DOMAIN, ARGININE FINGER,
KEYWDS 2 SIGNALING PROTEIN, LIPOPROTEIN, TRANSDUCER, GTPASE ACTIVITY, GTP
KEYWDS 3 BINDING, NUCLEOTIDE BINDING, ADP-RIBOSYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.BOSCH,F.S.WILLARD,A.J.KIMPLE,M.J.MILEY,D.P.SIDEROVSKI
REVDAT 3 13-SEP-23 3QE0 1 REMARK SEQADV LINK
REVDAT 2 14-MAR-12 3QE0 1 JRNL
REVDAT 1 25-JAN-12 3QE0 0
JRNL AUTH D.E.BOSCH,F.S.WILLARD,R.RAMANUJAM,A.J.KIMPLE,M.D.WILLARD,
JRNL AUTH 2 N.I.NAQVI,D.P.SIDEROVSKI
JRNL TITL A P-LOOP MUTATION IN GALPHA SUBUNITS PREVENTS TRANSITION TO
JRNL TITL 2 THE ACTIVE STATE: IMPLICATIONS FOR G-PROTEIN SIGNALING IN
JRNL TITL 3 FUNGAL PATHOGENESIS
JRNL REF PLOS PATHOG. V. 8 02553 2012
JRNL REFN ISSN 1553-7366
JRNL PMID 22383884
JRNL DOI 10.1371/JOURNAL.PPAT.1002553
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.A.JOHNSTON,F.S.WILLARD,M.R.JEZYK,Z.FREDERICKS,E.T.BODOR,
REMARK 1 AUTH 2 M.B.JONES,R.BLAESIUS,V.J.WATTS,T.K.HARDEN,J.SONDEK,
REMARK 1 AUTH 3 J.K.RAMER,D.P.SIDEROVSKI
REMARK 1 TITL STRUCTURE OF GALPHA(I1) BOUND TO A GDP-SELECTIVE PEPTIDE
REMARK 1 TITL 2 PROVIDES INSIGHT INTO GUANINE NUCLEOTIDE EXCHANGE.
REMARK 1 REF STRUCTURE V. 13 1069 2005
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 16004878
REMARK 1 DOI 10.1016/J.STR.2005.04.007
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.44
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 30770
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.249
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1555
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 39.4440 - 6.4617 0.95 3174 158 0.2418 0.2841
REMARK 3 2 6.4617 - 5.1324 0.97 2980 157 0.2414 0.2879
REMARK 3 3 5.1324 - 4.4846 0.97 2929 170 0.1914 0.2198
REMARK 3 4 4.4846 - 4.0751 0.97 2917 158 0.1968 0.2400
REMARK 3 5 4.0751 - 3.7832 0.97 2920 138 0.2335 0.2893
REMARK 3 6 3.7832 - 3.5603 0.97 2861 168 0.2558 0.3039
REMARK 3 7 3.5603 - 3.3821 0.98 2924 156 0.2805 0.3402
REMARK 3 8 3.3821 - 3.2350 0.97 2862 134 0.3032 0.3619
REMARK 3 9 3.2350 - 3.1105 0.97 2906 138 0.3234 0.3780
REMARK 3 10 3.1105 - 3.0032 0.95 2742 178 0.3509 0.4059
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 : 0.36
REMARK 3 B_SOL : 81.43
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 68.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.79570
REMARK 3 B22 (A**2) : -1.79570
REMARK 3 B33 (A**2) : 3.59140
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 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 : 0.002 7857
REMARK 3 ANGLE : 0.546 10597
REMARK 3 CHIRALITY : 0.036 1180
REMARK 3 PLANARITY : 0.001 1327
REMARK 3 DIHEDRAL : 12.164 2853
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 21
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 32:59)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.3629 -21.2829 -8.9091
REMARK 3 T TENSOR
REMARK 3 T11: 0.2479 T22: 0.0985
REMARK 3 T33: 0.3012 T12: 0.0446
REMARK 3 T13: -0.0063 T23: -0.0378
REMARK 3 L TENSOR
REMARK 3 L11: 0.6960 L22: 0.6403
REMARK 3 L33: 1.1350 L12: 0.7061
REMARK 3 L13: 0.3873 L23: 0.3497
REMARK 3 S TENSOR
REMARK 3 S11: 0.3084 S12: 0.0444 S13: 0.0443
REMARK 3 S21: 0.2593 S22: 0.0110 S23: 0.3365
REMARK 3 S31: 0.2239 S32: 0.0798 S33: -0.2869
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 60:77)
REMARK 3 ORIGIN FOR THE GROUP (A): 64.1299 -16.8228 -15.7830
REMARK 3 T TENSOR
REMARK 3 T11: 0.5418 T22: 0.2506
REMARK 3 T33: 0.1184 T12: 0.1284
REMARK 3 T13: 0.1621 T23: 0.1357
REMARK 3 L TENSOR
REMARK 3 L11: 0.8921 L22: 0.6594
REMARK 3 L33: 0.3866 L12: 0.1623
REMARK 3 L13: -0.4928 L23: -0.4022
REMARK 3 S TENSOR
REMARK 3 S11: -0.1401 S12: 0.6438 S13: -0.0482
REMARK 3 S21: -0.4486 S22: 0.2249 S23: -0.1155
REMARK 3 S31: 0.0953 S32: -0.2542 S33: 0.0393
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 78:159)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.3165 1.7496 -26.4101
REMARK 3 T TENSOR
REMARK 3 T11: 0.4845 T22: 0.3136
REMARK 3 T33: 0.1748 T12: -0.0614
REMARK 3 T13: 0.1493 T23: 0.1424
REMARK 3 L TENSOR
REMARK 3 L11: 0.8899 L22: 0.2019
REMARK 3 L33: 2.1772 L12: 0.2365
REMARK 3 L13: -0.5569 L23: -0.5381
REMARK 3 S TENSOR
REMARK 3 S11: -0.0909 S12: 0.0279 S13: -0.0281
REMARK 3 S21: -0.1449 S22: -0.0100 S23: -0.0633
REMARK 3 S31: -0.7115 S32: 0.0353 S33: -0.2170
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 160:212)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.9574 -21.1397 -13.1415
REMARK 3 T TENSOR
REMARK 3 T11: 0.2762 T22: 0.1165
REMARK 3 T33: 0.2119 T12: 0.0578
REMARK 3 T13: -0.0524 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.6339 L22: 1.2620
REMARK 3 L33: 2.5499 L12: -0.5077
REMARK 3 L13: -0.0857 L23: -0.4199
REMARK 3 S TENSOR
REMARK 3 S11: 0.1732 S12: 0.0657 S13: -0.2953
REMARK 3 S21: -0.2253 S22: -0.4606 S23: 0.2235
REMARK 3 S31: 0.6738 S32: 0.5263 S33: 0.1356
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 213:307)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4048 -8.3568 -12.0090
REMARK 3 T TENSOR
REMARK 3 T11: 0.0569 T22: 0.0881
REMARK 3 T33: 0.1642 T12: -0.0349
REMARK 3 T13: -0.1065 T23: -0.0413
REMARK 3 L TENSOR
REMARK 3 L11: 1.0969 L22: 0.5556
REMARK 3 L33: 1.2460 L12: -0.7387
REMARK 3 L13: 0.7415 L23: -0.3340
REMARK 3 S TENSOR
REMARK 3 S11: 0.0495 S12: -0.0071 S13: -0.0152
REMARK 3 S21: 0.0205 S22: -0.0469 S23: 0.2893
REMARK 3 S31: -0.2955 S32: -0.3706 S33: 0.0746
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 308:348)
REMARK 3 ORIGIN FOR THE GROUP (A): 37.0595 -16.7169 -0.5255
REMARK 3 T TENSOR
REMARK 3 T11: 0.1196 T22: 0.1362
REMARK 3 T33: 0.2373 T12: 0.0107
REMARK 3 T13: -0.0623 T23: -0.0678
REMARK 3 L TENSOR
REMARK 3 L11: 0.0981 L22: 1.3298
REMARK 3 L33: 1.2132 L12: 0.1314
REMARK 3 L13: 0.3121 L23: -0.6819
REMARK 3 S TENSOR
REMARK 3 S11: -0.1375 S12: -0.2211 S13: 0.2565
REMARK 3 S21: 0.0386 S22: 0.0166 S23: 0.3367
REMARK 3 S31: 0.0938 S32: -0.1707 S33: 0.0238
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 349:354)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0985 -30.4376 8.7125
REMARK 3 T TENSOR
REMARK 3 T11: 0.2715 T22: 0.6581
REMARK 3 T33: 0.1639 T12: -0.4129
REMARK 3 T13: -0.1179 T23: -0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 3.2827 L22: 0.8022
REMARK 3 L33: 3.7769 L12: 0.7559
REMARK 3 L13: 2.4125 L23: 0.5312
REMARK 3 S TENSOR
REMARK 3 S11: 0.0642 S12: -0.2059 S13: 0.1707
REMARK 3 S21: -0.0587 S22: 0.1719 S23: 0.1275
REMARK 3 S31: 0.6845 S32: -1.0857 S33: -0.1028
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 32:60)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8027 -40.7284 14.8544
REMARK 3 T TENSOR
REMARK 3 T11: 0.2300 T22: 0.2814
REMARK 3 T33: 0.1748 T12: -0.1081
REMARK 3 T13: 0.0505 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 1.2113 L22: 0.9556
REMARK 3 L33: 2.0573 L12: -0.3020
REMARK 3 L13: -0.7547 L23: 0.2043
REMARK 3 S TENSOR
REMARK 3 S11: -0.3212 S12: 0.0046 S13: 0.0786
REMARK 3 S21: 0.0705 S22: 0.0720 S23: -0.0333
REMARK 3 S31: 0.2037 S32: 0.3294 S33: 0.1709
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 61:176)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0810 -18.0411 28.5101
REMARK 3 T TENSOR
REMARK 3 T11: 0.4939 T22: 0.1078
REMARK 3 T33: 0.2154 T12: -0.1575
REMARK 3 T13: 0.1574 T23: -0.1225
REMARK 3 L TENSOR
REMARK 3 L11: 1.5845 L22: 1.2769
REMARK 3 L33: 1.2545 L12: 1.3471
REMARK 3 L13: -0.5806 L23: -0.9268
REMARK 3 S TENSOR
REMARK 3 S11: 0.4254 S12: -0.2299 S13: 0.3301
REMARK 3 S21: 0.4845 S22: -0.0658 S23: 0.2761
REMARK 3 S31: -0.7015 S32: 0.1691 S33: -0.1112
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 177:197)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5607 -41.3312 10.2970
REMARK 3 T TENSOR
REMARK 3 T11: 0.3550 T22: 0.2880
REMARK 3 T33: 0.1915 T12: -0.1655
REMARK 3 T13: 0.0729 T23: -0.0603
REMARK 3 L TENSOR
REMARK 3 L11: 2.9407 L22: 0.6391
REMARK 3 L33: 1.3492 L12: 0.9598
REMARK 3 L13: -1.0592 L23: -0.7034
REMARK 3 S TENSOR
REMARK 3 S11: -0.6302 S12: 0.2445 S13: -0.2213
REMARK 3 S21: -0.1784 S22: 0.2687 S23: -0.1675
REMARK 3 S31: 0.5169 S32: -0.4068 S33: 0.2956
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 198:215)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5792 -38.3585 6.1013
REMARK 3 T TENSOR
REMARK 3 T11: 0.4098 T22: 0.4537
REMARK 3 T33: 0.2919 T12: -0.3567
REMARK 3 T13: -0.1583 T23: 0.1155
REMARK 3 L TENSOR
REMARK 3 L11: 1.3061 L22: 0.7284
REMARK 3 L33: 0.2516 L12: 0.6461
REMARK 3 L13: -0.4315 L23: -0.4166
REMARK 3 S TENSOR
REMARK 3 S11: -0.6340 S12: 0.4544 S13: 0.1964
REMARK 3 S21: -0.2047 S22: 0.3310 S23: -0.1237
REMARK 3 S31: -0.1647 S32: 0.1264 S33: 0.2102
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 216:235)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8940 -39.6626 22.4413
REMARK 3 T TENSOR
REMARK 3 T11: 0.2376 T22: 0.4597
REMARK 3 T33: 0.3609 T12: -0.3277
REMARK 3 T13: -0.0568 T23: 0.0608
REMARK 3 L TENSOR
REMARK 3 L11: 1.4866 L22: 0.4277
REMARK 3 L33: 0.1300 L12: 0.4657
REMARK 3 L13: 0.4220 L23: 0.1965
REMARK 3 S TENSOR
REMARK 3 S11: -0.4623 S12: -0.2242 S13: 0.1627
REMARK 3 S21: -0.2372 S22: 0.6431 S23: 0.3300
REMARK 3 S31: -0.1214 S32: -0.2294 S33: -0.1209
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN B AND RESID 236:245)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2712 -31.5196 26.6228
REMARK 3 T TENSOR
REMARK 3 T11: 0.0172 T22: 0.6368
REMARK 3 T33: 0.5179 T12: -0.1578
REMARK 3 T13: 0.1687 T23: 0.2861
REMARK 3 L TENSOR
REMARK 3 L11: 3.4480 L22: 2.7567
REMARK 3 L33: 1.9075 L12: 0.1443
REMARK 3 L13: 2.4881 L23: -0.4628
REMARK 3 S TENSOR
REMARK 3 S11: -0.3560 S12: -0.4365 S13: 0.8902
REMARK 3 S21: -0.1582 S22: 0.4732 S23: 0.7402
REMARK 3 S31: 0.2690 S32: -0.6967 S33: -0.2489
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN B AND RESID 246:347)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2744 -46.9104 26.8019
REMARK 3 T TENSOR
REMARK 3 T11: -0.0890 T22: 0.3169
REMARK 3 T33: 0.1259 T12: -0.4530
REMARK 3 T13: 0.1629 T23: 0.1490
REMARK 3 L TENSOR
REMARK 3 L11: 1.4044 L22: 1.1871
REMARK 3 L33: 1.3388 L12: 0.8463
REMARK 3 L13: 1.0229 L23: 0.1110
REMARK 3 S TENSOR
REMARK 3 S11: -0.5444 S12: -0.3824 S13: 0.0940
REMARK 3 S21: 0.1509 S22: 0.1254 S23: -0.0283
REMARK 3 S31: 0.3065 S32: -1.0119 S33: -0.3470
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 34:101)
REMARK 3 ORIGIN FOR THE GROUP (A): 72.8039 -28.9992 12.5533
REMARK 3 T TENSOR
REMARK 3 T11: 0.6158 T22: 0.5266
REMARK 3 T33: 0.3294 T12: 0.1612
REMARK 3 T13: -0.0469 T23: 0.0503
REMARK 3 L TENSOR
REMARK 3 L11: 0.5519 L22: 1.0490
REMARK 3 L33: 1.0469 L12: -0.1333
REMARK 3 L13: 1.0725 L23: -0.0728
REMARK 3 S TENSOR
REMARK 3 S11: -0.0821 S12: 0.1810 S13: 0.1004
REMARK 3 S21: 0.0481 S22: -0.2954 S23: 0.1620
REMARK 3 S31: -0.3910 S32: 0.4024 S33: 0.2615
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN C AND RESID 102:165)
REMARK 3 ORIGIN FOR THE GROUP (A): 63.2828 -37.9291 10.0212
REMARK 3 T TENSOR
REMARK 3 T11: 0.3740 T22: 0.4643
REMARK 3 T33: 0.0204 T12: 0.2602
REMARK 3 T13: 0.0525 T23: -0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 2.4459 L22: 4.3002
REMARK 3 L33: 1.5033 L12: -1.4558
REMARK 3 L13: -0.3669 L23: -1.7632
REMARK 3 S TENSOR
REMARK 3 S11: -0.3463 S12: -0.3486 S13: -0.2078
REMARK 3 S21: 0.9363 S22: -0.4168 S23: 0.4088
REMARK 3 S31: -0.1523 S32: 0.2661 S33: 0.2907
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN C AND RESID 166:185)
REMARK 3 ORIGIN FOR THE GROUP (A): 72.4261 -22.9854 13.1800
REMARK 3 T TENSOR
REMARK 3 T11: 0.7147 T22: 0.3109
REMARK 3 T33: 0.7865 T12: 0.2935
REMARK 3 T13: -0.2152 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 1.0207 L22: 1.3602
REMARK 3 L33: 0.4349 L12: 1.1749
REMARK 3 L13: 0.1522 L23: 0.2453
REMARK 3 S TENSOR
REMARK 3 S11: -0.2314 S12: -0.2182 S13: 0.4559
REMARK 3 S21: -0.2064 S22: -0.2279 S23: -0.0634
REMARK 3 S31: -0.6701 S32: 0.1209 S33: 0.5206
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN C AND RESID 186:201)
REMARK 3 ORIGIN FOR THE GROUP (A): 87.4681 -11.3889 20.7847
REMARK 3 T TENSOR
REMARK 3 T11: 1.2000 T22: 0.8563
REMARK 3 T33: 0.7635 T12: -0.2311
REMARK 3 T13: -0.1415 T23: 0.3554
REMARK 3 L TENSOR
REMARK 3 L11: 0.6320 L22: 1.0931
REMARK 3 L33: 3.0861 L12: 0.4742
REMARK 3 L13: -0.0430 L23: -1.5463
REMARK 3 S TENSOR
REMARK 3 S11: -0.1035 S12: 0.1239 S13: 0.2842
REMARK 3 S21: 0.3453 S22: -0.5416 S23: -0.2183
REMARK 3 S31: -0.2448 S32: 0.4564 S33: 0.5754
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN C AND RESID 202:215)
REMARK 3 ORIGIN FOR THE GROUP (A): 97.0205 -23.1122 10.0222
REMARK 3 T TENSOR
REMARK 3 T11: 0.8720 T22: 1.3408
REMARK 3 T33: 1.3420 T12: 0.2127
REMARK 3 T13: 0.3360 T23: 0.1891
REMARK 3 L TENSOR
REMARK 3 L11: 6.6708 L22: 3.2480
REMARK 3 L33: 2.8614 L12: 2.9147
REMARK 3 L13: 0.6639 L23: 1.2477
REMARK 3 S TENSOR
REMARK 3 S11: 0.1349 S12: 1.4413 S13: 0.3988
REMARK 3 S21: 0.2979 S22: 0.1242 S23: 0.4253
REMARK 3 S31: 0.2333 S32: 1.0441 S33: -0.2222
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN C AND RESID 216:246)
REMARK 3 ORIGIN FOR THE GROUP (A): 88.7997 -33.7431 20.6317
REMARK 3 T TENSOR
REMARK 3 T11: 0.5804 T22: 1.1373
REMARK 3 T33: 0.2150 T12: 0.2797
REMARK 3 T13: 0.0332 T23: 0.2720
REMARK 3 L TENSOR
REMARK 3 L11: 0.4060 L22: 0.4621
REMARK 3 L33: 3.2438 L12: 0.3120
REMARK 3 L13: 1.0804 L23: 1.1342
REMARK 3 S TENSOR
REMARK 3 S11: -0.1346 S12: 0.4336 S13: 0.1407
REMARK 3 S21: -0.4034 S22: 0.1108 S23: 0.0383
REMARK 3 S31: -0.4419 S32: 1.2340 S33: 0.1320
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN C AND RESID 247:347)
REMARK 3 ORIGIN FOR THE GROUP (A): 88.8970 -30.9785 29.2322
REMARK 3 T TENSOR
REMARK 3 T11: 0.5013 T22: 0.7629
REMARK 3 T33: 0.3699 T12: 0.1117
REMARK 3 T13: -0.0475 T23: 0.2471
REMARK 3 L TENSOR
REMARK 3 L11: 0.5349 L22: 0.2246
REMARK 3 L33: 2.1426 L12: -0.0422
REMARK 3 L13: 0.8432 L23: 0.2976
REMARK 3 S TENSOR
REMARK 3 S11: -0.2029 S12: -0.2948 S13: 0.0403
REMARK 3 S21: 0.2802 S22: -0.3053 S23: -0.0570
REMARK 3 S31: -0.3258 S32: 0.2006 S33: 0.3807
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 34:109 OR RESSEQ
REMARK 3 121:176 OR RESSEQ 187:198 OR RESSEQ 215:
REMARK 3 230 OR RESSEQ 243:345 ) AND (NOT ELEMENT
REMARK 3 H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 34:109 OR RESSEQ
REMARK 3 121:176 OR RESSEQ 187:198 OR RESSEQ 215:
REMARK 3 230 OR RESSEQ 243:345 ) AND (NOT ELEMENT
REMARK 3 H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 2130
REMARK 3 RMSD : 0.012
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 34:109 OR RESSEQ
REMARK 3 121:176 OR RESSEQ 187:198 OR RESSEQ 215:
REMARK 3 230 OR RESSEQ 243:345 ) AND (NOT ELEMENT
REMARK 3 H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 34:109 OR RESSEQ
REMARK 3 121:176 OR RESSEQ 187:198 OR RESSEQ 215:
REMARK 3 230 OR RESSEQ 243:345 ) AND (NOT ELEMENT
REMARK 3 H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 2130
REMARK 3 RMSD : 0.010
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QE0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063525.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-10
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 : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : CUSTOM
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30772
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 39.441
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: PDB ENTRY 1Y3A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROPS WERE A 1:1 MIXTURE OF
REMARK 280 PROTEIN-PEPTIDE COMPLEX IN BUFFER (50 MM HEPES PH 8.0, 10 MM
REMARK 280 MAGNESIUM CHLORIDE, 10 MICROM GPPNHP, 1 MM EDTA, 5 MM DTT) AND
REMARK 280 WELL SOLUTION (17% (W/V) PEG MME 5K, 200 MM MAGNESIUM CHLORIDE,
REMARK 280 100 MM HEPES PH 7.0), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 151.68733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 303.37467
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 227.53100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 379.21833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.84367
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 151.68733
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 303.37467
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 379.21833
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 227.53100
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 75.84367
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 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: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 30
REMARK 465 ASN A 31
REMARK 465 ALA A 114
REMARK 465 GLU A 115
REMARK 465 GLU A 116
REMARK 465 GLY A 117
REMARK 465 GLY A 203
REMARK 465 GLN A 204
REMARK 465 ARG A 205
REMARK 465 GLU A 236
REMARK 465 ASP A 237
REMARK 465 SER B 30
REMARK 465 ASN B 31
REMARK 465 GLY B 112
REMARK 465 ALA B 113
REMARK 465 LEU B 348
REMARK 465 LYS B 349
REMARK 465 ASP B 350
REMARK 465 CYS B 351
REMARK 465 GLY B 352
REMARK 465 LEU B 353
REMARK 465 PHE B 354
REMARK 465 SER C 30
REMARK 465 ASN C 31
REMARK 465 ALA C 32
REMARK 465 GLU C 33
REMARK 465 ALA C 113
REMARK 465 ALA C 114
REMARK 465 GLU C 115
REMARK 465 GLU C 116
REMARK 465 GLU C 207
REMARK 465 ARG C 208
REMARK 465 LYS C 209
REMARK 465 LYS C 210
REMARK 465 TRP C 211
REMARK 465 LEU C 234
REMARK 465 ALA C 235
REMARK 465 GLU C 236
REMARK 465 ASP C 237
REMARK 465 GLU C 238
REMARK 465 GLU C 239
REMARK 465 LEU C 348
REMARK 465 LYS C 349
REMARK 465 ASP C 350
REMARK 465 CYS C 351
REMARK 465 GLY C 352
REMARK 465 LEU C 353
REMARK 465 PHE C 354
REMARK 465 ASP G 12
REMARK 465 THR G 13
REMARK 465 LYS G 14
REMARK 465 SER G 15
REMARK 465 ARG G 16
REMARK 465 SER F 1
REMARK 465 ARG F 2
REMARK 465 VAL F 3
REMARK 465 MET F 10
REMARK 465 GLU F 11
REMARK 465 ASP F 12
REMARK 465 THR F 13
REMARK 465 LYS F 14
REMARK 465 SER F 15
REMARK 465 ARG F 16
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 164 CD OE1 NE2
REMARK 480 LYS A 248 CD CE NZ
REMARK 480 LYS A 345 CE NZ
REMARK 480 ASN A 347 C O
REMARK 480 GLN B 164 CD OE1 NE2
REMARK 480 LYS B 248 CD CE NZ
REMARK 480 LYS B 345 CE NZ
REMARK 480 LYS C 248 CD CE NZ
REMARK 480 ASN C 347 C O
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 LYS A 92 66.08 60.67
REMARK 500 ASN A 166 39.83 38.64
REMARK 500 LYS A 180 92.60 -66.68
REMARK 500 ARG A 208 -74.02 -138.07
REMARK 500 HIS A 213 20.82 -78.31
REMARK 500 PHE A 259 51.07 -116.98
REMARK 500 ASP A 350 -71.67 -63.43
REMARK 500 CYS A 351 30.42 -69.87
REMARK 500 LYS B 92 66.08 60.05
REMARK 500 LEU B 110 -78.74 -54.88
REMARK 500 GLU B 116 47.84 -85.87
REMARK 500 ASN B 166 39.87 38.35
REMARK 500 ARG B 205 42.55 70.42
REMARK 500 PHE B 259 51.42 -116.85
REMARK 500 ASN C 166 40.18 37.94
REMARK 500 LYS C 180 74.74 -68.01
REMARK 500 PHE C 259 51.34 -117.19
REMARK 500 TYR G 6 -76.66 -59.82
REMARK 500 LEU G 9 3.20 -69.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 556 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 47 OG
REMARK 620 2 THR A 181 OG1 80.3
REMARK 620 3 GDP A 555 O1B 69.0 131.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 556 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 47 OG
REMARK 620 2 GDP B 355 O1B 73.0
REMARK 620 3 GDP B 355 O2B 122.2 49.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 552 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 47 OG
REMARK 620 2 THR C 181 OG1 73.3
REMARK 620 3 GDP C 551 O1B 117.1 168.6
REMARK 620 4 GDP C 551 O2B 68.7 131.4 54.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 556
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 555
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 556
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 551
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QI2 RELATED DB: PDB
REMARK 900 GALPHA-I1 G42R BOUND TO RGS14 GOLOCO
REMARK 900 RELATED ID: 2OM2 RELATED DB: PDB
REMARK 900 GALPHA-I1 WILDTYPE BOUND TO RGS14 GOLOCO
REMARK 900 RELATED ID: 1KJY RELATED DB: PDB
REMARK 900 GALPHA-I1 WILDTYPE BOUND TO RGS14 GOLOCO
REMARK 900 RELATED ID: 1Y3A RELATED DB: PDB
REMARK 900 WILDTYPE GALPHA-I1 BOUND TO THE GDP-SELECTIVE PHAGE DISPLAY PEPTIDE
REMARK 900 KB-752
DBREF 3QE0 A 33 354 UNP P63096 GNAI1_HUMAN 33 354
DBREF 3QE0 B 33 354 UNP P63096 GNAI1_HUMAN 33 354
DBREF 3QE0 C 33 354 UNP P63096 GNAI1_HUMAN 33 354
DBREF 3QE0 G 1 16 PDB 3QE0 3QE0 1 16
DBREF 3QE0 F 1 16 PDB 3QE0 3QE0 1 16
SEQADV 3QE0 SER A 30 UNP P63096 EXPRESSION TAG
SEQADV 3QE0 ASN A 31 UNP P63096 EXPRESSION TAG
SEQADV 3QE0 ALA A 32 UNP P63096 EXPRESSION TAG
SEQADV 3QE0 ARG A 42 UNP P63096 GLY 42 ENGINEERED MUTATION
SEQADV 3QE0 SER B 30 UNP P63096 EXPRESSION TAG
SEQADV 3QE0 ASN B 31 UNP P63096 EXPRESSION TAG
SEQADV 3QE0 ALA B 32 UNP P63096 EXPRESSION TAG
SEQADV 3QE0 ARG B 42 UNP P63096 GLY 42 ENGINEERED MUTATION
SEQADV 3QE0 SER C 30 UNP P63096 EXPRESSION TAG
SEQADV 3QE0 ASN C 31 UNP P63096 EXPRESSION TAG
SEQADV 3QE0 ALA C 32 UNP P63096 EXPRESSION TAG
SEQADV 3QE0 ARG C 42 UNP P63096 GLY 42 ENGINEERED MUTATION
SEQRES 1 A 325 SER ASN ALA GLU VAL LYS LEU LEU LEU LEU GLY ALA ARG
SEQRES 2 A 325 GLU SER GLY LYS SER THR ILE VAL LYS GLN MET LYS ILE
SEQRES 3 A 325 ILE HIS GLU ALA GLY TYR SER GLU GLU GLU CYS LYS GLN
SEQRES 4 A 325 TYR LYS ALA VAL VAL TYR SER ASN THR ILE GLN SER ILE
SEQRES 5 A 325 ILE ALA ILE ILE ARG ALA MET GLY ARG LEU LYS ILE ASP
SEQRES 6 A 325 PHE GLY ASP SER ALA ARG ALA ASP ASP ALA ARG GLN LEU
SEQRES 7 A 325 PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY PHE MET THR
SEQRES 8 A 325 ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU TRP LYS ASP
SEQRES 9 A 325 SER GLY VAL GLN ALA CYS PHE ASN ARG SER ARG GLU TYR
SEQRES 10 A 325 GLN LEU ASN ASP SER ALA ALA TYR TYR LEU ASN ASP LEU
SEQRES 11 A 325 ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO THR GLN GLN
SEQRES 12 A 325 ASP VAL LEU ARG THR ARG VAL LYS THR THR GLY ILE VAL
SEQRES 13 A 325 GLU THR HIS PHE THR PHE LYS ASP LEU HIS PHE LYS MET
SEQRES 14 A 325 PHE ASP VAL GLY GLY GLN ARG SER GLU ARG LYS LYS TRP
SEQRES 15 A 325 ILE HIS CYS PHE GLU GLY VAL THR ALA ILE ILE PHE CYS
SEQRES 16 A 325 VAL ALA LEU SER ASP TYR ASP LEU VAL LEU ALA GLU ASP
SEQRES 17 A 325 GLU GLU MET ASN ARG MET HIS GLU SER MET LYS LEU PHE
SEQRES 18 A 325 ASP SER ILE CYS ASN ASN LYS TRP PHE THR ASP THR SER
SEQRES 19 A 325 ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU PHE GLU GLU
SEQRES 20 A 325 LYS ILE LYS LYS SER PRO LEU THR ILE CYS TYR PRO GLU
SEQRES 21 A 325 TYR ALA GLY SER ASN THR TYR GLU GLU ALA ALA ALA TYR
SEQRES 22 A 325 ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS ARG LYS ASP
SEQRES 23 A 325 THR LYS GLU ILE TYR THR HIS PHE THR CYS ALA THR ASP
SEQRES 24 A 325 THR LYS ASN VAL GLN PHE VAL PHE ASP ALA VAL THR ASP
SEQRES 25 A 325 VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS GLY LEU PHE
SEQRES 1 B 325 SER ASN ALA GLU VAL LYS LEU LEU LEU LEU GLY ALA ARG
SEQRES 2 B 325 GLU SER GLY LYS SER THR ILE VAL LYS GLN MET LYS ILE
SEQRES 3 B 325 ILE HIS GLU ALA GLY TYR SER GLU GLU GLU CYS LYS GLN
SEQRES 4 B 325 TYR LYS ALA VAL VAL TYR SER ASN THR ILE GLN SER ILE
SEQRES 5 B 325 ILE ALA ILE ILE ARG ALA MET GLY ARG LEU LYS ILE ASP
SEQRES 6 B 325 PHE GLY ASP SER ALA ARG ALA ASP ASP ALA ARG GLN LEU
SEQRES 7 B 325 PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY PHE MET THR
SEQRES 8 B 325 ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU TRP LYS ASP
SEQRES 9 B 325 SER GLY VAL GLN ALA CYS PHE ASN ARG SER ARG GLU TYR
SEQRES 10 B 325 GLN LEU ASN ASP SER ALA ALA TYR TYR LEU ASN ASP LEU
SEQRES 11 B 325 ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO THR GLN GLN
SEQRES 12 B 325 ASP VAL LEU ARG THR ARG VAL LYS THR THR GLY ILE VAL
SEQRES 13 B 325 GLU THR HIS PHE THR PHE LYS ASP LEU HIS PHE LYS MET
SEQRES 14 B 325 PHE ASP VAL GLY GLY GLN ARG SER GLU ARG LYS LYS TRP
SEQRES 15 B 325 ILE HIS CYS PHE GLU GLY VAL THR ALA ILE ILE PHE CYS
SEQRES 16 B 325 VAL ALA LEU SER ASP TYR ASP LEU VAL LEU ALA GLU ASP
SEQRES 17 B 325 GLU GLU MET ASN ARG MET HIS GLU SER MET LYS LEU PHE
SEQRES 18 B 325 ASP SER ILE CYS ASN ASN LYS TRP PHE THR ASP THR SER
SEQRES 19 B 325 ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU PHE GLU GLU
SEQRES 20 B 325 LYS ILE LYS LYS SER PRO LEU THR ILE CYS TYR PRO GLU
SEQRES 21 B 325 TYR ALA GLY SER ASN THR TYR GLU GLU ALA ALA ALA TYR
SEQRES 22 B 325 ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS ARG LYS ASP
SEQRES 23 B 325 THR LYS GLU ILE TYR THR HIS PHE THR CYS ALA THR ASP
SEQRES 24 B 325 THR LYS ASN VAL GLN PHE VAL PHE ASP ALA VAL THR ASP
SEQRES 25 B 325 VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS GLY LEU PHE
SEQRES 1 C 325 SER ASN ALA GLU VAL LYS LEU LEU LEU LEU GLY ALA ARG
SEQRES 2 C 325 GLU SER GLY LYS SER THR ILE VAL LYS GLN MET LYS ILE
SEQRES 3 C 325 ILE HIS GLU ALA GLY TYR SER GLU GLU GLU CYS LYS GLN
SEQRES 4 C 325 TYR LYS ALA VAL VAL TYR SER ASN THR ILE GLN SER ILE
SEQRES 5 C 325 ILE ALA ILE ILE ARG ALA MET GLY ARG LEU LYS ILE ASP
SEQRES 6 C 325 PHE GLY ASP SER ALA ARG ALA ASP ASP ALA ARG GLN LEU
SEQRES 7 C 325 PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY PHE MET THR
SEQRES 8 C 325 ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU TRP LYS ASP
SEQRES 9 C 325 SER GLY VAL GLN ALA CYS PHE ASN ARG SER ARG GLU TYR
SEQRES 10 C 325 GLN LEU ASN ASP SER ALA ALA TYR TYR LEU ASN ASP LEU
SEQRES 11 C 325 ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO THR GLN GLN
SEQRES 12 C 325 ASP VAL LEU ARG THR ARG VAL LYS THR THR GLY ILE VAL
SEQRES 13 C 325 GLU THR HIS PHE THR PHE LYS ASP LEU HIS PHE LYS MET
SEQRES 14 C 325 PHE ASP VAL GLY GLY GLN ARG SER GLU ARG LYS LYS TRP
SEQRES 15 C 325 ILE HIS CYS PHE GLU GLY VAL THR ALA ILE ILE PHE CYS
SEQRES 16 C 325 VAL ALA LEU SER ASP TYR ASP LEU VAL LEU ALA GLU ASP
SEQRES 17 C 325 GLU GLU MET ASN ARG MET HIS GLU SER MET LYS LEU PHE
SEQRES 18 C 325 ASP SER ILE CYS ASN ASN LYS TRP PHE THR ASP THR SER
SEQRES 19 C 325 ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU PHE GLU GLU
SEQRES 20 C 325 LYS ILE LYS LYS SER PRO LEU THR ILE CYS TYR PRO GLU
SEQRES 21 C 325 TYR ALA GLY SER ASN THR TYR GLU GLU ALA ALA ALA TYR
SEQRES 22 C 325 ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS ARG LYS ASP
SEQRES 23 C 325 THR LYS GLU ILE TYR THR HIS PHE THR CYS ALA THR ASP
SEQRES 24 C 325 THR LYS ASN VAL GLN PHE VAL PHE ASP ALA VAL THR ASP
SEQRES 25 C 325 VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS GLY LEU PHE
SEQRES 1 G 16 SER ARG VAL THR TRP TYR ASP PHE LEU MET GLU ASP THR
SEQRES 2 G 16 LYS SER ARG
SEQRES 1 F 16 SER ARG VAL THR TRP TYR ASP PHE LEU MET GLU ASP THR
SEQRES 2 F 16 LYS SER ARG
HET MG A 556 1
HET GDP A 555 28
HET MG B 556 1
HET GDP B 355 28
HET MG C 552 1
HET GDP C 551 28
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 6 MG 3(MG 2+)
FORMUL 7 GDP 3(C10 H15 N5 O11 P2)
FORMUL 12 HOH *12(H2 O)
HELIX 1 1 GLY A 45 GLU A 58 1 14
HELIX 2 2 SER A 62 TYR A 69 1 8
HELIX 3 3 TYR A 69 LEU A 91 1 23
HELIX 4 4 ALA A 99 GLY A 112 1 14
HELIX 5 5 THR A 120 ASP A 133 1 14
HELIX 6 6 ASP A 133 ASN A 141 1 9
HELIX 7 7 ARG A 142 TYR A 146 5 5
HELIX 8 8 SER A 151 ASN A 157 1 7
HELIX 9 9 ASP A 158 GLN A 164 1 7
HELIX 10 10 THR A 170 THR A 177 1 8
HELIX 11 11 SER A 228 LEU A 232 5 5
HELIX 12 12 ASN A 241 ASN A 256 1 16
HELIX 13 13 LYS A 257 THR A 260 5 4
HELIX 14 14 LYS A 270 ILE A 278 1 9
HELIX 15 15 PRO A 282 CYS A 286 5 5
HELIX 16 16 THR A 295 ASP A 309 1 15
HELIX 17 17 ASP A 328 CYS A 351 1 24
HELIX 18 18 GLY B 45 GLU B 58 1 14
HELIX 19 19 SER B 62 TYR B 69 1 8
HELIX 20 20 TYR B 69 LEU B 91 1 23
HELIX 21 21 ALA B 99 ALA B 111 1 13
HELIX 22 22 THR B 120 ASP B 133 1 14
HELIX 23 23 ASP B 133 ASN B 141 1 9
HELIX 24 24 ARG B 142 TYR B 146 5 5
HELIX 25 25 SER B 151 ASN B 157 1 7
HELIX 26 26 ASP B 158 GLN B 164 1 7
HELIX 27 27 THR B 170 THR B 177 1 8
HELIX 28 28 GLU B 207 PHE B 215 1 9
HELIX 29 29 SER B 228 LEU B 232 5 5
HELIX 30 30 ASN B 241 ASN B 256 1 16
HELIX 31 31 LYS B 257 THR B 260 5 4
HELIX 32 32 LYS B 270 ILE B 278 1 9
HELIX 33 33 PRO B 282 CYS B 286 5 5
HELIX 34 34 THR B 295 ASP B 309 1 15
HELIX 35 35 ASP B 328 ASN B 346 1 19
HELIX 36 36 GLY C 45 GLU C 58 1 14
HELIX 37 37 SER C 62 TYR C 69 1 8
HELIX 38 38 TYR C 69 LEU C 91 1 23
HELIX 39 39 ALA C 99 ALA C 111 1 13
HELIX 40 40 THR C 120 ASP C 133 1 14
HELIX 41 41 ASP C 133 ASN C 141 1 9
HELIX 42 42 ARG C 142 TYR C 146 5 5
HELIX 43 43 SER C 151 ASN C 157 1 7
HELIX 44 44 ASP C 158 GLN C 164 1 7
HELIX 45 45 THR C 170 ARG C 176 1 7
HELIX 46 46 SER C 228 LEU C 232 5 5
HELIX 47 47 ASN C 241 ASN C 256 1 16
HELIX 48 48 LYS C 257 THR C 260 5 4
HELIX 49 49 LYS C 270 ILE C 278 1 9
HELIX 50 50 PRO C 282 CYS C 286 5 5
HELIX 51 51 THR C 295 ASP C 309 1 15
HELIX 52 52 ASP C 328 ASN C 346 1 19
HELIX 53 53 THR G 4 LEU G 9 1 6
HELIX 54 54 THR F 4 LEU F 9 1 6
SHEET 1 A 6 GLY A 183 PHE A 191 0
SHEET 2 A 6 LEU A 194 GLY A 202 -1 O MET A 198 N THR A 187
SHEET 3 A 6 GLU A 33 GLY A 40 1 N VAL A 34 O LYS A 197
SHEET 4 A 6 ALA A 220 ALA A 226 1 O ILE A 222 N LEU A 37
SHEET 5 A 6 SER A 263 ASN A 269 1 O ILE A 265 N ILE A 221
SHEET 6 A 6 ILE A 319 PHE A 323 1 O HIS A 322 N LEU A 266
SHEET 1 B 6 ILE B 184 PHE B 191 0
SHEET 2 B 6 LEU B 194 VAL B 201 -1 O MET B 198 N THR B 187
SHEET 3 B 6 GLU B 33 GLY B 40 1 N VAL B 34 O LYS B 197
SHEET 4 B 6 ALA B 220 ALA B 226 1 O ILE B 222 N LEU B 37
SHEET 5 B 6 SER B 263 ASN B 269 1 O ILE B 265 N ILE B 221
SHEET 6 B 6 ILE B 319 PHE B 323 1 O HIS B 322 N LEU B 266
SHEET 1 C 6 GLU C 186 PHE C 191 0
SHEET 2 C 6 LEU C 194 ASP C 200 -1 O MET C 198 N THR C 187
SHEET 3 C 6 LYS C 35 GLY C 40 1 N LEU C 38 O PHE C 199
SHEET 4 C 6 ALA C 220 ALA C 226 1 O ILE C 222 N LEU C 37
SHEET 5 C 6 SER C 263 ASN C 269 1 O ILE C 265 N ILE C 221
SHEET 6 C 6 ILE C 319 PHE C 323 1 O HIS C 322 N LEU C 266
LINK OG SER A 47 MG MG A 556 1555 1555 2.62
LINK OG1 THR A 181 MG MG A 556 1555 1555 2.72
LINK O1B GDP A 555 MG MG A 556 1555 1555 2.62
LINK OG SER B 47 MG MG B 556 1555 1555 2.38
LINK O1B GDP B 355 MG MG B 556 1555 1555 2.88
LINK O2B GDP B 355 MG MG B 556 1555 1555 2.99
LINK OG SER C 47 MG MG C 552 1555 1555 2.50
LINK OG1 THR C 181 MG MG C 552 1555 1555 2.65
LINK O1B GDP C 551 MG MG C 552 1555 1555 2.69
LINK O2B GDP C 551 MG MG C 552 1555 1555 2.75
SITE 1 AC1 3 SER A 47 THR A 181 GDP A 555
SITE 1 AC2 21 HOH A 7 ARG A 42 GLU A 43 SER A 44
SITE 2 AC2 21 GLY A 45 LYS A 46 SER A 47 THR A 48
SITE 3 AC2 21 SER A 151 LEU A 175 ARG A 176 THR A 177
SITE 4 AC2 21 ARG A 178 ASN A 269 LYS A 270 ASP A 272
SITE 5 AC2 21 LEU A 273 CYS A 325 ALA A 326 THR A 327
SITE 6 AC2 21 MG A 556
SITE 1 AC3 2 SER B 47 GDP B 355
SITE 1 AC4 19 GLU B 43 SER B 44 GLY B 45 LYS B 46
SITE 2 AC4 19 SER B 47 THR B 48 SER B 151 LEU B 175
SITE 3 AC4 19 ARG B 176 THR B 177 ARG B 178 ASN B 269
SITE 4 AC4 19 LYS B 270 ASP B 272 LEU B 273 CYS B 325
SITE 5 AC4 19 ALA B 326 THR B 327 MG B 556
SITE 1 AC5 4 SER C 47 VAL C 179 THR C 181 GDP C 551
SITE 1 AC6 21 ALA C 41 ARG C 42 GLU C 43 SER C 44
SITE 2 AC6 21 GLY C 45 LYS C 46 SER C 47 THR C 48
SITE 3 AC6 21 SER C 151 LEU C 175 ARG C 176 THR C 177
SITE 4 AC6 21 ARG C 178 ASN C 269 LYS C 270 ASP C 272
SITE 5 AC6 21 LEU C 273 CYS C 325 ALA C 326 THR C 327
SITE 6 AC6 21 MG C 552
CRYST1 106.637 106.637 455.062 90.00 90.00 120.00 P 61 2 2 36
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 0.009378 0.005414 0.000000 0.00000
SCALE2 0.000000 0.010828 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
