HEADER TRANSFERASE 19-DEC-07 3BPR
TITLE CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF THE PROTO-ONCOGENE TYROSINE-
TITLE 2 PROTEIN KINASE MER IN COMPLEX WITH INHIBITOR C52
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE MER;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN: RESIDUES 574-864;
COMPND 5 SYNONYM: C-MER, RECEPTOR TYROSINE KINASE MERTK;
COMPND 6 EC: 2.7.10.1;
COMPND 7 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: MERTK, MER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC
KEYWDS ATP-BINDING, DISEASE MUTATION, GLYCOPROTEIN, KINASE, NUCLEOTIDE-
KEYWDS 2 BINDING, PHOSPHORYLATION, PROTO-ONCOGENE, RECEPTOR, RETINITIS
KEYWDS 3 PIGMENTOSA, SENSORY TRANSDUCTION, TRANSFERASE, TYROSINE-PROTEIN
KEYWDS 4 KINASE, VISION, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 5 SGC, IMMUNOGLOBULIN DOMAIN, MEMBRANE, PHOSPHOPROTEIN, POLYMORPHISM,
KEYWDS 6 TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WALKER,X.HUANG,P.J.FINERTY JR,J.WEIGELT,C.H.ARROWSMITH,
AUTHOR 2 A.M.EDWARDS,A.BOCHKAREV,S.DHE-PAGANON,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (SGC)
REVDAT 4 30-AUG-23 3BPR 1 REMARK SEQADV LINK
REVDAT 3 19-MAY-10 3BPR 1 JRNL
REVDAT 2 24-FEB-09 3BPR 1 VERSN
REVDAT 1 29-JAN-08 3BPR 0
JRNL AUTH X.HUANG,P.FINERTY,J.R.WALKER,C.BUTLER-COLE,M.VEDADI,
JRNL AUTH 2 M.SCHAPIRA,S.A.PARKER,B.E.TURK,D.A.THOMPSON,S.DHE-PAGANON
JRNL TITL STRUCTURAL INSIGHTS INTO THE INHIBITED STATES OF THE MER
JRNL TITL 2 RECEPTOR TYROSINE KINASE.
JRNL REF J.STRUCT.BIOL. V. 165 88 2009
JRNL REFN ISSN 1047-8477
JRNL PMID 19028587
JRNL DOI 10.1016/J.JSB.2008.10.003
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 35338
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) : 0.275
REMARK 3 R VALUE (WORKING SET) : 0.274
REMARK 3 FREE R VALUE : 0.301
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1889
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2433
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.3480
REMARK 3 BIN FREE R VALUE SET COUNT : 128
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8073
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 99
REMARK 3 SOLVENT ATOMS : 131
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.24000
REMARK 3 B22 (A**2) : -4.73000
REMARK 3 B33 (A**2) : 9.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.07000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.719
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.420
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.385
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 39.320
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8447 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11451 ; 1.239 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1039 ; 5.649 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 346 ;36.029 ;23.555
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1440 ;18.727 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 53 ;17.442 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1297 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6244 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3918 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5860 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 341 ; 0.144 ; 0.200
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): 24 ; 0.139 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.131 ; 0.200
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): 5208 ; 0.490 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8368 ; 0.794 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3396 ; 1.261 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3083 ; 1.787 ; 7.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 575 A 863 1
REMARK 3 1 B 576 B 863 1
REMARK 3 1 C 575 C 863 1
REMARK 3 1 D 575 D 863 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1932 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 1932 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 1932 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 1932 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 1932 ; 0.06 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 1932 ; 0.07 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 1932 ; 0.07 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 1932 ; 0.06 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
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 575 A 651
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7345 26.5431 46.1250
REMARK 3 T TENSOR
REMARK 3 T11: 0.4289 T22: 0.1048
REMARK 3 T33: 0.1977 T12: -0.1082
REMARK 3 T13: -0.1655 T23: 0.0782
REMARK 3 L TENSOR
REMARK 3 L11: 6.9280 L22: 0.5432
REMARK 3 L33: 1.5241 L12: 1.9123
REMARK 3 L13: -1.0290 L23: -0.4292
REMARK 3 S TENSOR
REMARK 3 S11: -0.1605 S12: 1.2273 S13: 0.3015
REMARK 3 S21: -0.5974 S22: 0.2387 S23: 0.5525
REMARK 3 S31: 0.0432 S32: -0.1904 S33: -0.0781
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 652 A 695
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5969 16.9927 55.3203
REMARK 3 T TENSOR
REMARK 3 T11: 0.2000 T22: -0.0793
REMARK 3 T33: -0.0300 T12: -0.0558
REMARK 3 T13: -0.0813 T23: -0.0926
REMARK 3 L TENSOR
REMARK 3 L11: 4.1966 L22: 6.1192
REMARK 3 L33: 0.5212 L12: -0.1788
REMARK 3 L13: -1.3071 L23: -0.7793
REMARK 3 S TENSOR
REMARK 3 S11: -0.1986 S12: 0.2666 S13: 0.0451
REMARK 3 S21: -0.0057 S22: 0.1954 S23: -0.3494
REMARK 3 S31: -0.3355 S32: 0.3482 S33: 0.0032
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 696 A 730
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6654 15.0156 60.6221
REMARK 3 T TENSOR
REMARK 3 T11: 0.2057 T22: -0.1862
REMARK 3 T33: -0.0422 T12: 0.0447
REMARK 3 T13: -0.0272 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 7.8239 L22: 1.6546
REMARK 3 L33: 3.5118 L12: 0.7350
REMARK 3 L13: -0.2322 L23: 1.5700
REMARK 3 S TENSOR
REMARK 3 S11: -0.1487 S12: 0.0928 S13: 0.6900
REMARK 3 S21: 0.0052 S22: -0.0460 S23: 0.1488
REMARK 3 S31: 0.2311 S32: -0.2683 S33: 0.1947
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 731 A 863
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7176 4.1692 60.3569
REMARK 3 T TENSOR
REMARK 3 T11: 0.0778 T22: -0.1179
REMARK 3 T33: -0.0245 T12: 0.0012
REMARK 3 T13: 0.0232 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 4.3754 L22: 5.0305
REMARK 3 L33: 1.7731 L12: 0.0318
REMARK 3 L13: 0.2670 L23: 0.4725
REMARK 3 S TENSOR
REMARK 3 S11: -0.1915 S12: 0.1305 S13: 0.0002
REMARK 3 S21: -0.0753 S22: 0.0412 S23: 0.4161
REMARK 3 S31: 0.1209 S32: -0.0690 S33: 0.1504
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 576 B 650
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5153 -28.4962 45.8043
REMARK 3 T TENSOR
REMARK 3 T11: 0.4215 T22: 0.0960
REMARK 3 T33: 0.0937 T12: -0.1504
REMARK 3 T13: 0.1707 T23: -0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 3.7944 L22: 3.4496
REMARK 3 L33: 4.0447 L12: -0.0830
REMARK 3 L13: 1.9789 L23: 1.1319
REMARK 3 S TENSOR
REMARK 3 S11: -0.1783 S12: 1.1959 S13: -0.4139
REMARK 3 S21: -0.7683 S22: 0.3869 S23: -0.1429
REMARK 3 S31: -0.3504 S32: 0.2649 S33: -0.2086
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 651 B 695
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0826 -19.1642 56.7720
REMARK 3 T TENSOR
REMARK 3 T11: 0.1098 T22: -0.1033
REMARK 3 T33: -0.1118 T12: -0.0595
REMARK 3 T13: 0.1105 T23: 0.1031
REMARK 3 L TENSOR
REMARK 3 L11: 5.1698 L22: 10.0002
REMARK 3 L33: 8.0577 L12: -2.6929
REMARK 3 L13: -2.2140 L23: 7.2266
REMARK 3 S TENSOR
REMARK 3 S11: -0.1477 S12: 0.1525 S13: 0.0595
REMARK 3 S21: 0.0884 S22: 0.2685 S23: 0.1174
REMARK 3 S31: 0.3582 S32: -0.4211 S33: -0.1208
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 : B 696 B 730
REMARK 3 ORIGIN FOR THE GROUP (A): 26.7082 -16.8847 59.8378
REMARK 3 T TENSOR
REMARK 3 T11: 0.2418 T22: -0.1861
REMARK 3 T33: -0.0920 T12: 0.0197
REMARK 3 T13: 0.0790 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 7.7250 L22: 2.3894
REMARK 3 L33: 2.3280 L12: -0.0965
REMARK 3 L13: -0.8347 L23: -0.7514
REMARK 3 S TENSOR
REMARK 3 S11: -0.0734 S12: 0.1228 S13: -0.1723
REMARK 3 S21: -0.2239 S22: -0.0193 S23: -0.6850
REMARK 3 S31: 0.3256 S32: -0.0149 S33: 0.0927
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 : B 731 B 863
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0485 -6.4348 60.2619
REMARK 3 T TENSOR
REMARK 3 T11: 0.1370 T22: -0.0780
REMARK 3 T33: -0.1469 T12: 0.0184
REMARK 3 T13: 0.0189 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 4.2713 L22: 5.9330
REMARK 3 L33: 0.5370 L12: -0.2225
REMARK 3 L13: 0.2572 L23: -0.2180
REMARK 3 S TENSOR
REMARK 3 S11: -0.1766 S12: 0.0472 S13: 0.0920
REMARK 3 S21: -0.2241 S22: 0.0137 S23: -0.3998
REMARK 3 S31: -0.0085 S32: 0.0401 S33: 0.1629
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 575 C 659
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6033 -36.6096 14.4901
REMARK 3 T TENSOR
REMARK 3 T11: 0.0891 T22: 0.1464
REMARK 3 T33: 0.2843 T12: 0.1125
REMARK 3 T13: -0.1451 T23: -0.1094
REMARK 3 L TENSOR
REMARK 3 L11: 3.3086 L22: 2.3245
REMARK 3 L33: 5.0719 L12: 0.3806
REMARK 3 L13: -0.7179 L23: 0.6768
REMARK 3 S TENSOR
REMARK 3 S11: -0.1563 S12: -1.0723 S13: 0.3240
REMARK 3 S21: 0.7800 S22: 0.3100 S23: -0.4710
REMARK 3 S31: 0.0475 S32: 0.2051 S33: -0.1537
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 : C 661 C 674
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8451 -39.1546 15.6566
REMARK 3 T TENSOR
REMARK 3 T11: 0.0353 T22: 0.4391
REMARK 3 T33: 0.2278 T12: 0.1138
REMARK 3 T13: -0.0864 T23: -0.0795
REMARK 3 L TENSOR
REMARK 3 L11: 1.6518 L22: 3.6087
REMARK 3 L33: 0.0456 L12: 1.9695
REMARK 3 L13: 0.1775 L23: 0.3944
REMARK 3 S TENSOR
REMARK 3 S11: -0.2064 S12: -0.7782 S13: 0.0296
REMARK 3 S21: 0.5435 S22: 0.4838 S23: 0.0258
REMARK 3 S31: 2.0860 S32: -0.7405 S33: -0.2774
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 : C 675 C 731
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6497 -50.4095 -1.7062
REMARK 3 T TENSOR
REMARK 3 T11: -0.1148 T22: -0.1126
REMARK 3 T33: -0.0115 T12: -0.0096
REMARK 3 T13: -0.0427 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 8.2426 L22: 4.2768
REMARK 3 L33: 1.6864 L12: 1.5296
REMARK 3 L13: -0.5617 L23: -1.2192
REMARK 3 S TENSOR
REMARK 3 S11: -0.2970 S12: 0.1354 S13: 0.2665
REMARK 3 S21: -0.1048 S22: 0.0814 S23: -0.0574
REMARK 3 S31: -0.2162 S32: -0.1138 S33: 0.2157
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 : C 732 C 863
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5446 -59.0955 -0.0534
REMARK 3 T TENSOR
REMARK 3 T11: -0.1970 T22: -0.0137
REMARK 3 T33: 0.0724 T12: -0.0153
REMARK 3 T13: 0.0075 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 3.8169 L22: 6.5934
REMARK 3 L33: 1.3594 L12: 0.3958
REMARK 3 L13: -0.0183 L23: -1.1082
REMARK 3 S TENSOR
REMARK 3 S11: -0.1301 S12: -0.1371 S13: -0.3533
REMARK 3 S21: 0.1216 S22: -0.0413 S23: -0.3995
REMARK 3 S31: -0.0159 S32: 0.1223 S33: 0.1714
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 : D 575 D 650
REMARK 3 ORIGIN FOR THE GROUP (A): 56.5488 -45.9901 -14.0190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0667 T22: 0.1687
REMARK 3 T33: 0.4376 T12: -0.1259
REMARK 3 T13: 0.1516 T23: -0.0659
REMARK 3 L TENSOR
REMARK 3 L11: 3.8574 L22: 2.4959
REMARK 3 L33: 4.5402 L12: 1.2887
REMARK 3 L13: 1.9067 L23: 1.3094
REMARK 3 S TENSOR
REMARK 3 S11: -0.0626 S12: 1.2187 S13: -0.4007
REMARK 3 S21: -0.5931 S22: 0.4802 S23: -0.1721
REMARK 3 S31: -0.0883 S32: 0.5453 S33: -0.4177
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 : D 651 D 695
REMARK 3 ORIGIN FOR THE GROUP (A): 52.3149 -36.3751 -4.3460
REMARK 3 T TENSOR
REMARK 3 T11: -0.1321 T22: -0.0268
REMARK 3 T33: 0.1438 T12: -0.0410
REMARK 3 T13: 0.0923 T23: 0.1019
REMARK 3 L TENSOR
REMARK 3 L11: 3.6191 L22: 9.5066
REMARK 3 L33: 6.1570 L12: -0.5932
REMARK 3 L13: 0.6169 L23: 6.1909
REMARK 3 S TENSOR
REMARK 3 S11: -0.2382 S12: 0.2239 S13: -0.2526
REMARK 3 S21: -0.0831 S22: 0.1361 S23: 0.3836
REMARK 3 S31: 0.2708 S32: -0.2596 S33: 0.1022
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 : D 696 D 730
REMARK 3 ORIGIN FOR THE GROUP (A): 66.0837 -34.2500 -0.2647
REMARK 3 T TENSOR
REMARK 3 T11: -0.0839 T22: -0.0689
REMARK 3 T33: 0.0129 T12: 0.0296
REMARK 3 T13: 0.0560 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 8.5072 L22: 3.6332
REMARK 3 L33: 2.7624 L12: -0.1961
REMARK 3 L13: -1.4313 L23: -0.3907
REMARK 3 S TENSOR
REMARK 3 S11: -0.1426 S12: 0.1305 S13: -0.6734
REMARK 3 S21: -0.0612 S22: 0.0229 S23: -0.0677
REMARK 3 S31: 0.0665 S32: 0.3490 S33: 0.1197
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 : D 731 D 863
REMARK 3 ORIGIN FOR THE GROUP (A): 68.4521 -23.8130 0.1384
REMARK 3 T TENSOR
REMARK 3 T11: -0.2155 T22: -0.0209
REMARK 3 T33: 0.0153 T12: -0.0405
REMARK 3 T13: -0.0043 T23: -0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 4.6315 L22: 6.2080
REMARK 3 L33: 1.5880 L12: -0.6526
REMARK 3 L13: -0.3947 L23: -1.1730
REMARK 3 S TENSOR
REMARK 3 S11: -0.1913 S12: 0.1459 S13: 0.0674
REMARK 3 S21: -0.0017 S22: -0.0009 S23: -0.3036
REMARK 3 S31: -0.0178 S32: 0.0754 S33: 0.1922
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS, ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS
REMARK 4
REMARK 4 3BPR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000045814.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : CRYO-COOLED SI(111) DOUBLE-
REMARK 200 CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37537
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.15000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.53000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 2P0C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: COMPOUND C52 (50 MM IN DMSO) WAS ADDED
REMARK 280 TO 8 MG/ML MER PROTEIN TO THE FINAL CONCENTRATION OF 2.5 MM. THE
REMARK 280 MIXTURE WAS ROCKED AT 277 K OVERNIGHT AND FURTHER CONCENTRATED
REMARK 280 TO ABOUT 35 MG/ML. CRYSTALS WERE GROWN BY MIXING 2 MICROLITERS
REMARK 280 OF MER INHIBITOR SOLUTION AND 2 MICROLITERS OF RESERVOIR
REMARK 280 SOLUTION (100 MM TRIS-HCL PH 8.5, 3.64 M NACL) AT 287 K USING
REMARK 280 THE HANGING-DROP VAPOR-DIFFUSION METHOD. CRYSTALS WERE CRYO-
REMARK 280 PROTECTED WITH A SOLUTION COMPOSED OF GLYCEROL, ETHYLENE GLYCOL,
REMARK 280 GLUCOSE, AND FRUCTOSE., VAPOR DIFFUSION, HANGING DROP, PH 8.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 45.85100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 350
REMARK 350 BIOMOLECULE: 4
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: 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 MET A 552
REMARK 465 GLY A 553
REMARK 465 SER A 554
REMARK 465 SER A 555
REMARK 465 HIS A 556
REMARK 465 HIS A 557
REMARK 465 HIS A 558
REMARK 465 HIS A 559
REMARK 465 HIS A 560
REMARK 465 HIS A 561
REMARK 465 SER A 562
REMARK 465 SER A 563
REMARK 465 GLY A 564
REMARK 465 LEU A 565
REMARK 465 VAL A 566
REMARK 465 PRO A 567
REMARK 465 ARG A 568
REMARK 465 GLY A 569
REMARK 465 SER A 570
REMARK 465 GLU A 571
REMARK 465 GLU A 572
REMARK 465 LEU A 573
REMARK 465 GLN A 574
REMARK 465 LEU A 623
REMARK 465 ASP A 624
REMARK 465 ASN A 625
REMARK 465 SER A 626
REMARK 465 SER A 627
REMARK 465 GLN A 628
REMARK 465 GLN A 662
REMARK 465 GLY A 663
REMARK 465 ILE A 664
REMARK 465 PRO A 665
REMARK 465 LYS A 666
REMARK 465 LYS A 746
REMARK 465 LYS A 747
REMARK 465 ILE A 748
REMARK 465 TYR A 749
REMARK 465 SER A 750
REMARK 465 GLY A 751
REMARK 465 ASP A 752
REMARK 465 TYR A 753
REMARK 465 TYR A 754
REMARK 465 ARG A 755
REMARK 465 GLN A 756
REMARK 465 GLY A 757
REMARK 465 ARG A 758
REMARK 465 ILE A 759
REMARK 465 ALA A 760
REMARK 465 LYS A 761
REMARK 465 MET A 762
REMARK 465 VAL A 864
REMARK 465 MET B 552
REMARK 465 GLY B 553
REMARK 465 SER B 554
REMARK 465 SER B 555
REMARK 465 HIS B 556
REMARK 465 HIS B 557
REMARK 465 HIS B 558
REMARK 465 HIS B 559
REMARK 465 HIS B 560
REMARK 465 HIS B 561
REMARK 465 SER B 562
REMARK 465 SER B 563
REMARK 465 GLY B 564
REMARK 465 LEU B 565
REMARK 465 VAL B 566
REMARK 465 PRO B 567
REMARK 465 ARG B 568
REMARK 465 GLY B 569
REMARK 465 SER B 570
REMARK 465 GLU B 571
REMARK 465 GLU B 572
REMARK 465 LEU B 573
REMARK 465 GLN B 574
REMARK 465 ASN B 575
REMARK 465 GLY B 596
REMARK 465 ASP B 624
REMARK 465 ASN B 625
REMARK 465 SER B 626
REMARK 465 SER B 627
REMARK 465 GLN B 628
REMARK 465 ARG B 629
REMARK 465 GLU B 630
REMARK 465 SER B 660
REMARK 465 SER B 661
REMARK 465 GLN B 662
REMARK 465 GLY B 663
REMARK 465 ILE B 664
REMARK 465 PRO B 665
REMARK 465 LYS B 666
REMARK 465 LYS B 746
REMARK 465 LYS B 747
REMARK 465 ILE B 748
REMARK 465 TYR B 749
REMARK 465 SER B 750
REMARK 465 GLY B 751
REMARK 465 ASP B 752
REMARK 465 TYR B 753
REMARK 465 TYR B 754
REMARK 465 ARG B 755
REMARK 465 GLN B 756
REMARK 465 GLY B 757
REMARK 465 ARG B 758
REMARK 465 ILE B 759
REMARK 465 ALA B 760
REMARK 465 LYS B 761
REMARK 465 MET B 762
REMARK 465 VAL B 864
REMARK 465 MET C 552
REMARK 465 GLY C 553
REMARK 465 SER C 554
REMARK 465 SER C 555
REMARK 465 HIS C 556
REMARK 465 HIS C 557
REMARK 465 HIS C 558
REMARK 465 HIS C 559
REMARK 465 HIS C 560
REMARK 465 HIS C 561
REMARK 465 SER C 562
REMARK 465 SER C 563
REMARK 465 GLY C 564
REMARK 465 LEU C 565
REMARK 465 VAL C 566
REMARK 465 PRO C 567
REMARK 465 ARG C 568
REMARK 465 GLY C 569
REMARK 465 SER C 570
REMARK 465 GLU C 571
REMARK 465 GLU C 572
REMARK 465 LEU C 573
REMARK 465 GLN C 574
REMARK 465 LEU C 623
REMARK 465 ASP C 624
REMARK 465 ASN C 625
REMARK 465 SER C 626
REMARK 465 SER C 627
REMARK 465 GLN C 628
REMARK 465 ARG C 629
REMARK 465 GLU C 630
REMARK 465 SER C 660
REMARK 465 GLY C 663
REMARK 465 ILE C 664
REMARK 465 PRO C 665
REMARK 465 LYS C 666
REMARK 465 LYS C 746
REMARK 465 LYS C 747
REMARK 465 ILE C 748
REMARK 465 TYR C 749
REMARK 465 SER C 750
REMARK 465 GLY C 751
REMARK 465 ASP C 752
REMARK 465 TYR C 753
REMARK 465 TYR C 754
REMARK 465 ARG C 755
REMARK 465 GLN C 756
REMARK 465 GLY C 757
REMARK 465 ARG C 758
REMARK 465 ILE C 759
REMARK 465 ALA C 760
REMARK 465 LYS C 761
REMARK 465 MET C 762
REMARK 465 VAL C 864
REMARK 465 MET D 552
REMARK 465 GLY D 553
REMARK 465 SER D 554
REMARK 465 SER D 555
REMARK 465 HIS D 556
REMARK 465 HIS D 557
REMARK 465 HIS D 558
REMARK 465 HIS D 559
REMARK 465 HIS D 560
REMARK 465 HIS D 561
REMARK 465 SER D 562
REMARK 465 SER D 563
REMARK 465 GLY D 564
REMARK 465 LEU D 565
REMARK 465 VAL D 566
REMARK 465 PRO D 567
REMARK 465 ARG D 568
REMARK 465 GLY D 569
REMARK 465 SER D 570
REMARK 465 GLU D 571
REMARK 465 GLU D 572
REMARK 465 LEU D 573
REMARK 465 GLN D 574
REMARK 465 LEU D 623
REMARK 465 ASP D 624
REMARK 465 ASN D 625
REMARK 465 SER D 626
REMARK 465 SER D 627
REMARK 465 GLN D 628
REMARK 465 ARG D 629
REMARK 465 GLU D 630
REMARK 465 GLN D 662
REMARK 465 GLY D 663
REMARK 465 ILE D 664
REMARK 465 PRO D 665
REMARK 465 LYS D 666
REMARK 465 LYS D 746
REMARK 465 LYS D 747
REMARK 465 ILE D 748
REMARK 465 TYR D 749
REMARK 465 SER D 750
REMARK 465 GLY D 751
REMARK 465 ASP D 752
REMARK 465 TYR D 753
REMARK 465 TYR D 754
REMARK 465 ARG D 755
REMARK 465 GLN D 756
REMARK 465 GLY D 757
REMARK 465 ARG D 758
REMARK 465 ILE D 759
REMARK 465 ALA D 760
REMARK 465 LYS D 761
REMARK 465 MET D 762
REMARK 465 VAL D 864
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASN A 575 CG OD1 ND2
REMARK 470 LYS A 576 CD CE NZ
REMARK 470 LEU A 577 CB CG CD1 CD2
REMARK 470 GLU A 578 CG CD OE1 OE2
REMARK 470 LYS A 591 CD CE NZ
REMARK 470 GLU A 597 CG CD OE1 OE2
REMARK 470 PHE A 598 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 607 CG CD CE NZ
REMARK 470 LYS A 622 CG CD CE NZ
REMARK 470 ILE A 631 CD1
REMARK 470 GLU A 632 CG CD OE1 OE2
REMARK 470 GLU A 633 CG CD OE1 OE2
REMARK 470 LEU A 635 CG CD1 CD2
REMARK 470 LYS A 642 CE NZ
REMARK 470 ARG A 651 CG CD NE CZ NH1 NH2
REMARK 470 SER A 661 OG
REMARK 470 LYS A 693 CG CD CE NZ
REMARK 470 ASN A 718 CG OD1 ND2
REMARK 470 ARG A 727 NE CZ NH1 NH2
REMARK 470 ASP A 774 CG OD1 OD2
REMARK 470 ARG A 775 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 856 CG CD CE NZ
REMARK 470 GLU A 859 CD OE1 OE2
REMARK 470 LYS B 576 CG CD CE NZ
REMARK 470 LEU B 577 CB CG CD1 CD2
REMARK 470 GLU B 578 CG CD OE1 OE2
REMARK 470 ILE B 582 CG1 CG2 CD1
REMARK 470 LYS B 591 CD CE NZ
REMARK 470 GLU B 597 CG CD OE1 OE2
REMARK 470 PHE B 598 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 607 CG CD CE NZ
REMARK 470 GLU B 609 CG CD OE1 OE2
REMARK 470 LYS B 622 CG CD CE NZ
REMARK 470 LEU B 623 CG CD1 CD2
REMARK 470 ILE B 631 CD1
REMARK 470 GLU B 632 CG CD OE1 OE2
REMARK 470 ASP B 643 CG OD1 OD2
REMARK 470 MET B 659 CG SD CE
REMARK 470 LYS B 693 CG CD CE NZ
REMARK 470 ASP B 774 CG OD1 OD2
REMARK 470 ARG B 775 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 575 CG OD1 ND2
REMARK 470 LYS C 576 CD CE NZ
REMARK 470 LEU C 577 CB CG CD1 CD2
REMARK 470 GLU C 578 CG CD OE1 OE2
REMARK 470 LYS C 591 CD CE NZ
REMARK 470 LYS C 607 CG CD CE NZ
REMARK 470 ILE C 631 CD1
REMARK 470 GLU C 632 CG CD OE1 OE2
REMARK 470 GLU C 633 CG CD OE1 OE2
REMARK 470 LYS C 693 CG CD CE NZ
REMARK 470 ASP C 774 CG OD1 OD2
REMARK 470 ARG C 775 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 856 CG CD CE NZ
REMARK 470 ASN D 575 CG OD1 ND2
REMARK 470 LYS D 576 CD CE NZ
REMARK 470 LEU D 577 CB CG CD1 CD2
REMARK 470 GLU D 578 CG CD OE1 OE2
REMARK 470 LYS D 591 CD CE NZ
REMARK 470 GLU D 597 CG CD OE1 OE2
REMARK 470 PHE D 598 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE D 631 CD1
REMARK 470 GLU D 632 CG CD OE1 OE2
REMARK 470 GLU D 633 CG CD OE1 OE2
REMARK 470 LYS D 693 CG CD CE NZ
REMARK 470 ASP D 774 CG OD1 OD2
REMARK 470 ARG D 775 CG CD NE 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 PHE A 598 -79.34 -59.85
REMARK 500 ASP A 610 -34.12 -36.77
REMARK 500 SER A 660 96.60 -61.85
REMARK 500 THR A 690 -39.57 69.36
REMARK 500 PRO A 692 138.83 -33.44
REMARK 500 ASP A 723 47.35 -157.89
REMARK 500 ARG A 775 -14.08 80.37
REMARK 500 ASP A 824 44.05 -109.02
REMARK 500 PHE B 598 -79.34 -59.66
REMARK 500 ASP B 610 -33.64 -38.91
REMARK 500 THR B 690 -38.16 68.04
REMARK 500 PRO B 692 137.66 -35.95
REMARK 500 ASP B 723 47.49 -158.73
REMARK 500 ARG B 775 -15.75 82.51
REMARK 500 PHE C 598 -77.14 -61.55
REMARK 500 ASP C 610 -34.98 -39.91
REMARK 500 THR C 690 -36.64 69.39
REMARK 500 PRO C 692 137.97 -36.79
REMARK 500 ARG C 717 5.56 -68.79
REMARK 500 ASP C 723 49.65 -157.68
REMARK 500 ARG C 775 -17.17 82.57
REMARK 500 PHE D 598 -77.91 -60.24
REMARK 500 ASP D 610 -36.12 -39.19
REMARK 500 THR D 690 -38.45 70.48
REMARK 500 PRO D 692 136.37 -35.80
REMARK 500 ARG D 717 2.20 -69.64
REMARK 500 ASP D 723 49.26 -157.35
REMARK 500 ARG D 775 -16.09 80.58
REMARK 500 TYR D 801 65.91 60.73
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 NA B 1 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 823 OE1
REMARK 620 2 SER B 686 O 103.2
REMARK 620 3 LEU B 688 O 94.9 98.0
REMARK 620 4 PRO B 692 O 170.0 79.5 94.2
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 NA B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 133
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 134
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLP A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLP B 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLP C 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLP D 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2P0C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF THE PROTO-ONCOGENE
REMARK 900 TYROSINE-PROTEIN KINASE MER
REMARK 900 RELATED ID: 3BRB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF THE PROTO-ONCOGENE
REMARK 900 TYROSINE-PROTEIN KINASE MER IN COMPLEX WITH ADP
DBREF 3BPR A 570 864 UNP Q12866 MERTK_HUMAN 574 868
DBREF 3BPR B 570 864 UNP Q12866 MERTK_HUMAN 574 868
DBREF 3BPR C 570 864 UNP Q12866 MERTK_HUMAN 574 868
DBREF 3BPR D 570 864 UNP Q12866 MERTK_HUMAN 574 868
SEQADV 3BPR MET A 552 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR GLY A 553 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER A 554 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER A 555 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS A 556 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS A 557 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS A 558 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS A 559 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS A 560 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS A 561 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER A 562 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER A 563 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR GLY A 564 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR LEU A 565 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR VAL A 566 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR PRO A 567 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR ARG A 568 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR GLY A 569 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR MET B 552 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR GLY B 553 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER B 554 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER B 555 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS B 556 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS B 557 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS B 558 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS B 559 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS B 560 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS B 561 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER B 562 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER B 563 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR GLY B 564 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR LEU B 565 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR VAL B 566 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR PRO B 567 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR ARG B 568 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR GLY B 569 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR MET C 552 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR GLY C 553 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER C 554 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER C 555 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS C 556 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS C 557 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS C 558 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS C 559 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS C 560 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS C 561 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER C 562 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER C 563 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR GLY C 564 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR LEU C 565 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR VAL C 566 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR PRO C 567 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR ARG C 568 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR GLY C 569 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR MET D 552 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR GLY D 553 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER D 554 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER D 555 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS D 556 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS D 557 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS D 558 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS D 559 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS D 560 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR HIS D 561 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER D 562 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR SER D 563 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR GLY D 564 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR LEU D 565 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR VAL D 566 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR PRO D 567 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR ARG D 568 UNP Q12866 EXPRESSION TAG
SEQADV 3BPR GLY D 569 UNP Q12866 EXPRESSION TAG
SEQRES 1 A 313 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 313 LEU VAL PRO ARG GLY SER GLU GLU LEU GLN ASN LYS LEU
SEQRES 3 A 313 GLU ASP VAL VAL ILE ASP ARG ASN LEU LEU ILE LEU GLY
SEQRES 4 A 313 LYS ILE LEU GLY GLU GLY GLU PHE GLY SER VAL MET GLU
SEQRES 5 A 313 GLY ASN LEU LYS GLN GLU ASP GLY THR SER LEU LYS VAL
SEQRES 6 A 313 ALA VAL LYS THR MET LYS LEU ASP ASN SER SER GLN ARG
SEQRES 7 A 313 GLU ILE GLU GLU PHE LEU SER GLU ALA ALA CYS MET LYS
SEQRES 8 A 313 ASP PHE SER HIS PRO ASN VAL ILE ARG LEU LEU GLY VAL
SEQRES 9 A 313 CYS ILE GLU MET SER SER GLN GLY ILE PRO LYS PRO MET
SEQRES 10 A 313 VAL ILE LEU PRO PHE MET LYS TYR GLY ASP LEU HIS THR
SEQRES 11 A 313 TYR LEU LEU TYR SER ARG LEU GLU THR GLY PRO LYS HIS
SEQRES 12 A 313 ILE PRO LEU GLN THR LEU LEU LYS PHE MET VAL ASP ILE
SEQRES 13 A 313 ALA LEU GLY MET GLU TYR LEU SER ASN ARG ASN PHE LEU
SEQRES 14 A 313 HIS ARG ASP LEU ALA ALA ARG ASN CYS MET LEU ARG ASP
SEQRES 15 A 313 ASP MET THR VAL CYS VAL ALA ASP PHE GLY LEU SER LYS
SEQRES 16 A 313 LYS ILE TYR SER GLY ASP TYR TYR ARG GLN GLY ARG ILE
SEQRES 17 A 313 ALA LYS MET PRO VAL LYS TRP ILE ALA ILE GLU SER LEU
SEQRES 18 A 313 ALA ASP ARG VAL TYR THR SER LYS SER ASP VAL TRP ALA
SEQRES 19 A 313 PHE GLY VAL THR MET TRP GLU ILE ALA THR ARG GLY MET
SEQRES 20 A 313 THR PRO TYR PRO GLY VAL GLN ASN HIS GLU MET TYR ASP
SEQRES 21 A 313 TYR LEU LEU HIS GLY HIS ARG LEU LYS GLN PRO GLU ASP
SEQRES 22 A 313 CYS LEU ASP GLU LEU TYR GLU ILE MET TYR SER CYS TRP
SEQRES 23 A 313 ARG THR ASP PRO LEU ASP ARG PRO THR PHE SER VAL LEU
SEQRES 24 A 313 ARG LEU GLN LEU GLU LYS LEU LEU GLU SER LEU PRO ASP
SEQRES 25 A 313 VAL
SEQRES 1 B 313 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 313 LEU VAL PRO ARG GLY SER GLU GLU LEU GLN ASN LYS LEU
SEQRES 3 B 313 GLU ASP VAL VAL ILE ASP ARG ASN LEU LEU ILE LEU GLY
SEQRES 4 B 313 LYS ILE LEU GLY GLU GLY GLU PHE GLY SER VAL MET GLU
SEQRES 5 B 313 GLY ASN LEU LYS GLN GLU ASP GLY THR SER LEU LYS VAL
SEQRES 6 B 313 ALA VAL LYS THR MET LYS LEU ASP ASN SER SER GLN ARG
SEQRES 7 B 313 GLU ILE GLU GLU PHE LEU SER GLU ALA ALA CYS MET LYS
SEQRES 8 B 313 ASP PHE SER HIS PRO ASN VAL ILE ARG LEU LEU GLY VAL
SEQRES 9 B 313 CYS ILE GLU MET SER SER GLN GLY ILE PRO LYS PRO MET
SEQRES 10 B 313 VAL ILE LEU PRO PHE MET LYS TYR GLY ASP LEU HIS THR
SEQRES 11 B 313 TYR LEU LEU TYR SER ARG LEU GLU THR GLY PRO LYS HIS
SEQRES 12 B 313 ILE PRO LEU GLN THR LEU LEU LYS PHE MET VAL ASP ILE
SEQRES 13 B 313 ALA LEU GLY MET GLU TYR LEU SER ASN ARG ASN PHE LEU
SEQRES 14 B 313 HIS ARG ASP LEU ALA ALA ARG ASN CYS MET LEU ARG ASP
SEQRES 15 B 313 ASP MET THR VAL CYS VAL ALA ASP PHE GLY LEU SER LYS
SEQRES 16 B 313 LYS ILE TYR SER GLY ASP TYR TYR ARG GLN GLY ARG ILE
SEQRES 17 B 313 ALA LYS MET PRO VAL LYS TRP ILE ALA ILE GLU SER LEU
SEQRES 18 B 313 ALA ASP ARG VAL TYR THR SER LYS SER ASP VAL TRP ALA
SEQRES 19 B 313 PHE GLY VAL THR MET TRP GLU ILE ALA THR ARG GLY MET
SEQRES 20 B 313 THR PRO TYR PRO GLY VAL GLN ASN HIS GLU MET TYR ASP
SEQRES 21 B 313 TYR LEU LEU HIS GLY HIS ARG LEU LYS GLN PRO GLU ASP
SEQRES 22 B 313 CYS LEU ASP GLU LEU TYR GLU ILE MET TYR SER CYS TRP
SEQRES 23 B 313 ARG THR ASP PRO LEU ASP ARG PRO THR PHE SER VAL LEU
SEQRES 24 B 313 ARG LEU GLN LEU GLU LYS LEU LEU GLU SER LEU PRO ASP
SEQRES 25 B 313 VAL
SEQRES 1 C 313 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 313 LEU VAL PRO ARG GLY SER GLU GLU LEU GLN ASN LYS LEU
SEQRES 3 C 313 GLU ASP VAL VAL ILE ASP ARG ASN LEU LEU ILE LEU GLY
SEQRES 4 C 313 LYS ILE LEU GLY GLU GLY GLU PHE GLY SER VAL MET GLU
SEQRES 5 C 313 GLY ASN LEU LYS GLN GLU ASP GLY THR SER LEU LYS VAL
SEQRES 6 C 313 ALA VAL LYS THR MET LYS LEU ASP ASN SER SER GLN ARG
SEQRES 7 C 313 GLU ILE GLU GLU PHE LEU SER GLU ALA ALA CYS MET LYS
SEQRES 8 C 313 ASP PHE SER HIS PRO ASN VAL ILE ARG LEU LEU GLY VAL
SEQRES 9 C 313 CYS ILE GLU MET SER SER GLN GLY ILE PRO LYS PRO MET
SEQRES 10 C 313 VAL ILE LEU PRO PHE MET LYS TYR GLY ASP LEU HIS THR
SEQRES 11 C 313 TYR LEU LEU TYR SER ARG LEU GLU THR GLY PRO LYS HIS
SEQRES 12 C 313 ILE PRO LEU GLN THR LEU LEU LYS PHE MET VAL ASP ILE
SEQRES 13 C 313 ALA LEU GLY MET GLU TYR LEU SER ASN ARG ASN PHE LEU
SEQRES 14 C 313 HIS ARG ASP LEU ALA ALA ARG ASN CYS MET LEU ARG ASP
SEQRES 15 C 313 ASP MET THR VAL CYS VAL ALA ASP PHE GLY LEU SER LYS
SEQRES 16 C 313 LYS ILE TYR SER GLY ASP TYR TYR ARG GLN GLY ARG ILE
SEQRES 17 C 313 ALA LYS MET PRO VAL LYS TRP ILE ALA ILE GLU SER LEU
SEQRES 18 C 313 ALA ASP ARG VAL TYR THR SER LYS SER ASP VAL TRP ALA
SEQRES 19 C 313 PHE GLY VAL THR MET TRP GLU ILE ALA THR ARG GLY MET
SEQRES 20 C 313 THR PRO TYR PRO GLY VAL GLN ASN HIS GLU MET TYR ASP
SEQRES 21 C 313 TYR LEU LEU HIS GLY HIS ARG LEU LYS GLN PRO GLU ASP
SEQRES 22 C 313 CYS LEU ASP GLU LEU TYR GLU ILE MET TYR SER CYS TRP
SEQRES 23 C 313 ARG THR ASP PRO LEU ASP ARG PRO THR PHE SER VAL LEU
SEQRES 24 C 313 ARG LEU GLN LEU GLU LYS LEU LEU GLU SER LEU PRO ASP
SEQRES 25 C 313 VAL
SEQRES 1 D 313 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 313 LEU VAL PRO ARG GLY SER GLU GLU LEU GLN ASN LYS LEU
SEQRES 3 D 313 GLU ASP VAL VAL ILE ASP ARG ASN LEU LEU ILE LEU GLY
SEQRES 4 D 313 LYS ILE LEU GLY GLU GLY GLU PHE GLY SER VAL MET GLU
SEQRES 5 D 313 GLY ASN LEU LYS GLN GLU ASP GLY THR SER LEU LYS VAL
SEQRES 6 D 313 ALA VAL LYS THR MET LYS LEU ASP ASN SER SER GLN ARG
SEQRES 7 D 313 GLU ILE GLU GLU PHE LEU SER GLU ALA ALA CYS MET LYS
SEQRES 8 D 313 ASP PHE SER HIS PRO ASN VAL ILE ARG LEU LEU GLY VAL
SEQRES 9 D 313 CYS ILE GLU MET SER SER GLN GLY ILE PRO LYS PRO MET
SEQRES 10 D 313 VAL ILE LEU PRO PHE MET LYS TYR GLY ASP LEU HIS THR
SEQRES 11 D 313 TYR LEU LEU TYR SER ARG LEU GLU THR GLY PRO LYS HIS
SEQRES 12 D 313 ILE PRO LEU GLN THR LEU LEU LYS PHE MET VAL ASP ILE
SEQRES 13 D 313 ALA LEU GLY MET GLU TYR LEU SER ASN ARG ASN PHE LEU
SEQRES 14 D 313 HIS ARG ASP LEU ALA ALA ARG ASN CYS MET LEU ARG ASP
SEQRES 15 D 313 ASP MET THR VAL CYS VAL ALA ASP PHE GLY LEU SER LYS
SEQRES 16 D 313 LYS ILE TYR SER GLY ASP TYR TYR ARG GLN GLY ARG ILE
SEQRES 17 D 313 ALA LYS MET PRO VAL LYS TRP ILE ALA ILE GLU SER LEU
SEQRES 18 D 313 ALA ASP ARG VAL TYR THR SER LYS SER ASP VAL TRP ALA
SEQRES 19 D 313 PHE GLY VAL THR MET TRP GLU ILE ALA THR ARG GLY MET
SEQRES 20 D 313 THR PRO TYR PRO GLY VAL GLN ASN HIS GLU MET TYR ASP
SEQRES 21 D 313 TYR LEU LEU HIS GLY HIS ARG LEU LYS GLN PRO GLU ASP
SEQRES 22 D 313 CYS LEU ASP GLU LEU TYR GLU ILE MET TYR SER CYS TRP
SEQRES 23 D 313 ARG THR ASP PRO LEU ASP ARG PRO THR PHE SER VAL LEU
SEQRES 24 D 313 ARG LEU GLN LEU GLU LYS LEU LEU GLU SER LEU PRO ASP
SEQRES 25 D 313 VAL
HET OLP A 900 24
HET NA B 1 1
HET OLP B 900 24
HET CL C 133 1
HET OLP C 900 24
HET CL D 134 1
HET OLP D 900 24
HETNAM OLP 2-(2-HYDROXYETHYLAMINO)-6-(3-CHLOROANILINO)-9-
HETNAM 2 OLP ISOPROPYLPURINE
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
FORMUL 5 OLP 4(C16 H19 CL N6 O)
FORMUL 6 NA NA 1+
FORMUL 8 CL 2(CL 1-)
FORMUL 12 HOH *131(H2 O)
HELIX 1 1 ASP A 583 ASN A 585 5 3
HELIX 2 2 ILE A 631 PHE A 644 1 14
HELIX 3 3 ASP A 678 ARG A 687 1 10
HELIX 4 4 PRO A 696 ARG A 717 1 22
HELIX 5 5 ALA A 725 ARG A 727 5 3
HELIX 6 6 PRO A 763 ILE A 767 5 5
HELIX 7 7 ALA A 768 ARG A 775 1 8
HELIX 8 8 THR A 778 THR A 795 1 18
HELIX 9 9 GLN A 805 HIS A 807 5 3
HELIX 10 10 GLU A 808 HIS A 815 1 8
HELIX 11 11 LEU A 826 CYS A 836 1 11
HELIX 12 12 ASP A 840 ARG A 844 5 5
HELIX 13 13 THR A 846 LEU A 861 1 16
HELIX 14 14 ASP B 583 ASN B 585 5 3
HELIX 15 15 ILE B 631 PHE B 644 1 14
HELIX 16 16 ASP B 678 SER B 686 1 9
HELIX 17 17 PRO B 696 ARG B 717 1 22
HELIX 18 18 ALA B 725 ARG B 727 5 3
HELIX 19 19 PRO B 763 ILE B 767 5 5
HELIX 20 20 ALA B 768 ARG B 775 1 8
HELIX 21 21 THR B 778 THR B 795 1 18
HELIX 22 22 GLN B 805 HIS B 807 5 3
HELIX 23 23 GLU B 808 HIS B 815 1 8
HELIX 24 24 LEU B 826 CYS B 836 1 11
HELIX 25 25 ASP B 840 ARG B 844 5 5
HELIX 26 26 THR B 846 LEU B 861 1 16
HELIX 27 27 ASP C 583 ASN C 585 5 3
HELIX 28 28 ILE C 631 PHE C 644 1 14
HELIX 29 29 ASP C 678 SER C 686 1 9
HELIX 30 30 PRO C 696 ARG C 717 1 22
HELIX 31 31 ALA C 725 ARG C 727 5 3
HELIX 32 32 PRO C 763 ILE C 767 5 5
HELIX 33 33 ALA C 768 ARG C 775 1 8
HELIX 34 34 THR C 778 ARG C 796 1 19
HELIX 35 35 GLN C 805 HIS C 807 5 3
HELIX 36 36 GLU C 808 HIS C 815 1 8
HELIX 37 37 LEU C 826 CYS C 836 1 11
HELIX 38 38 ASP C 840 ARG C 844 5 5
HELIX 39 39 THR C 846 LEU C 861 1 16
HELIX 40 40 ASP D 583 ASN D 585 5 3
HELIX 41 41 ILE D 631 PHE D 644 1 14
HELIX 42 42 ASP D 678 ARG D 687 1 10
HELIX 43 43 PRO D 696 ARG D 717 1 22
HELIX 44 44 ALA D 725 ARG D 727 5 3
HELIX 45 45 PRO D 763 ILE D 767 5 5
HELIX 46 46 ALA D 768 ARG D 775 1 8
HELIX 47 47 THR D 778 ARG D 796 1 19
HELIX 48 48 GLN D 805 HIS D 807 5 3
HELIX 49 49 GLU D 808 HIS D 815 1 8
HELIX 50 50 LEU D 826 CYS D 836 1 11
HELIX 51 51 ASP D 840 ARG D 844 5 5
HELIX 52 52 THR D 846 LEU D 861 1 16
SHEET 1 A 5 LEU A 587 GLU A 595 0
SHEET 2 A 5 SER A 600 LYS A 607 -1 O GLU A 603 N GLY A 590
SHEET 3 A 5 SER A 613 THR A 620 -1 O VAL A 618 N MET A 602
SHEET 4 A 5 MET A 668 PRO A 672 -1 O LEU A 671 N ALA A 617
SHEET 5 A 5 GLY A 654 CYS A 656 -1 N CYS A 656 O MET A 668
SHEET 1 B 2 CYS A 729 LEU A 731 0
SHEET 2 B 2 VAL A 737 VAL A 739 -1 O CYS A 738 N MET A 730
SHEET 1 C 5 LEU B 587 GLY B 594 0
SHEET 2 C 5 SER B 600 LYS B 607 -1 O GLU B 603 N GLY B 590
SHEET 3 C 5 SER B 613 THR B 620 -1 O VAL B 618 N MET B 602
SHEET 4 C 5 MET B 668 PRO B 672 -1 O LEU B 671 N ALA B 617
SHEET 5 C 5 GLY B 654 CYS B 656 -1 N CYS B 656 O MET B 668
SHEET 1 D 2 CYS B 729 LEU B 731 0
SHEET 2 D 2 VAL B 737 VAL B 739 -1 O CYS B 738 N MET B 730
SHEET 1 E 5 LEU C 587 GLU C 595 0
SHEET 2 E 5 SER C 600 LYS C 607 -1 O GLU C 603 N GLY C 590
SHEET 3 E 5 SER C 613 THR C 620 -1 O VAL C 618 N MET C 602
SHEET 4 E 5 MET C 668 PRO C 672 -1 O LEU C 671 N ALA C 617
SHEET 5 E 5 GLY C 654 CYS C 656 -1 N CYS C 656 O MET C 668
SHEET 1 F 2 CYS C 729 LEU C 731 0
SHEET 2 F 2 VAL C 737 VAL C 739 -1 O CYS C 738 N MET C 730
SHEET 1 G 5 LEU D 587 GLU D 595 0
SHEET 2 G 5 SER D 600 LYS D 607 -1 O GLU D 603 N GLY D 590
SHEET 3 G 5 SER D 613 THR D 620 -1 O VAL D 618 N MET D 602
SHEET 4 G 5 MET D 668 PRO D 672 -1 O LEU D 671 N ALA D 617
SHEET 5 G 5 GLY D 654 CYS D 656 -1 N CYS D 656 O MET D 668
SHEET 1 H 2 CYS D 729 LEU D 731 0
SHEET 2 H 2 VAL D 737 VAL D 739 -1 O CYS D 738 N MET D 730
LINK OE1 GLU A 823 NA NA B 1 1555 1555 2.51
LINK NA NA B 1 O SER B 686 1555 1555 2.68
LINK NA NA B 1 O LEU B 688 1555 1555 2.84
LINK NA NA B 1 O PRO B 692 1555 1555 2.96
SITE 1 AC1 4 GLU A 823 SER B 686 LEU B 688 PRO B 692
SITE 1 AC2 3 PRO C 802 LEU C 819 LYS C 820
SITE 1 AC3 1 LYS D 820
SITE 1 AC4 9 HOH A 26 ALA A 617 PRO A 672 PHE A 673
SITE 2 AC4 9 MET A 674 LYS A 675 GLY A 677 ASP A 678
SITE 3 AC4 9 MET A 730
SITE 1 AC5 12 HOH B 39 HOH B 73 LEU B 593 VAL B 601
SITE 2 AC5 12 ALA B 617 PRO B 672 PHE B 673 MET B 674
SITE 3 AC5 12 LYS B 675 GLY B 677 ASP B 678 MET B 730
SITE 1 AC6 9 VAL C 601 ALA C 617 PRO C 672 PHE C 673
SITE 2 AC6 9 MET C 674 LYS C 675 GLY C 677 ASP C 678
SITE 3 AC6 9 MET C 730
SITE 1 AC7 9 VAL D 601 ALA D 617 PRO D 672 PHE D 673
SITE 2 AC7 9 MET D 674 LYS D 675 GLY D 677 ASP D 678
SITE 3 AC7 9 MET D 730
CRYST1 70.001 91.702 120.745 90.00 94.06 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014286 0.000000 0.001014 0.00000
SCALE2 0.000000 0.010905 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008303 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
