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HEADER HYDROLASE/VIRAL PROTEIN 29-JUL-14 4QZV
TITLE BAT-DERIVED CORONAVIRUS HKU4 USES MERS-COV RECEPTOR HUMAN CD26 FOR
TITLE 2 CELL ENTRY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,
COMPND 5 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,
COMPND 6 TP103, DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE IV
COMPND 7 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM, DIPEPTIDYL
COMPND 8 PEPTIDASE IV SOLUBLE FORM;
COMPND 9 EC: 3.4.14.5;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: SPIKE PROTEIN S1;
COMPND 13 CHAIN: B, D;
COMPND 14 FRAGMENT: RECEPTOR BINDING DOMAIN (UNP RESIDUES 372-611);
COMPND 15 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: DPP4, ADCP2, CD26;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: TYLONYCTERIS BAT CORONAVIRUS HKU4;
SOURCE 12 ORGANISM_COMMON: BTCOV;
SOURCE 13 ORGANISM_TAXID: 694007;
SOURCE 14 GENE: S, 2;
SOURCE 15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS 8-BLADED BETA-PROPELLER DOMAIN, ALPHA/BETA HYDROLASE DOMAIN, BLADES
KEYWDS 2 IV AND V, CD26 BETA-PROPELLER, HYDROLASE-VIRAL PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.G.GAO,Q.H.WANG,J.X.QI,G.W.LU
REVDAT 1 29-OCT-14 4QZV 0
JRNL AUTH Q.H.WANG,J.X.QI,Y.YUAN,Y.XUAN,P.HAN,Y.WAN,W.JI,Y.LI,Y.WU,
JRNL AUTH 2 J.WANG,A.IWAMOTO,P.C.WOO,K.Y.YUEN,J.YAN,G.W.LU,G.F.GAO
JRNL TITL BAT ORIGINS OF MERS-COV SUPPORTED BY BAT CORONAVIRUS HKU4
JRNL TITL 2 USAGE OF HUMAN RECEPTOR CD26.
JRNL REF CELL HOST MICROBE V. 16 328 2014
JRNL REFN ISSN 1931-3128
JRNL PMID 25211075
JRNL DOI 10.1016/J.CHOM.2014.08.009
REMARK 2
REMARK 2 RESOLUTION. 2.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 102311
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5112
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 46.3082 - 8.0394 0.99 3546 173 0.1938 0.2271
REMARK 3 2 8.0394 - 6.3864 1.00 3408 183 0.1894 0.2061
REMARK 3 3 6.3864 - 5.5807 1.00 3340 188 0.1731 0.1748
REMARK 3 4 5.5807 - 5.0711 1.00 3349 201 0.1482 0.1926
REMARK 3 5 5.0711 - 4.7080 1.00 3327 189 0.1366 0.1729
REMARK 3 6 4.7080 - 4.4307 1.00 3306 177 0.1332 0.1509
REMARK 3 7 4.4307 - 4.2090 1.00 3297 186 0.1390 0.1804
REMARK 3 8 4.2090 - 4.0258 1.00 3313 183 0.1515 0.1913
REMARK 3 9 4.0258 - 3.8709 1.00 3307 184 0.1621 0.1988
REMARK 3 10 3.8709 - 3.7374 1.00 3281 166 0.1769 0.2002
REMARK 3 11 3.7374 - 3.6206 1.00 3286 155 0.1782 0.2128
REMARK 3 12 3.6206 - 3.5172 0.99 3280 168 0.1912 0.2254
REMARK 3 13 3.5172 - 3.4246 0.99 3219 167 0.2006 0.2375
REMARK 3 14 3.4246 - 3.3411 0.99 3296 164 0.2107 0.2657
REMARK 3 15 3.3411 - 3.2651 0.99 3253 166 0.2247 0.2832
REMARK 3 16 3.2651 - 3.1957 0.99 3267 173 0.2182 0.2454
REMARK 3 17 3.1957 - 3.1318 0.99 3212 190 0.2210 0.2333
REMARK 3 18 3.1318 - 3.0727 0.99 3250 189 0.2161 0.2484
REMARK 3 19 3.0727 - 3.0178 0.98 3189 185 0.2262 0.2835
REMARK 3 20 3.0178 - 2.9667 0.97 3185 160 0.2368 0.2972
REMARK 3 21 2.9667 - 2.9188 0.99 3182 174 0.2373 0.2722
REMARK 3 22 2.9188 - 2.8739 0.97 3242 148 0.2286 0.2693
REMARK 3 23 2.8739 - 2.8317 0.98 3198 153 0.2383 0.2688
REMARK 3 24 2.8317 - 2.7918 0.97 3179 153 0.2462 0.2982
REMARK 3 25 2.7918 - 2.7540 0.96 3162 155 0.2440 0.2883
REMARK 3 26 2.7540 - 2.7183 0.97 3116 178 0.2472 0.2579
REMARK 3 27 2.7183 - 2.6843 0.95 3169 151 0.2483 0.2760
REMARK 3 28 2.6843 - 2.6520 0.96 3143 150 0.2505 0.3382
REMARK 3 29 2.6520 - 2.6211 0.96 3076 170 0.2596 0.3351
REMARK 3 30 2.6211 - 2.5917 0.85 2821 133 0.2808 0.3180
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.006 15885
REMARK 3 ANGLE : 0.944 21612
REMARK 3 CHIRALITY : 0.040 2365
REMARK 3 PLANARITY : 0.004 2734
REMARK 3 DIHEDRAL : 14.264 5664
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): 180.8006 251.3016 41.2624
REMARK 3 T TENSOR
REMARK 3 T11: 0.1984 T22: 0.2280
REMARK 3 T33: 0.1936 T12: -0.0018
REMARK 3 T13: 0.0173 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.1699 L22: 0.1628
REMARK 3 L33: 0.1481 L12: -0.0349
REMARK 3 L13: 0.0989 L23: -0.0233
REMARK 3 S TENSOR
REMARK 3 S11: -0.0121 S12: 0.0135 S13: 0.0083
REMARK 3 S21: -0.0238 S22: 0.0288 S23: -0.0263
REMARK 3 S31: -0.0031 S32: 0.0075 S33: 0.0000
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 4QZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-AUG-14.
REMARK 100 THE RCSB ID CODE IS RCSB086722.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 102311
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.592
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
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) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE, PH 5.5, 15% PEG
REMARK 280 6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
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 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 101.58300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 103.87650
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 101.58300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 103.87650
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 39
REMARK 465 HIS A 767
REMARK 465 HIS A 768
REMARK 465 HIS A 769
REMARK 465 HIS A 770
REMARK 465 HIS A 771
REMARK 465 HIS A 772
REMARK 465 GLU B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 ALA B 4
REMARK 465 THR B 5
REMARK 465 GLY B 6
REMARK 465 THR B 7
REMARK 465 PHE B 8
REMARK 465 ILE B 9
REMARK 465 GLU B 10
REMARK 465 GLN B 11
REMARK 465 PRO B 12
REMARK 465 ASN B 13
REMARK 465 ALA B 14
REMARK 465 ASP B 223
REMARK 465 LEU B 224
REMARK 465 GLY B 225
REMARK 465 ASP B 226
REMARK 465 SER B 227
REMARK 465 LEU B 228
REMARK 465 THR B 229
REMARK 465 ILE B 230
REMARK 465 THR B 231
REMARK 465 ASN B 232
REMARK 465 ARG B 233
REMARK 465 LEU B 234
REMARK 465 GLY B 235
REMARK 465 LYS B 236
REMARK 465 CYS B 237
REMARK 465 VAL B 238
REMARK 465 ASP B 239
REMARK 465 TYR B 240
REMARK 465 HIS B 241
REMARK 465 HIS B 242
REMARK 465 HIS B 243
REMARK 465 HIS B 244
REMARK 465 HIS B 245
REMARK 465 HIS B 246
REMARK 465 SER C 39
REMARK 465 HIS C 767
REMARK 465 HIS C 768
REMARK 465 HIS C 769
REMARK 465 HIS C 770
REMARK 465 HIS C 771
REMARK 465 HIS C 772
REMARK 465 GLU D 1
REMARK 465 ALA D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 THR D 5
REMARK 465 GLY D 6
REMARK 465 THR D 7
REMARK 465 PHE D 8
REMARK 465 ILE D 9
REMARK 465 GLU D 10
REMARK 465 GLN D 11
REMARK 465 PRO D 12
REMARK 465 ASN D 13
REMARK 465 ALA D 14
REMARK 465 ASP D 223
REMARK 465 LEU D 224
REMARK 465 GLY D 225
REMARK 465 ASP D 226
REMARK 465 SER D 227
REMARK 465 LEU D 228
REMARK 465 THR D 229
REMARK 465 ILE D 230
REMARK 465 THR D 231
REMARK 465 ASN D 232
REMARK 465 ARG D 233
REMARK 465 LEU D 234
REMARK 465 GLY D 235
REMARK 465 LYS D 236
REMARK 465 CYS D 237
REMARK 465 VAL D 238
REMARK 465 ASP D 239
REMARK 465 TYR D 240
REMARK 465 HIS D 241
REMARK 465 HIS D 242
REMARK 465 HIS D 243
REMARK 465 HIS D 244
REMARK 465 HIS D 245
REMARK 465 HIS D 246
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 SG CYS D 59 SG CYS D 112 1.69
REMARK 500 O HOH A 949 O HOH A 996 1.85
REMARK 500 NH1 ARG A 658 O HOH A 1029 1.88
REMARK 500 O HOH C 994 O HOH C 1094 1.93
REMARK 500 O HOH A 1062 O HOH C 1061 1.95
REMARK 500 OG SER D 63 OG SER D 66 1.96
REMARK 500 O HOH A 992 O HOH A 1057 1.96
REMARK 500 OG1 THR B 148 O HOH B 317 1.98
REMARK 500 O HOH C 1003 O HOH C 1048 2.00
REMARK 500 O HOH C 1035 O HOH C 1085 2.00
REMARK 500 O TYR D 157 O HOH D 307 2.04
REMARK 500 O HOH C 1076 O HOH C 1138 2.05
REMARK 500 O4 NAG A 809 O HOH A 935 2.07
REMARK 500 O PRO A 766 O HOH A 1040 2.07
REMARK 500 O LEU D 150 O HOH D 310 2.07
REMARK 500 O LYS A 122 O HOH A 993 2.08
REMARK 500 O VAL C 233 O HOH C 1015 2.08
REMARK 500 OD1 ASP C 302 O HOH C 931 2.10
REMARK 500 O HOH A 992 O HOH A 997 2.10
REMARK 500 OE1 GLU C 82 OH TYR C 467 2.11
REMARK 500 NH2 ARG D 138 O GLU D 183 2.11
REMARK 500 O HOH C 974 O HOH C 1126 2.12
REMARK 500 O HOH A 973 O HOH A 1087 2.13
REMARK 500 O HOH C 937 O HOH C 1079 2.13
REMARK 500 O4 NAG C 806 O5 BMA C 807 2.14
REMARK 500 O TRP A 734 O HOH A 914 2.14
REMARK 500 O ALA C 555 O HOH C 983 2.16
REMARK 500 OD2 ASP C 729 O HOH C 977 2.16
REMARK 500 O HOH B 304 O HOH B 318 2.16
REMARK 500 O HOH A 943 O HOH A 1035 2.17
REMARK 500 OE1 GLU C 67 O HOH C 964 2.18
REMARK 500 O PRO C 766 O HOH C 1064 2.18
REMARK 500 NH2 ARG C 40 O ASN C 506 2.19
REMARK 500 O PRO C 532 O HOH C 1114 2.19
REMARK 500 O LEU A 640 O HOH A 1048 2.19
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 GLU A 73 52.15 39.35
REMARK 500 ASN A 74 -3.24 69.92
REMARK 500 ASP A 96 30.04 -98.22
REMARK 500 GLN A 123 -100.36 -106.26
REMARK 500 TRP A 124 -148.60 -94.15
REMARK 500 HIS A 162 35.27 -154.24
REMARK 500 ASP A 192 -0.15 63.88
REMARK 500 SER A 242 -162.12 61.33
REMARK 500 GLN A 320 33.87 -82.74
REMARK 500 THR A 401 59.55 -92.33
REMARK 500 LYS A 423 16.71 52.64
REMARK 500 ASN A 450 70.06 -169.04
REMARK 500 ASN A 487 22.69 -140.85
REMARK 500 TYR A 547 -73.13 -124.55
REMARK 500 ARG A 597 54.72 -149.79
REMARK 500 THR A 600 -93.73 -124.70
REMARK 500 SER A 630 -120.13 58.52
REMARK 500 ASP A 678 -96.82 -108.41
REMARK 500 ASN A 710 -73.05 -92.68
REMARK 500 MET A 733 119.58 -160.40
REMARK 500 ASP A 739 -158.41 -99.24
REMARK 500 ASN B 40 71.50 44.35
REMARK 500 TYR B 82 124.17 -172.72
REMARK 500 ASP B 145 9.86 -154.26
REMARK 500 SER B 164 73.46 -164.10
REMARK 500 GLU B 183 2.22 -62.27
REMARK 500 ASP B 216 128.35 163.61
REMARK 500 SER C 64 -156.71 -143.77
REMARK 500 HIS C 66 13.92 -152.60
REMARK 500 GLU C 73 -62.19 -173.29
REMARK 500 GLU C 97 -19.49 -170.45
REMARK 500 HIS C 100 -165.56 -105.78
REMARK 500 GLN C 123 -98.63 -112.50
REMARK 500 TRP C 124 -151.04 -93.44
REMARK 500 TRP C 154 136.63 -170.47
REMARK 500 HIS C 162 30.04 -153.45
REMARK 500 ILE C 193 -65.21 -121.00
REMARK 500 VAL C 207 -62.74 -107.34
REMARK 500 SER C 242 -163.18 57.68
REMARK 500 THR C 307 -165.36 -128.88
REMARK 500 GLN C 320 36.03 -86.24
REMARK 500 ASN C 450 74.63 -173.80
REMARK 500 ASN C 520 82.39 16.58
REMARK 500 TYR C 547 -68.14 -124.56
REMARK 500 ARG C 597 58.41 -146.99
REMARK 500 THR C 600 -85.64 -130.07
REMARK 500 LYS C 615 39.54 -99.18
REMARK 500 SER C 630 -125.99 60.07
REMARK 500 ASP C 678 -90.71 -105.61
REMARK 500 ASN C 679 31.09 -141.45
REMARK 500
REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS.
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 ASN B 121 VAL B 122 148.10
REMARK 500 ASP C 96 GLU C 97 -141.29
REMARK 500 ASN D 121 VAL D 122 133.44
REMARK 500 THR D 215 ASP D 216 149.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C1135 DISTANCE = 6.07 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 85 RESIDUES 801 TO 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 812 BOUND
REMARK 800 TO ASN A 92
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 803 BOUND
REMARK 800 TO ASN A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 804 BOUND
REMARK 800 TO ASN A 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 229 RESIDUES 805 TO 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 281 RESIDUES 808 TO 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 321 RESIDUES 810 TO 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF SUGAR BOUND TO ASN C
REMARK 800 85 RESIDUES 801 TO 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG C 803 BOUND
REMARK 800 TO ASN C 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG C 804 BOUND
REMARK 800 TO ASN C 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF SUGAR BOUND TO ASN C
REMARK 800 229 RESIDUES 805 TO 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF SUGAR BOUND TO ASN C
REMARK 800 281 RESIDUES 808 TO 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF SUGAR BOUND TO ASN C
REMARK 800 321 RESIDUES 810 TO 811
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KR0 RELATED DB: PDB
REMARK 900 COMPLEX STRUCTURE OF MERS-COV SPIKE RBD BOUND TO HUMAN CD26
DBREF 4QZV A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 4QZV B 1 240 UNP A3EX94 SPIKE_BCHK4 372 611
DBREF 4QZV C 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 4QZV D 1 240 UNP A3EX94 SPIKE_BCHK4 372 611
SEQADV 4QZV HIS A 767 UNP P27487 EXPRESSION TAG
SEQADV 4QZV HIS A 768 UNP P27487 EXPRESSION TAG
SEQADV 4QZV HIS A 769 UNP P27487 EXPRESSION TAG
SEQADV 4QZV HIS A 770 UNP P27487 EXPRESSION TAG
SEQADV 4QZV HIS A 771 UNP P27487 EXPRESSION TAG
SEQADV 4QZV HIS A 772 UNP P27487 EXPRESSION TAG
SEQADV 4QZV HIS B 241 UNP A3EX94 EXPRESSION TAG
SEQADV 4QZV HIS B 242 UNP A3EX94 EXPRESSION TAG
SEQADV 4QZV HIS B 243 UNP A3EX94 EXPRESSION TAG
SEQADV 4QZV HIS B 244 UNP A3EX94 EXPRESSION TAG
SEQADV 4QZV HIS B 245 UNP A3EX94 EXPRESSION TAG
SEQADV 4QZV HIS B 246 UNP A3EX94 EXPRESSION TAG
SEQADV 4QZV HIS C 767 UNP P27487 EXPRESSION TAG
SEQADV 4QZV HIS C 768 UNP P27487 EXPRESSION TAG
SEQADV 4QZV HIS C 769 UNP P27487 EXPRESSION TAG
SEQADV 4QZV HIS C 770 UNP P27487 EXPRESSION TAG
SEQADV 4QZV HIS C 771 UNP P27487 EXPRESSION TAG
SEQADV 4QZV HIS C 772 UNP P27487 EXPRESSION TAG
SEQADV 4QZV HIS D 241 UNP A3EX94 EXPRESSION TAG
SEQADV 4QZV HIS D 242 UNP A3EX94 EXPRESSION TAG
SEQADV 4QZV HIS D 243 UNP A3EX94 EXPRESSION TAG
SEQADV 4QZV HIS D 244 UNP A3EX94 EXPRESSION TAG
SEQADV 4QZV HIS D 245 UNP A3EX94 EXPRESSION TAG
SEQADV 4QZV HIS D 246 UNP A3EX94 EXPRESSION TAG
SEQRES 1 A 734 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 A 734 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 A 734 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 734 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 A 734 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 A 734 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 A 734 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 734 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 734 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 A 734 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 734 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 A 734 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 A 734 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 734 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 734 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 734 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 734 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 A 734 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 A 734 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 A 734 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 A 734 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 A 734 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 734 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 A 734 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 A 734 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 A 734 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 734 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 A 734 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 A 734 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 734 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 A 734 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 A 734 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 734 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 A 734 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 734 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 A 734 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 A 734 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 A 734 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 734 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 A 734 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 A 734 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 734 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 734 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 734 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 A 734 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 A 734 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 734 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 734 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 A 734 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 734 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 A 734 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 734 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 734 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 A 734 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 734 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 734 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 57 A 734 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 246 GLU ALA SER ALA THR GLY THR PHE ILE GLU GLN PRO ASN
SEQRES 2 B 246 ALA THR GLU CYS ASP PHE SER PRO MET LEU THR GLY VAL
SEQRES 3 B 246 ALA PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE SER
SEQRES 4 B 246 ASN CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE
SEQRES 5 B 246 ALA VAL ASP GLU PHE SER CYS ASN GLY ILE SER PRO ASP
SEQRES 6 B 246 SER ILE ALA ARG GLY CYS TYR SER THR LEU THR VAL ASP
SEQRES 7 B 246 TYR PHE ALA TYR PRO LEU SER MET LYS SER TYR ILE ARG
SEQRES 8 B 246 PRO GLY SER ALA GLY ASN ILE PRO LEU TYR ASN TYR LYS
SEQRES 9 B 246 GLN SER PHE ALA ASN PRO THR CYS ARG VAL MET ALA SER
SEQRES 10 B 246 VAL LEU ALA ASN VAL THR ILE THR LYS PRO HIS ALA TYR
SEQRES 11 B 246 GLY TYR ILE SER LYS CYS SER ARG LEU THR GLY ALA ASN
SEQRES 12 B 246 GLN ASP VAL GLU THR PRO LEU TYR ILE ASN PRO GLY GLU
SEQRES 13 B 246 TYR SER ILE CYS ARG ASP PHE SER PRO GLY GLY PHE SER
SEQRES 14 B 246 GLU ASP GLY GLN VAL PHE LYS ARG THR LEU THR GLN PHE
SEQRES 15 B 246 GLU GLY GLY GLY LEU LEU ILE GLY VAL GLY THR ARG VAL
SEQRES 16 B 246 PRO MET THR ASP ASN LEU GLN MET SER PHE ILE ILE SER
SEQRES 17 B 246 VAL GLN TYR GLY THR GLY THR ASP SER VAL CYS PRO MET
SEQRES 18 B 246 LEU ASP LEU GLY ASP SER LEU THR ILE THR ASN ARG LEU
SEQRES 19 B 246 GLY LYS CYS VAL ASP TYR HIS HIS HIS HIS HIS HIS
SEQRES 1 C 734 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 C 734 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 C 734 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 C 734 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 C 734 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 C 734 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 C 734 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 C 734 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 C 734 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 C 734 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 C 734 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 C 734 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 C 734 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 C 734 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 C 734 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 C 734 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 C 734 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 C 734 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 C 734 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 C 734 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 C 734 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 C 734 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 C 734 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 C 734 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 C 734 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 C 734 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 C 734 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 C 734 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 C 734 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 C 734 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 C 734 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 C 734 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 C 734 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 C 734 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 C 734 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 C 734 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 C 734 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 C 734 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 C 734 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 C 734 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 C 734 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 C 734 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 C 734 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 C 734 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 C 734 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 C 734 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 C 734 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 C 734 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 C 734 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 C 734 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 C 734 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 C 734 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 C 734 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 C 734 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 C 734 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 C 734 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 57 C 734 HIS HIS HIS HIS HIS HIS
SEQRES 1 D 246 GLU ALA SER ALA THR GLY THR PHE ILE GLU GLN PRO ASN
SEQRES 2 D 246 ALA THR GLU CYS ASP PHE SER PRO MET LEU THR GLY VAL
SEQRES 3 D 246 ALA PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE SER
SEQRES 4 D 246 ASN CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE
SEQRES 5 D 246 ALA VAL ASP GLU PHE SER CYS ASN GLY ILE SER PRO ASP
SEQRES 6 D 246 SER ILE ALA ARG GLY CYS TYR SER THR LEU THR VAL ASP
SEQRES 7 D 246 TYR PHE ALA TYR PRO LEU SER MET LYS SER TYR ILE ARG
SEQRES 8 D 246 PRO GLY SER ALA GLY ASN ILE PRO LEU TYR ASN TYR LYS
SEQRES 9 D 246 GLN SER PHE ALA ASN PRO THR CYS ARG VAL MET ALA SER
SEQRES 10 D 246 VAL LEU ALA ASN VAL THR ILE THR LYS PRO HIS ALA TYR
SEQRES 11 D 246 GLY TYR ILE SER LYS CYS SER ARG LEU THR GLY ALA ASN
SEQRES 12 D 246 GLN ASP VAL GLU THR PRO LEU TYR ILE ASN PRO GLY GLU
SEQRES 13 D 246 TYR SER ILE CYS ARG ASP PHE SER PRO GLY GLY PHE SER
SEQRES 14 D 246 GLU ASP GLY GLN VAL PHE LYS ARG THR LEU THR GLN PHE
SEQRES 15 D 246 GLU GLY GLY GLY LEU LEU ILE GLY VAL GLY THR ARG VAL
SEQRES 16 D 246 PRO MET THR ASP ASN LEU GLN MET SER PHE ILE ILE SER
SEQRES 17 D 246 VAL GLN TYR GLY THR GLY THR ASP SER VAL CYS PRO MET
SEQRES 18 D 246 LEU ASP LEU GLY ASP SER LEU THR ILE THR ASN ARG LEU
SEQRES 19 D 246 GLY LYS CYS VAL ASP TYR HIS HIS HIS HIS HIS HIS
MODRES 4QZV ASN C 229 ASN GLYCOSYLATION SITE
MODRES 4QZV ASN A 321 ASN GLYCOSYLATION SITE
MODRES 4QZV ASN A 229 ASN GLYCOSYLATION SITE
MODRES 4QZV ASN C 321 ASN GLYCOSYLATION SITE
MODRES 4QZV ASN A 281 ASN GLYCOSYLATION SITE
MODRES 4QZV ASN A 92 ASN GLYCOSYLATION SITE
MODRES 4QZV ASN A 85 ASN GLYCOSYLATION SITE
MODRES 4QZV ASN C 150 ASN GLYCOSYLATION SITE
MODRES 4QZV ASN C 281 ASN GLYCOSYLATION SITE
MODRES 4QZV ASN C 85 ASN GLYCOSYLATION SITE
MODRES 4QZV ASN C 219 ASN GLYCOSYLATION SITE
MODRES 4QZV ASN A 150 ASN GLYCOSYLATION SITE
MODRES 4QZV ASN A 219 ASN GLYCOSYLATION SITE
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET NAG A 805 14
HET NAG A 806 14
HET BMA A 807 11
HET NAG A 808 14
HET NAG A 809 14
HET NAG A 810 14
HET NAG A 811 14
HET NAG A 812 14
HET NAG C 801 14
HET NAG C 802 14
HET NAG C 803 14
HET NAG C 804 14
HET NAG C 805 14
HET NAG C 806 14
HET BMA C 807 11
HET NAG C 808 14
HET NAG C 809 14
HET NAG C 810 14
HET NAG C 811 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
FORMUL 5 NAG 21(C8 H15 N O6)
FORMUL 8 BMA 2(C6 H12 O6)
FORMUL 18 HOH *476(H2 O)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 GLU A 91 ASP A 96 5 6
HELIX 3 3 ASP A 200 VAL A 207 1 8
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 VAL A 341 GLN A 344 5 4
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 LYS A 463 ALA A 465 5 3
HELIX 8 8 ASN A 497 GLN A 505 1 9
HELIX 9 9 ASN A 562 THR A 570 1 9
HELIX 10 10 GLY A 587 HIS A 592 1 6
HELIX 11 11 ALA A 593 ASN A 595 5 3
HELIX 12 12 THR A 600 LYS A 615 1 16
HELIX 13 13 SER A 630 GLY A 641 1 12
HELIX 14 14 ARG A 658 TYR A 662 5 5
HELIX 15 15 ASP A 663 GLY A 672 1 10
HELIX 16 16 ASN A 679 SER A 686 1 8
HELIX 17 17 VAL A 688 VAL A 698 5 11
HELIX 18 18 HIS A 712 ASP A 725 1 14
HELIX 19 19 SER A 744 PHE A 763 1 20
HELIX 20 20 GLN B 29 PHE B 33 5 5
HELIX 21 21 ASN B 44 SER B 50 1 7
HELIX 22 22 ASP B 65 ARG B 69 5 5
HELIX 23 23 PRO B 83 ARG B 91 5 9
HELIX 24 24 GLY B 96 ASN B 102 1 7
HELIX 25 25 CYS B 160 SER B 164 5 5
HELIX 26 26 THR C 44 LYS C 50 1 7
HELIX 27 27 ASP C 200 VAL C 207 1 8
HELIX 28 28 PRO C 290 ILE C 295 1 6
HELIX 29 29 VAL C 341 GLN C 344 5 4
HELIX 30 30 GLU C 421 MET C 425 5 5
HELIX 31 31 LYS C 463 ALA C 465 5 3
HELIX 32 32 ASN C 497 LEU C 504 1 8
HELIX 33 33 ASN C 562 THR C 570 1 9
HELIX 34 34 GLY C 587 HIS C 592 1 6
HELIX 35 35 ALA C 593 ASN C 595 5 3
HELIX 36 36 THR C 600 LYS C 615 1 16
HELIX 37 37 SER C 630 GLY C 641 1 12
HELIX 38 38 ARG C 658 TYR C 662 5 5
HELIX 39 39 ASP C 663 GLY C 672 1 10
HELIX 40 40 ASN C 679 SER C 686 1 8
HELIX 41 41 VAL C 688 VAL C 698 5 11
HELIX 42 42 HIS C 712 GLY C 727 1 16
HELIX 43 43 SER C 744 PHE C 763 1 20
HELIX 44 44 PHE D 19 LEU D 23 5 5
HELIX 45 45 GLN D 29 PHE D 33 5 5
HELIX 46 46 ASN D 44 LEU D 51 1 8
HELIX 47 47 SER D 63 ALA D 68 1 6
HELIX 48 48 PRO D 83 ARG D 91 5 9
HELIX 49 49 GLY D 96 ASN D 102 1 7
HELIX 50 50 CYS D 160 SER D 164 5 5
HELIX 51 51 THR D 180 GLY D 184 5 5
SHEET 1 A 2 LYS A 41 THR A 42 0
SHEET 2 A 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 B 4 ARG A 61 TRP A 62 0
SHEET 2 B 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 B 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 B 4 SER A 86 LEU A 90 -1 O LEU A 90 N ILE A 76
SHEET 1 C 4 ASP A 104 ILE A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 C 4 TYR A 128 ASP A 136 -1 O ASP A 133 N LEU A 116
SHEET 4 C 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 D 4 TRP A 154 TRP A 157 0
SHEET 2 D 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 D 4 ASP A 171 LYS A 175 -1 O TYR A 173 N TYR A 166
SHEET 4 D 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 E 3 ILE A 194 ASN A 196 0
SHEET 2 E 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 F 4 ILE A 194 ASN A 196 0
SHEET 2 F 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 F 4 THR A 265 ASN A 272 -1 O LYS A 267 N GLN A 227
SHEET 4 F 4 SER A 284 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 G 2 LEU A 235 PHE A 240 0
SHEET 2 G 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 H 4 HIS A 298 THR A 307 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 H 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 H 4 ARG A 336 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 I 4 HIS A 298 THR A 307 0
SHEET 2 I 4 ARG A 310 ARG A 317 -1 O ARG A 310 N ALA A 306
SHEET 3 I 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 I 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 J 4 HIS A 363 PHE A 364 0
SHEET 2 J 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 J 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 J 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 K 4 VAL A 404 LEU A 410 0
SHEET 2 K 4 TYR A 414 SER A 419 -1 O TYR A 416 N GLU A 408
SHEET 3 K 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 K 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 L 4 TYR A 457 PHE A 461 0
SHEET 2 L 4 TYR A 467 CYS A 472 -1 O GLN A 469 N SER A 460
SHEET 3 L 4 LEU A 479 SER A 484 -1 O THR A 481 N LEU A 470
SHEET 4 L 4 LYS A 489 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 M 8 SER A 511 ILE A 518 0
SHEET 2 M 8 LYS A 523 LEU A 530 -1 O LEU A 530 N SER A 511
SHEET 3 M 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 M 8 TYR A 540 VAL A 546 1 N ASP A 545 O ALA A 576
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ASP A 620 N TYR A 540
SHEET 6 M 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 M 8 GLU A 699 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 M 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 N 5 LYS B 34 PHE B 38 0
SHEET 2 N 5 THR B 74 ALA B 81 -1 O VAL B 77 N LEU B 36
SHEET 3 N 5 GLN B 202 GLN B 210 -1 O SER B 208 N THR B 76
SHEET 4 N 5 THR B 111 VAL B 118 -1 N ALA B 116 O MET B 203
SHEET 5 N 5 PHE B 52 ASN B 60 -1 N ASP B 55 O MET B 115
SHEET 1 O 4 VAL B 146 PRO B 149 0
SHEET 2 O 4 ALA B 129 THR B 140 -1 N THR B 140 O VAL B 146
SHEET 3 O 4 LEU B 187 PRO B 196 -1 O THR B 193 N TYR B 132
SHEET 4 O 4 GLN B 173 THR B 178 -1 N ARG B 177 O LEU B 188
SHEET 1 P 2 LYS C 41 THR C 42 0
SHEET 2 P 2 VAL C 507 GLN C 508 1 O GLN C 508 N LYS C 41
SHEET 1 Q 4 ARG C 61 TRP C 62 0
SHEET 2 Q 4 GLU C 67 LYS C 71 -1 O LEU C 69 N ARG C 61
SHEET 3 Q 4 ASN C 75 ASN C 80 -1 O PHE C 79 N TYR C 68
SHEET 4 Q 4 SER C 86 GLU C 91 -1 O SER C 87 N VAL C 78
SHEET 1 R 4 ASP C 104 ILE C 107 0
SHEET 2 R 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 R 4 TYR C 128 ASP C 136 -1 O SER C 131 N TYR C 118
SHEET 4 R 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 S 4 TRP C 154 TRP C 157 0
SHEET 2 S 4 LEU C 164 TRP C 168 -1 O VAL C 167 N TRP C 154
SHEET 3 S 4 ASP C 171 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 S 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 T 3 ILE C 194 ASN C 196 0
SHEET 2 T 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 T 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 U 4 ILE C 194 ASN C 196 0
SHEET 2 U 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 U 4 THR C 265 ASN C 272 -1 O LYS C 267 N GLN C 227
SHEET 4 U 4 SER C 284 GLN C 286 -1 O ILE C 285 N VAL C 270
SHEET 1 V 2 LEU C 235 PHE C 240 0
SHEET 2 V 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 W 4 HIS C 298 TRP C 305 0
SHEET 2 W 4 ARG C 310 ARG C 317 -1 O LEU C 316 N TYR C 299
SHEET 3 W 4 TYR C 322 ASP C 331 -1 O ASP C 326 N LEU C 313
SHEET 4 W 4 ARG C 336 CYS C 339 -1 O ASN C 338 N ASP C 329
SHEET 1 X 4 HIS C 298 TRP C 305 0
SHEET 2 X 4 ARG C 310 ARG C 317 -1 O LEU C 316 N TYR C 299
SHEET 3 X 4 TYR C 322 ASP C 331 -1 O ASP C 326 N LEU C 313
SHEET 4 X 4 HIS C 345 MET C 348 -1 O GLU C 347 N SER C 323
SHEET 1 Y 4 HIS C 363 PHE C 364 0
SHEET 2 Y 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 Y 4 ARG C 382 GLN C 388 -1 O PHE C 387 N PHE C 371
SHEET 4 Y 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 Z 4 VAL C 404 LEU C 410 0
SHEET 2 Z 4 TYR C 414 SER C 419 -1 O TYR C 416 N ALA C 409
SHEET 3 Z 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 Z 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AA 4 TYR C 457 PHE C 461 0
SHEET 2 AA 4 TYR C 467 CYS C 472 -1 O ARG C 471 N SER C 458
SHEET 3 AA 4 LEU C 479 SER C 484 -1 O LEU C 479 N CYS C 472
SHEET 4 AA 4 LYS C 489 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AB 8 SER C 511 ILE C 518 0
SHEET 2 AB 8 LYS C 523 LEU C 530 -1 O LEU C 530 N SER C 511
SHEET 3 AB 8 ILE C 574 ASP C 579 -1 O ASP C 579 N TRP C 525
SHEET 4 AB 8 TYR C 540 VAL C 546 1 N ASP C 545 O ALA C 576
SHEET 5 AB 8 VAL C 619 TRP C 629 1 O ALA C 625 N LEU C 544
SHEET 6 AB 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AB 8 GLU C 699 GLY C 705 1 O LEU C 701 N ALA C 652
SHEET 8 AB 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AC 5 LYS D 34 PHE D 38 0
SHEET 2 AC 5 LEU D 75 ALA D 81 -1 O LEU D 75 N PHE D 38
SHEET 3 AC 5 GLN D 202 VAL D 209 -1 O SER D 208 N THR D 76
SHEET 4 AC 5 THR D 111 VAL D 118 -1 N CYS D 112 O ILE D 207
SHEET 5 AC 5 PHE D 52 ASN D 60 -1 N ASP D 55 O MET D 115
SHEET 1 AD 2 CYS D 41 TYR D 43 0
SHEET 2 AD 2 VAL D 218 PRO D 220 1 O CYS D 219 N TYR D 43
SHEET 1 AE 4 VAL D 146 PRO D 149 0
SHEET 2 AE 4 ALA D 129 THR D 140 -1 N ARG D 138 O THR D 148
SHEET 3 AE 4 LEU D 187 PRO D 196 -1 O ILE D 189 N SER D 137
SHEET 4 AE 4 GLN D 173 THR D 178 -1 N ARG D 177 O LEU D 188
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.04
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.04
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.07
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.04
SSBOND 6 CYS B 17 CYS B 41 1555 1555 2.03
SSBOND 7 CYS B 59 CYS B 112 1555 1555 2.04
SSBOND 8 CYS B 71 CYS B 219 1555 1555 1.99
SSBOND 9 CYS B 136 CYS B 160 1555 1555 2.05
SSBOND 10 CYS C 328 CYS C 339 1555 1555 2.03
SSBOND 11 CYS C 385 CYS C 394 1555 1555 2.04
SSBOND 12 CYS C 444 CYS C 447 1555 1555 2.03
SSBOND 13 CYS C 454 CYS C 472 1555 1555 2.06
SSBOND 14 CYS C 649 CYS C 762 1555 1555 2.05
SSBOND 15 CYS D 17 CYS D 41 1555 1555 2.03
SSBOND 16 CYS D 71 CYS D 219 1555 1555 2.04
SSBOND 17 CYS D 136 CYS D 160 1555 1555 2.05
LINK O4 NAG C 805 C1 NAG C 806 1555 1555 1.42
LINK ND2 ASN C 229 C1 NAG C 805 1555 1555 1.42
LINK ND2 ASN A 321 C1 NAG A 810 1555 1555 1.43
LINK O4 NAG A 810 C1 NAG A 811 1555 1555 1.43
LINK ND2 ASN A 229 C1 NAG A 805 1555 1555 1.43
LINK ND2 ASN C 321 C1 NAG C 810 1555 1555 1.43
LINK O4 NAG C 810 C1 NAG C 811 1555 1555 1.44
LINK ND2 ASN A 281 C1 NAG A 808 1555 1555 1.44
LINK ND2 ASN A 92 C1 NAG A 812 1555 1555 1.44
LINK O4 NAG A 805 C1 NAG A 806 1555 1555 1.44
LINK O4 NAG A 808 C1 NAG A 809 1555 1555 1.44
LINK O4 NAG C 808 C1 NAG C 809 1555 1555 1.44
LINK ND2 ASN A 85 C1 NAG A 801 1555 1555 1.44
LINK ND2 ASN C 150 C1 NAG C 803 1555 1555 1.44
LINK ND2 ASN C 281 C1 NAG C 808 1555 1555 1.44
LINK ND2 ASN C 85 C1 NAG C 801 1555 1555 1.44
LINK ND2 ASN C 219 C1 NAG C 804 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG A 803 1555 1555 1.45
LINK O4 NAG C 806 C1 BMA C 807 1555 1555 1.45
LINK O4 NAG A 806 C1 BMA A 807 1555 1555 1.45
LINK ND2 ASN A 219 C1 NAG A 804 1555 1555 1.45
LINK O4 NAG C 801 C1 NAG C 802 1555 1555 1.45
LINK O4 NAG A 801 C1 NAG A 802 1555 1555 1.46
CISPEP 1 GLY A 474 PRO A 475 0 5.89
CISPEP 2 ALA B 95 GLY B 96 0 -6.36
CISPEP 3 GLY C 474 PRO C 475 0 8.43
CISPEP 4 ALA D 95 GLY D 96 0 1.64
SITE 1 AC1 7 GLU A 67 VAL A 78 ASN A 85 SER A 86
SITE 2 AC1 7 SER A 87 HOH A 905 HOH A1031
SITE 1 AC2 3 ASN A 74 ASN A 75 ASN A 92
SITE 1 AC3 2 ASN A 150 HOH A 926
SITE 1 AC4 5 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 2 AC4 5 HOH A 915
SITE 1 AC5 10 GLN A 227 ASN A 229 THR A 231 GLU A 232
SITE 2 AC5 10 LYS A 267 HOH A1061 HOH A1095 SER B 169
SITE 3 AC5 10 GLU B 170 GLN B 173
SITE 1 AC6 6 TRP A 187 VAL A 279 ASN A 281 HOH A 909
SITE 2 AC6 6 HOH A 935 HOH A 963
SITE 1 AC7 6 ASN A 321 MET A 348 SER A 349 ARG A 596
SITE 2 AC7 6 HOH A 965 HOH A1090
SITE 1 AC8 4 ASN C 85 SER C 87 HOH C1026 HOH C1123
SITE 1 AC9 2 ASN C 150 HOH C1022
SITE 1 BC1 5 ASN C 219 THR C 221 GLN C 308 GLU C 309
SITE 2 BC1 5 HOH C1023
SITE 1 BC2 10 ILE C 194 GLN C 227 ASN C 229 THR C 231
SITE 2 BC2 10 GLU C 232 LYS C 267 HOH C1130 SER D 169
SITE 3 BC2 10 GLU D 170 GLN D 173
SITE 1 BC3 5 TRP C 187 VAL C 279 ASN C 281 HOH C 932
SITE 2 BC3 5 HOH C 976
SITE 1 BC4 3 ASN C 321 MET C 348 SER C 349
CRYST1 78.801 203.166 207.753 90.00 90.00 90.00 P 2 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 0.012690 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004922 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004813 0.00000
TER 5958 PRO A 766
TER 7556 LEU B 222
TER 13514 PRO C 766
TER 15112 LEU D 222
MASTER 547 0 23 51 122 0 23 615900 4 363 152
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