HEADER IMMUNE SYSTEM 12-OCT-10 3P7H
TITLE STRUCTURE OF THE HUMAN LANGERIN CARBOHYDRATE RECOGNITION DOMAIN IN
TITLE 2 COMPLEX WITH MALTOSE
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 5 06-DEC-23 3P7H 1 REMARK
REVDAT 4 06-SEP-23 3P7H 1 HETSYN
REVDAT 3 29-JUL-20 3P7H 1 COMPND REMARK SEQADV HET
REVDAT 3 2 1 HETNAM FORMUL LINK SITE
REVDAT 3 3 1 ATOM
REVDAT 2 08-NOV-17 3P7H 1 REMARK
REVDAT 1 03-NOV-10 3P7H 0
SPRSDE 03-NOV-10 3P7H 3BC6
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. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 23863
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) : 0.181
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1280
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1753
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE SET COUNT : 97
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4273
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 204
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.57
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) : 0.13000
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): 0.388
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.236
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.154
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.666
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4551 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6217 ; 1.360 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 521 ; 6.644 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 218 ;34.564 ;24.220
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 663 ;14.420 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;14.351 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 629 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3532 ; 0.005 ; 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): 2618 ; 0.547 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4222 ; 1.091 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1933 ; 2.435 ; 3.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1995 ; 4.027 ;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 262
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9527 15.7419 -34.1143
REMARK 3 T TENSOR
REMARK 3 T11: 0.0873 T22: 0.0437
REMARK 3 T33: 0.1067 T12: 0.0151
REMARK 3 T13: -0.0889 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 3.6554 L22: 2.7975
REMARK 3 L33: 5.1057 L12: -0.5417
REMARK 3 L13: -1.3019 L23: -0.4246
REMARK 3 S TENSOR
REMARK 3 S11: -0.0183 S12: 0.0282 S13: -0.0819
REMARK 3 S21: -0.2329 S22: -0.0538 S23: 0.1008
REMARK 3 S31: 0.0861 S32: 0.0279 S33: 0.0720
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 263 A 322
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2263 25.8021 -33.9579
REMARK 3 T TENSOR
REMARK 3 T11: 0.1527 T22: 0.0974
REMARK 3 T33: 0.1721 T12: 0.0255
REMARK 3 T13: -0.0969 T23: -0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 3.6218 L22: 1.7349
REMARK 3 L33: 2.5099 L12: 0.2702
REMARK 3 L13: 0.6238 L23: -0.2495
REMARK 3 S TENSOR
REMARK 3 S11: -0.0747 S12: 0.1656 S13: 0.4572
REMARK 3 S21: -0.2790 S22: -0.0113 S23: 0.2377
REMARK 3 S31: -0.3018 S32: 0.0035 S33: 0.0859
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): 28.9473 4.4137 -28.8688
REMARK 3 T TENSOR
REMARK 3 T11: 0.8217 T22: 0.5786
REMARK 3 T33: 0.6195 T12: 0.2753
REMARK 3 T13: -0.3902 T23: -0.1578
REMARK 3 L TENSOR
REMARK 3 L11: 17.0552 L22: 13.4410
REMARK 3 L33: 0.7845 L12: 15.1380
REMARK 3 L13: 3.6539 L23: 3.2419
REMARK 3 S TENSOR
REMARK 3 S11: 1.2818 S12: -0.1164 S13: -3.0979
REMARK 3 S21: 1.3081 S22: -0.3841 S23: -2.7333
REMARK 3 S31: 0.3572 S32: -0.0145 S33: -0.8977
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 275
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3979 26.0397 -31.7639
REMARK 3 T TENSOR
REMARK 3 T11: 0.0666 T22: 0.0846
REMARK 3 T33: 0.0084 T12: 0.0065
REMARK 3 T13: 0.0059 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 3.6458 L22: 4.0019
REMARK 3 L33: 3.0312 L12: 0.0422
REMARK 3 L13: 0.7070 L23: -0.1453
REMARK 3 S TENSOR
REMARK 3 S11: 0.0441 S12: 0.1132 S13: 0.1118
REMARK 3 S21: -0.1574 S22: -0.1734 S23: -0.0377
REMARK 3 S31: -0.0177 S32: 0.0795 S33: 0.1294
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 276 B 305
REMARK 3 ORIGIN FOR THE GROUP (A): 37.3063 14.6543 -36.0788
REMARK 3 T TENSOR
REMARK 3 T11: 0.0841 T22: 0.1183
REMARK 3 T33: 0.1625 T12: 0.0171
REMARK 3 T13: 0.0710 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 3.9040 L22: 3.1993
REMARK 3 L33: 9.4394 L12: 0.8011
REMARK 3 L13: 0.7246 L23: 0.4165
REMARK 3 S TENSOR
REMARK 3 S11: -0.0635 S12: 0.3028 S13: -0.2364
REMARK 3 S21: -0.3546 S22: -0.0428 S23: -0.2404
REMARK 3 S31: 0.3342 S32: 0.3470 S33: 0.1063
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 306 B 325
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0409 26.5056 -30.1649
REMARK 3 T TENSOR
REMARK 3 T11: 0.0395 T22: 0.1304
REMARK 3 T33: 0.1004 T12: -0.0430
REMARK 3 T13: 0.0357 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 1.8529 L22: 3.0925
REMARK 3 L33: 3.8913 L12: 2.0640
REMARK 3 L13: -0.5364 L23: -2.0689
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: 0.0094 S13: 0.0405
REMARK 3 S21: 0.0236 S22: -0.0884 S23: -0.1374
REMARK 3 S31: -0.1629 S32: 0.1050 S33: 0.0864
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 259
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6325 15.0901 -5.4249
REMARK 3 T TENSOR
REMARK 3 T11: 0.0697 T22: 0.0301
REMARK 3 T33: 0.0486 T12: 0.0057
REMARK 3 T13: -0.0181 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 4.0052 L22: 1.6429
REMARK 3 L33: 4.3194 L12: 0.5571
REMARK 3 L13: -0.3932 L23: -0.5708
REMARK 3 S TENSOR
REMARK 3 S11: -0.0656 S12: -0.1542 S13: -0.0630
REMARK 3 S21: 0.1538 S22: 0.0062 S23: -0.0807
REMARK 3 S31: 0.1812 S32: 0.0392 S33: 0.0595
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 260 C 279
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9907 28.7099 -7.3616
REMARK 3 T TENSOR
REMARK 3 T11: 0.1739 T22: 0.1641
REMARK 3 T33: 0.1786 T12: 0.0750
REMARK 3 T13: -0.0375 T23: -0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 12.3601 L22: 11.7620
REMARK 3 L33: 1.4955 L12: -3.4878
REMARK 3 L13: 0.9739 L23: 3.6238
REMARK 3 S TENSOR
REMARK 3 S11: -0.0352 S12: -0.3359 S13: 1.3109
REMARK 3 S21: -0.3442 S22: -0.2131 S23: -0.0950
REMARK 3 S31: -0.1697 S32: -0.1826 S33: 0.2483
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 280 C 331
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4411 23.2202 -5.5366
REMARK 3 T TENSOR
REMARK 3 T11: 0.0901 T22: 0.0699
REMARK 3 T33: 0.1240 T12: 0.0125
REMARK 3 T13: -0.0393 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 5.1151 L22: 2.0223
REMARK 3 L33: 3.0044 L12: -0.0653
REMARK 3 L13: 0.8733 L23: 0.1362
REMARK 3 S TENSOR
REMARK 3 S11: -0.0146 S12: -0.1526 S13: 0.6789
REMARK 3 S21: 0.1261 S22: -0.0194 S23: -0.1296
REMARK 3 S31: -0.1594 S32: -0.0243 S33: 0.0340
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 253
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2684 27.4661 -5.9155
REMARK 3 T TENSOR
REMARK 3 T11: 0.0801 T22: 0.0918
REMARK 3 T33: 0.0851 T12: 0.0006
REMARK 3 T13: 0.0413 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 3.0061 L22: 4.4266
REMARK 3 L33: 4.4270 L12: -0.5758
REMARK 3 L13: -0.0625 L23: 1.6852
REMARK 3 S TENSOR
REMARK 3 S11: -0.0083 S12: -0.3160 S13: 0.2028
REMARK 3 S21: 0.1408 S22: -0.1892 S23: 0.2059
REMARK 3 S31: -0.2899 S32: -0.0569 S33: 0.1975
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 254 D 275
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5382 13.2790 -11.2686
REMARK 3 T TENSOR
REMARK 3 T11: 0.1352 T22: 0.1069
REMARK 3 T33: 0.1027 T12: 0.0207
REMARK 3 T13: 0.0268 T23: 0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 8.0647 L22: 7.2897
REMARK 3 L33: 5.2389 L12: 0.5212
REMARK 3 L13: 2.6191 L23: -2.1829
REMARK 3 S TENSOR
REMARK 3 S11: 0.1788 S12: 0.2895 S13: -0.5982
REMARK 3 S21: -0.4509 S22: -0.1111 S23: -0.1200
REMARK 3 S31: 0.6705 S32: 0.3653 S33: -0.0677
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 276 D 325
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4310 16.7786 -6.0426
REMARK 3 T TENSOR
REMARK 3 T11: 0.0945 T22: 0.1368
REMARK 3 T33: 0.1577 T12: -0.0008
REMARK 3 T13: 0.0784 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 3.1180 L22: 4.6599
REMARK 3 L33: 4.7352 L12: -0.6943
REMARK 3 L13: -0.5960 L23: 0.1647
REMARK 3 S TENSOR
REMARK 3 S11: -0.0954 S12: -0.2232 S13: -0.4438
REMARK 3 S21: 0.3677 S22: -0.0800 S23: 0.3183
REMARK 3 S31: 0.3972 S32: -0.1150 S33: 0.1754
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 3P7H 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_1000062052.
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
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 : 25136
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 98.5
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.18800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3P7G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 10MG/ML LANGERIN IN 10 MM
REMARK 280 TRIS/HCL PH 7.5, 5 MM MALTOSE; 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 45.47500
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 45.47500
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, E
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, F
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, G
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, H
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 SER C 326
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: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 202 117.56 -160.68
REMARK 500 LYS A 299 -64.26 -126.88
REMARK 500 ASN B 292 20.88 -142.64
REMARK 500 LYS B 299 -51.35 -125.30
REMARK 500 SER B 302 149.94 -174.83
REMARK 500 ASP C 269 5.48 86.92
REMARK 500 ASN C 292 10.10 -141.36
REMARK 500 LYS C 299 -58.72 -124.94
REMARK 500 ASN D 292 19.21 -145.86
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 71.5
REMARK 620 3 GLU A 293 OE1 145.7 76.8
REMARK 620 4 ASN A 307 OD1 69.9 140.0 143.2
REMARK 620 5 ASP A 308 O 129.2 144.9 73.7 72.1
REMARK 620 6 ASP A 308 OD1 72.3 88.6 94.5 89.7 75.2
REMARK 620 7 GLC E 2 O3 129.1 113.4 75.8 83.7 77.3 152.4
REMARK 620 8 GLC E 2 O4 70.8 79.8 116.3 77.8 130.8 143.1 61.2
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 72.3
REMARK 620 3 GLU B 293 OE1 146.1 79.6
REMARK 620 4 ASN B 307 OD1 69.0 140.0 140.3
REMARK 620 5 ASP B 308 OD1 72.3 87.5 88.3 89.9
REMARK 620 6 ASP B 308 O 125.4 140.9 68.8 73.4 69.6
REMARK 620 7 GLC F 2 O4 77.7 81.5 116.7 81.2 149.9 133.0
REMARK 620 8 GLC F 2 O3 131.3 124.9 80.6 77.0 142.4 72.8 63.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 285 OE1
REMARK 620 2 ASN C 287 OD1 77.0
REMARK 620 3 GLU C 293 OE1 145.5 70.7
REMARK 620 4 ASN C 307 OD1 67.4 143.7 145.6
REMARK 620 5 ASP C 308 OD1 72.9 87.9 93.8 88.2
REMARK 620 6 ASP C 308 O 131.3 139.2 72.7 74.3 77.1
REMARK 620 7 GLC G 2 O3 133.5 113.6 72.8 87.4 147.6 70.8
REMARK 620 8 GLC G 2 O4 71.5 81.9 114.5 80.5 144.2 130.5 66.1
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 75.2
REMARK 620 3 GLU D 293 OE1 147.3 74.5
REMARK 620 4 ASN D 307 OD1 65.6 140.6 144.6
REMARK 620 5 ASP D 308 OD1 74.1 86.4 92.0 87.0
REMARK 620 6 ASP D 308 O 129.8 143.2 73.1 72.1 77.9
REMARK 620 7 GLC H 2 O3 129.6 119.9 77.3 84.2 146.4 68.6
REMARK 620 8 GLC H 2 O4 78.2 84.2 110.4 83.9 152.2 123.4 58.4
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: 3P7G RELATED DB: PDB
DBREF 3P7H A 193 328 UNP Q9UJ71 CLC4K_HUMAN 193 328
DBREF 3P7H B 193 328 UNP Q9UJ71 CLC4K_HUMAN 193 328
DBREF 3P7H C 193 328 UNP Q9UJ71 CLC4K_HUMAN 193 328
DBREF 3P7H D 193 328 UNP Q9UJ71 CLC4K_HUMAN 193 328
SEQADV 3P7H SER A 329 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H ALA A 330 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H TRP A 331 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H SER A 332 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H HIS A 333 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H PRO A 334 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H GLN A 335 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H PHE A 336 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H GLU A 337 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H LYS A 338 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H SER B 329 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H ALA B 330 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H TRP B 331 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H SER B 332 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H HIS B 333 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H PRO B 334 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H GLN B 335 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H PHE B 336 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H GLU B 337 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H LYS B 338 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H SER C 329 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H ALA C 330 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H TRP C 331 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H SER C 332 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H HIS C 333 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H PRO C 334 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H GLN C 335 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H PHE C 336 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H GLU C 337 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H LYS C 338 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H SER D 329 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H ALA D 330 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H TRP D 331 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H SER D 332 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H HIS D 333 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H PRO D 334 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H GLN D 335 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H PHE D 336 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H GLU D 337 UNP Q9UJ71 EXPRESSION TAG
SEQADV 3P7H 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 3P7H MSE A 260 MET SELENOMETHIONINE
MODRES 3P7H MSE B 260 MET SELENOMETHIONINE
MODRES 3P7H MSE C 260 MET SELENOMETHIONINE
MODRES 3P7H MSE D 260 MET SELENOMETHIONINE
HET MSE A 260 8
HET MSE B 260 8
HET MSE C 260 8
HET MSE D 260 8
HET GLC E 1 12
HET GLC E 2 11
HET GLC F 1 12
HET GLC F 2 11
HET GLC G 1 12
HET GLC G 2 11
HET GLC H 1 12
HET GLC H 2 11
HET CA A 1 1
HET CA B 1 1
HET CA C 1 1
HET CA D 1 1
HETNAM MSE SELENOMETHIONINE
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 5 GLC 8(C6 H12 O6)
FORMUL 9 CA 4(CA 2+)
FORMUL 13 HOH *204(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 LYS D 274 TRP D 281 5 8
SHEET 1 A 5 LYS A 200 PHE A 202 0
SHEET 2 A 5 ASN A 205 PHE A 209 -1 O TYR A 207 N LYS A 200
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 SER A 265 N THR A 256
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 ALA A 309 N CYS A 295
SHEET 1 C 5 TRP B 199 PHE B 202 0
SHEET 2 C 5 ASN B 205 PHE B 209 -1 O TYR B 207 N LYS B 200
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 LYS C 200 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 TYR D 207 N LYS D 200
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 2.06
SSBOND 2 CYS A 295 CYS A 311 1555 1555 2.04
SSBOND 3 CYS B 223 CYS B 319 1555 1555 2.05
SSBOND 4 CYS B 295 CYS B 311 1555 1555 2.04
SSBOND 5 CYS C 223 CYS C 319 1555 1555 2.05
SSBOND 6 CYS C 295 CYS C 311 1555 1555 2.04
SSBOND 7 CYS D 223 CYS D 319 1555 1555 2.04
SSBOND 8 CYS D 295 CYS D 311 1555 1555 2.05
LINK C GLY A 259 N MSE A 260 1555 1555 1.32
LINK C MSE A 260 N GLU A 261 1555 1555 1.33
LINK C GLY B 259 N MSE B 260 1555 1555 1.33
LINK C MSE B 260 N GLU B 261 1555 1555 1.33
LINK C GLY C 259 N MSE C 260 1555 1555 1.34
LINK C MSE C 260 N GLU C 261 1555 1555 1.33
LINK C GLY D 259 N MSE D 260 1555 1555 1.33
LINK C MSE D 260 N GLU D 261 1555 1555 1.33
LINK O4 GLC E 1 C1 GLC E 2 1555 1555 1.45
LINK O4 GLC F 1 C1 GLC F 2 1555 1555 1.45
LINK O4 GLC G 1 C1 GLC G 2 1555 1555 1.44
LINK O4 GLC H 1 C1 GLC H 2 1555 1555 1.46
LINK CA CA A 1 OE1 GLU A 285 1555 1555 2.44
LINK CA CA A 1 OD1 ASN A 287 1555 1555 2.56
LINK CA CA A 1 OE1 GLU A 293 1555 1555 2.40
LINK CA CA A 1 OD1 ASN A 307 1555 1555 2.35
LINK CA CA A 1 O ASP A 308 1555 1555 2.53
LINK CA CA A 1 OD1 ASP A 308 1555 1555 2.54
LINK CA CA A 1 O3 GLC E 2 1555 1555 2.50
LINK CA CA A 1 O4 GLC E 2 1555 1555 2.72
LINK CA CA B 1 OE1 GLU B 285 1555 1555 2.34
LINK CA CA B 1 OD1 ASN B 287 1555 1555 2.34
LINK CA CA B 1 OE1 GLU B 293 1555 1555 2.35
LINK CA CA B 1 OD1 ASN B 307 1555 1555 2.56
LINK CA CA B 1 OD1 ASP B 308 1555 1555 2.39
LINK CA CA B 1 O ASP B 308 1555 1555 2.61
LINK CA CA B 1 O4 GLC F 2 1555 1555 2.62
LINK CA CA B 1 O3 GLC F 2 1555 1555 2.74
LINK CA CA C 1 OE1 GLU C 285 1555 1555 2.48
LINK CA CA C 1 OD1 ASN C 287 1555 1555 2.65
LINK CA CA C 1 OE1 GLU C 293 1555 1555 2.22
LINK CA CA C 1 OD1 ASN C 307 1555 1555 2.33
LINK CA CA C 1 OD1 ASP C 308 1555 1555 2.42
LINK CA CA C 1 O ASP C 308 1555 1555 2.46
LINK CA CA C 1 O3 GLC G 2 1555 1555 2.56
LINK CA CA C 1 O4 GLC G 2 1555 1555 2.57
LINK CA CA D 1 OE1 GLU D 285 1555 1555 2.25
LINK CA CA D 1 OD1 ASN D 287 1555 1555 2.50
LINK CA CA D 1 OE1 GLU D 293 1555 1555 2.23
LINK CA CA D 1 OD1 ASN D 307 1555 1555 2.41
LINK CA CA D 1 OD1 ASP D 308 1555 1555 2.55
LINK CA CA D 1 O ASP D 308 1555 1555 2.63
LINK CA CA D 1 O3 GLC H 2 1555 1555 2.79
LINK CA CA D 1 O4 GLC H 2 1555 1555 2.83
CISPEP 1 GLU A 285 PRO A 286 0 -0.89
CISPEP 2 GLU B 285 PRO B 286 0 -1.96
CISPEP 3 GLU C 285 PRO C 286 0 -6.79
CISPEP 4 GLU D 285 PRO D 286 0 2.02
CRYST1 79.970 79.970 90.950 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 0.012505 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012505 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010995 0.00000
(ATOM LINES ARE NOT SHOWN.)
END