HEADER IMMUNE SYSTEM 20-DEC-11 3V6O
TITLE LEPTIN RECEPTOR-ANTIBODY COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEPTIN RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LEPTIN BINDING DOMAIN OF HUMAN OBESITY RECEPTOR;
COMPND 5 SYNONYM: LEP-R, HUB219, OB RECEPTOR, OB-R;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MONOCLONAL ANTIBODY 9F8 FAB FRAGMENT HEAVY CHAIN;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: FAB FRAGMENT OF MONOCLONAL ANTIBODY H CHAIN;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: MONOCLONAL ANTIBODY 9F8 FAB FRAGMENT LIGHT CHAIN;
COMPND 13 CHAIN: E, F;
COMPND 14 FRAGMENT: FAB FRAGMENT OF MONOCLONAL ANTIBODY L CHAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DB, LEPR, OBR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A(+);
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 16 ORGANISM_TAXID: 10090
KEYWDS RECEPTOR-ANTIBODY COMPLEX, CYTOKINE RECEPTOR, ANTIBODY FAB FRAGMENT,
KEYWDS 2 IMMUNOGLOBULIN FOLD, LEPTIN RECEPTOR-ANTIBODY COMPLEX, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR B.CARPENTER,G.R.HEMSWORTH,R.J.ROSS,P.J.ARTYMIUK
REVDAT 4 27-DEC-23 3V6O 1 HETSYN SSBOND LINK
REVDAT 3 29-JUL-20 3V6O 1 COMPND REMARK DBREF HETNAM
REVDAT 3 2 1 LINK SITE
REVDAT 2 25-APR-12 3V6O 1 JRNL
REVDAT 1 14-MAR-12 3V6O 0
JRNL AUTH B.CARPENTER,G.R.HEMSWORTH,Z.WU,M.MAAMRA,C.J.STRASBURGER,
JRNL AUTH 2 R.J.ROSS,P.J.ARTYMIUK
JRNL TITL STRUCTURE OF THE HUMAN OBESITY RECEPTOR LEPTIN-BINDING
JRNL TITL 2 DOMAIN REVEALS THE MECHANISM OF LEPTIN ANTAGONISM BY A
JRNL TITL 3 MONOCLONAL ANTIBODY.
JRNL REF STRUCTURE V. 20 487 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22405007
JRNL DOI 10.1016/J.STR.2012.01.019
REMARK 2
REMARK 2 RESOLUTION. 1.95 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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6729
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9261
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 494
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9486
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 177
REMARK 3 SOLVENT ATOMS : 851
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.06000
REMARK 3 B22 (A**2) : -0.58000
REMARK 3 B33 (A**2) : -2.48000
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): 0.120
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.122
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.088
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.891
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9879 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6643 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13399 ; 1.840 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16236 ; 0.971 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1209 ; 7.593 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 383 ;35.733 ;24.256
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1572 ;13.547 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;19.748 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1509 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10720 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1893 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6134 ; 3.760 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2449 ; 1.535 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9982 ; 5.198 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3745 ; 7.340 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3417 ; 9.297 ; 4.500
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 431 A 533
REMARK 3 ORIGIN FOR THE GROUP (A): 47.1401 40.3999 -6.3344
REMARK 3 T TENSOR
REMARK 3 T11: 0.1644 T22: 0.0928
REMARK 3 T33: 0.0498 T12: 0.0260
REMARK 3 T13: -0.0076 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.5756 L22: 0.2765
REMARK 3 L33: 1.3628 L12: -0.3849
REMARK 3 L13: -0.0549 L23: 0.1699
REMARK 3 S TENSOR
REMARK 3 S11: -0.0086 S12: -0.0127 S13: 0.0153
REMARK 3 S21: 0.0472 S22: 0.0446 S23: -0.0006
REMARK 3 S31: 0.3160 S32: 0.1176 S33: -0.0360
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 534 A 701
REMARK 3 ORIGIN FOR THE GROUP (A): 71.6880 49.8452 16.4967
REMARK 3 T TENSOR
REMARK 3 T11: 0.0535 T22: 0.1912
REMARK 3 T33: 0.0948 T12: 0.0272
REMARK 3 T13: -0.0712 T23: -0.0367
REMARK 3 L TENSOR
REMARK 3 L11: 6.2909 L22: 0.1040
REMARK 3 L33: 2.1677 L12: -0.7761
REMARK 3 L13: 3.6901 L23: -0.4523
REMARK 3 S TENSOR
REMARK 3 S11: -0.1661 S12: 0.2046 S13: 0.2064
REMARK 3 S21: 0.0294 S22: 0.0249 S23: -0.0354
REMARK 3 S31: -0.1107 S32: 0.1343 S33: 0.1413
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 : B 430 B 533
REMARK 3 ORIGIN FOR THE GROUP (A): 40.4948 69.7290 5.7121
REMARK 3 T TENSOR
REMARK 3 T11: 0.2051 T22: 0.0489
REMARK 3 T33: 0.0585 T12: 0.0396
REMARK 3 T13: 0.0163 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.3086 L22: 0.8811
REMARK 3 L33: 1.3373 L12: 0.5091
REMARK 3 L13: -0.1572 L23: -0.0984
REMARK 3 S TENSOR
REMARK 3 S11: 0.0277 S12: 0.0158 S13: 0.0148
REMARK 3 S21: 0.0094 S22: 0.0142 S23: 0.0545
REMARK 3 S31: -0.3762 S32: -0.0600 S33: -0.0418
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 534 B 1001
REMARK 3 ORIGIN FOR THE GROUP (A): 66.6445 70.8737 -17.5072
REMARK 3 T TENSOR
REMARK 3 T11: 0.3189 T22: 0.1063
REMARK 3 T33: 0.0934 T12: -0.0579
REMARK 3 T13: 0.1447 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 7.8527 L22: 3.2828
REMARK 3 L33: 4.2211 L12: 5.0629
REMARK 3 L13: -5.6470 L23: -3.5866
REMARK 3 S TENSOR
REMARK 3 S11: -0.2508 S12: 0.1700 S13: -0.3972
REMARK 3 S21: -0.2202 S22: 0.0877 S23: -0.2930
REMARK 3 S31: -0.0185 S32: -0.1563 S33: 0.1630
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 : C 3 C 119
REMARK 3 ORIGIN FOR THE GROUP (A): 42.1843 51.5662 -31.9768
REMARK 3 T TENSOR
REMARK 3 T11: 0.0536 T22: 0.0976
REMARK 3 T33: 0.0616 T12: 0.0031
REMARK 3 T13: -0.0079 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.1904 L22: 0.4135
REMARK 3 L33: 1.9338 L12: 0.0514
REMARK 3 L13: -0.0007 L23: -0.1413
REMARK 3 S TENSOR
REMARK 3 S11: 0.0062 S12: -0.0466 S13: -0.0247
REMARK 3 S21: -0.0932 S22: 0.0125 S23: 0.0159
REMARK 3 S31: 0.0022 S32: 0.0670 S33: -0.0188
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 : C 120 C 222
REMARK 3 ORIGIN FOR THE GROUP (A): 44.0877 79.6554 -47.4473
REMARK 3 T TENSOR
REMARK 3 T11: 0.0831 T22: 0.0680
REMARK 3 T33: 0.0975 T12: -0.0033
REMARK 3 T13: -0.0303 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 0.1057 L22: 2.0165
REMARK 3 L33: 0.3970 L12: 0.4594
REMARK 3 L13: -0.0099 L23: -0.0964
REMARK 3 S TENSOR
REMARK 3 S11: 0.0039 S12: -0.0165 S13: -0.0156
REMARK 3 S21: 0.0468 S22: -0.0975 S23: -0.1045
REMARK 3 S31: 0.0307 S32: 0.0743 S33: 0.0936
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 : D 3 D 119
REMARK 3 ORIGIN FOR THE GROUP (A): 41.7388 56.3095 31.0013
REMARK 3 T TENSOR
REMARK 3 T11: 0.1469 T22: 0.0744
REMARK 3 T33: 0.0490 T12: 0.0120
REMARK 3 T13: 0.0184 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.1233 L22: 0.7446
REMARK 3 L33: 1.4736 L12: 0.2930
REMARK 3 L13: -0.0443 L23: -0.2435
REMARK 3 S TENSOR
REMARK 3 S11: 0.0397 S12: 0.0335 S13: -0.0095
REMARK 3 S21: 0.1682 S22: 0.0382 S23: -0.0007
REMARK 3 S31: -0.1566 S32: -0.0604 S33: -0.0779
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 : D 120 D 221
REMARK 3 ORIGIN FOR THE GROUP (A): 53.7546 31.6742 45.9256
REMARK 3 T TENSOR
REMARK 3 T11: 0.0780 T22: 0.0779
REMARK 3 T33: 0.1462 T12: -0.0549
REMARK 3 T13: -0.0105 T23: 0.0736
REMARK 3 L TENSOR
REMARK 3 L11: 0.1016 L22: 2.6376
REMARK 3 L33: 1.6223 L12: -0.4434
REMARK 3 L13: -0.2459 L23: 0.2906
REMARK 3 S TENSOR
REMARK 3 S11: 0.0320 S12: 0.0033 S13: 0.0001
REMARK 3 S21: -0.0564 S22: -0.2219 S23: -0.2560
REMARK 3 S31: -0.2461 S32: 0.2075 S33: 0.1898
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 : E 4 E 106
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6998 64.2918 -18.2720
REMARK 3 T TENSOR
REMARK 3 T11: 0.0877 T22: 0.1446
REMARK 3 T33: 0.0731 T12: 0.0577
REMARK 3 T13: 0.0055 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 0.0397 L22: 1.2691
REMARK 3 L33: 0.9642 L12: -0.1238
REMARK 3 L13: 0.1590 L23: -0.3101
REMARK 3 S TENSOR
REMARK 3 S11: -0.0404 S12: -0.0395 S13: -0.0313
REMARK 3 S21: 0.0866 S22: 0.0835 S23: 0.0082
REMARK 3 S31: -0.2556 S32: -0.2655 S33: -0.0431
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 : E 107 E 216
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2803 86.3012 -48.7786
REMARK 3 T TENSOR
REMARK 3 T11: 0.1881 T22: 0.0615
REMARK 3 T33: 0.0747 T12: -0.0205
REMARK 3 T13: -0.0660 T23: 0.0510
REMARK 3 L TENSOR
REMARK 3 L11: 0.2365 L22: 0.6937
REMARK 3 L33: 1.6005 L12: -0.1097
REMARK 3 L13: -0.2214 L23: -0.7047
REMARK 3 S TENSOR
REMARK 3 S11: -0.1806 S12: 0.0221 S13: 0.0580
REMARK 3 S21: 0.1303 S22: 0.1236 S23: -0.0116
REMARK 3 S31: -0.0069 S32: -0.1027 S33: 0.0570
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 : F 4 F 106
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0080 40.1922 17.3735
REMARK 3 T TENSOR
REMARK 3 T11: 0.0742 T22: 0.0994
REMARK 3 T33: 0.0674 T12: -0.0255
REMARK 3 T13: -0.0013 T23: 0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 0.0442 L22: 1.7518
REMARK 3 L33: 1.0009 L12: -0.2698
REMARK 3 L13: 0.0614 L23: -0.5981
REMARK 3 S TENSOR
REMARK 3 S11: 0.0021 S12: -0.0115 S13: 0.0040
REMARK 3 S21: -0.0938 S22: 0.0738 S23: 0.0341
REMARK 3 S31: 0.1854 S32: -0.1760 S33: -0.0759
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 : F 107 F 216
REMARK 3 ORIGIN FOR THE GROUP (A): 43.5243 19.5911 47.5619
REMARK 3 T TENSOR
REMARK 3 T11: 0.1345 T22: 0.0408
REMARK 3 T33: 0.0734 T12: 0.0186
REMARK 3 T13: 0.0124 T23: 0.0404
REMARK 3 L TENSOR
REMARK 3 L11: 0.0953 L22: 1.0711
REMARK 3 L33: 1.8592 L12: 0.0987
REMARK 3 L13: 0.3013 L23: -0.6128
REMARK 3 S TENSOR
REMARK 3 S11: -0.0302 S12: -0.0170 S13: -0.0138
REMARK 3 S21: -0.0308 S22: -0.0008 S23: -0.0638
REMARK 3 S31: -0.0408 S32: -0.0540 S33: 0.0310
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; U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3V6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069662.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127050
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 49.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.55600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PEG-4000, PH 4.6,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 44.90700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.64050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.41450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.64050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.90700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.41450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, 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 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 ILE A 428
REMARK 465 ASP A 429
REMARK 465 VAL A 430
REMARK 465 SER A 452
REMARK 465 THR A 453
REMARK 465 ILE A 454
REMARK 465 GLN A 455
REMARK 465 SER A 456
REMARK 465 LEU A 457
REMARK 465 ALA A 458
REMARK 465 GLU A 459
REMARK 465 HIS A 517
REMARK 465 SER A 518
REMARK 465 LEU A 519
REMARK 465 GLU A 559
REMARK 465 LYS A 560
REMARK 465 PRO A 561
REMARK 465 VAL A 562
REMARK 465 PHE A 563
REMARK 465 PRO A 564
REMARK 465 GLU A 565
REMARK 465 ASN A 566
REMARK 465 ALA A 591
REMARK 465 LYS A 592
REMARK 465 SER A 593
REMARK 465 ILE B 428
REMARK 465 ASP B 429
REMARK 465 ILE B 454
REMARK 465 GLN B 455
REMARK 465 SER B 456
REMARK 465 LEU B 457
REMARK 465 ALA B 458
REMARK 465 GLU B 459
REMARK 465 LYS B 560
REMARK 465 PRO B 561
REMARK 465 VAL B 562
REMARK 465 PHE B 563
REMARK 465 PRO B 564
REMARK 465 GLU B 565
REMARK 465 TYR B 589
REMARK 465 ASP B 590
REMARK 465 ALA B 591
REMARK 465 LYS B 592
REMARK 465 SER B 593
REMARK 465 LYS B 594
REMARK 465 VAL B 997
REMARK 465 VAL B 998
REMARK 465 ALA C 2
REMARK 465 ALA D 2
REMARK 465 ALA D 136
REMARK 465 GLN D 137
REMARK 465 THR D 138
REMARK 465 ASN D 139
REMARK 465 THR D 222
REMARK 465 ALA E 2
REMARK 465 GLU E 3
REMARK 465 ALA F 2
REMARK 465 GLU F 3
REMARK 465 SER F 9
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 VAL B 430 CG1 CG2
REMARK 470 GLU C 3 CG CD OE1 OE2
REMARK 470 THR C 222 CA C O CB OG1 CG2
REMARK 470 GLU D 3 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 1184 O HOH C 556 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 CYS B 498 CB CYS B 498 SG 0.107
REMARK 500 GLU C 83 CG GLU C 83 CD 0.094
REMARK 500 CYS C 97 CB CYS C 97 SG -0.130
REMARK 500 CYS C 146 CB CYS C 146 SG -0.108
REMARK 500 CYS C 201 CB CYS C 201 SG -0.118
REMARK 500 CYS E 196 CB CYS E 196 SG -0.108
REMARK 500 CYS F 196 CB CYS F 196 SG -0.099
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 ARG C 68 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 MET C 84 CG - SD - CE ANGL. DEV. = -9.8 DEGREES
REMARK 500 CYS E 25 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG E 32 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 MET E 177 CG - SD - CE ANGL. DEV. = -13.0 DEGREES
REMARK 500 CYS F 25 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG F 32 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG F 56 NE - CZ - NH2 ANGL. DEV. = -3.2 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 LEU A 471 -126.80 -119.30
REMARK 500 TYR A 472 -141.40 -110.58
REMARK 500 LYS A 579 -103.14 178.44
REMARK 500 SER B 452 -44.28 -25.93
REMARK 500 LEU B 471 -130.83 -123.24
REMARK 500 TYR B 472 -139.48 -107.37
REMARK 500 SER B 518 -126.05 47.24
REMARK 500 LEU B 519 52.94 -113.99
REMARK 500 SER C 17 -3.90 76.12
REMARK 500 SER C 166 -34.22 -130.18
REMARK 500 SER C 178 62.91 74.30
REMARK 500 ASP C 179 13.31 57.52
REMARK 500 SER D 17 -6.65 74.25
REMARK 500 SER D 86 70.56 50.91
REMARK 500 SER D 134 93.55 -65.44
REMARK 500 ASN D 161 56.74 36.11
REMARK 500 SER D 162 27.28 49.97
REMARK 500 ASP D 179 21.60 48.91
REMARK 500 ARG E 32 -116.16 56.52
REMARK 500 ALA E 53 -32.28 71.83
REMARK 500 ARG F 32 -122.86 58.52
REMARK 500 ALA F 53 -33.29 70.33
REMARK 500 SER F 173 18.79 59.75
REMARK 500 ASN F 214 68.54 -68.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 579 GLU A 580 144.52
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 NA C 305 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 191 O
REMARK 620 2 TRP C 194 O 87.4
REMARK 620 3 HOH C 554 O 91.1 103.3
REMARK 620 4 HOH C 555 O 86.0 81.9 174.0
REMARK 620 N 1 2 3
DBREF 3V6O A 428 633 UNP P48357 LEPR_HUMAN 428 633
DBREF 3V6O B 428 998 UNP P48357 LEPR_HUMAN 428 633
DBREF 3V6O C 2 222 PDB 3V6O 3V6O 2 222
DBREF 3V6O D 2 222 PDB 3V6O 3V6O 2 222
DBREF 3V6O E 2 216 PDB 3V6O 3V6O 2 216
DBREF 3V6O F 2 216 PDB 3V6O 3V6O 2 216
SEQRES 1 A 206 ILE ASP VAL ASN ILE ASN ILE SER CYS GLU THR ASP GLY
SEQRES 2 A 206 TYR LEU THR LYS MET THR CYS ARG TRP SER THR SER THR
SEQRES 3 A 206 ILE GLN SER LEU ALA GLU SER THR LEU GLN LEU ARG TYR
SEQRES 4 A 206 HIS ARG SER SER LEU TYR CYS SER ASP ILE PRO SER ILE
SEQRES 5 A 206 HIS PRO ILE SER GLU PRO LYS ASP CYS TYR LEU GLN SER
SEQRES 6 A 206 ASP GLY PHE TYR GLU CYS ILE PHE GLN PRO ILE PHE LEU
SEQRES 7 A 206 LEU SER GLY TYR THR MET TRP ILE ARG ILE ASN HIS SER
SEQRES 8 A 206 LEU GLY SER LEU ASP SER PRO PRO THR CYS VAL LEU PRO
SEQRES 9 A 206 ASP SER VAL VAL LYS PRO LEU PRO PRO SER SER VAL LYS
SEQRES 10 A 206 ALA GLU ILE THR ILE ASN ILE GLY LEU LEU LYS ILE SER
SEQRES 11 A 206 TRP GLU LYS PRO VAL PHE PRO GLU ASN ASN LEU GLN PHE
SEQRES 12 A 206 GLN ILE ARG TYR GLY LEU SER GLY LYS GLU VAL GLN TRP
SEQRES 13 A 206 LYS MET TYR GLU VAL TYR ASP ALA LYS SER LYS SER VAL
SEQRES 14 A 206 SER LEU PRO VAL PRO ASP LEU CYS ALA VAL TYR ALA VAL
SEQRES 15 A 206 GLN VAL ARG CYS LYS ARG LEU ASP GLY LEU GLY TYR TRP
SEQRES 16 A 206 SER ASN TRP SER ASN PRO ALA TYR THR VAL VAL
SEQRES 1 B 206 ILE ASP VAL ASN ILE ASN ILE SER CYS GLU THR ASP GLY
SEQRES 2 B 206 TYR LEU THR LYS MET THR CYS ARG TRP SER THR SER THR
SEQRES 3 B 206 ILE GLN SER LEU ALA GLU SER THR LEU GLN LEU ARG TYR
SEQRES 4 B 206 HIS ARG SER SER LEU TYR CYS SER ASP ILE PRO SER ILE
SEQRES 5 B 206 HIS PRO ILE SER GLU PRO LYS ASP CYS TYR LEU GLN SER
SEQRES 6 B 206 ASP GLY PHE TYR GLU CYS ILE PHE GLN PRO ILE PHE LEU
SEQRES 7 B 206 LEU SER GLY TYR THR MET TRP ILE ARG ILE ASN HIS SER
SEQRES 8 B 206 LEU GLY SER LEU ASP SER PRO PRO THR CYS VAL LEU PRO
SEQRES 9 B 206 ASP SER VAL VAL LYS PRO LEU PRO PRO SER SER VAL LYS
SEQRES 10 B 206 ALA GLU ILE THR ILE ASN ILE GLY LEU LEU LYS ILE SER
SEQRES 11 B 206 TRP GLU LYS PRO VAL PHE PRO GLU ASN ASN LEU GLN PHE
SEQRES 12 B 206 GLN ILE ARG TYR GLY LEU SER GLY LYS GLU VAL GLN TRP
SEQRES 13 B 206 LYS MET TYR GLU VAL TYR ASP ALA LYS SER LYS SER VAL
SEQRES 14 B 206 SER LEU PRO VAL PRO ASP LEU CYS ALA VAL TYR ALA VAL
SEQRES 15 B 206 GLN VAL ARG CYS LYS ARG LEU ASP GLY LEU GLY TYR TRP
SEQRES 16 B 206 SER ASN TRP SER ASN PRO ALA TYR THR VAL VAL
SEQRES 1 C 221 ALA GLU VAL LYS LEU LEU GLU SER GLY PRO GLY LEU VAL
SEQRES 2 C 221 ALA PRO SER GLU SER LEU SER ILE THR CYS THR ILE SER
SEQRES 3 C 221 GLY PHE SER LEU THR ASP ASP GLY VAL SER TRP ILE ARG
SEQRES 4 C 221 GLN PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE
SEQRES 5 C 221 TRP GLY GLY GLY SER THR TYR PHE ASN SER LEU PHE LYS
SEQRES 6 C 221 SER ARG LEU SER ILE THR ARG ASP ASN SER LYS SER GLN
SEQRES 7 C 221 VAL PHE LEU GLU MET ASP SER LEU GLN THR ASP ASP THR
SEQRES 8 C 221 ALA MET TYR TYR CYS ALA LYS HIS ASP GLY HIS GLU THR
SEQRES 9 C 221 MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER
SEQRES 10 C 221 SER SER LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA
SEQRES 11 C 221 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU
SEQRES 12 C 221 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR
SEQRES 13 C 221 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS
SEQRES 14 C 221 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU
SEQRES 15 C 221 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER
SEQRES 16 C 221 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER
SEQRES 17 C 221 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS THR
SEQRES 1 D 221 ALA GLU VAL LYS LEU LEU GLU SER GLY PRO GLY LEU VAL
SEQRES 2 D 221 ALA PRO SER GLU SER LEU SER ILE THR CYS THR ILE SER
SEQRES 3 D 221 GLY PHE SER LEU THR ASP ASP GLY VAL SER TRP ILE ARG
SEQRES 4 D 221 GLN PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE
SEQRES 5 D 221 TRP GLY GLY GLY SER THR TYR PHE ASN SER LEU PHE LYS
SEQRES 6 D 221 SER ARG LEU SER ILE THR ARG ASP ASN SER LYS SER GLN
SEQRES 7 D 221 VAL PHE LEU GLU MET ASP SER LEU GLN THR ASP ASP THR
SEQRES 8 D 221 ALA MET TYR TYR CYS ALA LYS HIS ASP GLY HIS GLU THR
SEQRES 9 D 221 MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER
SEQRES 10 D 221 SER SER LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA
SEQRES 11 D 221 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU
SEQRES 12 D 221 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR
SEQRES 13 D 221 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS
SEQRES 14 D 221 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU
SEQRES 15 D 221 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER
SEQRES 16 D 221 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER
SEQRES 17 D 221 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS THR
SEQRES 1 E 215 ALA GLU ILE VAL MET THR GLN SER PRO LYS PHE MET SER
SEQRES 2 E 215 THR SER ILE GLY ASP ARG VAL ASN ILE THR CYS LYS ALA
SEQRES 3 E 215 THR GLN ASN VAL ARG THR ALA VAL THR TRP TYR GLN GLN
SEQRES 4 E 215 LYS PRO GLY GLN SER PRO GLN ALA LEU ILE PHE LEU ALA
SEQRES 5 E 215 SER ASN ARG HIS THR GLY VAL PRO ALA ARG PHE THR GLY
SEQRES 6 E 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE ASN ASN
SEQRES 7 E 215 VAL LYS SER GLU ASP LEU ALA ASP TYR PHE CYS LEU GLN
SEQRES 8 E 215 HIS TRP ASN TYR PRO LEU THR PHE GLY SER GLY THR LYS
SEQRES 9 E 215 LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER
SEQRES 10 E 215 ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY
SEQRES 11 E 215 ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS
SEQRES 12 E 215 ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG
SEQRES 13 E 215 GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER
SEQRES 14 E 215 LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU
SEQRES 15 E 215 THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS
SEQRES 16 E 215 GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS
SEQRES 17 E 215 SER PHE ASN ARG ASN GLU CYS
SEQRES 1 F 215 ALA GLU ILE VAL MET THR GLN SER PRO LYS PHE MET SER
SEQRES 2 F 215 THR SER ILE GLY ASP ARG VAL ASN ILE THR CYS LYS ALA
SEQRES 3 F 215 THR GLN ASN VAL ARG THR ALA VAL THR TRP TYR GLN GLN
SEQRES 4 F 215 LYS PRO GLY GLN SER PRO GLN ALA LEU ILE PHE LEU ALA
SEQRES 5 F 215 SER ASN ARG HIS THR GLY VAL PRO ALA ARG PHE THR GLY
SEQRES 6 F 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE ASN ASN
SEQRES 7 F 215 VAL LYS SER GLU ASP LEU ALA ASP TYR PHE CYS LEU GLN
SEQRES 8 F 215 HIS TRP ASN TYR PRO LEU THR PHE GLY SER GLY THR LYS
SEQRES 9 F 215 LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER
SEQRES 10 F 215 ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY
SEQRES 11 F 215 ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS
SEQRES 12 F 215 ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG
SEQRES 13 F 215 GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER
SEQRES 14 F 215 LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU
SEQRES 15 F 215 THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS
SEQRES 16 F 215 GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS
SEQRES 17 F 215 SER PHE ASN ARG ASN GLU CYS
MODRES 3V6O ASN F 22 ASN GLYCOSYLATION SITE
HET CYS A 701 7
HET EDO A 702 4
HET EDO A 703 4
HET EDO A 704 4
HET EDO A 705 4
HET EDO A 706 4
HET EDO A 707 4
HET EDO A 708 4
HET EDO A 709 4
HET CYS B1001 7
HET EDO B1002 4
HET EDO B1003 4
HET EDO B1004 4
HET EDO B1005 4
HET EDO B1006 4
HET ACT C 301 4
HET ACT C 302 4
HET EDO C 303 4
HET EDO C 304 4
HET NA C 305 1
HET ACT D 301 4
HET EDO D 302 4
HET EDO D 303 4
HET EDO D 304 4
HET EDO D 305 4
HET EDO D 306 4
HET EDO D 307 4
HET EDO D 308 4
HET ACT E 301 4
HET EDO E 302 4
HET EDO E 303 4
HET EDO E 304 4
HET NAG F 301 14
HET ACT F 302 4
HET ACT F 303 4
HET EDO F 304 4
HET EDO F 305 4
HET EDO F 306 4
HET EDO F 307 4
HET EDO F 308 4
HET EDO F 309 4
HETNAM CYS CYSTEINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ACT ACETATE ION
HETNAM NA SODIUM ION
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN EDO ETHYLENE GLYCOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 7 CYS 2(C3 H7 N O2 S)
FORMUL 8 EDO 31(C2 H6 O2)
FORMUL 22 ACT 6(C2 H3 O2 1-)
FORMUL 26 NA NA 1+
FORMUL 39 NAG C8 H15 N O6
FORMUL 48 HOH *851(H2 O)
HELIX 1 1 LEU A 530 VAL A 535 5 6
HELIX 2 2 LEU B 530 VAL B 535 5 6
HELIX 3 3 SER C 63 LYS C 66 5 4
HELIX 4 4 ASN C 75 LYS C 77 5 3
HELIX 5 5 GLN C 88 THR C 92 5 5
HELIX 6 6 SER C 162 SER C 164 5 3
HELIX 7 7 SER C 192 TRP C 194 5 3
HELIX 8 8 PRO C 206 SER C 209 5 4
HELIX 9 9 SER D 63 LYS D 66 5 4
HELIX 10 10 GLN D 88 THR D 92 5 5
HELIX 11 11 SER D 162 SER D 164 5 3
HELIX 12 12 PRO D 206 SER D 209 5 4
HELIX 13 13 LYS E 81 LEU E 85 5 5
HELIX 14 14 SER E 123 GLY E 130 1 8
HELIX 15 15 LYS E 185 ARG E 190 1 6
HELIX 16 16 LYS F 81 LEU F 85 5 5
HELIX 17 17 SER F 123 SER F 129 1 7
HELIX 18 18 LYS F 185 GLU F 189 1 5
SHEET 1 A 4 SER A 435 THR A 438 0
SHEET 2 A 4 MET A 445 TRP A 449 -1 O THR A 446 N GLU A 437
SHEET 3 A 4 TYR A 496 PHE A 500 -1 O TYR A 496 N TRP A 449
SHEET 4 A 4 CYS A 488 LEU A 490 -1 N TYR A 489 O GLU A 497
SHEET 1 B 4 GLU A 484 LYS A 486 0
SHEET 2 B 4 THR A 461 ARG A 468 -1 N TYR A 466 O GLU A 484
SHEET 3 B 4 TYR A 509 ASN A 516 -1 O ARG A 514 N GLN A 463
SHEET 4 B 4 LEU A 522 ASP A 523 -1 O LEU A 522 N ILE A 515
SHEET 1 C 4 GLU A 484 LYS A 486 0
SHEET 2 C 4 THR A 461 ARG A 468 -1 N TYR A 466 O GLU A 484
SHEET 3 C 4 TYR A 509 ASN A 516 -1 O ARG A 514 N GLN A 463
SHEET 4 C 4 THR A 527 VAL A 529 -1 O THR A 527 N MET A 511
SHEET 1 D 3 LYS A 544 THR A 548 0
SHEET 2 D 3 LEU A 553 SER A 557 -1 O LYS A 555 N GLU A 546
SHEET 3 D 3 SER A 595 LEU A 598 -1 O VAL A 596 N ILE A 556
SHEET 1 E 4 LYS A 584 VAL A 588 0
SHEET 2 E 4 LEU A 568 LEU A 576 -1 N ILE A 572 O TYR A 586
SHEET 3 E 4 TYR A 607 ARG A 615 -1 O GLN A 610 N ARG A 573
SHEET 4 E 4 ALA A 629 TYR A 630 -1 O ALA A 629 N VAL A 609
SHEET 1 F 4 SER B 435 THR B 438 0
SHEET 2 F 4 MET B 445 SER B 450 -1 O THR B 446 N GLU B 437
SHEET 3 F 4 PHE B 495 PHE B 500 -1 O TYR B 496 N TRP B 449
SHEET 4 F 4 TYR B 489 LEU B 490 -1 N TYR B 489 O GLU B 497
SHEET 1 G 4 GLU B 484 LYS B 486 0
SHEET 2 G 4 THR B 461 ARG B 468 -1 N TYR B 466 O GLU B 484
SHEET 3 G 4 TYR B 509 HIS B 517 -1 O ARG B 514 N GLN B 463
SHEET 4 G 4 GLY B 520 ASP B 523 -1 O LEU B 522 N ILE B 515
SHEET 1 H 4 GLU B 484 LYS B 486 0
SHEET 2 H 4 THR B 461 ARG B 468 -1 N TYR B 466 O GLU B 484
SHEET 3 H 4 TYR B 509 HIS B 517 -1 O ARG B 514 N GLN B 463
SHEET 4 H 4 THR B 527 VAL B 529 -1 O THR B 527 N MET B 511
SHEET 1 I 3 LYS B 544 THR B 548 0
SHEET 2 I 3 LEU B 553 SER B 557 -1 O LEU B 553 N THR B 548
SHEET 3 I 3 VAL B 596 LEU B 598 -1 O VAL B 596 N ILE B 556
SHEET 1 J 4 LYS B 584 VAL B 588 0
SHEET 2 J 4 LEU B 568 LEU B 576 -1 N PHE B 570 O VAL B 588
SHEET 3 J 4 TYR B 607 ARG B 615 -1 O LYS B 614 N GLN B 569
SHEET 4 J 4 ALA B 629 TYR B 630 -1 O ALA B 629 N VAL B 609
SHEET 1 K 4 LYS C 5 SER C 9 0
SHEET 2 K 4 LEU C 20 SER C 27 -1 O THR C 25 N LEU C 7
SHEET 3 K 4 GLN C 79 MET C 84 -1 O VAL C 80 N CYS C 24
SHEET 4 K 4 LEU C 69 ASP C 74 -1 N THR C 72 O PHE C 81
SHEET 1 L 6 LEU C 13 VAL C 14 0
SHEET 2 L 6 THR C 113 VAL C 117 1 O THR C 116 N VAL C 14
SHEET 3 L 6 ALA C 93 ASP C 101 -1 N TYR C 95 O THR C 113
SHEET 4 L 6 VAL C 36 GLN C 41 -1 N ILE C 39 O TYR C 96
SHEET 5 L 6 GLU C 48 ILE C 53 -1 O LEU C 50 N TRP C 38
SHEET 6 L 6 THR C 59 PHE C 61 -1 O TYR C 60 N VAL C 52
SHEET 1 M 4 LEU C 13 VAL C 14 0
SHEET 2 M 4 THR C 113 VAL C 117 1 O THR C 116 N VAL C 14
SHEET 3 M 4 ALA C 93 ASP C 101 -1 N TYR C 95 O THR C 113
SHEET 4 M 4 THR C 105 TRP C 109 -1 O TYR C 108 N LYS C 99
SHEET 1 N 4 SER C 126 LEU C 130 0
SHEET 2 N 4 MET C 141 TYR C 151 -1 O GLY C 145 N LEU C 130
SHEET 3 N 4 TYR C 181 PRO C 190 -1 O TYR C 181 N TYR C 151
SHEET 4 N 4 VAL C 169 THR C 171 -1 N HIS C 170 O SER C 186
SHEET 1 O 4 SER C 126 LEU C 130 0
SHEET 2 O 4 MET C 141 TYR C 151 -1 O GLY C 145 N LEU C 130
SHEET 3 O 4 TYR C 181 PRO C 190 -1 O TYR C 181 N TYR C 151
SHEET 4 O 4 VAL C 175 LEU C 176 -1 N VAL C 175 O THR C 182
SHEET 1 P 3 THR C 157 TRP C 160 0
SHEET 2 P 3 THR C 200 HIS C 205 -1 O ASN C 202 N THR C 159
SHEET 3 P 3 THR C 210 LYS C 215 -1 O VAL C 212 N VAL C 203
SHEET 1 Q 4 LYS D 5 SER D 9 0
SHEET 2 Q 4 LEU D 20 SER D 27 -1 O THR D 25 N LEU D 7
SHEET 3 Q 4 GLN D 79 MET D 84 -1 O MET D 84 N LEU D 20
SHEET 4 Q 4 LEU D 69 ASP D 74 -1 N ASP D 74 O GLN D 79
SHEET 1 R 6 LEU D 13 VAL D 14 0
SHEET 2 R 6 THR D 113 VAL D 117 1 O THR D 116 N VAL D 14
SHEET 3 R 6 ALA D 93 ASP D 101 -1 N TYR D 95 O THR D 113
SHEET 4 R 6 VAL D 36 GLN D 41 -1 N ILE D 39 O TYR D 96
SHEET 5 R 6 GLU D 48 ILE D 53 -1 O LEU D 50 N TRP D 38
SHEET 6 R 6 THR D 59 PHE D 61 -1 O TYR D 60 N VAL D 52
SHEET 1 S 4 LEU D 13 VAL D 14 0
SHEET 2 S 4 THR D 113 VAL D 117 1 O THR D 116 N VAL D 14
SHEET 3 S 4 ALA D 93 ASP D 101 -1 N TYR D 95 O THR D 113
SHEET 4 S 4 THR D 105 TRP D 109 -1 O TYR D 108 N LYS D 99
SHEET 1 T 4 SER D 126 LEU D 130 0
SHEET 2 T 4 MET D 141 TYR D 151 -1 O LEU D 147 N TYR D 128
SHEET 3 T 4 LEU D 180 PRO D 190 -1 O VAL D 189 N VAL D 142
SHEET 4 T 4 VAL D 169 THR D 171 -1 N HIS D 170 O SER D 186
SHEET 1 U 4 SER D 126 LEU D 130 0
SHEET 2 U 4 MET D 141 TYR D 151 -1 O LEU D 147 N TYR D 128
SHEET 3 U 4 LEU D 180 PRO D 190 -1 O VAL D 189 N VAL D 142
SHEET 4 U 4 VAL D 175 GLN D 177 -1 N GLN D 177 O LEU D 180
SHEET 1 V 3 THR D 157 TRP D 160 0
SHEET 2 V 3 THR D 200 HIS D 205 -1 O ASN D 202 N THR D 159
SHEET 3 V 3 THR D 210 LYS D 215 -1 O VAL D 212 N VAL D 203
SHEET 1 W 4 MET E 6 THR E 7 0
SHEET 2 W 4 VAL E 21 ALA E 27 -1 O LYS E 26 N THR E 7
SHEET 3 W 4 ASP E 72 ILE E 77 -1 O LEU E 75 N ILE E 23
SHEET 4 W 4 PHE E 64 SER E 69 -1 N THR E 65 O THR E 76
SHEET 1 X 6 PHE E 12 SER E 16 0
SHEET 2 X 6 THR E 104 LYS E 109 1 O LYS E 109 N THR E 15
SHEET 3 X 6 ASP E 87 GLN E 92 -1 N TYR E 88 O THR E 104
SHEET 4 X 6 VAL E 35 GLN E 40 -1 N GLN E 40 O ASP E 87
SHEET 5 X 6 GLN E 47 PHE E 51 -1 O LEU E 49 N TRP E 37
SHEET 6 X 6 ASN E 55 ARG E 56 -1 O ASN E 55 N PHE E 51
SHEET 1 Y 4 PHE E 12 SER E 16 0
SHEET 2 Y 4 THR E 104 LYS E 109 1 O LYS E 109 N THR E 15
SHEET 3 Y 4 ASP E 87 GLN E 92 -1 N TYR E 88 O THR E 104
SHEET 4 Y 4 THR E 99 PHE E 100 -1 O THR E 99 N GLN E 92
SHEET 1 Z 4 THR E 116 PHE E 120 0
SHEET 2 Z 4 GLY E 131 PHE E 141 -1 O PHE E 137 N SER E 118
SHEET 3 Z 4 TYR E 175 THR E 184 -1 O LEU E 181 N VAL E 134
SHEET 4 Z 4 VAL E 161 TRP E 165 -1 N SER E 164 O SER E 178
SHEET 1 AA 4 SER E 155 ARG E 157 0
SHEET 2 AA 4 ASN E 147 ILE E 152 -1 N TRP E 150 O ARG E 157
SHEET 3 AA 4 SER E 193 THR E 199 -1 O GLU E 197 N LYS E 149
SHEET 4 AA 4 ILE E 207 ASN E 212 -1 O ILE E 207 N ALA E 198
SHEET 1 AB 4 MET F 6 THR F 7 0
SHEET 2 AB 4 VAL F 21 ALA F 27 -1 O LYS F 26 N THR F 7
SHEET 3 AB 4 ASP F 72 ILE F 77 -1 O ILE F 77 N VAL F 21
SHEET 4 AB 4 PHE F 64 SER F 69 -1 N THR F 65 O THR F 76
SHEET 1 AC 6 PHE F 12 SER F 16 0
SHEET 2 AC 6 THR F 104 LYS F 109 1 O LYS F 109 N THR F 15
SHEET 3 AC 6 ASP F 87 GLN F 92 -1 N TYR F 88 O THR F 104
SHEET 4 AC 6 VAL F 35 GLN F 40 -1 N TYR F 38 O PHE F 89
SHEET 5 AC 6 GLN F 47 PHE F 51 -1 O LEU F 49 N TRP F 37
SHEET 6 AC 6 ASN F 55 ARG F 56 -1 O ASN F 55 N PHE F 51
SHEET 1 AD 4 PHE F 12 SER F 16 0
SHEET 2 AD 4 THR F 104 LYS F 109 1 O LYS F 109 N THR F 15
SHEET 3 AD 4 ASP F 87 GLN F 92 -1 N TYR F 88 O THR F 104
SHEET 4 AD 4 THR F 99 PHE F 100 -1 O THR F 99 N GLN F 92
SHEET 1 AE 4 THR F 116 PHE F 120 0
SHEET 2 AE 4 GLY F 131 PHE F 141 -1 O ASN F 139 N THR F 116
SHEET 3 AE 4 TYR F 175 THR F 184 -1 O LEU F 181 N VAL F 134
SHEET 4 AE 4 VAL F 161 TRP F 165 -1 N SER F 164 O SER F 178
SHEET 1 AF 4 SER F 155 ARG F 157 0
SHEET 2 AF 4 ASN F 147 ILE F 152 -1 N TRP F 150 O ARG F 157
SHEET 3 AF 4 SER F 193 THR F 199 -1 O THR F 199 N ASN F 147
SHEET 4 AF 4 ILE F 207 ASN F 212 -1 O ILE F 207 N ALA F 198
SSBOND 1 CYS A 436 CYS A 447 1555 1555 2.09
SSBOND 2 CYS A 473 CYS A 528 1555 1555 2.14
SSBOND 3 CYS A 488 CYS A 498 1555 1555 2.07
SSBOND 4 CYS A 604 CYS A 701 1555 1555 2.07
SSBOND 5 CYS B 436 CYS B 447 1555 1555 2.11
SSBOND 6 CYS B 473 CYS B 528 1555 1555 2.12
SSBOND 7 CYS B 488 CYS B 498 1555 1555 2.07
SSBOND 8 CYS B 604 CYS B 1001 1555 1555 2.07
SSBOND 9 CYS C 24 CYS C 97 1555 1555 2.14
SSBOND 10 CYS C 146 CYS C 201 1555 1555 2.13
SSBOND 11 CYS C 221 CYS E 216 1555 1555 2.06
SSBOND 12 CYS D 24 CYS D 97 1555 1555 2.09
SSBOND 13 CYS D 146 CYS D 201 1555 1555 2.05
SSBOND 14 CYS D 221 CYS F 216 1555 1555 2.04
SSBOND 15 CYS E 25 CYS E 90 1555 1555 2.15
SSBOND 16 CYS E 136 CYS E 196 1555 1555 1.99
SSBOND 17 CYS F 25 CYS F 90 1555 1555 2.14
SSBOND 18 CYS F 136 CYS F 196 1555 1555 2.04
LINK ND2 ASN F 22 C1 NAG F 301 1555 1555 1.43
LINK O SER C 191 NA NA C 305 1555 1555 2.33
LINK O TRP C 194 NA NA C 305 1555 1555 2.42
LINK NA NA C 305 O HOH C 554 1555 1555 2.51
LINK NA NA C 305 O HOH C 555 1555 1555 2.33
CISPEP 1 GLN A 501 PRO A 502 0 -10.77
CISPEP 2 GLN B 501 PRO B 502 0 -3.60
CISPEP 3 ILE B 551 GLY B 552 0 -3.35
CISPEP 4 PHE C 152 PRO C 153 0 -5.38
CISPEP 5 GLU C 154 PRO C 155 0 1.91
CISPEP 6 TRP C 194 PRO C 195 0 3.17
CISPEP 7 PHE D 152 PRO D 153 0 -13.22
CISPEP 8 GLU D 154 PRO D 155 0 4.98
CISPEP 9 TRP D 194 PRO D 195 0 8.07
CISPEP 10 TYR E 96 PRO E 97 0 -13.74
CISPEP 11 TYR E 142 PRO E 143 0 1.95
CISPEP 12 TYR F 96 PRO F 97 0 -5.92
CISPEP 13 TYR F 142 PRO F 143 0 2.75
CRYST1 89.814 118.829 171.281 90.00 90.00 90.00 P 21 21 21 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 0.011134 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008415 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005838 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
