HEADER SIGNALING PROTEIN 11-JUL-18 6H15
TITLE STRUCTURE OF LRP6 P3E3P4E4 IN COMPLEX WITH VHH L-P2-B10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 6;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LRP-6;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: VHH L-P2-B10;
COMPND 8 CHAIN: C, D;
COMPND 9 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: LRP6;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA;
SOURCE 10 ORGANISM_COMMON: LLAMA;
SOURCE 11 ORGANISM_TAXID: 9844;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INHIBITOR, COMPLEX, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.GROS,R.C.VAN SCHERPENZEEL
REVDAT 3 17-JAN-24 6H15 1 HETSYN LINK
REVDAT 2 29-JUL-20 6H15 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE ATOM
REVDAT 1 30-JAN-19 6H15 0
JRNL AUTH N.FENDERICO,R.C.VAN SCHERPENZEEL,M.GOLDFLAM,D.PROVERBIO,
JRNL AUTH 2 I.JORDENS,T.KRALJ,S.STRYECK,T.Z.BASS,G.HERMANS,C.ULLMAN,
JRNL AUTH 3 T.AASTRUP,P.GROS,M.M.MAURICE
JRNL TITL ANTI-LRP5/6 VHHS PROMOTE DIFFERENTIATION OF
JRNL TITL 2 WNT-HYPERSENSITIVE INTESTINAL STEM CELLS.
JRNL REF NAT COMMUN V. 10 365 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 30664649
JRNL DOI 10.1038/S41467-018-08172-Z
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13RC1_2958
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 94.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 59939
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 3062
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 94.8693 - 7.2843 1.00 2626 157 0.1873 0.1889
REMARK 3 2 7.2843 - 5.7820 1.00 2627 150 0.1964 0.2240
REMARK 3 3 5.7820 - 5.0512 1.00 2616 146 0.1831 0.2227
REMARK 3 4 5.0512 - 4.5894 1.00 2638 126 0.1522 0.1901
REMARK 3 5 4.5894 - 4.2604 1.00 2594 151 0.1574 0.2080
REMARK 3 6 4.2604 - 4.0092 1.00 2644 119 0.1752 0.2450
REMARK 3 7 4.0092 - 3.8084 1.00 2587 154 0.1796 0.2431
REMARK 3 8 3.8084 - 3.6426 1.00 2618 145 0.1880 0.2500
REMARK 3 9 3.6426 - 3.5024 1.00 2618 139 0.1889 0.2534
REMARK 3 10 3.5024 - 3.3815 1.00 2614 148 0.2009 0.2481
REMARK 3 11 3.3815 - 3.2758 1.00 2623 129 0.2086 0.2976
REMARK 3 12 3.2758 - 3.1822 1.00 2598 147 0.2106 0.2535
REMARK 3 13 3.1822 - 3.0984 1.00 2597 144 0.2128 0.2376
REMARK 3 14 3.0984 - 3.0228 1.00 2598 157 0.2262 0.2817
REMARK 3 15 3.0228 - 2.9541 1.00 2606 139 0.2278 0.2683
REMARK 3 16 2.9541 - 2.8912 1.00 2595 131 0.2387 0.3422
REMARK 3 17 2.8912 - 2.8334 1.00 2651 141 0.2589 0.3172
REMARK 3 18 2.8334 - 2.7799 1.00 2625 124 0.2728 0.3296
REMARK 3 19 2.7799 - 2.7302 1.00 2580 135 0.2796 0.4035
REMARK 3 20 2.7302 - 2.6840 0.97 2533 145 0.2856 0.3189
REMARK 3 21 2.6840 - 2.6407 0.93 2441 130 0.2866 0.3147
REMARK 3 22 2.6407 - 2.6000 0.86 2248 105 0.2897 0.3500
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -64.2643 142.6105 -11.9393
REMARK 3 T TENSOR
REMARK 3 T11: 0.3143 T22: 0.2282
REMARK 3 T33: 0.2797 T12: -0.0083
REMARK 3 T13: -0.0304 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.1481 L22: 0.1317
REMARK 3 L33: 0.1827 L12: -0.0202
REMARK 3 L13: 0.0821 L23: -0.0174
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: 0.0037 S13: 0.0314
REMARK 3 S21: -0.0241 S22: -0.0221 S23: -0.0090
REMARK 3 S31: -0.0669 S32: -0.0201 S33: 0.0196
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6H15 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1200010886.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-OCT-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8731
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.32
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60113
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 249.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : 0.21900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 1.00400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 4A0P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, 0.2 M SODIUM
REMARK 280 ACETATE TRIHYDRATE PH 5.5, 10 % PEG W/V 4000, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 166.63400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 83.31700
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 124.97550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 41.65850
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 208.29250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 61160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, B, E, F, G, H, I
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 SER A 1005
REMARK 465 SER A 1006
REMARK 465 VAL A 1007
REMARK 465 PRO A 1008
REMARK 465 SER A 1009
REMARK 465 GLN A 1010
REMARK 465 ASN A 1011
REMARK 465 LEU A 1012
REMARK 465 SER B 1005
REMARK 465 SER B 1006
REMARK 465 VAL B 1007
REMARK 465 PRO B 1008
REMARK 465 SER B 1009
REMARK 465 GLN B 1010
REMARK 465 ASN B 1011
REMARK 465 LEU B 1012
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 ND2 ASN B 865 O5 NAG B 1307 2.12
REMARK 500 O PHE A 836 OG1 THR A 848 2.17
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 ARG A 639 -123.74 58.01
REMARK 500 ASN A 651 -128.81 -139.97
REMARK 500 SER A 665 -105.88 -125.68
REMARK 500 ASP A 705 -55.65 -130.50
REMARK 500 TRP A 744 -17.20 -154.48
REMARK 500 SER A 749 73.56 58.55
REMARK 500 ARG A 751 -99.36 -114.93
REMARK 500 TRP A 767 37.12 -99.71
REMARK 500 GLU A 782 51.77 39.90
REMARK 500 HIS A 834 73.50 -158.49
REMARK 500 GLN A 842 -126.84 60.50
REMARK 500 GLN A 864 -158.38 -101.48
REMARK 500 HIS A 902 -81.72 -124.86
REMARK 500 HIS A 919 -6.06 68.40
REMARK 500 ARG A 927 -43.36 -141.41
REMARK 500 GLN A 940 -166.61 -114.25
REMARK 500 ASN A 966 85.51 -151.40
REMARK 500 TYR A1017 -63.47 -103.28
REMARK 500 GLN A1056 -14.90 75.25
REMARK 500 ARG A1060 -93.76 -129.45
REMARK 500 SER A1080 72.97 -157.89
REMARK 500 SER A1102 -61.03 -137.20
REMARK 500 ASP A1141 25.23 -148.27
REMARK 500 PHE A1153 -91.38 -87.56
REMARK 500 GLU A1154 -88.08 -106.51
REMARK 500 SER A1189 -50.60 -126.44
REMARK 500 HIS A1216 -91.75 -132.04
REMARK 500 PRO A1231 -177.71 -67.14
REMARK 500 CYS C 11 -163.18 -167.16
REMARK 500 SER C 28 83.35 -69.94
REMARK 500 VAL C 49 -72.74 -109.44
REMARK 500 ALA C 76 -0.63 -161.00
REMARK 500 TYR C 104 90.59 64.16
REMARK 500 ASP C 106 99.30 -68.55
REMARK 500 ALA D 76 -36.37 -143.04
REMARK 500 ARG B 639 -121.82 59.88
REMARK 500 ASN B 651 104.35 -49.54
REMARK 500 SER B 665 -98.95 -129.49
REMARK 500 ASP B 705 -61.01 -128.65
REMARK 500 TRP B 744 -16.37 -152.55
REMARK 500 SER B 749 75.55 60.84
REMARK 500 ARG B 751 -99.61 -112.17
REMARK 500 HIS B 834 73.45 -158.15
REMARK 500 PHE B 836 -83.66 -141.34
REMARK 500 GLN B 842 -127.68 61.54
REMARK 500 THR B 861 -62.82 -97.21
REMARK 500 SER B 888 -169.15 -108.99
REMARK 500 SER B 896 16.26 -142.93
REMARK 500 HIS B 902 -80.57 -123.96
REMARK 500 HIS B 919 -4.49 72.91
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6H15 A 630 1244 UNP O75581 LRP6_HUMAN 630 1244
DBREF 6H15 C 3 125 PDB 6H15 6H15 3 125
DBREF 6H15 D 3 125 PDB 6H15 6H15 3 125
DBREF 6H15 B 630 1244 UNP O75581 LRP6_HUMAN 630 1244
SEQADV 6H15 ALA A 1245 UNP O75581 EXPRESSION TAG
SEQADV 6H15 ALA B 1245 UNP O75581 EXPRESSION TAG
SEQRES 1 A 616 PRO GLU ALA PHE LEU LEU PHE SER ARG ARG ALA ASP ILE
SEQRES 2 A 616 ARG ARG ILE SER LEU GLU THR ASN ASN ASN ASN VAL ALA
SEQRES 3 A 616 ILE PRO LEU THR GLY VAL LYS GLU ALA SER ALA LEU ASP
SEQRES 4 A 616 PHE ASP VAL THR ASP ASN ARG ILE TYR TRP THR ASP ILE
SEQRES 5 A 616 SER LEU LYS THR ILE SER ARG ALA PHE MET ASN GLY SER
SEQRES 6 A 616 ALA LEU GLU HIS VAL VAL GLU PHE GLY LEU ASP TYR PRO
SEQRES 7 A 616 GLU GLY MET ALA VAL ASP TRP LEU GLY LYS ASN LEU TYR
SEQRES 8 A 616 TRP ALA ASP THR GLY THR ASN ARG ILE GLU VAL SER LYS
SEQRES 9 A 616 LEU ASP GLY GLN HIS ARG GLN VAL LEU VAL TRP LYS ASP
SEQRES 10 A 616 LEU ASP SER PRO ARG ALA LEU ALA LEU ASP PRO ALA GLU
SEQRES 11 A 616 GLY PHE MET TYR TRP THR GLU TRP GLY GLY LYS PRO LYS
SEQRES 12 A 616 ILE ASP ARG ALA ALA MET ASP GLY SER GLU ARG THR THR
SEQRES 13 A 616 LEU VAL PRO ASN VAL GLY ARG ALA ASN GLY LEU THR ILE
SEQRES 14 A 616 ASP TYR ALA LYS ARG ARG LEU TYR TRP THR ASP LEU ASP
SEQRES 15 A 616 THR ASN LEU ILE GLU SER SER ASN MET LEU GLY LEU ASN
SEQRES 16 A 616 ARG GLU VAL ILE ALA ASP ASP LEU PRO HIS PRO PHE GLY
SEQRES 17 A 616 LEU THR GLN TYR GLN ASP TYR ILE TYR TRP THR ASP TRP
SEQRES 18 A 616 SER ARG ARG SER ILE GLU ARG ALA ASN LYS THR SER GLY
SEQRES 19 A 616 GLN ASN ARG THR ILE ILE GLN GLY HIS LEU ASP TYR VAL
SEQRES 20 A 616 MET ASP ILE LEU VAL PHE HIS SER SER ARG GLN SER GLY
SEQRES 21 A 616 TRP ASN GLU CYS ALA SER SER ASN GLY HIS CYS SER HIS
SEQRES 22 A 616 LEU CYS LEU ALA VAL PRO VAL GLY GLY PHE VAL CYS GLY
SEQRES 23 A 616 CYS PRO ALA HIS TYR SER LEU ASN ALA ASP ASN ARG THR
SEQRES 24 A 616 CYS SER ALA PRO THR THR PHE LEU LEU PHE SER GLN LYS
SEQRES 25 A 616 SER ALA ILE ASN ARG MET VAL ILE ASP GLU GLN GLN SER
SEQRES 26 A 616 PRO ASP ILE ILE LEU PRO ILE HIS SER LEU ARG ASN VAL
SEQRES 27 A 616 ARG ALA ILE ASP TYR ASP PRO LEU ASP LYS GLN LEU TYR
SEQRES 28 A 616 TRP ILE ASP SER ARG GLN ASN MET ILE ARG LYS ALA GLN
SEQRES 29 A 616 GLU ASP GLY SER GLN GLY PHE THR VAL VAL VAL SER SER
SEQRES 30 A 616 VAL PRO SER GLN ASN LEU GLU ILE GLN PRO TYR ASP LEU
SEQRES 31 A 616 SER ILE ASP ILE TYR SER ARG TYR ILE TYR TRP THR CYS
SEQRES 32 A 616 GLU ALA THR ASN VAL ILE ASN VAL THR ARG LEU ASP GLY
SEQRES 33 A 616 ARG SER VAL GLY VAL VAL LEU LYS GLY GLU GLN ASP ARG
SEQRES 34 A 616 PRO ARG ALA VAL VAL VAL ASN PRO GLU LYS GLY TYR MET
SEQRES 35 A 616 TYR PHE THR ASN LEU GLN GLU ARG SER PRO LYS ILE GLU
SEQRES 36 A 616 ARG ALA ALA LEU ASP GLY THR GLU ARG GLU VAL LEU PHE
SEQRES 37 A 616 PHE SER GLY LEU SER LYS PRO ILE ALA LEU ALA LEU ASP
SEQRES 38 A 616 SER ARG LEU GLY LYS LEU PHE TRP ALA ASP SER ASP LEU
SEQRES 39 A 616 ARG ARG ILE GLU SER SER ASP LEU SER GLY ALA ASN ARG
SEQRES 40 A 616 ILE VAL LEU GLU ASP SER ASN ILE LEU GLN PRO VAL GLY
SEQRES 41 A 616 LEU THR VAL PHE GLU ASN TRP LEU TYR TRP ILE ASP LYS
SEQRES 42 A 616 GLN GLN GLN MET ILE GLU LYS ILE ASP MET THR GLY ARG
SEQRES 43 A 616 GLU GLY ARG THR LYS VAL GLN ALA ARG ILE ALA GLN LEU
SEQRES 44 A 616 SER ASP ILE HIS ALA VAL LYS GLU LEU ASN LEU GLN GLU
SEQRES 45 A 616 TYR ARG GLN HIS PRO CYS ALA GLN ASP ASN GLY GLY CYS
SEQRES 46 A 616 SER HIS ILE CYS LEU VAL LYS GLY ASP GLY THR THR ARG
SEQRES 47 A 616 CYS SER CYS PRO MET HIS LEU VAL LEU LEU GLN ASP GLU
SEQRES 48 A 616 LEU SER CYS GLY ALA
SEQRES 1 C 123 VAL GLN LEU GLN GLU SER GLY GLY CYS LEU VAL GLN ALA
SEQRES 2 C 123 GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SER
SEQRES 3 C 123 THR PHE SER THR TYR THR ILE GLY TRP PHE ARG GLN ALA
SEQRES 4 C 123 PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE HIS TRP
SEQRES 5 C 123 ASP GLY GLY GLN THR TYR TYR ALA ASP SER VAL LYS GLY
SEQRES 6 C 123 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL
SEQRES 7 C 123 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA
SEQRES 8 C 123 VAL TYR TYR CYS ALA ALA ARG GLY ARG ARG TYR PHE ASP
SEQRES 9 C 123 PHE THR TYR SER ASP VAL TYR ASP TYR TRP GLY GLN GLY
SEQRES 10 C 123 THR GLN VAL THR VAL SER
SEQRES 1 D 123 VAL GLN LEU GLN GLU SER GLY GLY CYS LEU VAL GLN ALA
SEQRES 2 D 123 GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SER
SEQRES 3 D 123 THR PHE SER THR TYR THR ILE GLY TRP PHE ARG GLN ALA
SEQRES 4 D 123 PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE HIS TRP
SEQRES 5 D 123 ASP GLY GLY GLN THR TYR TYR ALA ASP SER VAL LYS GLY
SEQRES 6 D 123 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL
SEQRES 7 D 123 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA
SEQRES 8 D 123 VAL TYR TYR CYS ALA ALA ARG GLY ARG ARG TYR PHE ASP
SEQRES 9 D 123 PHE THR TYR SER ASP VAL TYR ASP TYR TRP GLY GLN GLY
SEQRES 10 D 123 THR GLN VAL THR VAL SER
SEQRES 1 B 616 PRO GLU ALA PHE LEU LEU PHE SER ARG ARG ALA ASP ILE
SEQRES 2 B 616 ARG ARG ILE SER LEU GLU THR ASN ASN ASN ASN VAL ALA
SEQRES 3 B 616 ILE PRO LEU THR GLY VAL LYS GLU ALA SER ALA LEU ASP
SEQRES 4 B 616 PHE ASP VAL THR ASP ASN ARG ILE TYR TRP THR ASP ILE
SEQRES 5 B 616 SER LEU LYS THR ILE SER ARG ALA PHE MET ASN GLY SER
SEQRES 6 B 616 ALA LEU GLU HIS VAL VAL GLU PHE GLY LEU ASP TYR PRO
SEQRES 7 B 616 GLU GLY MET ALA VAL ASP TRP LEU GLY LYS ASN LEU TYR
SEQRES 8 B 616 TRP ALA ASP THR GLY THR ASN ARG ILE GLU VAL SER LYS
SEQRES 9 B 616 LEU ASP GLY GLN HIS ARG GLN VAL LEU VAL TRP LYS ASP
SEQRES 10 B 616 LEU ASP SER PRO ARG ALA LEU ALA LEU ASP PRO ALA GLU
SEQRES 11 B 616 GLY PHE MET TYR TRP THR GLU TRP GLY GLY LYS PRO LYS
SEQRES 12 B 616 ILE ASP ARG ALA ALA MET ASP GLY SER GLU ARG THR THR
SEQRES 13 B 616 LEU VAL PRO ASN VAL GLY ARG ALA ASN GLY LEU THR ILE
SEQRES 14 B 616 ASP TYR ALA LYS ARG ARG LEU TYR TRP THR ASP LEU ASP
SEQRES 15 B 616 THR ASN LEU ILE GLU SER SER ASN MET LEU GLY LEU ASN
SEQRES 16 B 616 ARG GLU VAL ILE ALA ASP ASP LEU PRO HIS PRO PHE GLY
SEQRES 17 B 616 LEU THR GLN TYR GLN ASP TYR ILE TYR TRP THR ASP TRP
SEQRES 18 B 616 SER ARG ARG SER ILE GLU ARG ALA ASN LYS THR SER GLY
SEQRES 19 B 616 GLN ASN ARG THR ILE ILE GLN GLY HIS LEU ASP TYR VAL
SEQRES 20 B 616 MET ASP ILE LEU VAL PHE HIS SER SER ARG GLN SER GLY
SEQRES 21 B 616 TRP ASN GLU CYS ALA SER SER ASN GLY HIS CYS SER HIS
SEQRES 22 B 616 LEU CYS LEU ALA VAL PRO VAL GLY GLY PHE VAL CYS GLY
SEQRES 23 B 616 CYS PRO ALA HIS TYR SER LEU ASN ALA ASP ASN ARG THR
SEQRES 24 B 616 CYS SER ALA PRO THR THR PHE LEU LEU PHE SER GLN LYS
SEQRES 25 B 616 SER ALA ILE ASN ARG MET VAL ILE ASP GLU GLN GLN SER
SEQRES 26 B 616 PRO ASP ILE ILE LEU PRO ILE HIS SER LEU ARG ASN VAL
SEQRES 27 B 616 ARG ALA ILE ASP TYR ASP PRO LEU ASP LYS GLN LEU TYR
SEQRES 28 B 616 TRP ILE ASP SER ARG GLN ASN MET ILE ARG LYS ALA GLN
SEQRES 29 B 616 GLU ASP GLY SER GLN GLY PHE THR VAL VAL VAL SER SER
SEQRES 30 B 616 VAL PRO SER GLN ASN LEU GLU ILE GLN PRO TYR ASP LEU
SEQRES 31 B 616 SER ILE ASP ILE TYR SER ARG TYR ILE TYR TRP THR CYS
SEQRES 32 B 616 GLU ALA THR ASN VAL ILE ASN VAL THR ARG LEU ASP GLY
SEQRES 33 B 616 ARG SER VAL GLY VAL VAL LEU LYS GLY GLU GLN ASP ARG
SEQRES 34 B 616 PRO ARG ALA VAL VAL VAL ASN PRO GLU LYS GLY TYR MET
SEQRES 35 B 616 TYR PHE THR ASN LEU GLN GLU ARG SER PRO LYS ILE GLU
SEQRES 36 B 616 ARG ALA ALA LEU ASP GLY THR GLU ARG GLU VAL LEU PHE
SEQRES 37 B 616 PHE SER GLY LEU SER LYS PRO ILE ALA LEU ALA LEU ASP
SEQRES 38 B 616 SER ARG LEU GLY LYS LEU PHE TRP ALA ASP SER ASP LEU
SEQRES 39 B 616 ARG ARG ILE GLU SER SER ASP LEU SER GLY ALA ASN ARG
SEQRES 40 B 616 ILE VAL LEU GLU ASP SER ASN ILE LEU GLN PRO VAL GLY
SEQRES 41 B 616 LEU THR VAL PHE GLU ASN TRP LEU TYR TRP ILE ASP LYS
SEQRES 42 B 616 GLN GLN GLN MET ILE GLU LYS ILE ASP MET THR GLY ARG
SEQRES 43 B 616 GLU GLY ARG THR LYS VAL GLN ALA ARG ILE ALA GLN LEU
SEQRES 44 B 616 SER ASP ILE HIS ALA VAL LYS GLU LEU ASN LEU GLN GLU
SEQRES 45 B 616 TYR ARG GLN HIS PRO CYS ALA GLN ASP ASN GLY GLY CYS
SEQRES 46 B 616 SER HIS ILE CYS LEU VAL LYS GLY ASP GLY THR THR ARG
SEQRES 47 B 616 CYS SER CYS PRO MET HIS LEU VAL LEU LEU GLN ASP GLU
SEQRES 48 B 616 LEU SER CYS GLY ALA
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET BMA H 3 11
HET MAN H 4 11
HET NAG I 1 14
HET NAG I 2 14
HET BMA I 3 11
HET NAG A1303 14
HET NAG A1304 14
HET NAG A1305 14
HET CL A1309 1
HET CL A1310 1
HET CL C 201 1
HET CL C 202 1
HET NAG B1307 14
HET NAG B1308 14
HET CL B1312 1
HET CL B1313 1
HET CL B1314 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM CL CHLORIDE ION
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
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 5 NAG 15(C8 H15 N O6)
FORMUL 6 BMA 3(C6 H12 O6)
FORMUL 8 MAN C6 H12 O6
FORMUL 13 CL 7(CL 1-)
FORMUL 22 HOH *232(H2 O)
HELIX 1 AA1 HIS A 883 GLN A 887 5 5
HELIX 2 AA2 ASN A 891 CYS A 900 5 10
HELIX 3 AA3 ASN A 1198 GLN A 1204 1 7
HELIX 4 AA4 GLN A 1209 CYS A 1214 5 6
HELIX 5 AA5 THR C 29 THR C 32 5 4
HELIX 6 AA6 ASP C 63 LYS C 66 5 4
HELIX 7 AA7 LYS C 88 THR C 92 5 5
HELIX 8 AA8 TYR C 109 TYR C 113 5 5
HELIX 9 AA9 ASP D 63 LYS D 66 5 4
HELIX 10 AB1 LYS D 88 THR D 92 5 5
HELIX 11 AB2 TYR D 109 TYR D 113 5 5
HELIX 12 AB3 HIS B 883 GLN B 887 5 5
HELIX 13 AB4 ASN B 891 ASN B 897 1 7
HELIX 14 AB5 GLY B 898 CYS B 900 5 3
HELIX 15 AB6 ASN B 1198 GLN B 1204 1 7
HELIX 16 AB7 GLN B 1209 CYS B 1214 5 6
SHEET 1 AA1 4 VAL A 654 ALA A 655 0
SHEET 2 AA1 4 ASP A 641 SER A 646 -1 N ARG A 644 O VAL A 654
SHEET 3 AA1 4 PHE A 633 ARG A 638 -1 N LEU A 634 O ILE A 645
SHEET 4 AA1 4 ASP A 878 PHE A 882 -1 O PHE A 882 N PHE A 633
SHEET 1 AA2 4 ALA A 664 ASP A 670 0
SHEET 2 AA2 4 ARG A 675 ASP A 680 -1 O TYR A 677 N ASP A 668
SHEET 3 AA2 4 THR A 685 PHE A 690 -1 O THR A 685 N ASP A 680
SHEET 4 AA2 4 GLU A 697 VAL A 700 -1 O GLU A 697 N ARG A 688
SHEET 1 AA3 4 GLY A 709 ASP A 713 0
SHEET 2 AA3 4 ASN A 718 ASP A 723 -1 O ASN A 718 N ASP A 713
SHEET 3 AA3 4 ARG A 728 LYS A 733 -1 O SER A 732 N LEU A 719
SHEET 4 AA3 4 GLN A 740 VAL A 743 -1 O LEU A 742 N ILE A 729
SHEET 1 AA4 4 PRO A 750 ASP A 756 0
SHEET 2 AA4 4 PHE A 761 GLU A 766 -1 O TYR A 763 N ALA A 754
SHEET 3 AA4 4 LYS A 772 ALA A 777 -1 O ALA A 776 N MET A 762
SHEET 4 AA4 4 THR A 784 VAL A 787 -1 O THR A 784 N ARG A 775
SHEET 1 AA5 4 ALA A 793 ASP A 799 0
SHEET 2 AA5 4 ARG A 804 ASP A 809 -1 O ARG A 804 N ASP A 799
SHEET 3 AA5 4 LEU A 814 ASN A 819 -1 O SER A 818 N LEU A 805
SHEET 4 AA5 4 GLU A 826 ALA A 829 -1 O ILE A 828 N ILE A 815
SHEET 1 AA6 4 PRO A 835 TYR A 841 0
SHEET 2 AA6 4 TYR A 844 ASP A 849 -1 O TYR A 846 N THR A 839
SHEET 3 AA6 4 SER A 854 ASN A 859 -1 O GLU A 856 N TRP A 847
SHEET 4 AA6 4 THR A 867 GLY A 871 -1 O ILE A 869 N ILE A 855
SHEET 1 AA7 2 LEU A 903 VAL A 907 0
SHEET 2 AA7 2 GLY A 911 GLY A 915 -1 O GLY A 915 N LEU A 903
SHEET 1 AA8 2 SER A 921 LEU A 922 0
SHEET 2 AA8 2 CYS A 929 SER A 930 -1 O SER A 930 N SER A 921
SHEET 1 AA9 4 ILE A 957 ILE A 958 0
SHEET 2 AA9 4 ILE A 944 MET A 947 -1 N ARG A 946 O ILE A 957
SHEET 3 AA9 4 PHE A 935 SER A 939 -1 N LEU A 936 O MET A 947
SHEET 4 AA9 4 ASP A1190 VAL A1194 -1 O HIS A1192 N LEU A 937
SHEET 1 AB1 4 VAL A 967 ASP A 973 0
SHEET 2 AB1 4 GLN A 978 ASP A 983 -1 O TYR A 980 N ASP A 971
SHEET 3 AB1 4 MET A 988 ALA A 992 -1 O ALA A 992 N LEU A 979
SHEET 4 AB1 4 PHE A1000 VAL A1003 -1 O VAL A1002 N ILE A 989
SHEET 1 AB2 4 PRO A1016 ASP A1022 0
SHEET 2 AB2 4 TYR A1027 CYS A1032 -1 O TYR A1027 N ASP A1022
SHEET 3 AB2 4 VAL A1037 ARG A1042 -1 O THR A1041 N ILE A1028
SHEET 4 AB2 4 SER A1047 LEU A1052 -1 O GLY A1049 N VAL A1040
SHEET 1 AB3 4 PRO A1059 VAL A1064 0
SHEET 2 AB3 4 TYR A1070 GLN A1077 -1 O TYR A1072 N VAL A1063
SHEET 3 AB3 4 SER A1080 ALA A1087 -1 O LYS A1082 N ASN A1075
SHEET 4 AB3 4 GLU A1094 PHE A1097 -1 O GLU A1094 N ARG A1085
SHEET 1 AB4 4 PRO A1104 ASP A1110 0
SHEET 2 AB4 4 LYS A1115 ASP A1120 -1 O PHE A1117 N ALA A1108
SHEET 3 AB4 4 ARG A1125 ASP A1130 -1 O SER A1129 N LEU A1116
SHEET 4 AB4 4 ILE A1137 GLU A1140 -1 O LEU A1139 N ILE A1126
SHEET 1 AB5 4 THR A1151 VAL A1152 0
SHEET 2 AB5 4 TRP A1156 ASP A1161 -1 O TYR A1158 N THR A1151
SHEET 3 AB5 4 MET A1166 ASP A1171 -1 O MET A1166 N ASP A1161
SHEET 4 AB5 4 THR A1179 ALA A1183 -1 O GLN A1182 N ILE A1167
SHEET 1 AB6 2 ILE A1217 VAL A1220 0
SHEET 2 AB6 2 THR A1226 SER A1229 -1 O ARG A1227 N LEU A1219
SHEET 1 AB7 2 VAL A1235 LEU A1236 0
SHEET 2 AB7 2 CYS A1243 GLY A1244 -1 O GLY A1244 N VAL A1235
SHEET 1 AB8 4 GLN C 4 SER C 8 0
SHEET 2 AB8 4 LEU C 19 SER C 26 -1 O ALA C 24 N GLN C 6
SHEET 3 AB8 4 VAL C 80 MET C 84 -1 O MET C 84 N LEU C 19
SHEET 4 AB8 4 PHE C 69 ARG C 73 -1 N THR C 70 O GLN C 83
SHEET 1 AB9 6 LEU C 12 GLN C 14 0
SHEET 2 AB9 6 THR C 120 SER C 125 1 O SER C 125 N VAL C 13
SHEET 3 AB9 6 ALA C 93 ARG C 100 -1 N TYR C 95 O THR C 120
SHEET 4 AB9 6 THR C 34 GLN C 40 -1 N PHE C 38 O TYR C 96
SHEET 5 AB9 6 GLU C 47 HIS C 53 -1 O ALA C 50 N TRP C 37
SHEET 6 AB9 6 THR C 59 TYR C 61 -1 O TYR C 60 N ALA C 51
SHEET 1 AC1 4 LEU C 12 GLN C 14 0
SHEET 2 AC1 4 THR C 120 SER C 125 1 O SER C 125 N VAL C 13
SHEET 3 AC1 4 ALA C 93 ARG C 100 -1 N TYR C 95 O THR C 120
SHEET 4 AC1 4 TYR C 115 TRP C 116 -1 O TYR C 115 N ALA C 99
SHEET 1 AC2 4 GLN D 4 SER D 8 0
SHEET 2 AC2 4 LEU D 19 SER D 26 -1 O ALA D 24 N GLN D 6
SHEET 3 AC2 4 THR D 79 MET D 84 -1 O MET D 84 N LEU D 19
SHEET 4 AC2 4 PHE D 69 ARG D 73 -1 N THR D 70 O GLN D 83
SHEET 1 AC3 6 LEU D 12 GLN D 14 0
SHEET 2 AC3 6 THR D 120 SER D 125 1 O THR D 123 N VAL D 13
SHEET 3 AC3 6 ALA D 93 ARG D 100 -1 N TYR D 95 O THR D 120
SHEET 4 AC3 6 THR D 34 GLN D 40 -1 N GLY D 36 O ALA D 98
SHEET 5 AC3 6 GLU D 47 HIS D 53 -1 O ALA D 50 N TRP D 37
SHEET 6 AC3 6 THR D 59 TYR D 61 -1 O TYR D 60 N ALA D 51
SHEET 1 AC4 4 LEU D 12 GLN D 14 0
SHEET 2 AC4 4 THR D 120 SER D 125 1 O THR D 123 N VAL D 13
SHEET 3 AC4 4 ALA D 93 ARG D 100 -1 N TYR D 95 O THR D 120
SHEET 4 AC4 4 TYR D 115 TRP D 116 -1 O TYR D 115 N ALA D 99
SHEET 1 AC5 4 VAL B 654 ALA B 655 0
SHEET 2 AC5 4 ASP B 641 SER B 646 -1 N ARG B 644 O VAL B 654
SHEET 3 AC5 4 PHE B 633 ARG B 638 -1 N LEU B 634 O ILE B 645
SHEET 4 AC5 4 ILE B 879 PHE B 882 -1 O PHE B 882 N PHE B 633
SHEET 1 AC6 4 ALA B 664 ASP B 670 0
SHEET 2 AC6 4 ARG B 675 ASP B 680 -1 O TYR B 677 N ASP B 668
SHEET 3 AC6 4 THR B 685 PHE B 690 -1 O THR B 685 N ASP B 680
SHEET 4 AC6 4 GLU B 697 VAL B 700 -1 O GLU B 697 N ARG B 688
SHEET 1 AC7 4 GLY B 709 ASP B 713 0
SHEET 2 AC7 4 ASN B 718 ASP B 723 -1 O ALA B 722 N GLY B 709
SHEET 3 AC7 4 ARG B 728 LYS B 733 -1 O SER B 732 N LEU B 719
SHEET 4 AC7 4 GLN B 740 VAL B 743 -1 O GLN B 740 N VAL B 731
SHEET 1 AC8 4 PRO B 750 ASP B 756 0
SHEET 2 AC8 4 PHE B 761 GLU B 766 -1 O TYR B 763 N ALA B 754
SHEET 3 AC8 4 LYS B 772 ALA B 777 -1 O LYS B 772 N GLU B 766
SHEET 4 AC8 4 THR B 784 VAL B 787 -1 O THR B 784 N ARG B 775
SHEET 1 AC9 4 ALA B 793 ASP B 799 0
SHEET 2 AC9 4 ARG B 804 ASP B 809 -1 O TYR B 806 N THR B 797
SHEET 3 AC9 4 LEU B 814 ASN B 819 -1 O SER B 818 N LEU B 805
SHEET 4 AC9 4 GLU B 826 ALA B 829 -1 O ILE B 828 N ILE B 815
SHEET 1 AD1 4 PRO B 835 TYR B 841 0
SHEET 2 AD1 4 TYR B 844 ASP B 849 -1 O TYR B 846 N THR B 839
SHEET 3 AD1 4 SER B 854 ASN B 859 -1 O GLU B 856 N TRP B 847
SHEET 4 AD1 4 THR B 867 GLN B 870 -1 O ILE B 869 N ILE B 855
SHEET 1 AD2 2 LEU B 903 VAL B 907 0
SHEET 2 AD2 2 GLY B 911 GLY B 915 -1 O VAL B 913 N LEU B 905
SHEET 1 AD3 2 SER B 921 LEU B 922 0
SHEET 2 AD3 2 CYS B 929 SER B 930 -1 O SER B 930 N SER B 921
SHEET 1 AD4 4 ILE B 957 ILE B 958 0
SHEET 2 AD4 4 ILE B 944 MET B 947 -1 N ARG B 946 O ILE B 957
SHEET 3 AD4 4 PHE B 935 GLN B 940 -1 N LEU B 936 O MET B 947
SHEET 4 AD4 4 LEU B1188 VAL B1194 -1 O HIS B1192 N LEU B 937
SHEET 1 AD5 4 ASP B 971 ASP B 973 0
SHEET 2 AD5 4 GLN B 978 ASP B 983 -1 O TYR B 980 N ASP B 971
SHEET 3 AD5 4 MET B 988 ALA B 992 -1 O ALA B 992 N LEU B 979
SHEET 4 AD5 4 PHE B1000 VAL B1003 -1 O VAL B1002 N ILE B 989
SHEET 1 AD6 4 PRO B1016 ASP B1022 0
SHEET 2 AD6 4 TYR B1027 CYS B1032 -1 O THR B1031 N TYR B1017
SHEET 3 AD6 4 VAL B1037 ARG B1042 -1 O THR B1041 N ILE B1028
SHEET 4 AD6 4 SER B1047 LYS B1053 -1 O VAL B1051 N ILE B1038
SHEET 1 AD7 4 PRO B1059 ASN B1065 0
SHEET 2 AD7 4 TYR B1070 GLN B1077 -1 O TYR B1072 N VAL B1063
SHEET 3 AD7 4 SER B1080 ALA B1087 -1 O LYS B1082 N ASN B1075
SHEET 4 AD7 4 GLU B1094 PHE B1097 -1 O GLU B1094 N ARG B1085
SHEET 1 AD8 4 PRO B1104 ASP B1110 0
SHEET 2 AD8 4 LYS B1115 ASP B1120 -1 O PHE B1117 N ALA B1108
SHEET 3 AD8 4 ARG B1125 ASP B1130 -1 O SER B1129 N LEU B1116
SHEET 4 AD8 4 ILE B1137 GLU B1140 -1 O ILE B1137 N SER B1128
SHEET 1 AD9 4 THR B1151 VAL B1152 0
SHEET 2 AD9 4 TRP B1156 ASP B1161 -1 O TYR B1158 N THR B1151
SHEET 3 AD9 4 MET B1166 ASP B1171 -1 O MET B1166 N ASP B1161
SHEET 4 AD9 4 THR B1179 GLN B1182 -1 O VAL B1181 N ILE B1167
SHEET 1 AE1 2 ILE B1217 VAL B1220 0
SHEET 2 AE1 2 THR B1226 SER B1229 -1 O ARG B1227 N LEU B1219
SHEET 1 AE2 2 VAL B1235 LEU B1236 0
SHEET 2 AE2 2 CYS B1243 GLY B1244 -1 O GLY B1244 N VAL B1235
SSBOND 1 CYS A 893 CYS A 904 1555 1555 2.03
SSBOND 2 CYS A 900 CYS A 914 1555 1555 2.03
SSBOND 3 CYS A 916 CYS A 929 1555 1555 2.03
SSBOND 4 CYS A 1207 CYS A 1218 1555 1555 2.03
SSBOND 5 CYS A 1214 CYS A 1228 1555 1555 2.03
SSBOND 6 CYS A 1230 CYS A 1243 1555 1555 2.03
SSBOND 7 CYS C 23 CYS C 97 1555 1555 2.04
SSBOND 8 CYS D 23 CYS D 97 1555 1555 2.03
SSBOND 9 CYS B 893 CYS B 904 1555 1555 2.03
SSBOND 10 CYS B 900 CYS B 914 1555 1555 2.03
SSBOND 11 CYS B 916 CYS B 929 1555 1555 2.03
SSBOND 12 CYS B 1207 CYS B 1218 1555 1555 2.03
SSBOND 13 CYS B 1214 CYS B 1228 1555 1555 2.03
SSBOND 14 CYS B 1230 CYS B 1243 1555 1555 2.03
LINK ND2 ASN A 692 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN A 859 C1 NAG A1303 1555 1555 1.44
LINK ND2 ASN A 865 C1 NAG A1304 1555 1555 1.46
LINK ND2 ASN A 926 C1 NAG A1305 1555 1555 1.44
LINK ND2 ASN A1039 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN B 692 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN B 859 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN B 865 C1 NAG B1307 1555 1555 1.45
LINK ND2 ASN B 926 C1 NAG B1308 1555 1555 1.45
LINK ND2 ASN B1039 C1 NAG I 1 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.45
LINK O6 BMA H 3 C1 MAN H 4 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.44
CISPEP 1 PRO A 908 VAL A 909 0 -1.81
CISPEP 2 PRO B 908 VAL B 909 0 0.48
CRYST1 118.314 118.314 249.951 90.00 90.00 120.00 P 65 12
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 0.008452 0.004880 0.000000 0.00000
SCALE2 0.000000 0.009760 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004001 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
