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HEADER HYDROLASE 20-FEB-07 2OXE
TITLE STRUCTURE OF THE HUMAN PANCREATIC LIPASE-RELATED PROTEIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PANCREATIC LIPASE-RELATED PROTEIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 TISSUE: PANCREAS;
SOURCE 5 GENE: PNLIPRP2, PLRP2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HIGH5;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAB-BEE
KEYWDS GLYCOPROTEIN, HYDROLASE, LIPID DEGRADATION, PANCREATIC
KEYWDS 2 LIPASE, STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WALKER,T.DAVIS,A.SEITOVA,P.J.FINERTY JR.,C.BUTLER-COLE,
AUTHOR 2 I.KOZIERADZKI,J.WEIGELT,M.SUNDSTROM,C.H.ARROWSMITH,
AUTHOR 3 A.M.EDWARDS,A.BOCHKAREV,S.DHE-PAGANON,STRUCTURAL GENOMICS
AUTHOR 4 CONSORTIUM (SGC)
REVDAT 1 27-MAR-07 2OXE 0
JRNL AUTH J.R.WALKER,T.DAVIS,A.SEITOVA,P.J.FINERTY JR.,
JRNL AUTH 2 C.BUTLER-COLE,I.KOZIERADZKI,J.WEIGELT,M.SUNDSTROM,
JRNL AUTH 3 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,
JRNL AUTH 4 S.DHE-PAGANON
JRNL TITL HUMAN PANCREATIC LIPASE-RELATED PROTEIN 2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.SIAS,F.FERRATO,P.GRANDVAL,D.LAFONT,P.BOULLANGER,
REMARK 1 AUTH 2 A.DE CARO,B.LEBOEUF,R.VERGER,F.CARRIERE
REMARK 1 TITL HUMAN PANCREATIC LIPASE-RELATED PROTEIN 2 IS A
REMARK 1 TITL 2 GALACTOLIPASE
REMARK 1 REF BIOCHEMISTRY V. 43 10138 2004
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.GILLER,P.BUCHWALD,D.BLUM-KAELIN,W.HUNZIKER
REMARK 1 TITL TWO NOVEL HUMAN PANCREATIC LIPASE RELATED
REMARK 1 TITL 2 PROTEINS, HPLRP1 AND HPLRP2
REMARK 1 REF J.BIOL.CHEM. V. 267 16509 1992
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
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) : 29.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 34305
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1811
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2464
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.3380
REMARK 3 BIN FREE R VALUE SET COUNT : 122
REMARK 3 BIN FREE R VALUE : 0.4430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 6886
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.11000
REMARK 3 B22 (A**2) : 4.11000
REMARK 3 B33 (A**2) : -8.22000
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): 0.641
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.334
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.314
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.297
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6997 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9525 ; 1.142 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 868 ; 5.275 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 327 ;36.635 ;24.587
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1045 ;17.520 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;16.800 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1034 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5401 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3124 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4783 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 221 ; 0.133 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 5 ; 0.092 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 49 ; 0.169 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.079 ; 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): 4404 ; 0.322 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6915 ; 0.585 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2925 ; 0.885 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2610 ; 1.650 ; 4.500
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
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 18 A 63
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7530 -16.2590 50.2980
REMARK 3 T TENSOR
REMARK 3 T11: 0.2429 T22: 0.1912
REMARK 3 T33: 0.1878 T12: 0.0457
REMARK 3 T13: 0.0187 T23: 0.0940
REMARK 3 L TENSOR
REMARK 3 L11: 4.0568 L22: 2.5774
REMARK 3 L33: 1.6249 L12: -0.8243
REMARK 3 L13: -0.1866 L23: -0.3465
REMARK 3 S TENSOR
REMARK 3 S11: 0.2684 S12: -0.1971 S13: -0.0033
REMARK 3 S21: -0.1005 S22: -0.1928 S23: 0.1199
REMARK 3 S31: 0.3780 S32: -0.0100 S33: -0.0756
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 64 A 86
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7160 -24.9230 50.3660
REMARK 3 T TENSOR
REMARK 3 T11: 0.3034 T22: 0.2636
REMARK 3 T33: 0.3846 T12: 0.4909
REMARK 3 T13: 0.0950 T23: 0.1230
REMARK 3 L TENSOR
REMARK 3 L11: 2.7909 L22: 3.2326
REMARK 3 L33: 11.7935 L12: 2.3833
REMARK 3 L13: 1.9150 L23: 4.1921
REMARK 3 S TENSOR
REMARK 3 S11: 0.3900 S12: -0.5980 S13: -0.6397
REMARK 3 S21: 0.0637 S22: -0.0280 S23: -0.7258
REMARK 3 S31: 1.2455 S32: 0.9978 S33: -0.3620
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 87 A 172
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6680 -14.5190 46.1740
REMARK 3 T TENSOR
REMARK 3 T11: 0.1883 T22: 0.2839
REMARK 3 T33: 0.2986 T12: 0.1894
REMARK 3 T13: 0.1257 T23: 0.1297
REMARK 3 L TENSOR
REMARK 3 L11: 2.2570 L22: 1.6108
REMARK 3 L33: 1.7370 L12: -0.4256
REMARK 3 L13: 0.3245 L23: 0.5498
REMARK 3 S TENSOR
REMARK 3 S11: -0.0913 S12: 0.0174 S13: -0.0524
REMARK 3 S21: -0.2257 S22: -0.0428 S23: -0.2688
REMARK 3 S31: 0.5214 S32: 0.3487 S33: 0.1341
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 173 A 212
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5470 -3.9890 51.0930
REMARK 3 T TENSOR
REMARK 3 T11: 0.1017 T22: 0.2547
REMARK 3 T33: 0.3789 T12: 0.0609
REMARK 3 T13: 0.0883 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 1.9233 L22: 1.8564
REMARK 3 L33: 3.5426 L12: 0.8157
REMARK 3 L13: 0.3579 L23: 0.1873
REMARK 3 S TENSOR
REMARK 3 S11: 0.0643 S12: 0.0856 S13: -0.1640
REMARK 3 S21: -0.1610 S22: 0.0857 S23: 0.0301
REMARK 3 S31: -0.1614 S32: 0.1224 S33: -0.1500
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 213 A 249
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4270 3.8490 43.1950
REMARK 3 T TENSOR
REMARK 3 T11: 0.1066 T22: 0.2249
REMARK 3 T33: 0.4574 T12: 0.0451
REMARK 3 T13: 0.1645 T23: 0.0544
REMARK 3 L TENSOR
REMARK 3 L11: 1.5520 L22: 3.5500
REMARK 3 L33: 4.5152 L12: 1.2982
REMARK 3 L13: -2.2151 L23: -0.0265
REMARK 3 S TENSOR
REMARK 3 S11: 0.0184 S12: -0.2368 S13: 0.5269
REMARK 3 S21: 0.0040 S22: -0.0143 S23: 0.4057
REMARK 3 S31: -0.5860 S32: -0.3264 S33: -0.0041
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 250 A 303
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3920 0.2430 34.3590
REMARK 3 T TENSOR
REMARK 3 T11: 0.0984 T22: 0.2325
REMARK 3 T33: 0.4182 T12: 0.1041
REMARK 3 T13: 0.1818 T23: 0.0894
REMARK 3 L TENSOR
REMARK 3 L11: 0.6109 L22: 3.3725
REMARK 3 L33: 5.1912 L12: 0.7994
REMARK 3 L13: -1.1489 L23: 0.2070
REMARK 3 S TENSOR
REMARK 3 S11: 0.2572 S12: 0.4392 S13: 0.3579
REMARK 3 S21: -0.5727 S22: -0.2579 S23: -0.0339
REMARK 3 S31: -0.0498 S32: 0.2211 S33: 0.0007
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 304 A 327
REMARK 3 ORIGIN FOR THE GROUP (A): 34.8530 15.4710 40.1130
REMARK 3 T TENSOR
REMARK 3 T11: 0.0710 T22: 0.1798
REMARK 3 T33: 0.5069 T12: -0.0720
REMARK 3 T13: 0.3634 T23: -0.0412
REMARK 3 L TENSOR
REMARK 3 L11: 3.0225 L22: 9.2111
REMARK 3 L33: 9.5232 L12: 2.8303
REMARK 3 L13: -0.0553 L23: -2.3876
REMARK 3 S TENSOR
REMARK 3 S11: 0.2384 S12: -0.4434 S13: 0.9962
REMARK 3 S21: -0.1740 S22: -0.0351 S23: -0.2819
REMARK 3 S31: -1.2440 S32: 0.1058 S33: -0.2033
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 328 A 366
REMARK 3 ORIGIN FOR THE GROUP (A): 37.7700 9.8220 38.6010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0700 T22: 0.2713
REMARK 3 T33: 0.5476 T12: -0.0065
REMARK 3 T13: 0.2429 T23: 0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 2.8658 L22: 1.9236
REMARK 3 L33: 2.9555 L12: 2.2704
REMARK 3 L13: -2.3864 L23: -2.2384
REMARK 3 S TENSOR
REMARK 3 S11: 0.3708 S12: -0.3301 S13: 0.5511
REMARK 3 S21: 0.0438 S22: -0.1710 S23: -0.3255
REMARK 3 S31: -0.3630 S32: 0.4278 S33: -0.1998
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 367 A 397
REMARK 3 ORIGIN FOR THE GROUP (A): 43.4650 21.4890 19.1820
REMARK 3 T TENSOR
REMARK 3 T11: 0.0700 T22: 0.1127
REMARK 3 T33: 0.3777 T12: -0.0601
REMARK 3 T13: 0.3543 T23: 0.1395
REMARK 3 L TENSOR
REMARK 3 L11: 14.1182 L22: 14.9009
REMARK 3 L33: 5.7730 L12: -2.2561
REMARK 3 L13: -3.4704 L23: 2.3067
REMARK 3 S TENSOR
REMARK 3 S11: 0.2446 S12: 0.9448 S13: 0.9263
REMARK 3 S21: -0.4840 S22: 0.3499 S23: 0.6312
REMARK 3 S31: -0.7164 S32: -0.3641 S33: -0.5945
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 398 A 469
REMARK 3 ORIGIN FOR THE GROUP (A): 48.6810 22.6790 23.4510
REMARK 3 T TENSOR
REMARK 3 T11: 0.0406 T22: 0.0793
REMARK 3 T33: 0.5736 T12: -0.0550
REMARK 3 T13: 0.3078 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 6.0639 L22: 5.8218
REMARK 3 L33: 6.2832 L12: 3.1134
REMARK 3 L13: -4.3864 L23: -4.2600
REMARK 3 S TENSOR
REMARK 3 S11: 0.3189 S12: -0.0577 S13: 1.0425
REMARK 3 S21: -0.1904 S22: 0.3565 S23: 0.1671
REMARK 3 S31: -0.3056 S32: -0.2934 S33: -0.6755
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 18 B 63
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9730 13.4290 13.0120
REMARK 3 T TENSOR
REMARK 3 T11: 0.3385 T22: 0.2605
REMARK 3 T33: 0.0586 T12: 0.1210
REMARK 3 T13: -0.1972 T23: -0.0710
REMARK 3 L TENSOR
REMARK 3 L11: 3.7150 L22: 7.0938
REMARK 3 L33: 1.4876 L12: 0.1148
REMARK 3 L13: 0.0131 L23: 0.3334
REMARK 3 S TENSOR
REMARK 3 S11: -0.1965 S12: 0.2529 S13: -0.1019
REMARK 3 S21: -0.6480 S22: 0.0634 S23: 0.1155
REMARK 3 S31: -0.2393 S32: -0.6411 S33: 0.1331
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 : B 64 B 86
REMARK 3 ORIGIN FOR THE GROUP (A): -23.5600 35.1530 11.9290
REMARK 3 T TENSOR
REMARK 3 T11: 0.3849 T22: 0.2733
REMARK 3 T33: 0.5461 T12: 0.3700
REMARK 3 T13: -0.3599 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 9.1223 L22: 8.7586
REMARK 3 L33: 14.1609 L12: 4.2343
REMARK 3 L13: -8.4860 L23: -8.6073
REMARK 3 S TENSOR
REMARK 3 S11: -0.5574 S12: 1.1703 S13: 1.3852
REMARK 3 S21: -0.7267 S22: 0.9758 S23: 0.8889
REMARK 3 S31: -1.1151 S32: -1.8979 S33: -0.4183
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 : B 87 B 172
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6680 25.6570 17.1850
REMARK 3 T TENSOR
REMARK 3 T11: 0.3608 T22: 0.1744
REMARK 3 T33: 0.2250 T12: 0.1913
REMARK 3 T13: -0.1596 T23: -0.0385
REMARK 3 L TENSOR
REMARK 3 L11: 2.9955 L22: 2.0983
REMARK 3 L33: 2.4803 L12: 0.9991
REMARK 3 L13: 0.4596 L23: 1.4147
REMARK 3 S TENSOR
REMARK 3 S11: -0.2056 S12: 0.1623 S13: 0.1988
REMARK 3 S21: -0.0950 S22: 0.0323 S23: 0.2632
REMARK 3 S31: -0.4762 S32: -0.5247 S33: 0.1732
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 : B 173 B 212
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7730 17.1870 12.8260
REMARK 3 T TENSOR
REMARK 3 T11: 0.3142 T22: 0.1427
REMARK 3 T33: 0.2357 T12: -0.0019
REMARK 3 T13: -0.0570 T23: -0.0945
REMARK 3 L TENSOR
REMARK 3 L11: 0.3852 L22: 7.0607
REMARK 3 L33: 6.6380 L12: 0.4162
REMARK 3 L13: -0.0940 L23: 0.4298
REMARK 3 S TENSOR
REMARK 3 S11: -0.0472 S12: 0.2286 S13: -0.1347
REMARK 3 S21: -0.5216 S22: 0.0490 S23: 0.0453
REMARK 3 S31: -0.0287 S32: 0.1465 S33: -0.0018
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 : B 213 B 253
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8860 18.2050 22.3160
REMARK 3 T TENSOR
REMARK 3 T11: 0.2569 T22: 0.1360
REMARK 3 T33: 0.3136 T12: 0.0290
REMARK 3 T13: -0.0299 T23: -0.0728
REMARK 3 L TENSOR
REMARK 3 L11: 2.1737 L22: 3.9393
REMARK 3 L33: 2.5598 L12: 1.5172
REMARK 3 L13: -1.1704 L23: 0.2565
REMARK 3 S TENSOR
REMARK 3 S11: -0.2529 S12: 0.0487 S13: -0.3415
REMARK 3 S21: -0.1693 S22: 0.1054 S23: -0.5748
REMARK 3 S31: -0.1881 S32: 0.1506 S33: 0.1475
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 : B 254 B 303
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1660 26.6470 29.4570
REMARK 3 T TENSOR
REMARK 3 T11: 0.4201 T22: 0.1585
REMARK 3 T33: 0.3323 T12: 0.0482
REMARK 3 T13: -0.0866 T23: -0.0742
REMARK 3 L TENSOR
REMARK 3 L11: 0.4462 L22: 1.4102
REMARK 3 L33: 1.0418 L12: 0.3687
REMARK 3 L13: -0.6177 L23: -0.0559
REMARK 3 S TENSOR
REMARK 3 S11: 0.1273 S12: -0.4184 S13: 0.1878
REMARK 3 S21: 0.2200 S22: -0.0994 S23: 0.2720
REMARK 3 S31: -0.4351 S32: -0.1240 S33: -0.0279
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 : B 304 B 327
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7650 28.0710 24.9540
REMARK 3 T TENSOR
REMARK 3 T11: 0.3849 T22: 0.0869
REMARK 3 T33: 0.4115 T12: -0.2010
REMARK 3 T13: 0.0151 T23: -0.1562
REMARK 3 L TENSOR
REMARK 3 L11: 8.8774 L22: 1.6739
REMARK 3 L33: 8.4874 L12: 0.6451
REMARK 3 L13: 2.0778 L23: -3.4571
REMARK 3 S TENSOR
REMARK 3 S11: -0.3165 S12: 0.4260 S13: 0.0903
REMARK 3 S21: -0.4771 S22: -0.1875 S23: -0.9723
REMARK 3 S31: -0.4195 S32: 1.2771 S33: 0.5041
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 : B 328 B 366
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1550 31.8010 26.2020
REMARK 3 T TENSOR
REMARK 3 T11: 0.4590 T22: 0.0047
REMARK 3 T33: 0.3253 T12: -0.0748
REMARK 3 T13: 0.0145 T23: -0.0858
REMARK 3 L TENSOR
REMARK 3 L11: 3.0257 L22: 1.6328
REMARK 3 L33: 3.1353 L12: 1.6757
REMARK 3 L13: 2.1666 L23: 2.2564
REMARK 3 S TENSOR
REMARK 3 S11: -0.2105 S12: 0.2475 S13: 0.2822
REMARK 3 S21: -0.3497 S22: 0.3449 S23: -0.3200
REMARK 3 S31: -0.4595 S32: 0.5299 S33: -0.1344
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 : B 367 B 398
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9870 36.6540 46.4890
REMARK 3 T TENSOR
REMARK 3 T11: 0.1839 T22: -0.0678
REMARK 3 T33: 0.4383 T12: -0.0190
REMARK 3 T13: -0.0458 T23: -0.1598
REMARK 3 L TENSOR
REMARK 3 L11: 7.9036 L22: 7.1360
REMARK 3 L33: 11.2234 L12: -2.3686
REMARK 3 L13: 3.1522 L23: 0.8050
REMARK 3 S TENSOR
REMARK 3 S11: 0.0502 S12: -1.2230 S13: -0.1091
REMARK 3 S21: 0.7916 S22: 0.2052 S23: -0.1562
REMARK 3 S31: 0.7032 S32: -0.4561 S33: -0.2553
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 399 B 469
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5070 41.6460 41.9600
REMARK 3 T TENSOR
REMARK 3 T11: 0.1273 T22: 0.0535
REMARK 3 T33: 0.4489 T12: -0.0421
REMARK 3 T13: 0.0042 T23: -0.2369
REMARK 3 L TENSOR
REMARK 3 L11: 5.8107 L22: 3.3079
REMARK 3 L33: 5.6235 L12: 0.7766
REMARK 3 L13: 3.2048 L23: 3.8097
REMARK 3 S TENSOR
REMARK 3 S11: -0.2419 S12: -0.2859 S13: 0.2090
REMARK 3 S21: -0.1154 S22: 0.4869 S23: -0.4107
REMARK 3 S31: 0.1214 S32: 0.2969 S33: -0.2450
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 : 1.40
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
REMARK 3 RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL
REMARK 3 B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS
REMARK 4
REMARK 4 2OXE COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-2007.
REMARK 100 THE RCSB ID CODE IS RCSB041703.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
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) : 1.00000
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
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 : 36137
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09200
REMARK 200 FOR THE DATA SET : 12.7000
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.78500
REMARK 200 FOR SHELL : 2.760
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 1BU8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.17M AMMONIUM SULFATE, 0.1M SODIUM
REMARK 280 CACODYLATE PH 5.5, 0.04M NACL, CRYOPROTECTED WITH 15%
REMARK 280 GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K, PH
REMARK 280 5.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,1/2-Y,1/2+Z
REMARK 290 3555 -Y,1/2+X,1/4+Z
REMARK 290 4555 1/2+Y,-X,3/4+Z
REMARK 290 5555 1/2-X,Y,3/4-Z
REMARK 290 6555 X,1/2-Y,1/4-Z
REMARK 290 7555 1/2+Y,1/2+X,1/2-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 1/2+X,1/2+Y,1/2+Z
REMARK 290 10555 1-X,1-Y,1+Z
REMARK 290 11555 1/2-Y,1+X,3/4+Z
REMARK 290 12555 1+Y,1/2-X,5/4+Z
REMARK 290 13555 1-X,1/2+Y,5/4-Z
REMARK 290 14555 1/2+X,1-Y,3/4-Z
REMARK 290 15555 1+Y,1+X,1-Z
REMARK 290 16555 1/2-Y,1/2-X,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 108.46100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 108.46100
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.80900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 108.46100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.90450
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 108.46100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 92.71350
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 108.46100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 92.71350
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 108.46100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 30.90450
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 108.46100
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 108.46100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 61.80900
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 108.46100
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 108.46100
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 61.80900
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 216.92200
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 216.92200
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 123.61800
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 108.46100
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 216.92200
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 92.71350
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 216.92200
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 108.46100
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 154.52250
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 216.92200
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 108.46100
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 154.52250
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 108.46100
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 216.92200
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 92.71350
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 216.92200
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 216.92200
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 123.61800
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 108.46100
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 108.46100
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 61.80900
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 ALA A 16
REMARK 465 ALA A 17
REMARK 465 LYS A 257
REMARK 465 LYS A 258
REMARK 465 ASN A 259
REMARK 465 VAL A 260
REMARK 465 LEU A 261
REMARK 465 SER A 262
REMARK 465 THR A 263
REMARK 465 ILE A 264
REMARK 465 THR A 265
REMARK 465 ASP A 266
REMARK 465 ILE A 267
REMARK 465 ARG A 425
REMARK 465 GLY A 426
REMARK 465 ILE A 427
REMARK 465 ASN A 428
REMARK 465 LEU A 429
REMARK 465 SER A 430
REMARK 465 GLU A 470
REMARK 465 PHE A 471
REMARK 465 VAL A 472
REMARK 465 GLU A 473
REMARK 465 HIS A 474
REMARK 465 HIS A 475
REMARK 465 HIS A 476
REMARK 465 HIS A 477
REMARK 465 HIS A 478
REMARK 465 HIS A 479
REMARK 465 HIS A 480
REMARK 465 HIS A 481
REMARK 465 ALA B 16
REMARK 465 ALA B 17
REMARK 465 LYS B 257
REMARK 465 LYS B 258
REMARK 465 ASN B 259
REMARK 465 VAL B 260
REMARK 465 LEU B 261
REMARK 465 SER B 262
REMARK 465 THR B 263
REMARK 465 ILE B 264
REMARK 465 THR B 265
REMARK 465 ASP B 266
REMARK 465 ILE B 267
REMARK 465 ASP B 268
REMARK 465 GLY B 269
REMARK 465 ILE B 270
REMARK 465 TRP B 271
REMARK 465 GLU B 272
REMARK 465 ARG B 425
REMARK 465 GLY B 426
REMARK 465 ILE B 427
REMARK 465 ASN B 428
REMARK 465 LEU B 429
REMARK 465 GLU B 470
REMARK 465 PHE B 471
REMARK 465 VAL B 472
REMARK 465 GLU B 473
REMARK 465 HIS B 474
REMARK 465 HIS B 475
REMARK 465 HIS B 476
REMARK 465 HIS B 477
REMARK 465 HIS B 478
REMARK 465 HIS B 479
REMARK 465 HIS B 480
REMARK 465 HIS B 481
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 LYS A 18 CG CD CE NZ
REMARK 470 LYS A 251 CD CE NZ
REMARK 470 ILE A 274 O
REMARK 470 LYS A 314 CG CD CE NZ
REMARK 470 GLU A 321 CG CD OE1 OE2
REMARK 470 LYS A 334 CD CE NZ
REMARK 470 LYS A 368 CG CD CE NZ
REMARK 470 GLU A 369 CG CD OE1 OE2
REMARK 470 LYS A 370 CB CG CD CE NZ
REMARK 470 ARG A 376 CD NE CZ NH1 NH2
REMARK 470 GLU A 384 CG CD OE1 OE2
REMARK 470 LYS A 393 CG CD CE NZ
REMARK 470 LYS A 397 CG CD CE NZ
REMARK 470 LYS A 417 CG CD CE NZ
REMARK 470 LYS A 424 CG CD CE NZ
REMARK 470 GLU A 459 CB CG CD OE1 OE2
REMARK 470 LYS B 18 CG CD CE NZ
REMARK 470 GLU B 31 CG CD OE1 OE2
REMARK 470 LYS B 88 CD CE NZ
REMARK 470 LYS B 117 CG CD CE NZ
REMARK 470 LEU B 158 CG CD1 CD2
REMARK 470 GLU B 321 CG CD OE1 OE2
REMARK 470 LYS B 334 CG CD CE NZ
REMARK 470 LYS B 368 CG CD CE NZ
REMARK 470 LYS B 370 CB CG CD CE NZ
REMARK 470 GLU B 384 CG CD OE1 OE2
REMARK 470 LYS B 393 CE NZ
REMARK 470 LYS B 397 CG CD CE NZ
REMARK 470 LYS B 424 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 432 CB PRO A 432 CG 0.058
REMARK 500 PRO B 196 CG PRO B 196 CD -0.045
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 105 C - N - CA ANGL. DEV. = -6.8 DEGREES
REMARK 500 PRO A 105 C - N - CD ANGL. DEV. = 8.4 DEGREES
REMARK 500 THR A 223 N - CA - C ANGL. DEV. = 6.9 DEGREES
REMARK 500 LEU A 283 CA - CB - CG ANGL. DEV. = 7.4 DEGREES
REMARK 500 LEU A 379 CA - CB - CG ANGL. DEV. = 6.4 DEGREES
REMARK 500 PRO B 33 C - N - CA ANGL. DEV. = 6.9 DEGREES
REMARK 500 TRP B 104 N - CA - C ANGL. DEV. = 6.9 DEGREES
REMARK 500 LEU B 243 CA - CB - CG ANGL. DEV. = 6.8 DEGREES
REMARK 500 PRO B 317 C - N - CA ANGL. DEV. = 6.9 DEGREES
REMARK 500 LEU B 434 CA - CB - CG ANGL. DEV. = 6.6 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 171 -119.04 60.27
REMARK 500 SER B 171 -108.63 43.78
DBREF 2OXE A 18 469 UNP P54317 LIPR2_HUMAN 18 469
DBREF 2OXE B 18 469 UNP P54317 LIPR2_HUMAN 18 469
SEQADV 2OXE ALA A 16 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE ALA A 17 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE GLU A 470 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE PHE A 471 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE VAL A 472 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE GLU A 473 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS A 474 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS A 475 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS A 476 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS A 477 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS A 478 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS A 479 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS A 480 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS A 481 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE ALA B 16 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE ALA B 17 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE GLU B 470 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE PHE B 471 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE VAL B 472 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE GLU B 473 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS B 474 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS B 475 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS B 476 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS B 477 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS B 478 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS B 479 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS B 480 UNP P54317 CLONING ARTIFACT
SEQADV 2OXE HIS B 481 UNP P54317 CLONING ARTIFACT
SEQRES 1 A 466 ALA ALA LYS GLU VAL CYS TYR GLY GLN LEU GLY CYS PHE
SEQRES 2 A 466 SER ASP GLU LYS PRO TRP ALA GLY THR LEU GLN ARG PRO
SEQRES 3 A 466 VAL LYS LEU LEU PRO TRP SER PRO GLU ASP ILE ASP THR
SEQRES 4 A 466 ARG PHE LEU LEU TYR THR ASN GLU ASN PRO ASN ASN PHE
SEQRES 5 A 466 GLN LEU ILE THR GLY THR GLU PRO ASP THR ILE GLU ALA
SEQRES 6 A 466 SER ASN PHE GLN LEU ASP ARG LYS THR ARG PHE ILE ILE
SEQRES 7 A 466 HIS GLY PHE LEU ASP LYS ALA GLU ASP SER TRP PRO SER
SEQRES 8 A 466 ASP MET CYS LYS LYS MET PHE GLU VAL GLU LYS VAL ASN
SEQRES 9 A 466 CYS ILE CYS VAL ASP TRP ARG HIS GLY SER ARG ALA MET
SEQRES 10 A 466 TYR THR GLN ALA VAL GLN ASN ILE ARG VAL VAL GLY ALA
SEQRES 11 A 466 GLU THR ALA PHE LEU ILE GLN ALA LEU SER THR GLN LEU
SEQRES 12 A 466 GLY TYR SER LEU GLU ASP VAL HIS VAL ILE GLY HIS SER
SEQRES 13 A 466 LEU GLY ALA HIS THR ALA ALA GLU ALA GLY ARG ARG LEU
SEQRES 14 A 466 GLY GLY ARG VAL GLY ARG ILE THR GLY LEU ASP PRO ALA
SEQRES 15 A 466 GLY PRO CYS PHE GLN ASP GLU PRO GLU GLU VAL ARG LEU
SEQRES 16 A 466 ASP PRO SER ASP ALA VAL PHE VAL ASP VAL ILE HIS THR
SEQRES 17 A 466 ASP SER SER PRO ILE VAL PRO SER LEU GLY PHE GLY MET
SEQRES 18 A 466 SER GLN LYS VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY
SEQRES 19 A 466 GLY LYS GLU MET PRO GLY CYS LYS LYS ASN VAL LEU SER
SEQRES 20 A 466 THR ILE THR ASP ILE ASP GLY ILE TRP GLU GLY ILE GLY
SEQRES 21 A 466 GLY PHE VAL SER CYS ASN HIS LEU ARG SER PHE GLU TYR
SEQRES 22 A 466 TYR SER SER SER VAL LEU ASN PRO ASP GLY PHE LEU GLY
SEQRES 23 A 466 TYR PRO CYS ALA SER TYR ASP GLU PHE GLN GLU SER LYS
SEQRES 24 A 466 CYS PHE PRO CYS PRO ALA GLU GLY CYS PRO LYS MET GLY
SEQRES 25 A 466 HIS TYR ALA ASP GLN PHE LYS GLY LYS THR SER ALA VAL
SEQRES 26 A 466 GLU GLN THR PHE PHE LEU ASN THR GLY GLU SER GLY ASN
SEQRES 27 A 466 PHE THR SER TRP ARG TYR LYS VAL SER VAL THR LEU SER
SEQRES 28 A 466 GLY LYS GLU LYS VAL ASN GLY TYR ILE ARG ILE ALA LEU
SEQRES 29 A 466 TYR GLY SER ASN GLU ASN SER LYS GLN TYR GLU ILE PHE
SEQRES 30 A 466 LYS GLY SER LEU LYS PRO ASP ALA SER HIS THR CYS ALA
SEQRES 31 A 466 ILE ASP VAL ASP PHE ASN VAL GLY LYS ILE GLN LYS VAL
SEQRES 32 A 466 LYS PHE LEU TRP ASN LYS ARG GLY ILE ASN LEU SER GLU
SEQRES 33 A 466 PRO LYS LEU GLY ALA SER GLN ILE THR VAL GLN SER GLY
SEQRES 34 A 466 GLU ASP GLY THR GLU TYR ASN PHE CYS SER SER ASP THR
SEQRES 35 A 466 VAL GLU GLU ASN VAL LEU GLN SER LEU TYR PRO CYS GLU
SEQRES 36 A 466 PHE VAL GLU HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 466 ALA ALA LYS GLU VAL CYS TYR GLY GLN LEU GLY CYS PHE
SEQRES 2 B 466 SER ASP GLU LYS PRO TRP ALA GLY THR LEU GLN ARG PRO
SEQRES 3 B 466 VAL LYS LEU LEU PRO TRP SER PRO GLU ASP ILE ASP THR
SEQRES 4 B 466 ARG PHE LEU LEU TYR THR ASN GLU ASN PRO ASN ASN PHE
SEQRES 5 B 466 GLN LEU ILE THR GLY THR GLU PRO ASP THR ILE GLU ALA
SEQRES 6 B 466 SER ASN PHE GLN LEU ASP ARG LYS THR ARG PHE ILE ILE
SEQRES 7 B 466 HIS GLY PHE LEU ASP LYS ALA GLU ASP SER TRP PRO SER
SEQRES 8 B 466 ASP MET CYS LYS LYS MET PHE GLU VAL GLU LYS VAL ASN
SEQRES 9 B 466 CYS ILE CYS VAL ASP TRP ARG HIS GLY SER ARG ALA MET
SEQRES 10 B 466 TYR THR GLN ALA VAL GLN ASN ILE ARG VAL VAL GLY ALA
SEQRES 11 B 466 GLU THR ALA PHE LEU ILE GLN ALA LEU SER THR GLN LEU
SEQRES 12 B 466 GLY TYR SER LEU GLU ASP VAL HIS VAL ILE GLY HIS SER
SEQRES 13 B 466 LEU GLY ALA HIS THR ALA ALA GLU ALA GLY ARG ARG LEU
SEQRES 14 B 466 GLY GLY ARG VAL GLY ARG ILE THR GLY LEU ASP PRO ALA
SEQRES 15 B 466 GLY PRO CYS PHE GLN ASP GLU PRO GLU GLU VAL ARG LEU
SEQRES 16 B 466 ASP PRO SER ASP ALA VAL PHE VAL ASP VAL ILE HIS THR
SEQRES 17 B 466 ASP SER SER PRO ILE VAL PRO SER LEU GLY PHE GLY MET
SEQRES 18 B 466 SER GLN LYS VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY
SEQRES 19 B 466 GLY LYS GLU MET PRO GLY CYS LYS LYS ASN VAL LEU SER
SEQRES 20 B 466 THR ILE THR ASP ILE ASP GLY ILE TRP GLU GLY ILE GLY
SEQRES 21 B 466 GLY PHE VAL SER CYS ASN HIS LEU ARG SER PHE GLU TYR
SEQRES 22 B 466 TYR SER SER SER VAL LEU ASN PRO ASP GLY PHE LEU GLY
SEQRES 23 B 466 TYR PRO CYS ALA SER TYR ASP GLU PHE GLN GLU SER LYS
SEQRES 24 B 466 CYS PHE PRO CYS PRO ALA GLU GLY CYS PRO LYS MET GLY
SEQRES 25 B 466 HIS TYR ALA ASP GLN PHE LYS GLY LYS THR SER ALA VAL
SEQRES 26 B 466 GLU GLN THR PHE PHE LEU ASN THR GLY GLU SER GLY ASN
SEQRES 27 B 466 PHE THR SER TRP ARG TYR LYS VAL SER VAL THR LEU SER
SEQRES 28 B 466 GLY LYS GLU LYS VAL ASN GLY TYR ILE ARG ILE ALA LEU
SEQRES 29 B 466 TYR GLY SER ASN GLU ASN SER LYS GLN TYR GLU ILE PHE
SEQRES 30 B 466 LYS GLY SER LEU LYS PRO ASP ALA SER HIS THR CYS ALA
SEQRES 31 B 466 ILE ASP VAL ASP PHE ASN VAL GLY LYS ILE GLN LYS VAL
SEQRES 32 B 466 LYS PHE LEU TRP ASN LYS ARG GLY ILE ASN LEU SER GLU
SEQRES 33 B 466 PRO LYS LEU GLY ALA SER GLN ILE THR VAL GLN SER GLY
SEQRES 34 B 466 GLU ASP GLY THR GLU TYR ASN PHE CYS SER SER ASP THR
SEQRES 35 B 466 VAL GLU GLU ASN VAL LEU GLN SER LEU TYR PRO CYS GLU
SEQRES 36 B 466 PHE VAL GLU HIS HIS HIS HIS HIS HIS HIS HIS
MODRES 2OXE ASN A 353 ASN GLYCOSYLATION SITE
MODRES 2OXE ASN B 353 ASN GLYCOSYLATION SITE
HET NAG A 500 14
HET NAG A 501 14
HET MAN A 502 11
HET MAN A 503 11
HET MAN A 504 11
HET NAG B 500 14
HET NAG B 501 14
HET MAN B 502 11
HET MAN B 503 11
HET MAN B 504 11
HET CA A 600 1
HET CA B 600 1
HET CL 1 1
HET CL 2 1
HET CL 3 1
HET CL 4 1
HET CL 5 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETSYN NAG NAG
FORMUL 3 NAG 4(C8 H15 N1 O6)
FORMUL 3 MAN 6(C6 H12 O6)
FORMUL 5 CA 2(CA1 2+)
FORMUL 7 CL 5(CL1 1-)
FORMUL 12 HOH *76(H2 O1)
HELIX 1 1 GLY A 23 LEU A 25 5 3
HELIX 2 2 SER A 48 ASP A 53 1 6
HELIX 3 3 PRO A 75 SER A 81 1 7
HELIX 4 4 SER A 103 PHE A 113 1 11
HELIX 5 5 TRP A 125 ARG A 130 1 6
HELIX 6 6 MET A 132 GLY A 159 1 28
HELIX 7 7 SER A 161 GLU A 163 5 3
HELIX 8 8 LEU A 172 LEU A 184 1 13
HELIX 9 9 ASP A 211 ALA A 215 5 5
HELIX 10 10 GLY A 275 VAL A 278 5 4
HELIX 11 11 SER A 279 ASN A 295 1 17
HELIX 12 12 SER A 306 GLU A 312 1 7
HELIX 13 13 TYR A 329 PHE A 333 5 5
HELIX 14 14 GLY B 23 LEU B 25 5 3
HELIX 15 15 SER B 48 ASP B 53 1 6
HELIX 16 16 PRO B 75 ALA B 80 1 6
HELIX 17 17 SER B 103 GLU B 116 1 14
HELIX 18 18 TRP B 125 ARG B 130 1 6
HELIX 19 19 TYR B 133 GLY B 159 1 27
HELIX 20 20 SER B 161 GLU B 163 5 3
HELIX 21 21 SER B 171 LEU B 184 1 14
HELIX 22 22 ASP B 211 ALA B 215 5 5
HELIX 23 23 GLY B 275 SER B 279 5 5
HELIX 24 24 SER B 285 ASN B 295 1 11
HELIX 25 25 SER B 306 GLU B 312 1 7
HELIX 26 26 TYR B 329 PHE B 333 5 5
SHEET 1 A 2 GLU A 19 CYS A 21 0
SHEET 2 A 2 CYS A 27 SER A 29 -1 O PHE A 28 N VAL A 20
SHEET 1 B10 ASN A 63 ILE A 70 0
SHEET 2 B10 ARG A 55 THR A 60 -1 N LEU A 58 O GLN A 68
SHEET 3 B10 VAL A 118 ASP A 124 -1 O CYS A 120 N TYR A 59
SHEET 4 B10 LYS A 88 ILE A 93 1 N ARG A 90 O ILE A 121
SHEET 5 B10 VAL A 165 HIS A 170 1 O HIS A 166 N PHE A 91
SHEET 6 B10 ARG A 190 LEU A 194 1 O LEU A 194 N GLY A 169
SHEET 7 B10 VAL A 218 ILE A 221 1 O ILE A 221 N GLY A 193
SHEET 8 B10 LEU A 243 PRO A 247 1 O PHE A 245 N VAL A 220
SHEET 9 B10 GLN A 342 LEU A 346 1 O PHE A 344 N PHE A 246
SHEET 10 B10 TYR A 302 PRO A 303 -1 N TYR A 302 O PHE A 345
SHEET 1 C 2 SER A 225 SER A 226 0
SHEET 2 C 2 GLY A 235 MET A 236 1 O GLY A 235 N SER A 226
SHEET 1 D 8 ASN A 385 LEU A 396 0
SHEET 2 D 8 VAL A 371 TYR A 380 -1 N LEU A 379 O SER A 386
SHEET 3 D 8 LYS A 417 ASN A 423 -1 O LEU A 421 N ARG A 376
SHEET 4 D 8 GLN A 464 PRO A 468 -1 O GLN A 464 N PHE A 420
SHEET 5 D 8 GLU A 449 CYS A 453 -1 N CYS A 453 O TYR A 467
SHEET 6 D 8 LEU A 434 SER A 443 -1 N VAL A 441 O TYR A 450
SHEET 7 D 8 TRP A 357 GLY A 367 -1 N SER A 362 O THR A 440
SHEET 8 D 8 SER A 401 VAL A 408 -1 O VAL A 408 N TRP A 357
SHEET 1 E 2 GLU B 19 CYS B 21 0
SHEET 2 E 2 CYS B 27 SER B 29 -1 O PHE B 28 N VAL B 20
SHEET 1 F10 GLN B 68 ILE B 70 0
SHEET 2 F10 ARG B 55 TYR B 59 -1 N LEU B 58 O GLN B 68
SHEET 3 F10 VAL B 118 ASP B 124 -1 O CYS B 120 N TYR B 59
SHEET 4 F10 LYS B 88 ILE B 93 1 N ARG B 90 O ILE B 121
SHEET 5 F10 VAL B 165 HIS B 170 1 O HIS B 166 N PHE B 91
SHEET 6 F10 ARG B 190 LEU B 194 1 O LEU B 194 N GLY B 169
SHEET 7 F10 PHE B 217 ILE B 221 1 O PHE B 217 N ILE B 191
SHEET 8 F10 LEU B 243 PRO B 247 1 O LEU B 243 N VAL B 220
SHEET 9 F10 GLN B 342 LEU B 346 1 O GLN B 342 N ASP B 244
SHEET 10 F10 TYR B 302 PRO B 303 -1 N TYR B 302 O PHE B 345
SHEET 1 G 2 SER B 225 SER B 226 0
SHEET 2 G 2 GLY B 235 MET B 236 1 O GLY B 235 N SER B 226
SHEET 1 H 8 TYR B 389 LEU B 396 0
SHEET 2 H 8 VAL B 371 TYR B 380 -1 N ILE B 377 O TYR B 389
SHEET 3 H 8 LYS B 417 ASN B 423 -1 O LEU B 421 N ARG B 376
SHEET 4 H 8 GLN B 464 PRO B 468 -1 O GLN B 464 N PHE B 420
SHEET 5 H 8 GLU B 449 CYS B 453 -1 N CYS B 453 O TYR B 467
SHEET 6 H 8 LEU B 434 SER B 443 -1 N VAL B 441 O TYR B 450
SHEET 7 H 8 TRP B 357 GLY B 367 -1 N LYS B 360 O GLN B 442
SHEET 8 H 8 SER B 401 VAL B 408 -1 O HIS B 402 N VAL B 363
SSBOND 1 CYS A 21 CYS A 27
SSBOND 2 CYS A 109 CYS A 120
SSBOND 3 CYS A 256 CYS A 280
SSBOND 4 CYS A 304 CYS A 315
SSBOND 5 CYS A 318 CYS A 323
SSBOND 6 CYS A 453 CYS A 469
SSBOND 7 CYS B 21 CYS B 27
SSBOND 8 CYS B 109 CYS B 120
SSBOND 9 CYS B 256 CYS B 280
SSBOND 10 CYS B 304 CYS B 315
SSBOND 11 CYS B 318 CYS B 323
SSBOND 12 CYS B 453 CYS B 469
LINK C1 NAG A 500 ND2 ASN A 353
LINK C1 NAG B 500 ND2 ASN B 353
LINK O4 NAG A 500 C1 NAG A 501
LINK O4 NAG A 501 C1 MAN A 502
LINK O6 MAN A 502 C1 MAN A 503
LINK O3 MAN A 502 C1 MAN A 504
LINK O4 NAG B 500 C1 NAG B 501
LINK O4 NAG B 501 C1 MAN B 502
LINK O6 MAN B 502 C1 MAN B 503
LINK O3 MAN B 502 C1 MAN B 504
CISPEP 1 LYS A 32 PRO A 33 0 2.63
CISPEP 2 VAL A 229 PRO A 230 0 -1.08
CISPEP 3 PHE A 316 PRO A 317 0 -5.22
CISPEP 4 LYS B 32 PRO B 33 0 9.53
CISPEP 5 VAL B 229 PRO B 230 0 0.43
CISPEP 6 PHE B 316 PRO B 317 0 -5.25
CRYST1 216.922 216.922 123.618 90.00 90.00 90.00 I 41 2 2 32
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 0.004610 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004610 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008089 0.00000
END |