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HEADER HYDROLASE 30-APR-07 2PPL
TITLE HUMAN PANCREATIC LIPASE-RELATED PROTEIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PANCREATIC LIPASE-RELATED PROTEIN 1;
COMPND 3 CHAIN: A;
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 GENE: PNLIPRP1, PLRP1;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HIGH5;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFHMSP-LIC N
KEYWDS HYDROLASE, LIPID DEGRADATION, PANCREATIC LIPASE, STRUCTURAL
KEYWDS 2 GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WALKER,T.DAVIS,A.SEITOVA,C.BUTLER-COLE,J.WEIGELT,
AUTHOR 2 M.SUNDSTROM,C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,S.DHE-
AUTHOR 3 PAGANON,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 1 05-JUN-07 2PPL 0
JRNL AUTH J.R.WALKER,T.DAVIS,A.SEITOVA,C.BUTLER-COLE,
JRNL AUTH 2 J.WEIGELT,M.SUNDSTROM,C.H.ARROWSMITH,A.M.EDWARDS,
JRNL AUTH 3 A.BOCHKAREV,S.DHE-PAGANON
JRNL TITL STRUCTURE OF THE HUMAN PANCREATIC LIPASE-RELATED
JRNL TITL 2 PROTEIN 1.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
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. DIFFERENCES IN
REMARK 1 TITL 3 COLIPASE DEPENDENCE AND IN LIPASE ACTIVITY
REMARK 1 REF J.BIOL.CHEM. V. 267 16509 1992
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 30748
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1660
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2189
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.59
REMARK 3 BIN R VALUE (WORKING SET) : 0.2200
REMARK 3 BIN FREE R VALUE SET COUNT : 125
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 3822
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.29000
REMARK 3 B22 (A**2) : 2.29000
REMARK 3 B33 (A**2) : -4.58000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.905
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3721 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5056 ; 1.218 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 472 ; 5.936 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 172 ;39.496 ;24.826
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 592 ;15.636 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;19.414 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 544 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2897 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1597 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2514 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 230 ; 0.123 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 9 ; 0.123 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 28 ; 0.212 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.080 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 1 ; 0.120 ; 0.200
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): 2325 ; 2.134 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3748 ; 3.456 ; 4.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1446 ; 4.561 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1308 ; 6.353 ; 7.000
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 : 13
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 17 A 48
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4570 -10.2310 14.1860
REMARK 3 T TENSOR
REMARK 3 T11: 0.1064 T22: 0.1691
REMARK 3 T33: 0.2018 T12: -0.0366
REMARK 3 T13: 0.0175 T23: -0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 2.1799 L22: 2.8569
REMARK 3 L33: 6.6754 L12: -0.0520
REMARK 3 L13: 0.3123 L23: 2.2759
REMARK 3 S TENSOR
REMARK 3 S11: -0.0680 S12: 0.0397 S13: 0.0573
REMARK 3 S21: -0.0365 S22: 0.2221 S23: -0.2388
REMARK 3 S31: -0.2126 S32: 0.4789 S33: -0.1540
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 49 A 100
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7530 -24.6500 4.5940
REMARK 3 T TENSOR
REMARK 3 T11: 0.1840 T22: 0.1520
REMARK 3 T33: 0.2013 T12: -0.0063
REMARK 3 T13: 0.0113 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 1.1266 L22: 0.2070
REMARK 3 L33: 1.8930 L12: 0.1357
REMARK 3 L13: 0.7297 L23: 0.1979
REMARK 3 S TENSOR
REMARK 3 S11: -0.0025 S12: 0.0589 S13: -0.0936
REMARK 3 S21: -0.0145 S22: 0.0496 S23: -0.0116
REMARK 3 S31: 0.0884 S32: 0.0866 S33: -0.0471
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 101 A 130
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1280 -26.6710 12.5880
REMARK 3 T TENSOR
REMARK 3 T11: 0.1884 T22: 0.1384
REMARK 3 T33: 0.1727 T12: 0.0003
REMARK 3 T13: 0.0146 T23: -0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 6.7435 L22: 1.1210
REMARK 3 L33: 1.3826 L12: 1.1554
REMARK 3 L13: 1.9902 L23: -0.3922
REMARK 3 S TENSOR
REMARK 3 S11: 0.0473 S12: -0.0764 S13: -0.3627
REMARK 3 S21: -0.0146 S22: 0.0030 S23: -0.0561
REMARK 3 S31: 0.0633 S32: -0.0722 S33: -0.0503
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 131 A 162
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8920 -14.6830 6.1490
REMARK 3 T TENSOR
REMARK 3 T11: 0.2005 T22: 0.2054
REMARK 3 T33: 0.2085 T12: -0.0184
REMARK 3 T13: -0.0029 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.9363 L22: 0.0042
REMARK 3 L33: 1.4985 L12: 0.0031
REMARK 3 L13: 0.9736 L23: 0.0485
REMARK 3 S TENSOR
REMARK 3 S11: -0.0508 S12: 0.1545 S13: -0.0176
REMARK 3 S21: -0.0446 S22: 0.0172 S23: -0.0507
REMARK 3 S31: -0.0483 S32: 0.1352 S33: 0.0336
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 163 A 231
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2510 -12.2850 20.6970
REMARK 3 T TENSOR
REMARK 3 T11: 0.1827 T22: 0.1889
REMARK 3 T33: 0.2029 T12: -0.0115
REMARK 3 T13: 0.0069 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.3511 L22: 0.4573
REMARK 3 L33: 0.9807 L12: -0.1470
REMARK 3 L13: -0.1189 L23: -0.0735
REMARK 3 S TENSOR
REMARK 3 S11: -0.0036 S12: -0.0512 S13: 0.0013
REMARK 3 S21: -0.0173 S22: 0.0241 S23: -0.0151
REMARK 3 S31: -0.0361 S32: 0.0164 S33: -0.0205
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 232 A 256
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7010 -15.3330 31.0800
REMARK 3 T TENSOR
REMARK 3 T11: 0.1676 T22: 0.1825
REMARK 3 T33: 0.1561 T12: -0.0054
REMARK 3 T13: -0.0043 T23: -0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 1.1221 L22: 3.2150
REMARK 3 L33: 1.3898 L12: -0.5673
REMARK 3 L13: -0.0165 L23: -0.5932
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: 0.0005 S13: 0.0270
REMARK 3 S21: 0.0811 S22: 0.0396 S23: 0.0522
REMARK 3 S31: -0.0862 S32: 0.0206 S33: -0.0372
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 257 A 273
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5600 -25.0930 33.0060
REMARK 3 T TENSOR
REMARK 3 T11: 0.2609 T22: 0.0671
REMARK 3 T33: 0.1813 T12: -0.0222
REMARK 3 T13: 0.0010 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 6.3049 L22: 0.8333
REMARK 3 L33: 10.2247 L12: 0.1156
REMARK 3 L13: -3.5990 L23: -1.1357
REMARK 3 S TENSOR
REMARK 3 S11: -0.0372 S12: -0.2738 S13: 0.0255
REMARK 3 S21: 0.2441 S22: 0.0346 S23: 0.0190
REMARK 3 S31: 0.1777 S32: 0.2910 S33: 0.0026
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 274 A 330
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2630 -17.3610 29.6280
REMARK 3 T TENSOR
REMARK 3 T11: 0.1718 T22: 0.1676
REMARK 3 T33: 0.1929 T12: -0.0209
REMARK 3 T13: 0.0009 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 1.2835 L22: 0.4059
REMARK 3 L33: 0.8846 L12: -0.3716
REMARK 3 L13: -0.0706 L23: -0.1347
REMARK 3 S TENSOR
REMARK 3 S11: 0.0054 S12: -0.0023 S13: -0.0269
REMARK 3 S21: -0.0094 S22: -0.0068 S23: 0.0169
REMARK 3 S31: 0.0589 S32: -0.0421 S33: 0.0014
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 331 A 353
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2640 -14.6150 28.9980
REMARK 3 T TENSOR
REMARK 3 T11: 0.1331 T22: 0.1716
REMARK 3 T33: 0.1728 T12: 0.0136
REMARK 3 T13: 0.0151 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 1.7191 L22: 4.3999
REMARK 3 L33: 2.5123 L12: 0.4325
REMARK 3 L13: 0.3133 L23: -2.3478
REMARK 3 S TENSOR
REMARK 3 S11: 0.0398 S12: -0.0841 S13: 0.0968
REMARK 3 S21: 0.0593 S22: -0.0673 S23: 0.0924
REMARK 3 S31: -0.0176 S32: -0.0035 S33: 0.0274
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 354 A 373
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9920 -19.5050 48.3230
REMARK 3 T TENSOR
REMARK 3 T11: 0.1530 T22: 0.1915
REMARK 3 T33: 0.1929 T12: -0.0021
REMARK 3 T13: -0.0039 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.4782 L22: 0.6471
REMARK 3 L33: 4.5139 L12: 0.1601
REMARK 3 L13: -1.4116 L23: -0.0187
REMARK 3 S TENSOR
REMARK 3 S11: 0.0623 S12: 0.0551 S13: 0.0008
REMARK 3 S21: 0.0349 S22: 0.0688 S23: 0.0065
REMARK 3 S31: -0.0267 S32: -0.1256 S33: -0.1311
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 374 A 396
REMARK 3 ORIGIN FOR THE GROUP (A): -11.7520 -23.5620 45.9980
REMARK 3 T TENSOR
REMARK 3 T11: 0.1594 T22: 0.1588
REMARK 3 T33: 0.1999 T12: 0.0132
REMARK 3 T13: 0.0026 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.8891 L22: 1.8475
REMARK 3 L33: 6.6140 L12: 0.9705
REMARK 3 L13: 0.3857 L23: 2.5384
REMARK 3 S TENSOR
REMARK 3 S11: -0.0194 S12: -0.0124 S13: -0.0777
REMARK 3 S21: 0.0237 S22: 0.0618 S23: -0.0793
REMARK 3 S31: 0.1402 S32: -0.0747 S33: -0.0424
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 397 A 443
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6810 -21.5530 48.1280
REMARK 3 T TENSOR
REMARK 3 T11: 0.1484 T22: 0.1620
REMARK 3 T33: 0.1886 T12: 0.0137
REMARK 3 T13: -0.0066 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.3431 L22: 0.4598
REMARK 3 L33: 3.3468 L12: 0.1015
REMARK 3 L13: -0.4062 L23: -0.5998
REMARK 3 S TENSOR
REMARK 3 S11: -0.0382 S12: 0.0026 S13: -0.0167
REMARK 3 S21: -0.0225 S22: 0.0318 S23: 0.0153
REMARK 3 S31: -0.0046 S32: -0.0963 S33: 0.0064
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 444 A 468
REMARK 3 ORIGIN FOR THE GROUP (A): -21.3090 -20.3650 46.8970
REMARK 3 T TENSOR
REMARK 3 T11: 0.1828 T22: 0.2240
REMARK 3 T33: 0.1903 T12: 0.0096
REMARK 3 T13: -0.0102 T23: -0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 2.4514 L22: 1.1721
REMARK 3 L33: 4.6607 L12: -0.1075
REMARK 3 L13: -0.7784 L23: -1.4182
REMARK 3 S TENSOR
REMARK 3 S11: 0.0433 S12: 0.0458 S13: -0.1709
REMARK 3 S21: 0.0114 S22: -0.0187 S23: 0.0985
REMARK 3 S31: 0.0598 S32: -0.1981 S33: -0.0246
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 2PPL COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-2007.
REMARK 100 THE RCSB ID CODE IS RCSB042643.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAR-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
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) : 0.97923
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32518
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 12.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11300
REMARK 200 FOR THE DATA SET : 27.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.30600
REMARK 200 FOR SHELL : 4.400
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 1RP1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.2M CA ACETATE, 0.1
REMARK 280 NA CACODYLATE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291.0K, PH 6.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 3555 1/2-Y,1/2+X,1/4+Z
REMARK 290 4555 1/2+Y,1/2-X,3/4+Z
REMARK 290 5555 1/2-X,1/2+Y,1/4-Z
REMARK 290 6555 1/2+X,1/2-Y,3/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 153.14000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.43550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.43550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 76.57000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.43550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.43550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 229.71000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.43550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.43550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 76.57000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.43550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.43550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 229.71000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
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 153.14000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 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 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 -7
REMARK 465 PRO A -6
REMARK 465 GLU A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 ASP A 2
REMARK 465 TYR A 3
REMARK 465 ASP A 4
REMARK 465 ILE A 5
REMARK 465 PRO A 6
REMARK 465 THR A 7
REMARK 465 THR A 8
REMARK 465 GLU A 9
REMARK 465 ASN A 10
REMARK 465 LEU A 11
REMARK 465 TYR A 12
REMARK 465 PHE A 13
REMARK 465 GLN A 14
REMARK 465 GLY A 15
REMARK 465 ALA A 16
REMARK 465 THR A 336
REMARK 465 SER A 337
REMARK 465 GLU A 338
REMARK 465 SER A 469
REMARK 465 LEU A 470
REMARK 465 SER A 471
REMARK 465 ARG A 472
REMARK 465 SER A 473
REMARK 465 THR A 474
REMARK 465 ARG A 475
REMARK 465 GLY A 476
REMARK 465 SER A 477
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 CE NZ
REMARK 470 LYS A 99 CG CD CE NZ
REMARK 470 LYS A 126 NZ
REMARK 470 LYS A 307 CD CE NZ
REMARK 470 LYS A 395 CD CE NZ
REMARK 470 LYS A 445 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 ILE A 373 CG1 ILE A 373 CD1 0.063
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 LYS A 18 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 LEU A 172 CA - CB - CG ANGL. DEV. = 7.4 DEGREES
REMARK 500 PRO A 229 C - N - CA ANGL. DEV. = 8.4 DEGREES
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OXE RELATED DB: PDB
REMARK 900 PANCREATIC LIPASE-RELATED PROTEIN 2
DBREF 2PPL A 18 467 UNP P54315 LIPR1_HUMAN 18 467
SEQADV 2PPL ALA A -7 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL PRO A -6 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL GLU A -5 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL HIS A -4 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL HIS A -3 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL HIS A -2 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL HIS A -1 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL HIS A 0 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL HIS A 1 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL ASP A 2 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL TYR A 3 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL ASP A 4 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL ILE A 5 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL PRO A 6 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL THR A 7 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL THR A 8 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL GLU A 9 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL ASN A 10 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL LEU A 11 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL TYR A 12 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL PHE A 13 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL GLN A 14 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL GLY A 15 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL ALA A 16 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL MET A 17 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL ASP A 414 UNP P54315 GLU 414 VARIANT
SEQADV 2PPL PRO A 468 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL SER A 469 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL LEU A 470 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL SER A 471 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL ARG A 472 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL SER A 473 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL THR A 474 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL ARG A 475 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL GLY A 476 UNP P54315 CLONING ARTIFACT
SEQADV 2PPL SER A 477 UNP P54315 CLONING ARTIFACT
SEQRES 1 A 485 ALA PRO GLU HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE
SEQRES 2 A 485 PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET LYS
SEQRES 3 A 485 GLU VAL CYS TYR GLU ASP LEU GLY CYS PHE SER ASP THR
SEQRES 4 A 485 GLU PRO TRP GLY GLY THR ALA ILE ARG PRO LEU LYS ILE
SEQRES 5 A 485 LEU PRO TRP SER PRO GLU LYS ILE GLY THR ARG PHE LEU
SEQRES 6 A 485 LEU TYR THR ASN GLU ASN PRO ASN ASN PHE GLN ILE LEU
SEQRES 7 A 485 LEU LEU SER ASP PRO SER THR ILE GLU ALA SER ASN PHE
SEQRES 8 A 485 GLN MET ASP ARG LYS THR ARG PHE ILE ILE HIS GLY PHE
SEQRES 9 A 485 ILE ASP LYS GLY ASP GLU SER TRP VAL THR ASP MET CYS
SEQRES 10 A 485 LYS LYS LEU PHE GLU VAL GLU GLU VAL ASN CYS ILE CYS
SEQRES 11 A 485 VAL ASP TRP LYS LYS GLY SER GLN ALA THR TYR THR GLN
SEQRES 12 A 485 ALA ALA ASN ASN VAL ARG VAL VAL GLY ALA GLN VAL ALA
SEQRES 13 A 485 GLN MET LEU ASP ILE LEU LEU THR GLU TYR SER TYR PRO
SEQRES 14 A 485 PRO SER LYS VAL HIS LEU ILE GLY HIS SER LEU GLY ALA
SEQRES 15 A 485 HIS VAL ALA GLY GLU ALA GLY SER LYS THR PRO GLY LEU
SEQRES 16 A 485 SER ARG ILE THR GLY LEU ASP PRO VAL GLU ALA SER PHE
SEQRES 17 A 485 GLU SER THR PRO GLU GLU VAL ARG LEU ASP PRO SER ASP
SEQRES 18 A 485 ALA ASP PHE VAL ASP VAL ILE HIS THR ASP ALA ALA PRO
SEQRES 19 A 485 LEU ILE PRO PHE LEU GLY PHE GLY THR ASN GLN GLN MET
SEQRES 20 A 485 GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY GLU SER MET
SEQRES 21 A 485 PRO GLY CYS LYS LYS ASN ALA LEU SER GLN ILE VAL ASP
SEQRES 22 A 485 LEU ASP GLY ILE TRP ALA GLY THR ARG ASP PHE VAL ALA
SEQRES 23 A 485 CYS ASN HIS LEU ARG SER TYR LYS TYR TYR LEU GLU SER
SEQRES 24 A 485 ILE LEU ASN PRO ASP GLY PHE ALA ALA TYR PRO CYS THR
SEQRES 25 A 485 SER TYR LYS SER PHE GLU SER ASP LYS CYS PHE PRO CYS
SEQRES 26 A 485 PRO ASP GLN GLY CYS PRO GLN MET GLY HIS TYR ALA ASP
SEQRES 27 A 485 LYS PHE ALA GLY ARG THR SER GLU GLU GLN GLN LYS PHE
SEQRES 28 A 485 PHE LEU ASN THR GLY GLU ALA SER ASN PHE ALA ARG TRP
SEQRES 29 A 485 ARG TYR GLY VAL SER ILE THR LEU SER GLY ARG THR ALA
SEQRES 30 A 485 THR GLY GLN ILE LYS VAL ALA LEU PHE GLY ASN LYS GLY
SEQRES 31 A 485 ASN THR HIS GLN TYR SER ILE PHE ARG GLY ILE LEU LYS
SEQRES 32 A 485 PRO GLY SER THR HIS SER TYR GLU PHE ASP ALA LYS LEU
SEQRES 33 A 485 ASP VAL GLY THR ILE ASP LYS VAL LYS PHE LEU TRP ASN
SEQRES 34 A 485 ASN ASN VAL ILE ASN PRO THR LEU PRO LYS VAL GLY ALA
SEQRES 35 A 485 THR LYS ILE THR VAL GLN LYS GLY GLU GLU LYS THR VAL
SEQRES 36 A 485 TYR ASN PHE CYS SER GLU ASP THR VAL ARG GLU ASP THR
SEQRES 37 A 485 LEU LEU THR LEU THR PRO CYS PRO SER LEU SER ARG SER
SEQRES 38 A 485 THR ARG GLY SER
HET CA 1 1
HET NA 2 1
HET NA 3 1
HET CA 4 1
HET CA 5 1
HET NA 6 1
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
FORMUL 2 CA 3(CA1 2+)
FORMUL 3 NA 3(NA1 1+)
FORMUL 8 HOH *218(H2 O1)
HELIX 1 1 SER A 48 GLY A 53 1 6
HELIX 2 2 PRO A 75 SER A 81 1 7
HELIX 3 3 SER A 103 GLU A 116 1 14
HELIX 4 4 TRP A 125 GLN A 130 1 6
HELIX 5 5 THR A 132 SER A 159 1 28
HELIX 6 6 PRO A 161 SER A 163 5 3
HELIX 7 7 LEU A 172 LYS A 183 1 12
HELIX 8 8 ASP A 210 ALA A 214 5 5
HELIX 9 9 PRO A 226 LEU A 231 1 6
HELIX 10 10 ASP A 265 ALA A 271 1 7
HELIX 11 11 ALA A 278 ASN A 294 1 17
HELIX 12 12 SER A 305 SER A 311 1 7
HELIX 13 13 GLY A 326 PHE A 332 5 7
SHEET 1 A 2 GLU A 19 TYR A 22 0
SHEET 2 A 2 GLY A 26 SER A 29 -1 O PHE A 28 N VAL A 20
SHEET 1 B10 GLN A 68 LEU A 70 0
SHEET 2 B10 ARG A 55 TYR A 59 -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 ILE A 92 O ILE A 121
SHEET 5 B10 VAL A 165 HIS A 170 1 O ILE A 168 N PHE A 91
SHEET 6 B10 ARG A 189 LEU A 193 1 O THR A 191 N GLY A 169
SHEET 7 B10 PHE A 216 ILE A 220 1 O ILE A 220 N GLY A 192
SHEET 8 B10 LEU A 242 PRO A 246 1 O PHE A 244 N VAL A 219
SHEET 9 B10 GLN A 341 LEU A 345 1 O PHE A 343 N ASP A 243
SHEET 10 B10 TYR A 301 PRO A 302 -1 N TYR A 301 O PHE A 344
SHEET 1 C 8 GLY A 382 ASN A 383 0
SHEET 2 C 8 ALA A 369 GLY A 379 -1 N GLY A 379 O GLY A 382
SHEET 3 C 8 ILE A 413 ASN A 421 -1 O ASN A 421 N GLN A 372
SHEET 4 C 8 LEU A 462 PRO A 466 -1 O LEU A 464 N VAL A 416
SHEET 5 C 8 VAL A 447 CYS A 451 -1 N CYS A 451 O THR A 465
SHEET 6 C 8 VAL A 432 LYS A 441 -1 N ILE A 437 O PHE A 450
SHEET 7 C 8 TRP A 356 GLY A 366 -1 N GLY A 359 O GLN A 440
SHEET 8 C 8 THR A 399 ALA A 406 -1 O ALA A 406 N TRP A 356
SHEET 1 D 7 TYR A 387 LEU A 394 0
SHEET 2 D 7 ALA A 369 GLY A 379 -1 N ALA A 369 O LEU A 394
SHEET 3 D 7 ILE A 413 ASN A 421 -1 O ASN A 421 N GLN A 372
SHEET 4 D 7 LEU A 462 PRO A 466 -1 O LEU A 464 N VAL A 416
SHEET 5 D 7 VAL A 447 CYS A 451 -1 N CYS A 451 O THR A 465
SHEET 6 D 7 VAL A 432 LYS A 441 -1 N ILE A 437 O PHE A 450
SHEET 7 D 7 THR A 455 VAL A 456 -1 O VAL A 456 N VAL A 432
SSBOND 1 CYS A 21 CYS A 27
SSBOND 2 CYS A 109 CYS A 120
SSBOND 3 CYS A 255 CYS A 279
SSBOND 4 CYS A 303 CYS A 314
SSBOND 5 CYS A 317 CYS A 322
SSBOND 6 CYS A 451 CYS A 467
LINK O GLU A 79 NA NA 2
LINK O SER A 81 NA NA 2
LINK O LYS A 183 NA NA 6
LINK OE1 GLU A 197 NA NA 3
LINK O AGLU A 205 CA CA 1
LINK O BGLU A 205 CA CA 1
LINK O ARG A 208 CA CA 1
LINK OD1 ASP A 210 CA CA 1
LINK OD1 ASP A 213 CA CA 1
LINK OD2 ASP A 213 CA CA 1
LINK O ALA A 225 NA NA 3
LINK O GLY A 232 NA NA 3
LINK O GLY A 234 NA NA 3
LINK OD1 ASN A 421 CA CA 4
LINK O ASN A 422 CA CA 4
LINK OD1 ASN A 422 CA CA 5
LINK O VAL A 424 CA CA 5
LINK OD1 ASN A 426 CA CA 5
LINK OE1 GLU A 458 CA CA 5
LINK OE2 GLU A 458 CA CA 4
LINK OE2 GLU A 458 CA CA 5
LINK CA CA 1 O HOH 104
LINK CA CA 1 O HOH 61
LINK NA NA 2 O HOH 126
LINK NA NA 2 O HOH 9
LINK NA NA 2 O HOH 221
LINK NA NA 2 O HOH 222
LINK NA NA 3 O HOH 112
LINK CA CA 5 O HOH 130
LINK NA NA 6 O HOH 80
LINK NA NA 6 O HOH 92
LINK NA NA 6 O HOH 150
CISPEP 1 GLU A 32 PRO A 33 0 2.51
CISPEP 2 ILE A 228 PRO A 229 0 2.58
CISPEP 3 PHE A 315 PRO A 316 0 -3.78
CISPEP 4 SER A 351 ASN A 352 0 -0.30
CRYST1 62.871 62.871 306.280 90.00 90.00 90.00 P 41 21 2 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 0.015906 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015906 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003265 0.00000
END |