HEADER CELL ADHESION 07-NOV-08 3F78
TITLE CRYSTAL STRUCTURE OF WILD TYPE LFA1 I DOMAIN COMPLEXED WITH ISOFLURANE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-L;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 153-332, VWFA DOMAIN, I DOMAIN;
COMPND 5 SYNONYM: LEUKOCYTE ADHESION GLYCOPROTEIN LFA-1 ALPHA CHAIN, LFA-1A,
COMPND 6 LEUKOCYTE FUNCTION-ASSOCIATED MOLECULE 1 ALPHA CHAIN, CD11 ANTIGEN-
COMPND 7 LIKE FAMILY MEMBER A;
COMPND 8 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: CD11A, INTEGRIN LFA1, ITGAL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS INTEGRIN, LFA1, I DOMAIN, INACTIVE CONFORMATION, WILD TYPE, VOLATILE
KEYWDS 2 ANESTHETIC, ISOFLURANE, INHIBITOR OF INTEGRIN, CELL ADHESION,
KEYWDS 3 GLYCOPROTEIN, MAGNESIUM, MEMBRANE, RECEPTOR, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ZHANG,J.-H.WANG
REVDAT 5 06-SEP-23 3F78 1 REMARK SEQADV
REVDAT 4 25-OCT-17 3F78 1 REMARK
REVDAT 3 13-JUL-11 3F78 1 VERSN
REVDAT 2 11-AUG-09 3F78 1 JRNL
REVDAT 1 23-JUN-09 3F78 0
JRNL AUTH H.ZHANG,N.S.ASTROF,J.H.LIU,J.H.WANG,M.SHIMAOKA
JRNL TITL CRYSTAL STRUCTURE OF ISOFLURANE BOUND TO INTEGRIN LFA-1
JRNL TITL 2 SUPPORTS A UNIFIED MECHANISM OF VOLATILE ANESTHETIC ACTION
JRNL TITL 3 IN THE IMMUNE AND CENTRAL NERVOUS SYSTEMS.
JRNL REF FASEB J. V. 23 2735 2009
JRNL REFN ISSN 0892-6638
JRNL PMID 19332643
JRNL DOI 10.1096/FJ.09-129908
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0044
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 76778
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) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3872
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4715
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 233
REMARK 3 BIN FREE R VALUE : 0.2520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4362
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 644
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.78000
REMARK 3 B22 (A**2) : -0.75000
REMARK 3 B33 (A**2) : -0.64000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.42000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.079
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.317
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4604 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3166 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6220 ; 1.187 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7794 ; 0.831 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 572 ; 5.673 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 210 ;33.488 ;25.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 878 ;12.202 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;21.474 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 702 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5008 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 919 ; 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): 2742 ; 0.714 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1107 ; 0.193 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4462 ; 1.302 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1862 ; 2.140 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1740 ; 3.171 ; 5.000
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 : 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 128 A 173
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6730 24.3990 -2.5750
REMARK 3 T TENSOR
REMARK 3 T11: -0.0177 T22: 0.0300
REMARK 3 T33: 0.0490 T12: -0.0050
REMARK 3 T13: 0.0024 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 1.0971 L22: 2.0845
REMARK 3 L33: 1.5922 L12: -0.4454
REMARK 3 L13: -0.3480 L23: 0.8998
REMARK 3 S TENSOR
REMARK 3 S11: -0.0298 S12: 0.0766 S13: 0.0236
REMARK 3 S21: 0.0643 S22: -0.0443 S23: 0.2755
REMARK 3 S31: 0.0452 S32: -0.2477 S33: 0.0740
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 174 A 202
REMARK 3 ORIGIN FOR THE GROUP (A): 32.2790 32.9090 -5.0940
REMARK 3 T TENSOR
REMARK 3 T11: 0.0136 T22: 0.0047
REMARK 3 T33: 0.0537 T12: 0.0208
REMARK 3 T13: -0.0117 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 2.0600 L22: 1.8107
REMARK 3 L33: 0.5824 L12: -1.4694
REMARK 3 L13: -0.8991 L23: 0.9580
REMARK 3 S TENSOR
REMARK 3 S11: 0.1174 S12: 0.1748 S13: 0.1030
REMARK 3 S21: -0.1774 S22: -0.1073 S23: 0.1784
REMARK 3 S31: -0.1840 S32: -0.1152 S33: -0.0102
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 203 A 229
REMARK 3 ORIGIN FOR THE GROUP (A): 39.8660 30.1780 4.7510
REMARK 3 T TENSOR
REMARK 3 T11: 0.0336 T22: 0.0137
REMARK 3 T33: 0.0409 T12: -0.0125
REMARK 3 T13: -0.0030 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 1.3110 L22: 1.3423
REMARK 3 L33: 0.9667 L12: -0.3830
REMARK 3 L13: 0.1143 L23: 0.0355
REMARK 3 S TENSOR
REMARK 3 S11: -0.0704 S12: -0.1293 S13: 0.1687
REMARK 3 S21: 0.2045 S22: 0.0467 S23: 0.0526
REMARK 3 S31: -0.1431 S32: -0.0034 S33: 0.0238
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 230 A 265
REMARK 3 ORIGIN FOR THE GROUP (A): 38.8190 18.7810 5.3290
REMARK 3 T TENSOR
REMARK 3 T11: 0.0236 T22: 0.0219
REMARK 3 T33: 0.0139 T12: -0.0022
REMARK 3 T13: -0.0081 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.5808 L22: 0.7614
REMARK 3 L33: 0.9767 L12: 0.1211
REMARK 3 L13: -0.4508 L23: -0.3114
REMARK 3 S TENSOR
REMARK 3 S11: -0.0145 S12: -0.0980 S13: 0.0135
REMARK 3 S21: 0.0781 S22: 0.0420 S23: -0.0363
REMARK 3 S31: 0.0160 S32: 0.0166 S33: -0.0275
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 266 A 286
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2800 9.6220 7.6450
REMARK 3 T TENSOR
REMARK 3 T11: 0.0285 T22: 0.0280
REMARK 3 T33: 0.0318 T12: -0.0104
REMARK 3 T13: -0.0062 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 1.7489 L22: 2.5248
REMARK 3 L33: 1.9047 L12: -0.3218
REMARK 3 L13: -0.5407 L23: 0.8348
REMARK 3 S TENSOR
REMARK 3 S11: -0.0468 S12: 0.0148 S13: -0.1574
REMARK 3 S21: 0.0875 S22: 0.0886 S23: -0.0927
REMARK 3 S31: 0.1822 S32: -0.0014 S33: -0.0417
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 287 A 307
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8280 14.5410 1.5870
REMARK 3 T TENSOR
REMARK 3 T11: -0.0382 T22: 0.0305
REMARK 3 T33: 0.0288 T12: -0.0300
REMARK 3 T13: -0.0150 T23: -0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 1.3429 L22: 2.2253
REMARK 3 L33: 4.4203 L12: -1.7287
REMARK 3 L13: -1.7064 L23: 2.1903
REMARK 3 S TENSOR
REMARK 3 S11: 0.0909 S12: 0.1604 S13: -0.2293
REMARK 3 S21: -0.0933 S22: -0.2222 S23: 0.3467
REMARK 3 S31: -0.0592 S32: -0.5370 S33: 0.1314
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 128 B 200
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2780 3.1040 35.1830
REMARK 3 T TENSOR
REMARK 3 T11: 0.0414 T22: 0.0303
REMARK 3 T33: -0.0151 T12: 0.0590
REMARK 3 T13: 0.0139 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.4447 L22: 1.0513
REMARK 3 L33: 0.8613 L12: -0.4616
REMARK 3 L13: -0.2468 L23: -0.0225
REMARK 3 S TENSOR
REMARK 3 S11: -0.0483 S12: 0.0686 S13: -0.1526
REMARK 3 S21: -0.0103 S22: -0.0087 S23: -0.0346
REMARK 3 S31: 0.2520 S32: 0.0765 S33: 0.0570
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 201 B 250
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4310 15.2290 34.3380
REMARK 3 T TENSOR
REMARK 3 T11: -0.0101 T22: 0.0649
REMARK 3 T33: -0.0109 T12: 0.0239
REMARK 3 T13: -0.0120 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 0.7917 L22: 1.0244
REMARK 3 L33: 1.3796 L12: -0.4318
REMARK 3 L13: -0.5067 L23: -0.2488
REMARK 3 S TENSOR
REMARK 3 S11: -0.0164 S12: -0.0491 S13: 0.0517
REMARK 3 S21: 0.0088 S22: 0.0029 S23: -0.1585
REMARK 3 S31: -0.0035 S32: 0.2435 S33: 0.0135
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 : B 251 B 264
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3350 15.5660 27.3430
REMARK 3 T TENSOR
REMARK 3 T11: 0.0392 T22: 0.0497
REMARK 3 T33: -0.0011 T12: 0.0238
REMARK 3 T13: -0.0004 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 3.7154 L22: 2.0737
REMARK 3 L33: 3.4642 L12: -0.4408
REMARK 3 L13: -1.1936 L23: 0.0459
REMARK 3 S TENSOR
REMARK 3 S11: -0.0579 S12: -0.0633 S13: 0.2461
REMARK 3 S21: 0.0350 S22: 0.1039 S23: -0.0541
REMARK 3 S31: -0.0345 S32: -0.0163 S33: -0.0460
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 : B 265 B 296
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9420 16.2850 24.9140
REMARK 3 T TENSOR
REMARK 3 T11: -0.0247 T22: 0.0781
REMARK 3 T33: -0.0116 T12: 0.0170
REMARK 3 T13: -0.0092 T23: 0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 1.6635 L22: 1.5089
REMARK 3 L33: 2.6073 L12: -0.2041
REMARK 3 L13: -1.0895 L23: -0.3664
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: 0.1256 S13: -0.0134
REMARK 3 S21: -0.0409 S22: 0.0680 S23: 0.1885
REMARK 3 S31: 0.0128 S32: -0.3929 S33: -0.0738
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 : B 297 B 307
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1130 3.4440 18.9480
REMARK 3 T TENSOR
REMARK 3 T11: 0.0702 T22: -0.0424
REMARK 3 T33: -0.0203 T12: -0.0284
REMARK 3 T13: 0.0337 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 20.3293 L22: 4.3707
REMARK 3 L33: 6.8197 L12: 6.2131
REMARK 3 L13: -8.8726 L23: -1.1358
REMARK 3 S TENSOR
REMARK 3 S11: -0.3599 S12: 0.0883 S13: -0.4319
REMARK 3 S21: -0.0856 S22: -0.1062 S23: 0.2612
REMARK 3 S31: 0.7398 S32: -0.3413 S33: 0.4660
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 128 C 189
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3760 -3.0890 0.0210
REMARK 3 T TENSOR
REMARK 3 T11: 0.0082 T22: 0.0260
REMARK 3 T33: 0.0291 T12: 0.0283
REMARK 3 T13: -0.0076 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.2976 L22: 2.0245
REMARK 3 L33: 0.6564 L12: -0.7523
REMARK 3 L13: -0.0715 L23: 0.1293
REMARK 3 S TENSOR
REMARK 3 S11: 0.0826 S12: 0.0738 S13: 0.1037
REMARK 3 S21: -0.0831 S22: -0.0951 S23: -0.0756
REMARK 3 S31: -0.0680 S32: -0.0463 S33: 0.0125
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 : C 190 C 217
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0710 1.5110 -0.6160
REMARK 3 T TENSOR
REMARK 3 T11: -0.0082 T22: 0.0122
REMARK 3 T33: 0.0289 T12: 0.0389
REMARK 3 T13: -0.0259 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 1.7670 L22: 1.3678
REMARK 3 L33: 1.8592 L12: -0.6464
REMARK 3 L13: -0.7848 L23: 0.3851
REMARK 3 S TENSOR
REMARK 3 S11: 0.0926 S12: 0.1053 S13: 0.0195
REMARK 3 S21: -0.1101 S22: -0.0765 S23: 0.0165
REMARK 3 S31: -0.0566 S32: -0.0359 S33: -0.0162
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 : C 218 C 250
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3770 -6.9020 5.4690
REMARK 3 T TENSOR
REMARK 3 T11: -0.0232 T22: 0.0397
REMARK 3 T33: 0.0258 T12: 0.0077
REMARK 3 T13: -0.0060 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 1.4050 L22: 2.5130
REMARK 3 L33: 0.9723 L12: -0.9128
REMARK 3 L13: -0.3623 L23: 0.7220
REMARK 3 S TENSOR
REMARK 3 S11: -0.0092 S12: 0.0823 S13: -0.1090
REMARK 3 S21: 0.0373 S22: -0.0416 S23: 0.2919
REMARK 3 S31: 0.0027 S32: -0.1952 S33: 0.0509
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 : C 251 C 289
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0120 -0.5970 17.6040
REMARK 3 T TENSOR
REMARK 3 T11: 0.0314 T22: 0.0414
REMARK 3 T33: -0.0081 T12: 0.0376
REMARK 3 T13: -0.0335 T23: -0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 2.4744 L22: 3.8636
REMARK 3 L33: 2.0122 L12: 0.1310
REMARK 3 L13: -0.4084 L23: 0.2088
REMARK 3 S TENSOR
REMARK 3 S11: -0.0900 S12: -0.2139 S13: 0.1385
REMARK 3 S21: 0.3401 S22: 0.0733 S23: -0.0075
REMARK 3 S31: -0.0444 S32: -0.0868 S33: 0.0166
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 : C 290 C 307
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9620 -3.9910 11.7880
REMARK 3 T TENSOR
REMARK 3 T11: 0.0002 T22: -0.0006
REMARK 3 T33: 0.0681 T12: 0.0075
REMARK 3 T13: -0.0220 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 0.4543 L22: 6.6407
REMARK 3 L33: 1.4990 L12: -0.5739
REMARK 3 L13: 0.2245 L23: -0.9934
REMARK 3 S TENSOR
REMARK 3 S11: -0.0497 S12: -0.1345 S13: 0.2473
REMARK 3 S21: 0.1802 S22: -0.0349 S23: -0.3838
REMARK 3 S31: -0.1290 S32: 0.0647 S33: 0.0847
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3F78 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-08.
REMARK 100 THE DEPOSITION ID IS D_1000050233.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76838
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2220
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.61600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1LFA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE PH7.5, 0.2M
REMARK 280 AMMONIUM ACETATE, 25% PEG3350, 10MM ISOFLURANE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
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 42.90000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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 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 127
REMARK 465 MET B 127
REMARK 465 MET C 127
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 326 O HOH B 506 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 174 -107.50 -146.08
REMARK 500 LEU A 204 -133.59 -123.31
REMARK 500 SER B 174 -101.39 -148.09
REMARK 500 LEU B 204 -130.70 -128.12
REMARK 500 SER C 174 -103.91 -147.58
REMARK 500 SER C 176 -169.34 -119.21
REMARK 500 LEU C 204 -133.45 -123.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ICF A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ICF B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F74 RELATED DB: PDB
DBREF 3F78 A 128 307 UNP P20701 ITAL_HUMAN 153 332
DBREF 3F78 B 128 307 UNP P20701 ITAL_HUMAN 153 332
DBREF 3F78 C 128 307 UNP P20701 ITAL_HUMAN 153 332
SEQADV 3F78 MET A 127 UNP P20701 EXPRESSION TAG
SEQADV 3F78 TRP A 189 UNP P20701 ARG 214 VARIANT
SEQADV 3F78 MET B 127 UNP P20701 EXPRESSION TAG
SEQADV 3F78 TRP B 189 UNP P20701 ARG 214 VARIANT
SEQADV 3F78 MET C 127 UNP P20701 EXPRESSION TAG
SEQADV 3F78 TRP C 189 UNP P20701 ARG 214 VARIANT
SEQRES 1 A 181 MET GLY ASN VAL ASP LEU VAL PHE LEU PHE ASP GLY SER
SEQRES 2 A 181 MET SER LEU GLN PRO ASP GLU PHE GLN LYS ILE LEU ASP
SEQRES 3 A 181 PHE MET LYS ASP VAL MET LYS LYS LEU SER ASN THR SER
SEQRES 4 A 181 TYR GLN PHE ALA ALA VAL GLN PHE SER THR SER TYR LYS
SEQRES 5 A 181 THR GLU PHE ASP PHE SER ASP TYR VAL LYS TRP LYS ASP
SEQRES 6 A 181 PRO ASP ALA LEU LEU LYS HIS VAL LYS HIS MET LEU LEU
SEQRES 7 A 181 LEU THR ASN THR PHE GLY ALA ILE ASN TYR VAL ALA THR
SEQRES 8 A 181 GLU VAL PHE ARG GLU GLU LEU GLY ALA ARG PRO ASP ALA
SEQRES 9 A 181 THR LYS VAL LEU ILE ILE ILE THR ASP GLY GLU ALA THR
SEQRES 10 A 181 ASP SER GLY ASN ILE ASP ALA ALA LYS ASP ILE ILE ARG
SEQRES 11 A 181 TYR ILE ILE GLY ILE GLY LYS HIS PHE GLN THR LYS GLU
SEQRES 12 A 181 SER GLN GLU THR LEU HIS LYS PHE ALA SER LYS PRO ALA
SEQRES 13 A 181 SER GLU PHE VAL LYS ILE LEU ASP THR PHE GLU LYS LEU
SEQRES 14 A 181 LYS ASP LEU PHE THR GLU LEU GLN LYS LYS ILE TYR
SEQRES 1 B 181 MET GLY ASN VAL ASP LEU VAL PHE LEU PHE ASP GLY SER
SEQRES 2 B 181 MET SER LEU GLN PRO ASP GLU PHE GLN LYS ILE LEU ASP
SEQRES 3 B 181 PHE MET LYS ASP VAL MET LYS LYS LEU SER ASN THR SER
SEQRES 4 B 181 TYR GLN PHE ALA ALA VAL GLN PHE SER THR SER TYR LYS
SEQRES 5 B 181 THR GLU PHE ASP PHE SER ASP TYR VAL LYS TRP LYS ASP
SEQRES 6 B 181 PRO ASP ALA LEU LEU LYS HIS VAL LYS HIS MET LEU LEU
SEQRES 7 B 181 LEU THR ASN THR PHE GLY ALA ILE ASN TYR VAL ALA THR
SEQRES 8 B 181 GLU VAL PHE ARG GLU GLU LEU GLY ALA ARG PRO ASP ALA
SEQRES 9 B 181 THR LYS VAL LEU ILE ILE ILE THR ASP GLY GLU ALA THR
SEQRES 10 B 181 ASP SER GLY ASN ILE ASP ALA ALA LYS ASP ILE ILE ARG
SEQRES 11 B 181 TYR ILE ILE GLY ILE GLY LYS HIS PHE GLN THR LYS GLU
SEQRES 12 B 181 SER GLN GLU THR LEU HIS LYS PHE ALA SER LYS PRO ALA
SEQRES 13 B 181 SER GLU PHE VAL LYS ILE LEU ASP THR PHE GLU LYS LEU
SEQRES 14 B 181 LYS ASP LEU PHE THR GLU LEU GLN LYS LYS ILE TYR
SEQRES 1 C 181 MET GLY ASN VAL ASP LEU VAL PHE LEU PHE ASP GLY SER
SEQRES 2 C 181 MET SER LEU GLN PRO ASP GLU PHE GLN LYS ILE LEU ASP
SEQRES 3 C 181 PHE MET LYS ASP VAL MET LYS LYS LEU SER ASN THR SER
SEQRES 4 C 181 TYR GLN PHE ALA ALA VAL GLN PHE SER THR SER TYR LYS
SEQRES 5 C 181 THR GLU PHE ASP PHE SER ASP TYR VAL LYS TRP LYS ASP
SEQRES 6 C 181 PRO ASP ALA LEU LEU LYS HIS VAL LYS HIS MET LEU LEU
SEQRES 7 C 181 LEU THR ASN THR PHE GLY ALA ILE ASN TYR VAL ALA THR
SEQRES 8 C 181 GLU VAL PHE ARG GLU GLU LEU GLY ALA ARG PRO ASP ALA
SEQRES 9 C 181 THR LYS VAL LEU ILE ILE ILE THR ASP GLY GLU ALA THR
SEQRES 10 C 181 ASP SER GLY ASN ILE ASP ALA ALA LYS ASP ILE ILE ARG
SEQRES 11 C 181 TYR ILE ILE GLY ILE GLY LYS HIS PHE GLN THR LYS GLU
SEQRES 12 C 181 SER GLN GLU THR LEU HIS LYS PHE ALA SER LYS PRO ALA
SEQRES 13 C 181 SER GLU PHE VAL LYS ILE LEU ASP THR PHE GLU LYS LEU
SEQRES 14 C 181 LYS ASP LEU PHE THR GLU LEU GLN LYS LYS ILE TYR
HET ICF A 1 10
HET GOL A 2 6
HET ICF B 2 10
HET GOL B 3 6
HET GOL B 4 6
HET MG C 1 1
HET GOL C 308 6
HETNAM ICF 1-CHLORO-2,2,2-TRIFLUOROETHYL DIFLUOROMETHYL ETHER
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETSYN ICF ISOFLURANE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 ICF 2(C3 H2 CL F5 O)
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 MG MG 2+
FORMUL 11 HOH *644(H2 O)
HELIX 1 1 GLN A 143 LEU A 161 1 19
HELIX 2 2 ASP A 182 LYS A 190 1 9
HELIX 3 3 ASP A 191 LEU A 196 1 6
HELIX 4 4 ASN A 207 VAL A 219 1 13
HELIX 5 5 ARG A 221 GLY A 225 5 5
HELIX 6 6 ILE A 248 LYS A 252 5 5
HELIX 7 7 LYS A 263 GLN A 266 5 4
HELIX 8 8 THR A 267 THR A 273 1 7
HELIX 9 9 LEU A 274 ALA A 278 5 5
HELIX 10 10 PRO A 281 PHE A 285 1 5
HELIX 11 11 THR A 291 ASP A 297 5 7
HELIX 12 12 LEU A 298 LYS A 305 1 8
HELIX 13 13 GLN B 143 LEU B 161 1 19
HELIX 14 14 ASP B 182 LYS B 190 1 9
HELIX 15 15 ASP B 191 LEU B 196 1 6
HELIX 16 16 ASN B 207 VAL B 219 1 13
HELIX 17 17 ARG B 221 GLY B 225 5 5
HELIX 18 18 ILE B 248 LYS B 252 5 5
HELIX 19 19 LYS B 263 GLN B 266 5 4
HELIX 20 20 THR B 267 THR B 273 1 7
HELIX 21 21 LEU B 274 ALA B 278 5 5
HELIX 22 22 PRO B 281 PHE B 285 1 5
HELIX 23 23 THR B 291 ASP B 297 5 7
HELIX 24 24 LEU B 298 LYS B 305 1 8
HELIX 25 25 GLN C 143 LEU C 161 1 19
HELIX 26 26 ASP C 182 LYS C 190 1 9
HELIX 27 27 ASP C 191 LEU C 196 1 6
HELIX 28 28 ASN C 207 VAL C 219 1 13
HELIX 29 29 ARG C 221 GLY C 225 5 5
HELIX 30 30 ILE C 248 LYS C 252 5 5
HELIX 31 31 LYS C 263 GLN C 266 5 4
HELIX 32 32 THR C 267 THR C 273 1 7
HELIX 33 33 LEU C 274 ALA C 278 5 5
HELIX 34 34 PRO C 281 PHE C 285 1 5
HELIX 35 35 THR C 291 GLN C 303 5 13
SHEET 1 A 6 TYR A 177 PHE A 181 0
SHEET 2 A 6 TYR A 166 PHE A 173 -1 N ALA A 170 O PHE A 181
SHEET 3 A 6 VAL A 130 ASP A 137 1 N PHE A 134 O VAL A 171
SHEET 4 A 6 THR A 231 THR A 238 1 O ILE A 235 N LEU A 135
SHEET 5 A 6 ILE A 255 ILE A 261 1 O ILE A 259 N ILE A 236
SHEET 6 A 6 VAL A 286 LEU A 289 1 O LYS A 287 N ILE A 258
SHEET 1 B 6 TYR B 177 PHE B 181 0
SHEET 2 B 6 TYR B 166 PHE B 173 -1 N GLN B 172 O LYS B 178
SHEET 3 B 6 VAL B 130 ASP B 137 1 N PHE B 134 O VAL B 171
SHEET 4 B 6 THR B 231 THR B 238 1 O ILE B 235 N LEU B 135
SHEET 5 B 6 ILE B 255 ILE B 261 1 O ILE B 255 N LEU B 234
SHEET 6 B 6 VAL B 286 LEU B 289 1 O LYS B 287 N GLY B 260
SHEET 1 C 6 TYR C 177 PHE C 181 0
SHEET 2 C 6 TYR C 166 PHE C 173 -1 N ALA C 170 O GLU C 180
SHEET 3 C 6 VAL C 130 ASP C 137 1 N PHE C 134 O VAL C 171
SHEET 4 C 6 THR C 231 THR C 238 1 O ILE C 235 N LEU C 135
SHEET 5 C 6 ILE C 255 ILE C 261 1 O ILE C 259 N ILE C 236
SHEET 6 C 6 VAL C 286 LEU C 289 1 O LYS C 287 N ILE C 258
CISPEP 1 LYS A 280 PRO A 281 0 8.58
CISPEP 2 LYS B 280 PRO B 281 0 5.36
CISPEP 3 LYS C 280 PRO C 281 0 -1.31
SITE 1 AC1 7 ILE A 235 TYR A 257 LYS A 287 GLU A 301
SITE 2 AC1 7 LEU A 302 LYS A 305 TYR A 307
SITE 1 AC2 7 HIS A 275 ALA A 282 SER A 283 VAL A 286
SITE 2 AC2 7 HOH A 330 HOH A 342 HOH A 364
SITE 1 AC3 9 ILE B 235 TYR B 257 ILE B 259 LYS B 287
SITE 2 AC3 9 LEU B 298 GLU B 301 LEU B 302 LYS B 305
SITE 3 AC3 9 TYR B 307
SITE 1 AC4 4 GLY B 246 ASN B 247 HOH B 323 HOH B 356
SITE 1 AC5 4 HOH A 88 LEU B 205 ASN B 207 THR B 243
SITE 1 AC6 6 SER C 139 SER C 141 ASP C 239 HOH C 312
SITE 2 AC6 6 HOH C 394 HOH C 589
SITE 1 AC7 5 HOH C 119 ILE C 255 LYS C 280 PHE C 285
SITE 2 AC7 5 HOH C 373
CRYST1 62.679 85.800 63.917 90.00 118.18 90.00 P 1 21 1 6
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 0.015954 0.000000 0.008547 0.00000
SCALE2 0.000000 0.011655 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017749 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
