HEADER IMMUNE SYSTEM 12-OCT-10 3P7G
TITLE STRUCTURE OF THE HUMAN LANGERIN CARBOHYDRATE RECOGNITION DOMAIN IN
TITLE 2 COMPLEX WITH MANNOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-TYPE LECTIN DOMAIN FAMILY 4 MEMBER K;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUES 193-328);
COMPND 5 SYNONYM: LANGERIN;
COMPND 6 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: CD207, CLEC4K, LEUCOCYTE CDNA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM83;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PLA1
KEYWDS C-TYPE LECTIN, MEMBRANE PROTEIN, GLYCOPROTEIN, LANGERIN, DC-SIGN,
KEYWDS 2 CARBOHYDRATE BINDING PROTEIN, CALCIUM BINDING, SUGAR BINDING, IMMUNE
KEYWDS 3 SYSTEM, LANGERHANS CELLS, CD207
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SKERRA,A.SCHIEFNER
REVDAT 3 29-JUL-20 3P7G 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 LINK SITE
REVDAT 2 08-NOV-17 3P7G 1 REMARK
REVDAT 1 03-NOV-10 3P7G 0
SPRSDE 03-NOV-10 3P7G 3BC7
JRNL AUTH L.CHATWELL,A.HOLLA,B.B.KAUFER,A.SKERRA
JRNL TITL THE CARBOHYDRATE RECOGNITION DOMAIN OF LANGERIN REVEALS HIGH
JRNL TITL 2 STRUCTURAL SIMILARITY WITH THE ONE OF DC-SIGN BUT AN
JRNL TITL 3 ADDITIONAL, CALCIUM-INDEPENDENT SUGAR-BINDING SITE.
JRNL REF MOL.IMMUNOL. V. 45 1981 2008
JRNL REFN ISSN 0161-5890
JRNL PMID 18061677
JRNL DOI 10.1016/J.MOLIMM.2007.10.030
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 87378
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1789
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6390
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 137
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4279
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 593
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : -0.07000
REMARK 3 B33 (A**2) : 0.14000
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): 0.071
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.049
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.791
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4582 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6264 ; 1.862 ; 1.925
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 538 ; 6.863 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 223 ;34.086 ;24.260
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 678 ;12.440 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ; 8.833 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 618 ; 0.132 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3625 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2671 ; 1.174 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4319 ; 1.898 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1911 ; 3.161 ; 3.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1945 ; 4.560 ;10.000
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 : 12
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 198 A 263
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0972 16.1689 -33.4657
REMARK 3 T TENSOR
REMARK 3 T11: 0.0641 T22: 0.0592
REMARK 3 T33: 0.0872 T12: 0.0420
REMARK 3 T13: -0.0683 T23: -0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 2.7184 L22: 1.5640
REMARK 3 L33: 3.3394 L12: -0.2760
REMARK 3 L13: -0.6673 L23: 0.1823
REMARK 3 S TENSOR
REMARK 3 S11: -0.0542 S12: -0.0384 S13: 0.0329
REMARK 3 S21: -0.0925 S22: -0.0505 S23: 0.0301
REMARK 3 S31: 0.0300 S32: -0.0264 S33: 0.1048
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 264 A 322
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1837 25.7813 -33.5852
REMARK 3 T TENSOR
REMARK 3 T11: 0.0951 T22: 0.0725
REMARK 3 T33: 0.1221 T12: 0.0534
REMARK 3 T13: -0.0861 T23: -0.0600
REMARK 3 L TENSOR
REMARK 3 L11: 2.2517 L22: 1.8792
REMARK 3 L33: 1.7274 L12: 0.1685
REMARK 3 L13: 0.3615 L23: -0.2172
REMARK 3 S TENSOR
REMARK 3 S11: -0.0684 S12: -0.0059 S13: 0.3000
REMARK 3 S21: -0.1330 S22: -0.0595 S23: 0.1260
REMARK 3 S31: -0.2069 S32: -0.0874 S33: 0.1279
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 323 A 332
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9966 4.4132 -28.7554
REMARK 3 T TENSOR
REMARK 3 T11: 0.4060 T22: 0.3870
REMARK 3 T33: 0.3943 T12: 0.1213
REMARK 3 T13: -0.1864 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 17.4837 L22: 0.8108
REMARK 3 L33: 11.7312 L12: 3.7404
REMARK 3 L13: 14.3067 L23: 3.0450
REMARK 3 S TENSOR
REMARK 3 S11: 1.5953 S12: 0.6680 S13: -2.2428
REMARK 3 S21: 0.3171 S22: 0.1432 S23: -0.5077
REMARK 3 S31: 1.2628 S32: 0.6255 S33: -1.7385
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 : B 196 B 267
REMARK 3 ORIGIN FOR THE GROUP (A): 31.9390 26.9726 -31.3437
REMARK 3 T TENSOR
REMARK 3 T11: 0.0223 T22: 0.0423
REMARK 3 T33: 0.0300 T12: 0.0112
REMARK 3 T13: 0.0100 T23: 0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 2.2719 L22: 3.1963
REMARK 3 L33: 2.7707 L12: -0.6551
REMARK 3 L13: 0.8982 L23: -0.4063
REMARK 3 S TENSOR
REMARK 3 S11: 0.0245 S12: 0.1332 S13: 0.1928
REMARK 3 S21: -0.1276 S22: -0.1071 S23: -0.0206
REMARK 3 S31: -0.1209 S32: 0.0291 S33: 0.0826
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 268 B 279
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8629 15.1270 -35.1477
REMARK 3 T TENSOR
REMARK 3 T11: 0.0664 T22: 0.0590
REMARK 3 T33: 0.0588 T12: 0.0175
REMARK 3 T13: -0.0053 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 5.0156 L22: 8.2550
REMARK 3 L33: 7.5502 L12: 0.7034
REMARK 3 L13: -1.1373 L23: 5.3194
REMARK 3 S TENSOR
REMARK 3 S11: -0.1702 S12: 0.1717 S13: -0.3354
REMARK 3 S21: -0.2555 S22: -0.0836 S23: 0.0700
REMARK 3 S31: 0.1770 S32: -0.0700 S33: 0.2538
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 280 B 325
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8235 19.9247 -32.6228
REMARK 3 T TENSOR
REMARK 3 T11: 0.0245 T22: 0.0790
REMARK 3 T33: 0.0387 T12: 0.0084
REMARK 3 T13: 0.0184 T23: 0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 1.5721 L22: 2.8639
REMARK 3 L33: 2.8886 L12: -0.3092
REMARK 3 L13: 0.1983 L23: 0.2108
REMARK 3 S TENSOR
REMARK 3 S11: 0.0288 S12: 0.1790 S13: -0.0371
REMARK 3 S21: -0.1304 S22: -0.0689 S23: -0.1762
REMARK 3 S31: 0.1012 S32: 0.2535 S33: 0.0401
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 : C 198 C 239
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2374 12.9876 -7.0324
REMARK 3 T TENSOR
REMARK 3 T11: 0.0630 T22: 0.0147
REMARK 3 T33: 0.0242 T12: -0.0167
REMARK 3 T13: -0.0173 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 3.8464 L22: 2.5389
REMARK 3 L33: 4.7380 L12: 0.7345
REMARK 3 L13: -1.1934 L23: -0.8482
REMARK 3 S TENSOR
REMARK 3 S11: -0.0546 S12: -0.1444 S13: -0.2336
REMARK 3 S21: 0.0471 S22: 0.0283 S23: -0.0082
REMARK 3 S31: 0.3100 S32: -0.1304 S33: 0.0262
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 : C 240 C 287
REMARK 3 ORIGIN FOR THE GROUP (A): 29.3248 25.9999 -3.9331
REMARK 3 T TENSOR
REMARK 3 T11: 0.0694 T22: 0.0610
REMARK 3 T33: 0.0759 T12: -0.0010
REMARK 3 T13: -0.0100 T23: -0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 4.3476 L22: 2.6525
REMARK 3 L33: 2.4622 L12: -0.7387
REMARK 3 L13: 0.6827 L23: 0.2152
REMARK 3 S TENSOR
REMARK 3 S11: -0.1262 S12: -0.2235 S13: 0.5563
REMARK 3 S21: 0.1170 S22: 0.0387 S23: -0.0394
REMARK 3 S31: -0.2951 S32: -0.2095 S33: 0.0876
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 288 C 331
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9005 20.7470 -6.7152
REMARK 3 T TENSOR
REMARK 3 T11: 0.0286 T22: 0.0075
REMARK 3 T33: 0.0296 T12: 0.0121
REMARK 3 T13: -0.0199 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 3.3764 L22: 2.7383
REMARK 3 L33: 2.9173 L12: -0.0176
REMARK 3 L13: 0.1382 L23: -0.3630
REMARK 3 S TENSOR
REMARK 3 S11: -0.0973 S12: -0.1130 S13: 0.2795
REMARK 3 S21: 0.0230 S22: 0.0335 S23: -0.0537
REMARK 3 S31: -0.0368 S32: 0.0127 S33: 0.0637
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 : D 196 D 204
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8518 34.4148 -1.6682
REMARK 3 T TENSOR
REMARK 3 T11: 0.1253 T22: 0.0907
REMARK 3 T33: 0.1221 T12: -0.0516
REMARK 3 T13: 0.0339 T23: -0.0530
REMARK 3 L TENSOR
REMARK 3 L11: 16.1569 L22: 8.8594
REMARK 3 L33: 9.8254 L12: -3.8180
REMARK 3 L13: 4.3043 L23: -1.7298
REMARK 3 S TENSOR
REMARK 3 S11: -0.0875 S12: -0.3417 S13: 0.4407
REMARK 3 S21: 0.0238 S22: 0.0062 S23: 0.2349
REMARK 3 S31: -0.6242 S32: -0.3570 S33: 0.0813
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 : D 205 D 261
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2577 24.1869 -7.5285
REMARK 3 T TENSOR
REMARK 3 T11: 0.0135 T22: 0.0749
REMARK 3 T33: 0.0697 T12: -0.0147
REMARK 3 T13: 0.0216 T23: -0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 2.6372 L22: 3.1857
REMARK 3 L33: 4.6784 L12: -0.0524
REMARK 3 L13: -0.1172 L23: 0.9127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0468 S12: -0.0381 S13: -0.0336
REMARK 3 S21: 0.0302 S22: -0.2186 S23: 0.2359
REMARK 3 S31: -0.0729 S32: -0.1431 S33: 0.1718
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 : D 262 D 325
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0011 15.9074 -6.6970
REMARK 3 T TENSOR
REMARK 3 T11: 0.0718 T22: 0.0965
REMARK 3 T33: 0.1099 T12: -0.0464
REMARK 3 T13: 0.0515 T23: -0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 2.7332 L22: 2.1791
REMARK 3 L33: 2.8302 L12: -0.8621
REMARK 3 L13: -0.2041 L23: 0.5739
REMARK 3 S TENSOR
REMARK 3 S11: -0.0296 S12: -0.1051 S13: -0.3681
REMARK 3 S21: 0.1629 S22: -0.1659 S23: 0.2776
REMARK 3 S31: 0.3158 S32: -0.1699 S33: 0.1955
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3P7G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000062051.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796, 0.9798, 0.9080
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89165
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.33600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD, SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 10MG/ML LANGERIN IN 10 MM
REMARK 280 TRIS/HCL PH 7.5, 5 MM MANNOSE; RESERVOIR: 0.1 M NA-CACODYLATE,
REMARK 280 13 %(W/V) PEG4000, 0.1 M MGCL2, 5MM CACL2, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K, PH 6.9
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z+1/2
REMARK 290 4555 Y,-X,Z+1/2
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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 44.99000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.99000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLN A 193
REMARK 465 VAL A 194
REMARK 465 VAL A 195
REMARK 465 SER A 196
REMARK 465 GLN A 197
REMARK 465 HIS A 333
REMARK 465 PRO A 334
REMARK 465 GLN A 335
REMARK 465 PHE A 336
REMARK 465 GLU A 337
REMARK 465 LYS A 338
REMARK 465 GLN B 193
REMARK 465 VAL B 194
REMARK 465 VAL B 195
REMARK 465 SER B 326
REMARK 465 GLU B 327
REMARK 465 PRO B 328
REMARK 465 SER B 329
REMARK 465 ALA B 330
REMARK 465 TRP B 331
REMARK 465 SER B 332
REMARK 465 HIS B 333
REMARK 465 PRO B 334
REMARK 465 GLN B 335
REMARK 465 PHE B 336
REMARK 465 GLU B 337
REMARK 465 LYS B 338
REMARK 465 GLN C 193
REMARK 465 VAL C 194
REMARK 465 VAL C 195
REMARK 465 SER C 196
REMARK 465 GLN C 197
REMARK 465 GLU C 327
REMARK 465 PRO C 328
REMARK 465 SER C 329
REMARK 465 ALA C 330
REMARK 465 SER C 332
REMARK 465 HIS C 333
REMARK 465 PRO C 334
REMARK 465 GLN C 335
REMARK 465 PHE C 336
REMARK 465 GLU C 337
REMARK 465 LYS C 338
REMARK 465 GLN D 193
REMARK 465 VAL D 194
REMARK 465 VAL D 195
REMARK 465 SER D 326
REMARK 465 GLU D 327
REMARK 465 PRO D 328
REMARK 465 SER D 329
REMARK 465 ALA D 330
REMARK 465 TRP D 331
REMARK 465 SER D 332
REMARK 465 HIS D 333
REMARK 465 PRO D 334
REMARK 465 GLN D 335
REMARK 465 PHE D 336
REMARK 465 GLU D 337
REMARK 465 LYS D 338
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR B 208 CZ TYR B 208 CE2 -0.079
REMARK 500 ASN C 291 CG ASN C 291 OD1 0.180
REMARK 500 ASN C 291 CG ASN C 291 ND2 0.279
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR B 217 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 TYR B 217 CZ - CE2 - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP B 268 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TYR C 201 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TYR C 217 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
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 PRO A 328 155.55 -47.03
REMARK 500 ASN B 292 24.72 -141.34
REMARK 500 ASN C 292 30.30 -146.04
REMARK 500 LYS C 299 -54.12 -120.54
REMARK 500 ASP D 269 3.56 82.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 285 OE1
REMARK 620 2 ASN A 287 OD1 74.3
REMARK 620 3 GLU A 293 OE1 144.2 74.4
REMARK 620 4 ASN A 307 OD1 70.6 143.1 142.4
REMARK 620 5 ASP A 308 OD1 75.4 88.6 87.0 92.9
REMARK 620 6 ASP A 308 O 129.9 142.5 71.6 72.2 74.3
REMARK 620 7 MAN A 339 O4 75.6 78.0 113.9 82.9 150.3 130.8
REMARK 620 8 MAN A 339 O3 135.9 116.1 74.6 83.3 142.7 69.2 66.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 285 OE1
REMARK 620 2 ASN B 287 OD1 74.8
REMARK 620 3 GLU B 293 OE1 142.3 71.6
REMARK 620 4 ASN B 307 OD1 70.3 143.8 144.6
REMARK 620 5 ASP B 308 OD1 73.7 86.9 87.7 92.6
REMARK 620 6 ASP B 308 O 131.0 139.6 71.7 74.2 75.2
REMARK 620 7 MAN B 339 O4 73.1 77.2 114.7 83.4 146.0 134.5
REMARK 620 8 MAN B 339 O3 134.4 115.9 77.2 83.2 145.9 71.1 67.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 285 OE1
REMARK 620 2 ASN C 287 OD1 70.7
REMARK 620 3 GLU C 293 OE1 142.6 75.8
REMARK 620 4 ASN C 307 OD1 69.2 138.8 145.3
REMARK 620 5 ASP C 308 OD1 70.2 84.9 90.9 90.6
REMARK 620 6 ASP C 308 O 129.4 143.1 72.7 73.9 76.9
REMARK 620 7 MAN C 339 O4 75.1 77.0 113.2 83.8 144.6 133.6
REMARK 620 8 MAN C 339 O3 130.9 122.3 81.5 79.2 148.2 71.4 64.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 285 OE1
REMARK 620 2 ASN D 287 OD1 89.8
REMARK 620 3 GLU D 293 OE1 148.4 63.1
REMARK 620 4 ASN D 307 OD1 77.2 163.8 132.0
REMARK 620 5 ASP D 308 OD1 84.6 90.8 80.1 97.5
REMARK 620 6 ASP D 308 O 135.0 125.7 63.8 70.4 70.0
REMARK 620 7 MAN D 339 O3 133.5 107.5 73.9 75.9 136.0 66.8
REMARK 620 8 MAN D 339 O4 70.2 80.7 117.2 85.8 153.3 134.9 70.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P7F RELATED DB: PDB
REMARK 900 RELATED ID: 3P7H RELATED DB: PDB
DBREF 3P7G A 193 328 UNP Q9UJ71 CLC4K_HUMAN 193 328
DBREF 3P7G B 193 328 UNP Q9UJ71 CLC4K_HUMAN 193 328
DBREF 3P7G C 193 328 UNP Q9UJ71 CLC4K_HUMAN 193 328
DBREF 3P7G D 193 328 UNP Q9UJ71 CLC4K_HUMAN 193 328
SEQADV 3P7G SER A 329 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G ALA A 330 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G TRP A 331 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G SER A 332 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G HIS A 333 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G PRO A 334 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G GLN A 335 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G PHE A 336 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G GLU A 337 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G LYS A 338 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G SER B 329 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G ALA B 330 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G TRP B 331 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G SER B 332 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G HIS B 333 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G PRO B 334 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G GLN B 335 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G PHE B 336 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G GLU B 337 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G LYS B 338 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G SER C 329 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G ALA C 330 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G TRP C 331 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G SER C 332 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G HIS C 333 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G PRO C 334 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G GLN C 335 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G PHE C 336 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G GLU C 337 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G LYS C 338 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G SER D 329 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G ALA D 330 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G TRP D 331 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G SER D 332 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G HIS D 333 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G PRO D 334 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G GLN D 335 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G PHE D 336 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G GLU D 337 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7G LYS D 338 UNP Q9UJ71 EXPRESSION TAG
SEQRES 1 A 146 GLN VAL VAL SER GLN GLY TRP LYS TYR PHE LYS GLY ASN
SEQRES 2 A 146 PHE TYR TYR PHE SER LEU ILE PRO LYS THR TRP TYR SER
SEQRES 3 A 146 ALA GLU GLN PHE CYS VAL SER ARG ASN SER HIS LEU THR
SEQRES 4 A 146 SER VAL THR SER GLU SER GLU GLN GLU PHE LEU TYR LYS
SEQRES 5 A 146 THR ALA GLY GLY LEU ILE TYR TRP ILE GLY LEU THR LYS
SEQRES 6 A 146 ALA GLY MSE GLU GLY ASP TRP SER TRP VAL ASP ASP THR
SEQRES 7 A 146 PRO PHE ASN LYS VAL GLN SER VAL ARG PHE TRP ILE PRO
SEQRES 8 A 146 GLY GLU PRO ASN ASN ALA GLY ASN ASN GLU HIS CYS GLY
SEQRES 9 A 146 ASN ILE LYS ALA PRO SER LEU GLN ALA TRP ASN ASP ALA
SEQRES 10 A 146 PRO CYS ASP LYS THR PHE LEU PHE ILE CYS LYS ARG PRO
SEQRES 11 A 146 TYR VAL PRO SER GLU PRO SER ALA TRP SER HIS PRO GLN
SEQRES 12 A 146 PHE GLU LYS
SEQRES 1 B 146 GLN VAL VAL SER GLN GLY TRP LYS TYR PHE LYS GLY ASN
SEQRES 2 B 146 PHE TYR TYR PHE SER LEU ILE PRO LYS THR TRP TYR SER
SEQRES 3 B 146 ALA GLU GLN PHE CYS VAL SER ARG ASN SER HIS LEU THR
SEQRES 4 B 146 SER VAL THR SER GLU SER GLU GLN GLU PHE LEU TYR LYS
SEQRES 5 B 146 THR ALA GLY GLY LEU ILE TYR TRP ILE GLY LEU THR LYS
SEQRES 6 B 146 ALA GLY MSE GLU GLY ASP TRP SER TRP VAL ASP ASP THR
SEQRES 7 B 146 PRO PHE ASN LYS VAL GLN SER VAL ARG PHE TRP ILE PRO
SEQRES 8 B 146 GLY GLU PRO ASN ASN ALA GLY ASN ASN GLU HIS CYS GLY
SEQRES 9 B 146 ASN ILE LYS ALA PRO SER LEU GLN ALA TRP ASN ASP ALA
SEQRES 10 B 146 PRO CYS ASP LYS THR PHE LEU PHE ILE CYS LYS ARG PRO
SEQRES 11 B 146 TYR VAL PRO SER GLU PRO SER ALA TRP SER HIS PRO GLN
SEQRES 12 B 146 PHE GLU LYS
SEQRES 1 C 146 GLN VAL VAL SER GLN GLY TRP LYS TYR PHE LYS GLY ASN
SEQRES 2 C 146 PHE TYR TYR PHE SER LEU ILE PRO LYS THR TRP TYR SER
SEQRES 3 C 146 ALA GLU GLN PHE CYS VAL SER ARG ASN SER HIS LEU THR
SEQRES 4 C 146 SER VAL THR SER GLU SER GLU GLN GLU PHE LEU TYR LYS
SEQRES 5 C 146 THR ALA GLY GLY LEU ILE TYR TRP ILE GLY LEU THR LYS
SEQRES 6 C 146 ALA GLY MSE GLU GLY ASP TRP SER TRP VAL ASP ASP THR
SEQRES 7 C 146 PRO PHE ASN LYS VAL GLN SER VAL ARG PHE TRP ILE PRO
SEQRES 8 C 146 GLY GLU PRO ASN ASN ALA GLY ASN ASN GLU HIS CYS GLY
SEQRES 9 C 146 ASN ILE LYS ALA PRO SER LEU GLN ALA TRP ASN ASP ALA
SEQRES 10 C 146 PRO CYS ASP LYS THR PHE LEU PHE ILE CYS LYS ARG PRO
SEQRES 11 C 146 TYR VAL PRO SER GLU PRO SER ALA TRP SER HIS PRO GLN
SEQRES 12 C 146 PHE GLU LYS
SEQRES 1 D 146 GLN VAL VAL SER GLN GLY TRP LYS TYR PHE LYS GLY ASN
SEQRES 2 D 146 PHE TYR TYR PHE SER LEU ILE PRO LYS THR TRP TYR SER
SEQRES 3 D 146 ALA GLU GLN PHE CYS VAL SER ARG ASN SER HIS LEU THR
SEQRES 4 D 146 SER VAL THR SER GLU SER GLU GLN GLU PHE LEU TYR LYS
SEQRES 5 D 146 THR ALA GLY GLY LEU ILE TYR TRP ILE GLY LEU THR LYS
SEQRES 6 D 146 ALA GLY MSE GLU GLY ASP TRP SER TRP VAL ASP ASP THR
SEQRES 7 D 146 PRO PHE ASN LYS VAL GLN SER VAL ARG PHE TRP ILE PRO
SEQRES 8 D 146 GLY GLU PRO ASN ASN ALA GLY ASN ASN GLU HIS CYS GLY
SEQRES 9 D 146 ASN ILE LYS ALA PRO SER LEU GLN ALA TRP ASN ASP ALA
SEQRES 10 D 146 PRO CYS ASP LYS THR PHE LEU PHE ILE CYS LYS ARG PRO
SEQRES 11 D 146 TYR VAL PRO SER GLU PRO SER ALA TRP SER HIS PRO GLN
SEQRES 12 D 146 PHE GLU LYS
MODRES 3P7G MSE A 260 MET SELENOMETHIONINE
MODRES 3P7G MSE B 260 MET SELENOMETHIONINE
MODRES 3P7G MSE C 260 MET SELENOMETHIONINE
MODRES 3P7G MSE D 260 MET SELENOMETHIONINE
HET MSE A 260 16
HET MSE B 260 8
HET MSE C 260 8
HET MSE D 260 8
HET CA A 1 1
HET MAN A 339 12
HET CA B 1 1
HET MAN B 339 12
HET CA C 1 1
HET MAN C 339 12
HET CA D 1 1
HET MAN D 339 12
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
HETNAM MAN ALPHA-D-MANNOPYRANOSE
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 5 CA 4(CA 2+)
FORMUL 6 MAN 4(C6 H12 O6)
FORMUL 13 HOH *593(H2 O)
HELIX 1 1 THR A 215 ARG A 226 1 12
HELIX 2 2 SER A 235 GLY A 247 1 13
HELIX 3 3 ASN A 273 VAL A 278 1 6
HELIX 4 4 ARG A 279 TRP A 281 5 3
HELIX 5 5 ASN A 288 ASN A 292 5 5
HELIX 6 6 THR B 215 ARG B 226 1 12
HELIX 7 7 SER B 235 GLY B 247 1 13
HELIX 8 8 ASN B 273 VAL B 278 1 6
HELIX 9 9 ARG B 279 TRP B 281 5 3
HELIX 10 10 ASN B 288 ASN B 292 5 5
HELIX 11 11 THR C 215 ARG C 226 1 12
HELIX 12 12 SER C 235 GLY C 247 1 13
HELIX 13 13 ASN C 273 VAL C 278 1 6
HELIX 14 14 ARG C 279 TRP C 281 5 3
HELIX 15 15 ASN C 288 ASN C 292 5 5
HELIX 16 16 THR D 215 ARG D 226 1 12
HELIX 17 17 SER D 235 GLY D 247 1 13
HELIX 18 18 ASN D 273 VAL D 278 1 6
HELIX 19 19 ARG D 279 TRP D 281 5 3
HELIX 20 20 ASN D 288 ASN D 292 5 5
SHEET 1 A 5 LYS A 200 PHE A 202 0
SHEET 2 A 5 ASN A 205 PHE A 209 -1 O ASN A 205 N PHE A 202
SHEET 3 A 5 LEU A 316 PRO A 322 -1 O ARG A 321 N PHE A 206
SHEET 4 A 5 TYR A 251 ALA A 258 1 N TRP A 252 O LEU A 316
SHEET 5 A 5 ASP A 263 TRP A 266 -1 O ASP A 263 N ALA A 258
SHEET 1 B 5 HIS A 229 LEU A 230 0
SHEET 2 B 5 LEU A 316 PRO A 322 -1 O LYS A 320 N HIS A 229
SHEET 3 B 5 TYR A 251 ALA A 258 1 N TRP A 252 O LEU A 316
SHEET 4 B 5 CYS A 295 ILE A 298 -1 O ILE A 298 N TYR A 251
SHEET 5 B 5 TRP A 306 ALA A 309 -1 O ASN A 307 N ASN A 297
SHEET 1 C 5 TRP B 199 PHE B 202 0
SHEET 2 C 5 ASN B 205 PHE B 209 -1 O ASN B 205 N PHE B 202
SHEET 3 C 5 LEU B 316 PRO B 322 -1 O ARG B 321 N PHE B 206
SHEET 4 C 5 TYR B 251 ALA B 258 1 N TRP B 252 O LEU B 316
SHEET 5 C 5 ASP B 263 TRP B 266 -1 O SER B 265 N THR B 256
SHEET 1 D 5 HIS B 229 LEU B 230 0
SHEET 2 D 5 LEU B 316 PRO B 322 -1 O LYS B 320 N HIS B 229
SHEET 3 D 5 TYR B 251 ALA B 258 1 N TRP B 252 O LEU B 316
SHEET 4 D 5 CYS B 295 ILE B 298 -1 O ILE B 298 N TYR B 251
SHEET 5 D 5 TRP B 306 ALA B 309 -1 O ASN B 307 N ASN B 297
SHEET 1 E 5 TRP C 199 PHE C 202 0
SHEET 2 E 5 ASN C 205 PHE C 209 -1 O ASN C 205 N PHE C 202
SHEET 3 E 5 LEU C 316 PRO C 322 -1 O ARG C 321 N PHE C 206
SHEET 4 E 5 TYR C 251 ALA C 258 1 N TRP C 252 O LEU C 316
SHEET 5 E 5 ASP C 263 TRP C 266 -1 O ASP C 263 N ALA C 258
SHEET 1 F 5 HIS C 229 LEU C 230 0
SHEET 2 F 5 LEU C 316 PRO C 322 -1 O LYS C 320 N HIS C 229
SHEET 3 F 5 TYR C 251 ALA C 258 1 N TRP C 252 O LEU C 316
SHEET 4 F 5 CYS C 295 ILE C 298 -1 O ILE C 298 N TYR C 251
SHEET 5 F 5 TRP C 306 ALA C 309 -1 O ASN C 307 N ASN C 297
SHEET 1 G 5 LYS D 200 PHE D 202 0
SHEET 2 G 5 ASN D 205 PHE D 209 -1 O ASN D 205 N PHE D 202
SHEET 3 G 5 LEU D 316 PRO D 322 -1 O ARG D 321 N PHE D 206
SHEET 4 G 5 TYR D 251 ALA D 258 1 N TRP D 252 O LEU D 316
SHEET 5 G 5 ASP D 263 TRP D 266 -1 O ASP D 263 N ALA D 258
SHEET 1 H 5 HIS D 229 LEU D 230 0
SHEET 2 H 5 LEU D 316 PRO D 322 -1 O LYS D 320 N HIS D 229
SHEET 3 H 5 TYR D 251 ALA D 258 1 N TRP D 252 O LEU D 316
SHEET 4 H 5 CYS D 295 ILE D 298 -1 O ILE D 298 N TYR D 251
SHEET 5 H 5 TRP D 306 ALA D 309 -1 O ALA D 309 N CYS D 295
SSBOND 1 CYS A 223 CYS A 319 1555 1555 2.04
SSBOND 2 CYS A 295 CYS A 311 1555 1555 2.05
SSBOND 3 CYS B 223 CYS B 319 1555 1555 2.03
SSBOND 4 CYS B 295 CYS B 311 1555 1555 2.05
SSBOND 5 CYS C 223 CYS C 319 1555 1555 2.04
SSBOND 6 CYS C 295 CYS C 311 1555 1555 2.06
SSBOND 7 CYS D 223 CYS D 319 1555 1555 2.05
SSBOND 8 CYS D 295 CYS D 311 1555 1555 2.04
LINK C GLY A 259 N AMSE A 260 1555 1555 1.34
LINK C GLY A 259 N BMSE A 260 1555 1555 1.34
LINK C AMSE A 260 N GLU A 261 1555 1555 1.34
LINK C BMSE A 260 N GLU A 261 1555 1555 1.33
LINK C GLY B 259 N MSE B 260 1555 1555 1.32
LINK C MSE B 260 N AGLU B 261 1555 1555 1.34
LINK C MSE B 260 N BGLU B 261 1555 1555 1.34
LINK C GLY C 259 N MSE C 260 1555 1555 1.33
LINK C MSE C 260 N AGLU C 261 1555 1555 1.34
LINK C MSE C 260 N BGLU C 261 1555 1555 1.33
LINK C GLY D 259 N MSE D 260 1555 1555 1.32
LINK C MSE D 260 N GLU D 261 1555 1555 1.34
LINK CA CA A 1 OE1 GLU A 285 1555 1555 2.40
LINK CA CA A 1 OD1 ASN A 287 1555 1555 2.33
LINK CA CA A 1 OE1 GLU A 293 1555 1555 2.41
LINK CA CA A 1 OD1 ASN A 307 1555 1555 2.44
LINK CA CA A 1 OD1 ASP A 308 1555 1555 2.21
LINK CA CA A 1 O ASP A 308 1555 1555 2.54
LINK CA CA A 1 O4 MAN A 339 1555 1555 2.57
LINK CA CA A 1 O3 MAN A 339 1555 1555 2.71
LINK CA CA B 1 OE1 GLU B 285 1555 1555 2.59
LINK CA CA B 1 OD1 ASN B 287 1555 1555 2.44
LINK CA CA B 1 OE1 GLU B 293 1555 1555 2.41
LINK CA CA B 1 OD1 ASN B 307 1555 1555 2.42
LINK CA CA B 1 OD1 ASP B 308 1555 1555 2.36
LINK CA CA B 1 O ASP B 308 1555 1555 2.54
LINK CA CA B 1 O4 MAN B 339 1555 1555 2.47
LINK CA CA B 1 O3 MAN B 339 1555 1555 2.58
LINK CA CA C 1 OE1 GLU C 285 1555 1555 2.57
LINK CA CA C 1 OD1 ASN C 287 1555 1555 2.27
LINK CA CA C 1 OE1 GLU C 293 1555 1555 2.14
LINK CA CA C 1 OD1 ASN C 307 1555 1555 2.56
LINK CA CA C 1 OD1 ASP C 308 1555 1555 2.33
LINK CA CA C 1 O ASP C 308 1555 1555 2.46
LINK CA CA C 1 O4 MAN C 339 1555 1555 2.45
LINK CA CA C 1 O3 MAN C 339 1555 1555 2.53
LINK CA CA D 1 OE1 GLU D 285 1555 1555 2.23
LINK CA CA D 1 OD1 ASN D 287 1555 1555 2.29
LINK CA CA D 1 OE1 GLU D 293 1555 1555 2.77
LINK CA CA D 1 OD1 ASN D 307 1555 1555 2.36
LINK CA CA D 1 OD1 ASP D 308 1555 1555 2.28
LINK CA CA D 1 O ASP D 308 1555 1555 2.76
LINK CA CA D 1 O3 MAN D 339 1555 1555 2.54
LINK CA CA D 1 O4 MAN D 339 1555 1555 2.57
CISPEP 1 GLU A 285 PRO A 286 0 -0.94
CISPEP 2 GLU B 285 PRO B 286 0 -2.39
CISPEP 3 GLU C 285 PRO C 286 0 -4.90
CISPEP 4 GLU D 285 PRO D 286 0 -6.71
CRYST1 79.710 79.710 89.980 90.00 90.00 90.00 P 42 16
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 0.012545 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012545 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011114 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
