HEADER MEMBRANE PROTEIN 06-APR-12 4EIY
TITLE CRYSTAL STRUCTURE OF THE CHIMERIC PROTEIN OF A2AAR-BRIL IN COMPLEX
TITLE 2 WITH ZM241385 AT 1.8A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A/SOLUBLE CYTOCHROME B562 CHIMERA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOCHROME B-562;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 562;
SOURCE 5 GENE: AA2AR_HUMAN, ADORA2, ADORA2A, CYBC;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS NOVEL PROTEIN ENGINEERING, GPCR NETWORK, PSI-BIOLOGY, STRUCTURAL
KEYWDS 2 GENOMICS, MEMBRANE PROTEIN, GPCR
EXPDTA X-RAY DIFFRACTION
AUTHOR W.LIU,E.CHUN,A.A.THOMPSON,P.CHUBUKOV,F.XU,V.KATRITCH,G.W.HAN,
AUTHOR 2 L.H.HEITMAN,A.P.IJZERMAN,V.CHEREZOV,R.C.STEVENS,GPCR NETWORK (GPCR)
REVDAT 4 13-SEP-23 4EIY 1 REMARK SEQADV LINK
REVDAT 3 16-AUG-17 4EIY 1 SOURCE REMARK
REVDAT 2 01-AUG-12 4EIY 1 JRNL
REVDAT 1 25-JUL-12 4EIY 0
JRNL AUTH W.LIU,E.CHUN,A.A.THOMPSON,P.CHUBUKOV,F.XU,V.KATRITCH,
JRNL AUTH 2 G.W.HAN,C.B.ROTH,L.H.HEITMAN,A.P.IJZERMAN,V.CHEREZOV,
JRNL AUTH 3 R.C.STEVENS
JRNL TITL STRUCTURAL BASIS FOR ALLOSTERIC REGULATION OF GPCRS BY
JRNL TITL 2 SODIUM IONS.
JRNL REF SCIENCE V. 337 232 2012
JRNL REFN ISSN 0036-8075
JRNL PMID 22798613
JRNL DOI 10.1126/SCIENCE.1219218
REMARK 2
REMARK 2 RESOLUTION. 1.80 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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 42032
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2222
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2809
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 147
REMARK 3 BIN FREE R VALUE : 0.3290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3012
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 481
REMARK 3 SOLVENT ATOMS : 177
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : 0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.122
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.764
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3653 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2680 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4891 ; 1.584 ; 2.065
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6560 ; 1.098 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 412 ; 4.711 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 124 ;38.746 ;23.548
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 524 ;13.558 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;21.081 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 550 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3778 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 717 ; 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): 2011 ; 1.481 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 812 ; 0.450 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3253 ; 2.270 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1642 ; 4.026 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1638 ; 5.791 ;11.000
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
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 -1 A 34
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9918 -3.9454 6.8744
REMARK 3 T TENSOR
REMARK 3 T11: 0.0567 T22: 0.1036
REMARK 3 T33: 0.0127 T12: 0.0019
REMARK 3 T13: -0.0020 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 1.3047 L22: 20.5751
REMARK 3 L33: 3.2950 L12: 1.6923
REMARK 3 L13: -0.5264 L23: -6.2518
REMARK 3 S TENSOR
REMARK 3 S11: 0.0484 S12: 0.0377 S13: 0.0063
REMARK 3 S21: 0.0644 S22: 0.1134 S23: 0.4664
REMARK 3 S31: -0.1330 S32: -0.1228 S33: -0.1617
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 35 A 38
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3295 -29.8316 14.7622
REMARK 3 T TENSOR
REMARK 3 T11: 0.2441 T22: 0.0949
REMARK 3 T33: 0.5072 T12: -0.0184
REMARK 3 T13: -0.0766 T23: 0.0845
REMARK 3 L TENSOR
REMARK 3 L11: 19.5268 L22: 23.9520
REMARK 3 L33: 15.0509 L12: 16.1895
REMARK 3 L13: -12.9421 L23: -2.7492
REMARK 3 S TENSOR
REMARK 3 S11: -0.9559 S12: 0.0523 S13: -0.4134
REMARK 3 S21: -0.1951 S22: 0.6010 S23: 0.4029
REMARK 3 S31: 1.1611 S32: 0.3751 S33: 0.3549
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 39 A 73
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1582 -5.0186 17.3034
REMARK 3 T TENSOR
REMARK 3 T11: 0.0468 T22: 0.0853
REMARK 3 T33: 0.0164 T12: -0.0017
REMARK 3 T13: 0.0043 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 1.7642 L22: 3.6582
REMARK 3 L33: 1.3426 L12: -1.0193
REMARK 3 L13: 0.5252 L23: -0.8230
REMARK 3 S TENSOR
REMARK 3 S11: -0.0068 S12: -0.0812 S13: -0.0569
REMARK 3 S21: -0.0716 S22: 0.1231 S23: 0.1718
REMARK 3 S31: 0.0548 S32: -0.1406 S33: -0.1163
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 74 A 108
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9496 -10.7814 24.2306
REMARK 3 T TENSOR
REMARK 3 T11: 0.0518 T22: 0.0923
REMARK 3 T33: 0.0150 T12: -0.0024
REMARK 3 T13: -0.0169 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 3.8666 L22: 14.9615
REMARK 3 L33: 0.8786 L12: -6.6088
REMARK 3 L13: -0.2160 L23: 0.1919
REMARK 3 S TENSOR
REMARK 3 S11: -0.1526 S12: -0.1627 S13: 0.1288
REMARK 3 S21: 0.3771 S22: 0.1149 S23: -0.3673
REMARK 3 S31: 0.0801 S32: 0.0110 S33: 0.0377
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 109 A 117
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9067 -33.0684 28.5603
REMARK 3 T TENSOR
REMARK 3 T11: 0.3188 T22: 0.2568
REMARK 3 T33: 0.1925 T12: -0.0056
REMARK 3 T13: -0.0231 T23: 0.0979
REMARK 3 L TENSOR
REMARK 3 L11: 14.8029 L22: 21.7072
REMARK 3 L33: 10.3164 L12: -10.1338
REMARK 3 L13: -9.5771 L23: -1.2422
REMARK 3 S TENSOR
REMARK 3 S11: -0.6072 S12: -0.7783 S13: -0.4910
REMARK 3 S21: -0.0576 S22: 0.1444 S23: -0.0296
REMARK 3 S31: 0.6201 S32: 0.6694 S33: 0.4628
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 118 A 137
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8641 -13.8650 29.7137
REMARK 3 T TENSOR
REMARK 3 T11: 0.1981 T22: 0.1135
REMARK 3 T33: 0.0599 T12: 0.0268
REMARK 3 T13: -0.0007 T23: 0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 1.2035 L22: 21.4041
REMARK 3 L33: 0.5095 L12: -1.2283
REMARK 3 L13: -0.1009 L23: -1.9229
REMARK 3 S TENSOR
REMARK 3 S11: -0.1843 S12: -0.0734 S13: -0.2107
REMARK 3 S21: 0.6621 S22: 0.2288 S23: 0.2235
REMARK 3 S31: 0.1749 S32: 0.0245 S33: -0.0444
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 : A 138 A 161
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9818 17.0669 27.1623
REMARK 3 T TENSOR
REMARK 3 T11: 0.2985 T22: 0.1563
REMARK 3 T33: 0.5053 T12: 0.0409
REMARK 3 T13: 0.0697 T23: 0.0315
REMARK 3 L TENSOR
REMARK 3 L11: 6.1179 L22: 3.2583
REMARK 3 L33: 3.7961 L12: -3.8310
REMARK 3 L13: 3.2495 L23: -1.1023
REMARK 3 S TENSOR
REMARK 3 S11: -0.3817 S12: 0.1872 S13: 0.9081
REMARK 3 S21: 0.1153 S22: -0.1820 S23: -0.1317
REMARK 3 S31: -0.8552 S32: -0.0753 S33: 0.5638
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 : A 162 A 186
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4102 7.2803 25.4330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0515 T22: 0.0812
REMARK 3 T33: 0.0453 T12: -0.0136
REMARK 3 T13: 0.0054 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 4.6764 L22: 5.4095
REMARK 3 L33: 2.3606 L12: -3.7345
REMARK 3 L13: 1.1163 L23: -0.4474
REMARK 3 S TENSOR
REMARK 3 S11: 0.0343 S12: 0.0099 S13: 0.0618
REMARK 3 S21: -0.0091 S22: -0.0933 S23: 0.1967
REMARK 3 S31: -0.1207 S32: 0.0175 S33: 0.0590
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 : A 187 A 208
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0473 -20.8720 21.8023
REMARK 3 T TENSOR
REMARK 3 T11: 0.1107 T22: 0.1176
REMARK 3 T33: 0.1639 T12: 0.0272
REMARK 3 T13: -0.0205 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 2.0881 L22: 21.8699
REMARK 3 L33: 2.4787 L12: -5.4485
REMARK 3 L13: -1.6028 L23: 6.2025
REMARK 3 S TENSOR
REMARK 3 S11: -0.0124 S12: -0.0747 S13: 0.0098
REMARK 3 S21: 0.2971 S22: 0.1410 S23: -0.8825
REMARK 3 S31: 0.1498 S32: 0.1408 S33: -0.1286
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 : A 219 A 259
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6709 -13.3465 15.0381
REMARK 3 T TENSOR
REMARK 3 T11: 0.0731 T22: 0.0946
REMARK 3 T33: 0.0742 T12: 0.0299
REMARK 3 T13: 0.0115 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.7200 L22: 6.3930
REMARK 3 L33: 0.8604 L12: 0.5337
REMARK 3 L13: 0.2162 L23: 0.6548
REMARK 3 S TENSOR
REMARK 3 S11: -0.0305 S12: 0.0484 S13: -0.1623
REMARK 3 S21: -0.2663 S22: 0.1347 S23: -0.3255
REMARK 3 S31: 0.1498 S32: 0.1210 S33: -0.1042
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 : A 260 A 265
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1396 16.2083 17.3125
REMARK 3 T TENSOR
REMARK 3 T11: 0.2705 T22: 0.1962
REMARK 3 T33: 0.2057 T12: 0.0384
REMARK 3 T13: 0.0381 T23: 0.0520
REMARK 3 L TENSOR
REMARK 3 L11: 7.0264 L22: 8.2942
REMARK 3 L33: 21.0838 L12: -4.2003
REMARK 3 L13: 10.9282 L23: -1.6781
REMARK 3 S TENSOR
REMARK 3 S11: -0.9217 S12: -0.0670 S13: 0.4910
REMARK 3 S21: 0.4595 S22: 0.5554 S23: -0.6952
REMARK 3 S31: -1.2802 S32: 0.4163 S33: 0.3662
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 : A 266 A 292
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4175 -5.0165 8.2951
REMARK 3 T TENSOR
REMARK 3 T11: 0.0569 T22: 0.1070
REMARK 3 T33: 0.0179 T12: 0.0221
REMARK 3 T13: 0.0004 T23: 0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 0.9128 L22: 13.7330
REMARK 3 L33: 1.1449 L12: 2.0947
REMARK 3 L13: 0.4242 L23: 1.0745
REMARK 3 S TENSOR
REMARK 3 S11: -0.0166 S12: 0.0785 S13: 0.0003
REMARK 3 S21: -0.4142 S22: -0.0077 S23: -0.0309
REMARK 3 S31: 0.0272 S32: 0.0363 S33: 0.0242
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 293 A 307
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4870 -25.2207 2.7877
REMARK 3 T TENSOR
REMARK 3 T11: 0.3223 T22: 0.1721
REMARK 3 T33: 0.1214 T12: -0.0784
REMARK 3 T13: -0.0227 T23: -0.0436
REMARK 3 L TENSOR
REMARK 3 L11: 22.3732 L22: 11.2448
REMARK 3 L33: 13.3027 L12: -1.2770
REMARK 3 L13: 6.3190 L23: -0.0488
REMARK 3 S TENSOR
REMARK 3 S11: 0.2163 S12: 1.1420 S13: -0.7201
REMARK 3 S21: -0.9830 S22: -0.0720 S23: 0.5361
REMARK 3 S31: 0.6687 S32: -0.3328 S33: -0.1443
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1001 A 1021
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7603 -49.3985 16.1997
REMARK 3 T TENSOR
REMARK 3 T11: 0.2887 T22: 0.2415
REMARK 3 T33: 0.6371 T12: 0.0665
REMARK 3 T13: 0.1044 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 14.3514 L22: 38.5212
REMARK 3 L33: 1.7664 L12: -19.9233
REMARK 3 L13: -1.9101 L23: 1.4838
REMARK 3 S TENSOR
REMARK 3 S11: 0.2725 S12: 0.1460 S13: 0.4350
REMARK 3 S21: -0.9890 S22: -0.5419 S23: -1.6647
REMARK 3 S31: 0.1872 S32: 0.1640 S33: 0.2694
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1022 A 1042
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5547 -53.4454 25.5883
REMARK 3 T TENSOR
REMARK 3 T11: 0.3548 T22: 0.3251
REMARK 3 T33: 0.8615 T12: 0.0591
REMARK 3 T13: -0.2118 T23: -0.2213
REMARK 3 L TENSOR
REMARK 3 L11: 17.2785 L22: 24.2101
REMARK 3 L33: 6.7690 L12: -13.6158
REMARK 3 L13: -2.7492 L23: -4.7961
REMARK 3 S TENSOR
REMARK 3 S11: -0.4648 S12: -1.1799 S13: 1.7658
REMARK 3 S21: 1.0732 S22: 0.6136 S23: -1.4639
REMARK 3 S31: -0.5001 S32: 0.2215 S33: -0.1488
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1058 A 1081
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0374 -57.9403 23.7417
REMARK 3 T TENSOR
REMARK 3 T11: 0.2375 T22: 0.2831
REMARK 3 T33: 0.5244 T12: 0.0551
REMARK 3 T13: 0.0497 T23: 0.0772
REMARK 3 L TENSOR
REMARK 3 L11: 27.1612 L22: 23.1118
REMARK 3 L33: 13.8851 L12: -17.4107
REMARK 3 L13: 8.3216 L23: -9.6204
REMARK 3 S TENSOR
REMARK 3 S11: -0.4466 S12: -1.3740 S13: 0.1430
REMARK 3 S21: 0.6583 S22: 1.3132 S23: 1.4145
REMARK 3 S31: -0.2563 S32: -1.0919 S33: -0.8665
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1082 A 1093
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5360 -65.9659 18.9084
REMARK 3 T TENSOR
REMARK 3 T11: 0.2893 T22: 0.1325
REMARK 3 T33: 0.4557 T12: 0.0763
REMARK 3 T13: 0.0226 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 24.1901 L22: 18.4892
REMARK 3 L33: 14.5502 L12: -14.5038
REMARK 3 L13: 6.7759 L23: -2.9948
REMARK 3 S TENSOR
REMARK 3 S11: -0.3005 S12: -0.4649 S13: 0.2023
REMARK 3 S21: -0.7867 S22: -0.0522 S23: -0.1043
REMARK 3 S31: 0.7266 S32: 0.2125 S33: 0.3527
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1094 A 1101
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9315 -55.6010 12.9640
REMARK 3 T TENSOR
REMARK 3 T11: 0.4562 T22: 0.1950
REMARK 3 T33: 0.6100 T12: 0.0590
REMARK 3 T13: -0.1223 T23: 0.0722
REMARK 3 L TENSOR
REMARK 3 L11: 11.3951 L22: 32.8026
REMARK 3 L33: 15.6122 L12: -14.2936
REMARK 3 L13: 8.2104 L23: 1.7017
REMARK 3 S TENSOR
REMARK 3 S11: 1.4333 S12: 0.4974 S13: -0.6457
REMARK 3 S21: -1.9857 S22: -0.4732 S23: 0.2107
REMARK 3 S31: 0.8320 S32: 0.4045 S33: -0.9601
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1102 A 1106
REMARK 3 ORIGIN FOR THE GROUP (A): 11.8641 -47.5550 13.4572
REMARK 3 T TENSOR
REMARK 3 T11: 0.3548 T22: 0.1207
REMARK 3 T33: 0.5447 T12: 0.0913
REMARK 3 T13: -0.1500 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 44.0898 L22: 40.5722
REMARK 3 L33: 16.1501 L12: 7.5080
REMARK 3 L13: -6.9520 L23: -11.0641
REMARK 3 S TENSOR
REMARK 3 S11: -0.2723 S12: -0.4155 S13: -1.6832
REMARK 3 S21: -1.7480 S22: 0.1661 S23: 0.4682
REMARK 3 S31: 0.5312 S32: 0.0561 S33: 0.1062
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: 1. A SODIUM ION IS MODELLED BASED ON
REMARK 3 CRYSTALLIZATION CONDITION AND COORDINATION GEOMETRY. SODIUM ION
REMARK 3 IS COORDINATED IN AN OCTAHEDRAL GEOMETRY TO OD1 OF ASP52, OG OF
REMARK 3 SER 91 AND THREE WATER MOLECULES OF HOH2529, HOH2552 AND
REMARK 3 HOH2579. 2. THERE IS SOME UNKNOWN AND UNMODELLED DENSITY LOCATED
REMARK 3 NEAR THE PHENOL RING OF THE ZMA LIGAND, WHICH LIKELY REPRESENT
REMARK 3 AN ALTERNATIVE CONFORMATION OF THIS FLEXIBLE MOIETY. 3.
REMARK 3 DISORDERED LIPIDS INCLUDING OLA-2417, OLA-2419, OLC-2423, OLC-
REMARK 3 2427, OLC-2428 COULD REPRESENT FRAGMENTS OF PHOSPHOLIPID,
REMARK 3 CHOLESTEROL OR 1-OLEOYL-RAC-GLYCEROL.
REMARK 4
REMARK 4 4EIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071676.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-11; 10-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 55
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 23-ID-D; 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0330; 1.0330
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; MARMOSAIC
REMARK 200 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44413
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 29.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.81000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3EML
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-28% (V/V) PEG 400, 0.04-0.06M
REMARK 280 SODIUM THIOCYANATE, 2% (V/V) 2,5-HEXANEDIOL, 100MM SODIUM
REMARK 280 CITRATE, PH 5.0, LIPID CUBIC PHASE (LCP), TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.15350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.15350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 19.72100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.75800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.72100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.75800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.15350
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.72100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.75800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.15350
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.72100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.75800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED
REMARK 300 BY THE TWO FOLD AXIS:-X,Y,-Z+1/2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -24
REMARK 465 LYS A -23
REMARK 465 THR A -22
REMARK 465 ILE A -21
REMARK 465 ILE A -20
REMARK 465 ALA A -19
REMARK 465 LEU A -18
REMARK 465 SER A -17
REMARK 465 TYR A -16
REMARK 465 ILE A -15
REMARK 465 PHE A -14
REMARK 465 CYS A -13
REMARK 465 LEU A -12
REMARK 465 VAL A -11
REMARK 465 PHE A -10
REMARK 465 ALA A -9
REMARK 465 ASP A -8
REMARK 465 TYR A -7
REMARK 465 LYS A -6
REMARK 465 ASP A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 ALA A 1043
REMARK 465 THR A 1044
REMARK 465 PRO A 1045
REMARK 465 PRO A 1046
REMARK 465 LYS A 1047
REMARK 465 LEU A 1048
REMARK 465 GLU A 1049
REMARK 465 ASP A 1050
REMARK 465 LYS A 1051
REMARK 465 SER A 1052
REMARK 465 PRO A 1053
REMARK 465 ASP A 1054
REMARK 465 SER A 1055
REMARK 465 PRO A 1056
REMARK 465 GLU A 1057
REMARK 465 LEU A 308
REMARK 465 ARG A 309
REMARK 465 GLN A 310
REMARK 465 GLN A 311
REMARK 465 GLU A 312
REMARK 465 PRO A 313
REMARK 465 PHE A 314
REMARK 465 LYS A 315
REMARK 465 ALA A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 148 OE1 NE2
REMARK 470 GLU A 161 CG CD OE1 OE2
REMARK 470 LYS A1042 CD CE NZ
REMARK 470 MET A1058 CG SD CE
REMARK 470 LYS A1059 CG CD CE NZ
REMARK 470 ARG A 220 CD NE CZ NH1 NH2
REMARK 470 ARG A 293 CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 58 -53.24 -122.64
REMARK 500 TYR A1101 -54.84 -126.06
REMARK 500 HIS A 306 -71.44 -106.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLA A 2407
REMARK 610 OLA A 2408
REMARK 610 OLA A 2409
REMARK 610 OLA A 2410
REMARK 610 OLA A 2411
REMARK 610 OLA A 2412
REMARK 610 OLA A 2413
REMARK 610 OLA A 2414
REMARK 610 OLA A 2415
REMARK 610 OLA A 2416
REMARK 610 OLA A 2419
REMARK 610 OLA A 2420
REMARK 610 OLA A 2421
REMARK 610 OLC A 2422
REMARK 610 OLC A 2423
REMARK 610 OLC A 2424
REMARK 610 OLC A 2425
REMARK 610 OLB A 2426
REMARK 610 OLC A 2427
REMARK 610 OLC A 2428
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 NA A2402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 52 OD1
REMARK 620 2 SER A 91 OG 125.5
REMARK 620 3 HOH A2529 O 107.1 122.9
REMARK 620 4 HOH A2552 O 84.9 115.1 87.8
REMARK 620 5 HOH A2579 O 78.1 72.1 102.0 162.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMA A 2401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 2402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 2403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 2404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 2405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2413
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2415
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2416
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2417
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2418
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2419
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2420
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2421
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2422
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2423
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2424
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2425
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLB A 2426
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2427
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2428
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 2430
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EML RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CHIMERIC PROTEIN OF A2AAR-T4L IN COMPLEX
REMARK 900 WITH ZM241385
REMARK 900 RELATED ID: GPCR-6 RELATED DB: TARGETTRACK
DBREF 4EIY A 2 208 UNP P29274 AA2AR_HUMAN 2 208
DBREF 4EIY A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128
DBREF 4EIY A 219 316 UNP P29274 AA2AR_HUMAN 219 316
SEQADV 4EIY MET A -24 UNP P29274 EXPRESSION TAG
SEQADV 4EIY LYS A -23 UNP P29274 EXPRESSION TAG
SEQADV 4EIY THR A -22 UNP P29274 EXPRESSION TAG
SEQADV 4EIY ILE A -21 UNP P29274 EXPRESSION TAG
SEQADV 4EIY ILE A -20 UNP P29274 EXPRESSION TAG
SEQADV 4EIY ALA A -19 UNP P29274 EXPRESSION TAG
SEQADV 4EIY LEU A -18 UNP P29274 EXPRESSION TAG
SEQADV 4EIY SER A -17 UNP P29274 EXPRESSION TAG
SEQADV 4EIY TYR A -16 UNP P29274 EXPRESSION TAG
SEQADV 4EIY ILE A -15 UNP P29274 EXPRESSION TAG
SEQADV 4EIY PHE A -14 UNP P29274 EXPRESSION TAG
SEQADV 4EIY CYS A -13 UNP P29274 EXPRESSION TAG
SEQADV 4EIY LEU A -12 UNP P29274 EXPRESSION TAG
SEQADV 4EIY VAL A -11 UNP P29274 EXPRESSION TAG
SEQADV 4EIY PHE A -10 UNP P29274 EXPRESSION TAG
SEQADV 4EIY ALA A -9 UNP P29274 EXPRESSION TAG
SEQADV 4EIY ASP A -8 UNP P29274 EXPRESSION TAG
SEQADV 4EIY TYR A -7 UNP P29274 EXPRESSION TAG
SEQADV 4EIY LYS A -6 UNP P29274 EXPRESSION TAG
SEQADV 4EIY ASP A -5 UNP P29274 EXPRESSION TAG
SEQADV 4EIY ASP A -4 UNP P29274 EXPRESSION TAG
SEQADV 4EIY ASP A -3 UNP P29274 EXPRESSION TAG
SEQADV 4EIY ASP A -2 UNP P29274 EXPRESSION TAG
SEQADV 4EIY GLY A -1 UNP P29274 EXPRESSION TAG
SEQADV 4EIY ALA A 0 UNP P29274 EXPRESSION TAG
SEQADV 4EIY PRO A 1 UNP P29274 EXPRESSION TAG
SEQADV 4EIY TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 4EIY ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 4EIY LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION
SEQADV 4EIY HIS A 317 UNP P29274 EXPRESSION TAG
SEQADV 4EIY HIS A 318 UNP P29274 EXPRESSION TAG
SEQADV 4EIY HIS A 319 UNP P29274 EXPRESSION TAG
SEQADV 4EIY HIS A 320 UNP P29274 EXPRESSION TAG
SEQADV 4EIY HIS A 321 UNP P29274 EXPRESSION TAG
SEQADV 4EIY HIS A 322 UNP P29274 EXPRESSION TAG
SEQADV 4EIY HIS A 323 UNP P29274 EXPRESSION TAG
SEQADV 4EIY HIS A 324 UNP P29274 EXPRESSION TAG
SEQADV 4EIY HIS A 325 UNP P29274 EXPRESSION TAG
SEQADV 4EIY HIS A 326 UNP P29274 EXPRESSION TAG
SEQRES 1 A 447 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU
SEQRES 2 A 447 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO
SEQRES 3 A 447 PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU LEU
SEQRES 4 A 447 ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL
SEQRES 5 A 447 CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN VAL
SEQRES 6 A 447 THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP ILE
SEQRES 7 A 447 ALA VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR ILE
SEQRES 8 A 447 SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE
SEQRES 9 A 447 ILE ALA CYS PHE VAL LEU VAL LEU THR GLN SER SER ILE
SEQRES 10 A 447 PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA
SEQRES 11 A 447 ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR GLY
SEQRES 12 A 447 THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL LEU
SEQRES 13 A 447 SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP ASN
SEQRES 14 A 447 ASN CYS GLY GLN PRO LYS GLU GLY LYS ASN HIS SER GLN
SEQRES 15 A 447 GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP
SEQRES 16 A 447 VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE PHE
SEQRES 17 A 447 ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY VAL
SEQRES 18 A 447 TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU ALA
SEQRES 19 A 447 ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU
SEQRES 20 A 447 LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS
SEQRES 21 A 447 ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA
SEQRES 22 A 447 GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO
SEQRES 23 A 447 ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP
SEQRES 24 A 447 ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA
SEQRES 25 A 447 ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU
SEQRES 26 A 447 GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR
SEQRES 27 A 447 LEU GLU ARG ALA ARG SER THR LEU GLN LYS GLU VAL HIS
SEQRES 28 A 447 ALA ALA LYS SER LEU ALA ILE ILE VAL GLY LEU PHE ALA
SEQRES 29 A 447 LEU CYS TRP LEU PRO LEU HIS ILE ILE ASN CYS PHE THR
SEQRES 30 A 447 PHE PHE CYS PRO ASP CYS SER HIS ALA PRO LEU TRP LEU
SEQRES 31 A 447 MET TYR LEU ALA ILE VAL LEU SER HIS THR ASN SER VAL
SEQRES 32 A 447 VAL ASN PRO PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE
SEQRES 33 A 447 ARG GLN THR PHE ARG LYS ILE ILE ARG SER HIS VAL LEU
SEQRES 34 A 447 ARG GLN GLN GLU PRO PHE LYS ALA HIS HIS HIS HIS HIS
SEQRES 35 A 447 HIS HIS HIS HIS HIS
HET ZMA A2401 25
HET NA A2402 1
HET CLR A2403 28
HET CLR A2404 28
HET CLR A2405 28
HET OLA A2406 20
HET OLA A2407 15
HET OLA A2408 11
HET OLA A2409 19
HET OLA A2410 11
HET OLA A2411 9
HET OLA A2412 8
HET OLA A2413 10
HET OLA A2414 9
HET OLA A2415 12
HET OLA A2416 18
HET OLA A2417 20
HET OLA A2418 20
HET OLA A2419 15
HET OLA A2420 15
HET OLA A2421 19
HET OLC A2422 17
HET OLC A2423 15
HET OLC A2424 22
HET OLC A2425 17
HET OLB A2426 18
HET OLC A2427 16
HET OLC A2428 21
HET PEG A2429 7
HET PEG A2430 7
HETNAM ZMA 4-{2-[(7-AMINO-2-FURAN-2-YL[1,2,4]TRIAZOLO[1,5-A][1,3,
HETNAM 2 ZMA 5]TRIAZIN-5-YL)AMINO]ETHYL}PHENOL
HETNAM NA SODIUM ION
HETNAM CLR CHOLESTEROL
HETNAM OLA OLEIC ACID
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 ZMA C16 H15 N7 O2
FORMUL 3 NA NA 1+
FORMUL 4 CLR 3(C27 H46 O)
FORMUL 7 OLA 16(C18 H34 O2)
FORMUL 23 OLC 6(C21 H40 O4)
FORMUL 27 OLB C21 H40 O4
FORMUL 30 PEG 2(C4 H10 O3)
FORMUL 32 HOH *177(H2 O)
HELIX 1 1 PRO A 1 ASN A 34 1 34
HELIX 2 2 SER A 35 GLN A 38 5 4
HELIX 3 3 ASN A 39 LEU A 58 1 20
HELIX 4 4 LEU A 58 THR A 68 1 11
HELIX 5 5 CYS A 74 ILE A 108 1 35
HELIX 6 6 ILE A 108 VAL A 116 1 9
HELIX 7 7 THR A 117 LEU A 137 1 21
HELIX 8 8 THR A 138 GLY A 142 5 5
HELIX 9 9 LYS A 150 GLN A 157 1 8
HELIX 10 10 LEU A 167 VAL A 172 1 6
HELIX 11 11 PRO A 173 PHE A 180 1 8
HELIX 12 12 VAL A 186 LYS A 1019 1 42
HELIX 13 13 ASN A 1022 LYS A 1042 1 21
HELIX 14 14 LYS A 1059 GLU A 1081 1 23
HELIX 15 15 LYS A 1083 GLN A 1093 1 11
HELIX 16 16 GLN A 1093 TYR A 1101 1 9
HELIX 17 17 TYR A 1101 CYS A 259 1 47
HELIX 18 18 PRO A 266 ILE A 292 1 27
HELIX 19 19 ILE A 292 HIS A 306 1 15
SHEET 1 A 2 CYS A 71 ALA A 73 0
SHEET 2 A 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72
SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.10
SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03
SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.00
SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.05
LINK OD1 ASP A 52 NA NA A2402 1555 1555 2.45
LINK OG SER A 91 NA NA A2402 1555 1555 2.54
LINK NA NA A2402 O HOH A2529 1555 1555 2.44
LINK NA NA A2402 O HOH A2552 1555 1555 2.20
LINK NA NA A2402 O HOH A2579 1555 1555 2.60
SITE 1 AC1 13 LEU A 85 PHE A 168 GLU A 169 MET A 177
SITE 2 AC1 13 TRP A 246 LEU A 249 HIS A 250 ASN A 253
SITE 3 AC1 13 MET A 270 HOH A2521 HOH A2524 HOH A2585
SITE 4 AC1 13 HOH A2668
SITE 1 AC2 5 ASP A 52 SER A 91 HOH A2529 HOH A2552
SITE 2 AC2 5 HOH A2579
SITE 1 AC3 7 ALA A 72 ALA A 73 GLY A 76 ILE A 80
SITE 2 AC3 7 CLR A2405 OLC A2424 OLC A2427
SITE 1 AC4 5 LEU A 247 PRO A 248 CYS A 262 SER A 263
SITE 2 AC4 5 OLA A2409
SITE 1 AC5 9 LEU A 187 CYS A 254 PHE A 255 PHE A 258
SITE 2 AC5 9 CLR A2403 OLA A2409 OLC A2424 OLC A2427
SITE 3 AC5 9 HOH A2603
SITE 1 AC6 5 THR A 65 THR A 68 OLA A2408 OLC A2424
SITE 2 AC6 5 HOH A2657
SITE 1 AC7 1 HIS A 264
SITE 1 AC8 3 ILE A 10 OLA A2406 OLA A2420
SITE 1 AC9 5 PHE A 255 CYS A 262 CLR A2404 CLR A2405
SITE 2 AC9 5 OLC A2424
SITE 1 BC1 4 ILE A 3 SER A 7 THR A 11 HOH A2667
SITE 1 BC2 3 PHE A 44 ALA A 97 HOH A2671
SITE 1 BC3 1 HOH A2611
SITE 1 BC4 3 LEU A 198 ARG A 199 LEU A 202
SITE 1 BC5 4 LEU A 19 LEU A 22 TRP A 29 VAL A 307
SITE 1 BC6 5 GLY A 5 SER A 6 TYR A 271 VAL A 275
SITE 2 BC6 5 HOH A2504
SITE 1 BC7 1 LEU A 192
SITE 1 BC8 3 PHE A 133 MET A 140 OLC A2425
SITE 1 BC9 2 TYR A 290 ARG A 291
SITE 1 CC1 2 OLA A2408 HOH A2605
SITE 1 CC2 4 TRP A 32 VAL A 229 LYS A 233 HOH A2673
SITE 1 CC3 6 TYR A 179 PHE A 258 OLC A2423 OLC A2425
SITE 2 CC3 6 OLC A2427 HOH A2600
SITE 1 CC4 2 OLC A2422 OLC A2427
SITE 1 CC5 9 PRO A 61 THR A 65 PHE A 70 CLR A2403
SITE 2 CC5 9 CLR A2405 OLA A2406 OLA A2409 HOH A2657
SITE 3 CC5 9 HOH A2674
SITE 1 CC6 6 MET A 140 LEU A 141 TYR A 179 ALA A 184
SITE 2 CC6 6 OLA A2418 OLC A2422
SITE 1 CC7 4 CYS A 28 VAL A 31 TRP A 32 ARG A 205
SITE 1 CC8 5 PHE A 258 CLR A2403 CLR A2405 OLC A2422
SITE 2 CC8 5 OLC A2423
SITE 1 CC9 4 TYR A 43 VAL A 46 PHE A 83 TRP A 129
SITE 1 DC1 1 ARG A 120
CRYST1 39.442 179.516 140.307 90.00 90.00 90.00 C 2 2 21 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 0.025354 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005571 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007127 0.00000
(ATOM LINES ARE NOT SHOWN.)
END