HEADER TRANSFERASE/IMMUNE SYSTEM 16-MAY-13 4KRO
TITLE NANOBODY/VHH DOMAIN EGA1 IN COMPLEX WITH THE EXTRACELLULAR REGION OF
TITLE 2 EGFR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRACELLULAR REGION (UNP RESIDUES 25-642);
COMPND 5 SYNONYM: PROTO-ONCOGENE C-ERBB-1, RECEPTOR TYROSINE-PROTEIN KINASE
COMPND 6 ERBB-1;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: NANOBODY/VHH DOMAIN EGA1;
COMPND 11 CHAIN: B;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: CETUXIMAB LIGHT CHAIN;
COMPND 15 CHAIN: C;
COMPND 16 FRAGMENT: FAB;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: CETUXIMAB HEAVY CHAIN;
COMPND 20 CHAIN: D;
COMPND 21 FRAGMENT: FAB;
COMPND 22 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: EGFR, ERBB, ERBB1, HER1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: LAMA GLAMA;
SOURCE 14 ORGANISM_COMMON: LLAMA;
SOURCE 15 ORGANISM_TAXID: 9844;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PET22B;
SOURCE 20 MOL_ID: 3;
SOURCE 21 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;
SOURCE 22 ORGANISM_COMMON: MOUSE, HUMAN;
SOURCE 23 ORGANISM_TAXID: 10090, 9606;
SOURCE 24 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 25 EXPRESSION_SYSTEM_COMMON: MOUSE;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 27 EXPRESSION_SYSTEM_STRAIN: SP2/0-AG15;
SOURCE 28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 29 EXPRESSION_SYSTEM_PLASMID: PDHL2;
SOURCE 30 MOL_ID: 4;
SOURCE 31 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;
SOURCE 32 ORGANISM_COMMON: MOUSE, HUMAN;
SOURCE 33 ORGANISM_TAXID: 10090, 9606;
SOURCE 34 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 35 EXPRESSION_SYSTEM_COMMON: MOUSE;
SOURCE 36 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 37 EXPRESSION_SYSTEM_STRAIN: SP2/0-AG15;
SOURCE 38 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 39 EXPRESSION_SYSTEM_PLASMID: PDHL2
KEYWDS CELL SURFACE RECEPTOR, GLYCOPROTEIN, NANOBODY, VHH DOMAIN, CAMELID VH
KEYWDS 2 DOMAIN, ANTIBODY, ANTIGEN, ANTIBODY COMPLEX, TRANSFERASE-IMMUNE
KEYWDS 3 SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.FERGUSON,K.R.SCHMITZ
REVDAT 3 20-SEP-23 4KRO 1 HETSYN
REVDAT 2 29-JUL-20 4KRO 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 2 1 LINK SITE ATOM
REVDAT 1 28-AUG-13 4KRO 0
JRNL AUTH K.R.SCHMITZ,A.BAGCHI,R.C.ROOVERS,
JRNL AUTH 2 P.M.VAN BERGEN EN HENEGOUWEN,K.M.FERGUSON
JRNL TITL STRUCTURAL EVALUATION OF EGFR INHIBITION MECHANISMS FOR
JRNL TITL 2 NANOBODIES/VHH DOMAINS.
JRNL REF STRUCTURE V. 21 1214 2013
JRNL REFN ISSN 0969-2126
JRNL PMID 23791944
JRNL DOI 10.1016/J.STR.2013.05.008
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 29786
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1507
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 38.1963 - 6.7795 0.95 2529 143 0.2231 0.2795
REMARK 3 2 6.7795 - 5.3859 0.98 2573 152 0.2245 0.2617
REMARK 3 3 5.3859 - 4.7065 0.99 2556 143 0.1817 0.2375
REMARK 3 4 4.7065 - 4.2768 0.99 2591 130 0.1726 0.2309
REMARK 3 5 4.2768 - 3.9706 0.99 2586 148 0.1985 0.2495
REMARK 3 6 3.9706 - 3.7367 0.99 2566 140 0.2122 0.3036
REMARK 3 7 3.7367 - 3.5497 0.99 2581 133 0.2207 0.2880
REMARK 3 8 3.5497 - 3.3953 0.99 2607 125 0.2367 0.3063
REMARK 3 9 3.3953 - 3.2647 1.00 2580 134 0.2664 0.3475
REMARK 3 10 3.2647 - 3.1521 1.00 2556 127 0.2856 0.3276
REMARK 3 11 3.1521 - 3.0540 0.97 2554 132 0.3131 0.3903
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) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.700
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.93
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 : 0.005 8141
REMARK 3 ANGLE : 0.897 11168
REMARK 3 CHIRALITY : 0.033 1310
REMARK 3 PLANARITY : 0.004 1447
REMARK 3 DIHEDRAL : 13.990 2705
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4KRO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079709.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : SINGLE-CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29807
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.46300
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: PDB ENTRY 1YY9 AND 4KRN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17.5% PEG3350, 1.5 M SODIUM CHLORIDE,
REMARK 280 5% GLYCEROL, 0.1 M MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 48.14400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, 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 LEU A 1
REMARK 465 GLU A 2
REMARK 465 GLU A 3
REMARK 465 TYR A 101
REMARK 465 ASP A 102
REMARK 465 ALA A 103
REMARK 465 ASN A 104
REMARK 465 LYS A 105
REMARK 465 THR A 106
REMARK 465 GLY A 107
REMARK 465 GLN A 184
REMARK 465 LYS A 185
REMARK 465 LEU A 186
REMARK 465 THR A 187
REMARK 465 LYS A 188
REMARK 465 ILE A 189
REMARK 465 ILE A 190
REMARK 465 CYS A 191
REMARK 465 ALA A 192
REMARK 465 GLN A 193
REMARK 465 GLN A 194
REMARK 465 CYS A 195
REMARK 465 SER A 196
REMARK 465 GLY A 197
REMARK 465 ARG A 198
REMARK 465 CYS A 199
REMARK 465 ARG A 200
REMARK 465 GLY A 201
REMARK 465 LYS A 202
REMARK 465 SER A 203
REMARK 465 PRO A 204
REMARK 465 SER A 205
REMARK 465 ASP A 206
REMARK 465 CYS A 207
REMARK 465 THR A 605
REMARK 465 GLY A 606
REMARK 465 PRO A 607
REMARK 465 GLY A 608
REMARK 465 LEU A 609
REMARK 465 GLU A 610
REMARK 465 GLY A 611
REMARK 465 CYS A 612
REMARK 465 PRO A 613
REMARK 465 THR A 614
REMARK 465 ASN A 615
REMARK 465 GLY A 616
REMARK 465 PRO A 617
REMARK 465 LYS A 618
REMARK 465 HIS A 619
REMARK 465 HIS A 620
REMARK 465 HIS A 621
REMARK 465 HIS A 622
REMARK 465 HIS A 623
REMARK 465 HIS A 624
REMARK 465 GLY B 8
REMARK 465 GLY B 9
REMARK 465 GLY B 10
REMARK 465 LEU B 11
REMARK 465 VAL B 12
REMARK 465 GLN B 13
REMARK 465 PRO B 14
REMARK 465 GLY B 15
REMARK 465 GLY B 16
REMARK 465 SER B 17
REMARK 465 LEU B 18
REMARK 465 ARG B 19
REMARK 465 SER B 129
REMARK 465 SER B 130
REMARK 465 LEU B 131
REMARK 465 GLU B 132
REMARK 465 HIS B 133
REMARK 465 HIS B 134
REMARK 465 HIS B 135
REMARK 465 HIS B 136
REMARK 465 HIS B 137
REMARK 465 HIS B 138
REMARK 465 SER D 136
REMARK 465 THR D 137
REMARK 465 SER D 138
REMARK 465 GLY D 139
REMARK 465 GLY D 140
REMARK 465 PRO D 219
REMARK 465 LYS D 220
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 LYS A 4 CG CD CE NZ
REMARK 470 LYS A 5 CG CD CE NZ
REMARK 470 GLN A 8 CG CD OE1 NE2
REMARK 470 LYS A 13 CG CD CE NZ
REMARK 470 LEU A 14 CG CD1 CD2
REMARK 470 GLN A 16 CG CD OE1 NE2
REMARK 470 LEU A 17 CG CD1 CD2
REMARK 470 PHE A 20 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 21 CG CD OE1 OE2
REMARK 470 ASP A 22 CG OD1 OD2
REMARK 470 LEU A 25 CG CD1 CD2
REMARK 470 GLN A 28 CG CD OE1 NE2
REMARK 470 ARG A 29 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 33 CG OD1 ND2
REMARK 470 ASN A 40 CG OD1 ND2
REMARK 470 GLU A 42 CG CD OE1 OE2
REMARK 470 TYR A 45 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 47 CG CD OE1 NE2
REMARK 470 ARG A 48 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 49 CG OD1 ND2
REMARK 470 TYR A 50 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 51 CG OD1 OD2
REMARK 470 LEU A 52 CG CD1 CD2
REMARK 470 LEU A 55 CG CD1 CD2
REMARK 470 LYS A 56 CG CD CE NZ
REMARK 470 LEU A 66 CG CD1 CD2
REMARK 470 ILE A 67 CG1 CG2 CD1
REMARK 470 LEU A 69 CG CD1 CD2
REMARK 470 VAL A 72 CG1 CG2
REMARK 470 GLU A 73 CG CD OE1 OE2
REMARK 470 ARG A 74 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 78 CG CD OE1 OE2
REMARK 470 ASN A 79 CG OD1 ND2
REMARK 470 ARG A 84 CG CD NE CZ NH1 NH2
REMARK 470 MET A 87 CG SD CE
REMARK 470 GLU A 90 CG CD OE1 OE2
REMARK 470 ASN A 91 CG OD1 ND2
REMARK 470 LEU A 108 CG CD1 CD2
REMARK 470 LYS A 109 CG CD CE NZ
REMARK 470 GLU A 110 CG CD OE1 OE2
REMARK 470 ARG A 114 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 117 CG CD OE1 NE2
REMARK 470 GLU A 118 CG CD OE1 OE2
REMARK 470 LEU A 120 CG CD1 CD2
REMARK 470 HIS A 121 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 125 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 128 CG OD1 ND2
REMARK 470 GLU A 136 CG CD OE1 OE2
REMARK 470 SER A 137 OG
REMARK 470 GLN A 139 CG CD OE1 NE2
REMARK 470 ARG A 141 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 142 CG OD1 OD2
REMARK 470 SER A 145 OG
REMARK 470 SER A 146 OG
REMARK 470 ASP A 147 CG OD1 OD2
REMARK 470 PHE A 148 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 149 CG CD1 CD2
REMARK 470 SER A 150 OG
REMARK 470 ASN A 151 CG OD1 ND2
REMARK 470 MET A 152 CG SD CE
REMARK 470 MET A 154 CG SD CE
REMARK 470 ASP A 155 CG OD1 OD2
REMARK 470 PHE A 156 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 157 CG CD OE1 NE2
REMARK 470 ASN A 158 CB CG OD1 ND2
REMARK 470 HIS A 159 CB CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 160 CG CD1 CD2
REMARK 470 SER A 162 OG
REMARK 470 GLN A 164 CG CD OE1 NE2
REMARK 470 LYS A 165 CG CD CE NZ
REMARK 470 ASP A 167 CG OD1 OD2
REMARK 470 ASN A 172 CG OD1 ND2
REMARK 470 GLU A 180 CG CD OE1 OE2
REMARK 470 GLU A 181 CG CD OE1 OE2
REMARK 470 ASN A 182 CG OD1 ND2
REMARK 470 HIS A 209 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 210 CG OD1 ND2
REMARK 470 GLN A 211 CG CD OE1 NE2
REMARK 470 ARG A 220 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 225 CG CD1 CD2
REMARK 470 VAL A 226 CG1 CG2
REMARK 470 ARG A 228 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 229 CG CD CE NZ
REMARK 470 GLU A 233 CG CD OE1 OE2
REMARK 470 LYS A 237 CG CD CE NZ
REMARK 470 ASP A 238 CG OD1 OD2
REMARK 470 LEU A 243 CG CD1 CD2
REMARK 470 TYR A 246 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR A 249 OG1 CG2
REMARK 470 THR A 250 OG1 CG2
REMARK 470 GLN A 252 CG CD OE1 NE2
REMARK 470 ASP A 254 CG OD1 OD2
REMARK 470 ASN A 256 CG OD1 ND2
REMARK 470 GLU A 258 CG CD OE1 OE2
REMARK 470 LYS A 260 CG CD CE NZ
REMARK 470 VAL A 268 CG1 CG2
REMARK 470 LYS A 269 CG CD CE NZ
REMARK 470 LYS A 270 CG CD CE NZ
REMARK 470 ASP A 279 CG OD1 OD2
REMARK 470 ARG A 285 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 290 CG OD1 OD2
REMARK 470 GLU A 293 CG CD OE1 OE2
REMARK 470 MET A 294 CG SD CE
REMARK 470 VAL A 299 CG1 CG2
REMARK 470 ARG A 300 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 301 CG CD CE NZ
REMARK 470 LYS A 303 CG CD CE NZ
REMARK 470 LYS A 304 CG CD CE NZ
REMARK 470 GLU A 306 CG CD OE1 OE2
REMARK 470 GLU A 320 CG CD OE1 OE2
REMARK 470 LYS A 322 CG CD CE NZ
REMARK 470 LYS A 333 CG CD CE NZ
REMARK 470 PHE A 357 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS A 359 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 366 CG CD OE1 NE2
REMARK 470 GLU A 367 CG CD OE1 OE2
REMARK 470 LYS A 372 CG CD CE NZ
REMARK 470 ARG A 390 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 430 CG CD CE NZ
REMARK 470 LYS A 455 CG CD CE NZ
REMARK 470 SER A 474 OG
REMARK 470 GLU A 495 CG CD OE1 OE2
REMARK 470 ARG A 509 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 514 CG CD CE NZ
REMARK 470 GLU A 519 CG CD OE1 OE2
REMARK 470 GLU A 521 CG CD OE1 OE2
REMARK 470 GLU A 527 CG CD OE1 OE2
REMARK 470 SER A 529 OG
REMARK 470 GLU A 537 CG CD OE1 OE2
REMARK 470 LEU A 539 CG CD1 CD2
REMARK 470 ASN A 544 CG OD1 ND2
REMARK 470 GLN A 557 CG CD OE1 NE2
REMARK 470 HIS A 560 CG ND1 CD2 CE1 NE2
REMARK 470 TYR A 561 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A 562 CG1 CG2 CD1
REMARK 470 ASP A 563 CG OD1 OD2
REMARK 470 LYS A 569 CG CD CE NZ
REMARK 470 THR A 570 OG1 CG2
REMARK 470 MET A 576 CG SD CE
REMARK 470 THR A 581 OG1 CG2
REMARK 470 LEU A 582 CG CD1 CD2
REMARK 470 TRP A 584 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 584 CZ3 CH2
REMARK 470 LYS A 585 CG CD CE NZ
REMARK 470 TYR A 586 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS A 597 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 599 CG OD1 ND2
REMARK 470 THR A 601 OG1 CG2
REMARK 470 TYR A 602 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 1 CG CD OE1 NE2
REMARK 470 SER B 7 OG
REMARK 470 ARG B 38 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 43 CG CD CE NZ
REMARK 470 GLN B 44 CG CD OE1 NE2
REMARK 470 GLU B 46 CG CD OE1 OE2
REMARK 470 VAL B 64 CG1 CG2
REMARK 470 LYS B 65 CG CD CE NZ
REMARK 470 ARG B 67 CG CD NE CZ NH1 NH2
REMARK 470 THR B 69 OG1 CG2
REMARK 470 ILE B 70 CG1 CG2 CD1
REMARK 470 SER B 71 OG
REMARK 470 ARG B 72 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 73 CG OD1 OD2
REMARK 470 ASN B 74 CG OD1 ND2
REMARK 470 LYS B 76 CG CD CE NZ
REMARK 470 THR B 77 OG1 CG2
REMARK 470 GLN B 82 CG CD OE1 NE2
REMARK 470 MET B 83 CG SD CE
REMARK 470 ASN B 84 CG OD1 ND2
REMARK 470 LEU B 86 CG CD1 CD2
REMARK 470 LYS B 87 CG CD CE NZ
REMARK 470 GLU B 89 CG CD OE1 OE2
REMARK 470 ASP B 90 CG OD1 OD2
REMARK 470 THR B 91 OG1 CG2
REMARK 470 TYR B 94 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL B 126 CG1 CG2
REMARK 470 VAL B 128 CG1 CG2
REMARK 470 ARG C 24 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 123 CG CD OE1 OE2
REMARK 470 LYS C 126 CG CD CE NZ
REMARK 470 GLU C 143 CG CD OE1 OE2
REMARK 470 LYS C 145 CG CD CE NZ
REMARK 470 LYS C 149 CG CD CE NZ
REMARK 470 ASN C 152 CG OD1 ND2
REMARK 470 LYS C 169 CG CD CE NZ
REMARK 470 LYS C 188 CG CD CE NZ
REMARK 470 LYS C 190 CG CD CE NZ
REMARK 470 GLU C 195 CG CD OE1 OE2
REMARK 470 GLN C 199 CG CD OE1 NE2
REMARK 470 LYS D 5 CG CD CE NZ
REMARK 470 LYS D 43 CG CD CE NZ
REMARK 470 LYS D 75 CG CD CE NZ
REMARK 470 LYS D 135 CG CD CE NZ
REMARK 470 LYS D 207 CG CD CE NZ
REMARK 470 LYS D 212 CG CD CE NZ
REMARK 470 LYS D 215 CG CD CE NZ
REMARK 470 ARG D 216 CG CD NE CZ NH1 NH2
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 HD21 ASN A 389 C1 NAG A 704 1.32
REMARK 500 ND2 ASN D 88 O5 NAG D 301 1.72
REMARK 500 ND2 ASN A 337 C2 NAG A 703 2.09
REMARK 500 O LEU A 518 NH2 ARG A 523 2.18
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 LYS A 13 -132.92 57.90
REMARK 500 GLN A 47 -178.90 -69.54
REMARK 500 ASP A 51 98.00 -65.17
REMARK 500 ASN A 91 -105.60 52.28
REMARK 500 SER A 92 46.64 -145.16
REMARK 500 LEU A 116 94.27 -68.06
REMARK 500 ALA A 123 -168.99 -105.76
REMARK 500 ASN A 134 -36.15 69.55
REMARK 500 HIS A 159 -73.03 -60.11
REMARK 500 HIS A 209 -106.16 70.88
REMARK 500 ALA A 213 39.84 -166.43
REMARK 500 ALA A 214 51.01 -161.52
REMARK 500 ARG A 220 -173.70 -171.35
REMARK 500 ARG A 228 -84.68 -91.03
REMARK 500 ASP A 232 104.45 -163.84
REMARK 500 ALA A 234 -30.91 70.03
REMARK 500 THR A 250 -7.02 -151.56
REMARK 500 GLU A 258 42.41 -91.56
REMARK 500 TYR A 261 -167.12 -78.35
REMARK 500 PRO A 272 -177.42 -66.35
REMARK 500 ASN A 274 -16.95 64.81
REMARK 500 THR A 278 -169.67 -78.62
REMARK 500 HIS A 280 30.24 -155.46
REMARK 500 ALA A 286 158.47 63.25
REMARK 500 MET A 294 -163.81 -116.65
REMARK 500 GLU A 295 81.14 -161.61
REMARK 500 ASP A 297 -111.93 59.14
REMARK 500 TRP A 386 144.95 -173.36
REMARK 500 GLN A 411 -52.35 -128.13
REMARK 500 TYR A 447 -137.10 65.69
REMARK 500 ALA A 448 -64.58 68.39
REMARK 500 ASN A 469 -162.66 -117.75
REMARK 500 ASN A 504 -77.97 -102.48
REMARK 500 LEU A 518 -56.72 76.32
REMARK 500 ASN A 528 60.30 60.83
REMARK 500 PRO A 540 178.20 -58.27
REMARK 500 HIS A 560 -94.55 -128.93
REMARK 500 CYS A 567 89.59 -63.74
REMARK 500 ASN A 580 70.97 48.15
REMARK 500 LEU A 582 104.35 -58.22
REMARK 500 ALA A 587 -156.10 -76.82
REMARK 500 CYS B 22 86.58 -159.22
REMARK 500 THR B 28 105.09 -59.29
REMARK 500 PHE B 29 43.15 -82.71
REMARK 500 VAL B 48 -66.81 -137.26
REMARK 500 THR B 61 -168.47 -79.62
REMARK 500 ALA B 75 168.29 68.42
REMARK 500 THR B 77 126.54 -172.75
REMARK 500 PRO B 88 33.54 -72.12
REMARK 500 ASP B 90 37.78 -84.05
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KRL RELATED DB: PDB
REMARK 900 RELATED ID: 4KRM RELATED DB: PDB
REMARK 900 RELATED ID: 4KRN RELATED DB: PDB
REMARK 900 RELATED ID: 4KRP RELATED DB: PDB
DBREF 4KRO A 1 618 UNP P00533 EGFR_HUMAN 25 642
DBREF 4KRO B 1 138 PDB 4KRO 4KRO 1 138
DBREF 4KRO C 1 211 PDB 4KRO 4KRO 1 211
DBREF 4KRO D 1 220 PDB 4KRO 4KRO 1 220
SEQADV 4KRO HIS A 619 UNP P00533 EXPRESSION TAG
SEQADV 4KRO HIS A 620 UNP P00533 EXPRESSION TAG
SEQADV 4KRO HIS A 621 UNP P00533 EXPRESSION TAG
SEQADV 4KRO HIS A 622 UNP P00533 EXPRESSION TAG
SEQADV 4KRO HIS A 623 UNP P00533 EXPRESSION TAG
SEQADV 4KRO HIS A 624 UNP P00533 EXPRESSION TAG
SEQRES 1 A 624 LEU GLU GLU LYS LYS VAL CYS GLN GLY THR SER ASN LYS
SEQRES 2 A 624 LEU THR GLN LEU GLY THR PHE GLU ASP HIS PHE LEU SER
SEQRES 3 A 624 LEU GLN ARG MET PHE ASN ASN CYS GLU VAL VAL LEU GLY
SEQRES 4 A 624 ASN LEU GLU ILE THR TYR VAL GLN ARG ASN TYR ASP LEU
SEQRES 5 A 624 SER PHE LEU LYS THR ILE GLN GLU VAL ALA GLY TYR VAL
SEQRES 6 A 624 LEU ILE ALA LEU ASN THR VAL GLU ARG ILE PRO LEU GLU
SEQRES 7 A 624 ASN LEU GLN ILE ILE ARG GLY ASN MET TYR TYR GLU ASN
SEQRES 8 A 624 SER TYR ALA LEU ALA VAL LEU SER ASN TYR ASP ALA ASN
SEQRES 9 A 624 LYS THR GLY LEU LYS GLU LEU PRO MET ARG ASN LEU GLN
SEQRES 10 A 624 GLU ILE LEU HIS GLY ALA VAL ARG PHE SER ASN ASN PRO
SEQRES 11 A 624 ALA LEU CYS ASN VAL GLU SER ILE GLN TRP ARG ASP ILE
SEQRES 12 A 624 VAL SER SER ASP PHE LEU SER ASN MET SER MET ASP PHE
SEQRES 13 A 624 GLN ASN HIS LEU GLY SER CYS GLN LYS CYS ASP PRO SER
SEQRES 14 A 624 CYS PRO ASN GLY SER CYS TRP GLY ALA GLY GLU GLU ASN
SEQRES 15 A 624 CYS GLN LYS LEU THR LYS ILE ILE CYS ALA GLN GLN CYS
SEQRES 16 A 624 SER GLY ARG CYS ARG GLY LYS SER PRO SER ASP CYS CYS
SEQRES 17 A 624 HIS ASN GLN CYS ALA ALA GLY CYS THR GLY PRO ARG GLU
SEQRES 18 A 624 SER ASP CYS LEU VAL CYS ARG LYS PHE ARG ASP GLU ALA
SEQRES 19 A 624 THR CYS LYS ASP THR CYS PRO PRO LEU MET LEU TYR ASN
SEQRES 20 A 624 PRO THR THR TYR GLN MET ASP VAL ASN PRO GLU GLY LYS
SEQRES 21 A 624 TYR SER PHE GLY ALA THR CYS VAL LYS LYS CYS PRO ARG
SEQRES 22 A 624 ASN TYR VAL VAL THR ASP HIS GLY SER CYS VAL ARG ALA
SEQRES 23 A 624 CYS GLY ALA ASP SER TYR GLU MET GLU GLU ASP GLY VAL
SEQRES 24 A 624 ARG LYS CYS LYS LYS CYS GLU GLY PRO CYS ARG LYS VAL
SEQRES 25 A 624 CYS ASN GLY ILE GLY ILE GLY GLU PHE LYS ASP SER LEU
SEQRES 26 A 624 SER ILE ASN ALA THR ASN ILE LYS HIS PHE LYS ASN CYS
SEQRES 27 A 624 THR SER ILE SER GLY ASP LEU HIS ILE LEU PRO VAL ALA
SEQRES 28 A 624 PHE ARG GLY ASP SER PHE THR HIS THR PRO PRO LEU ASP
SEQRES 29 A 624 PRO GLN GLU LEU ASP ILE LEU LYS THR VAL LYS GLU ILE
SEQRES 30 A 624 THR GLY PHE LEU LEU ILE GLN ALA TRP PRO GLU ASN ARG
SEQRES 31 A 624 THR ASP LEU HIS ALA PHE GLU ASN LEU GLU ILE ILE ARG
SEQRES 32 A 624 GLY ARG THR LYS GLN HIS GLY GLN PHE SER LEU ALA VAL
SEQRES 33 A 624 VAL SER LEU ASN ILE THR SER LEU GLY LEU ARG SER LEU
SEQRES 34 A 624 LYS GLU ILE SER ASP GLY ASP VAL ILE ILE SER GLY ASN
SEQRES 35 A 624 LYS ASN LEU CYS TYR ALA ASN THR ILE ASN TRP LYS LYS
SEQRES 36 A 624 LEU PHE GLY THR SER GLY GLN LYS THR LYS ILE ILE SER
SEQRES 37 A 624 ASN ARG GLY GLU ASN SER CYS LYS ALA THR GLY GLN VAL
SEQRES 38 A 624 CYS HIS ALA LEU CYS SER PRO GLU GLY CYS TRP GLY PRO
SEQRES 39 A 624 GLU PRO ARG ASP CYS VAL SER CYS ARG ASN VAL SER ARG
SEQRES 40 A 624 GLY ARG GLU CYS VAL ASP LYS CYS ASN LEU LEU GLU GLY
SEQRES 41 A 624 GLU PRO ARG GLU PHE VAL GLU ASN SER GLU CYS ILE GLN
SEQRES 42 A 624 CYS HIS PRO GLU CYS LEU PRO GLN ALA MET ASN ILE THR
SEQRES 43 A 624 CYS THR GLY ARG GLY PRO ASP ASN CYS ILE GLN CYS ALA
SEQRES 44 A 624 HIS TYR ILE ASP GLY PRO HIS CYS VAL LYS THR CYS PRO
SEQRES 45 A 624 ALA GLY VAL MET GLY GLU ASN ASN THR LEU VAL TRP LYS
SEQRES 46 A 624 TYR ALA ASP ALA GLY HIS VAL CYS HIS LEU CYS HIS PRO
SEQRES 47 A 624 ASN CYS THR TYR GLY CYS THR GLY PRO GLY LEU GLU GLY
SEQRES 48 A 624 CYS PRO THR ASN GLY PRO LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 138 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 B 138 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 B 138 ARG THR PHE SER SER TYR ALA MET GLY TRP PHE ARG GLN
SEQRES 4 B 138 ALA PRO GLY LYS GLN ARG GLU PHE VAL ALA ALA ILE ARG
SEQRES 5 B 138 TRP SER GLY GLY TYR THR TYR TYR THR ASP SER VAL LYS
SEQRES 6 B 138 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS THR THR
SEQRES 7 B 138 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR
SEQRES 8 B 138 ALA VAL TYR TYR CYS ALA ALA THR TYR LEU SER SER ASP
SEQRES 9 B 138 TYR SER ARG TYR ALA LEU PRO GLN ARG PRO LEU ASP TYR
SEQRES 10 B 138 ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER
SEQRES 11 B 138 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 211 ASP ILE LEU LEU THR GLN SER PRO VAL ILE LEU SER VAL
SEQRES 2 C 211 SER PRO GLY GLU ARG VAL SER PHE SER CYS ARG ALA SER
SEQRES 3 C 211 GLN SER ILE GLY THR ASN ILE HIS TRP TYR GLN GLN ARG
SEQRES 4 C 211 THR ASN GLY SER PRO ARG LEU LEU ILE LYS TYR ALA SER
SEQRES 5 C 211 GLU SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER
SEQRES 6 C 211 GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL
SEQRES 7 C 211 GLU SER GLU ASP ILE ALA ASP TYR TYR CYS GLN GLN ASN
SEQRES 8 C 211 ASN ASN TRP PRO THR THR PHE GLY ALA GLY THR LYS LEU
SEQRES 9 C 211 GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 C 211 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 C 211 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 C 211 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 C 211 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 C 211 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 C 211 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 C 211 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 C 211 PHE ASN ARG
SEQRES 1 D 220 GLN VAL GLN LEU LYS GLN SER GLY PRO GLY LEU VAL GLN
SEQRES 2 D 220 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY
SEQRES 3 D 220 PHE SER LEU THR ASN TYR GLY VAL HIS TRP VAL ARG GLN
SEQRES 4 D 220 SER PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP
SEQRES 5 D 220 SER GLY GLY ASN THR ASP TYR ASN THR PRO PHE THR SER
SEQRES 6 D 220 ARG LEU SER ILE ASN LYS ASP ASN SER LYS SER GLN VAL
SEQRES 7 D 220 PHE PHE LYS MET ASN SER LEU GLN SER ASN ASP THR ALA
SEQRES 8 D 220 ILE TYR TYR CYS ALA ARG ALA LEU THR TYR TYR ASP TYR
SEQRES 9 D 220 GLU PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 D 220 SER ALA ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 D 220 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 D 220 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 D 220 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 D 220 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 D 220 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 D 220 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 D 220 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS
MODRES 4KRO ASN D 88 ASN GLYCOSYLATION SITE
MODRES 4KRO ASN A 420 ASN GLYCOSYLATION SITE
MODRES 4KRO ASN A 328 ASN GLYCOSYLATION SITE
MODRES 4KRO ASN A 337 ASN GLYCOSYLATION SITE
MODRES 4KRO ASN A 389 ASN GLYCOSYLATION SITE
HET NAG E 1 26
HET NAG E 2 27
HET NAG F 1 26
HET NAG F 2 27
HET NAG A 703 27
HET NAG A 704 27
HET NAG D 301 27
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
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 5 NAG 7(C8 H15 N O6)
FORMUL 10 HOH *12(H2 O)
HELIX 1 1 THR A 19 ASN A 32 1 14
HELIX 2 2 LEU A 52 ILE A 58 5 7
HELIX 3 3 ASN A 134 ILE A 138 5 5
HELIX 4 4 GLN A 139 ILE A 143 5 5
HELIX 5 5 PHE A 148 MET A 152 5 5
HELIX 6 6 CYS A 170 SER A 174 5 5
HELIX 7 7 GLY A 179 CYS A 183 5 5
HELIX 8 8 THR A 330 LYS A 336 5 7
HELIX 9 9 LEU A 348 GLY A 354 1 7
HELIX 10 10 ASP A 355 HIS A 359 5 5
HELIX 11 11 ASP A 364 VAL A 374 5 11
HELIX 12 12 LEU A 393 GLU A 397 5 5
HELIX 13 13 LYS A 407 GLY A 410 5 4
HELIX 14 14 ASN A 452 LEU A 456 5 5
HELIX 15 15 GLY A 471 THR A 478 1 8
HELIX 16 16 GLU A 495 CYS A 499 5 5
HELIX 17 17 ARG B 113 TYR B 117 5 5
HELIX 18 18 GLU C 79 ILE C 83 5 5
HELIX 19 19 SER C 121 GLY C 128 1 8
HELIX 20 20 LYS C 183 LYS C 188 1 6
HELIX 21 21 THR D 61 SER D 65 5 5
HELIX 22 22 GLN D 86 THR D 90 5 5
HELIX 23 23 SER D 162 ALA D 164 5 3
HELIX 24 24 PRO D 191 LEU D 195 5 5
HELIX 25 25 LYS D 207 ASN D 210 5 4
SHEET 1 A 5 VAL A 6 CYS A 7 0
SHEET 2 A 5 VAL A 36 VAL A 37 1 O VAL A 36 N CYS A 7
SHEET 3 A 5 GLU A 60 VAL A 61 1 O GLU A 60 N VAL A 37
SHEET 4 A 5 ILE A 82 ILE A 83 1 O ILE A 82 N VAL A 61
SHEET 5 A 5 GLU A 118 ILE A 119 1 O GLU A 118 N ILE A 83
SHEET 1 B 5 LEU A 41 THR A 44 0
SHEET 2 B 5 VAL A 65 ALA A 68 1 O LEU A 66 N LEU A 41
SHEET 3 B 5 TYR A 93 LEU A 98 1 O ALA A 94 N VAL A 65
SHEET 4 B 5 ALA A 123 SER A 127 1 O ARG A 125 N VAL A 97
SHEET 5 B 5 SER A 153 MET A 154 1 O SER A 153 N VAL A 124
SHEET 1 C 2 PHE A 230 ASP A 232 0
SHEET 2 C 2 THR A 235 LYS A 237 -1 O THR A 235 N ASP A 232
SHEET 1 D 2 MET A 244 TYR A 246 0
SHEET 2 D 2 MET A 253 VAL A 255 -1 O ASP A 254 N LEU A 245
SHEET 1 E 3 SER A 262 PHE A 263 0
SHEET 2 E 3 SER A 282 ARG A 285 1 O CYS A 283 N SER A 262
SHEET 3 E 3 TYR A 275 VAL A 277 -1 N VAL A 276 O VAL A 284
SHEET 1 F 2 SER A 291 MET A 294 0
SHEET 2 F 2 LYS A 301 LYS A 304 -1 O LYS A 303 N TYR A 292
SHEET 1 G 5 VAL A 312 ASN A 314 0
SHEET 2 G 5 SER A 340 SER A 342 1 O SER A 342 N CYS A 313
SHEET 3 G 5 GLU A 376 ILE A 377 1 O GLU A 376 N ILE A 341
SHEET 4 G 5 ILE A 401 ILE A 402 1 O ILE A 401 N ILE A 377
SHEET 5 G 5 GLU A 431 ILE A 432 1 O GLU A 431 N ILE A 402
SHEET 1 H 5 LEU A 345 ILE A 347 0
SHEET 2 H 5 LEU A 381 ILE A 383 1 O LEU A 382 N LEU A 345
SHEET 3 H 5 PHE A 412 VAL A 417 1 O SER A 413 N LEU A 381
SHEET 4 H 5 ASP A 436 SER A 440 1 O ILE A 438 N VAL A 416
SHEET 5 H 5 THR A 464 ILE A 467 1 O LYS A 465 N ILE A 439
SHEET 1 I 4 GLU A 510 VAL A 512 0
SHEET 2 I 4 VAL A 505 ARG A 507 -1 N VAL A 505 O VAL A 512
SHEET 3 I 4 GLU A 530 GLN A 533 1 O CYS A 531 N SER A 506
SHEET 4 I 4 GLU A 524 VAL A 526 -1 N PHE A 525 O ILE A 532
SHEET 1 J 2 LYS A 585 TYR A 586 0
SHEET 2 J 2 HIS A 594 LEU A 595 -1 O HIS A 594 N TYR A 586
SHEET 1 K 2 GLN B 3 GLN B 5 0
SHEET 2 K 2 ALA B 23 SER B 25 -1 O SER B 25 N GLN B 3
SHEET 1 L 5 THR B 58 TYR B 60 0
SHEET 2 L 5 ARG B 45 ARG B 52 -1 N ALA B 50 O TYR B 59
SHEET 3 L 5 TYR B 32 GLN B 39 -1 N ARG B 38 O GLU B 46
SHEET 4 L 5 VAL B 93 TYR B 100 -1 O VAL B 93 N GLN B 39
SHEET 5 L 5 TYR B 119 TRP B 120 -1 O TYR B 119 N ALA B 98
SHEET 1 M 4 LEU C 4 SER C 7 0
SHEET 2 M 4 VAL C 19 ALA C 25 -1 O ARG C 24 N THR C 5
SHEET 3 M 4 ASP C 70 ILE C 75 -1 O LEU C 73 N PHE C 21
SHEET 4 M 4 PHE C 62 SER C 67 -1 N SER C 63 O SER C 74
SHEET 1 N 6 ILE C 10 VAL C 13 0
SHEET 2 N 6 THR C 102 LEU C 106 1 O GLU C 105 N VAL C 13
SHEET 3 N 6 ALA C 84 GLN C 90 -1 N ALA C 84 O LEU C 104
SHEET 4 N 6 ILE C 33 GLN C 38 -1 N GLN C 38 O ASP C 85
SHEET 5 N 6 ARG C 45 LYS C 49 -1 O ARG C 45 N GLN C 37
SHEET 6 N 6 GLU C 53 SER C 54 -1 O GLU C 53 N LYS C 49
SHEET 1 O 4 ILE C 10 VAL C 13 0
SHEET 2 O 4 THR C 102 LEU C 106 1 O GLU C 105 N VAL C 13
SHEET 3 O 4 ALA C 84 GLN C 90 -1 N ALA C 84 O LEU C 104
SHEET 4 O 4 THR C 97 PHE C 98 -1 O THR C 97 N GLN C 90
SHEET 1 P 4 SER C 114 PHE C 118 0
SHEET 2 P 4 THR C 129 PHE C 139 -1 O VAL C 133 N PHE C 118
SHEET 3 P 4 TYR C 173 SER C 182 -1 O LEU C 179 N VAL C 132
SHEET 4 P 4 SER C 159 GLN C 160 -1 N GLN C 160 O THR C 178
SHEET 1 Q 3 LYS C 145 GLN C 147 0
SHEET 2 Q 3 VAL C 191 THR C 197 -1 O GLU C 195 N GLN C 147
SHEET 3 Q 3 VAL C 205 ASN C 210 -1 O VAL C 205 N VAL C 196
SHEET 1 R 2 LYS C 149 VAL C 150 0
SHEET 2 R 2 ALA C 153 LEU C 154 -1 O ALA C 153 N VAL C 150
SHEET 1 S 4 GLN D 3 SER D 7 0
SHEET 2 S 4 LEU D 18 SER D 25 -1 O SER D 25 N GLN D 3
SHEET 3 S 4 GLN D 77 MET D 82 -1 O MET D 82 N LEU D 18
SHEET 4 S 4 LEU D 67 ASP D 72 -1 N ASN D 70 O PHE D 79
SHEET 1 T 6 LEU D 11 VAL D 12 0
SHEET 2 T 6 THR D 113 VAL D 117 1 O THR D 116 N VAL D 12
SHEET 3 T 6 ALA D 91 ALA D 98 -1 N TYR D 93 O THR D 113
SHEET 4 T 6 VAL D 34 GLN D 39 -1 N VAL D 37 O TYR D 94
SHEET 5 T 6 LEU D 45 ILE D 51 -1 O GLU D 46 N ARG D 38
SHEET 6 T 6 THR D 57 TYR D 59 -1 O ASP D 58 N VAL D 50
SHEET 1 U 4 LEU D 11 VAL D 12 0
SHEET 2 U 4 THR D 113 VAL D 117 1 O THR D 116 N VAL D 12
SHEET 3 U 4 ALA D 91 ALA D 98 -1 N TYR D 93 O THR D 113
SHEET 4 U 4 PHE D 106 TRP D 109 -1 O TYR D 108 N ARG D 97
SHEET 1 V 4 SER D 126 LEU D 130 0
SHEET 2 V 4 ALA D 142 TYR D 151 -1 O GLY D 145 N LEU D 130
SHEET 3 V 4 TYR D 182 VAL D 190 -1 O TYR D 182 N TYR D 151
SHEET 4 V 4 VAL D 169 THR D 171 -1 N HIS D 170 O VAL D 187
SHEET 1 W 4 SER D 126 LEU D 130 0
SHEET 2 W 4 ALA D 142 TYR D 151 -1 O GLY D 145 N LEU D 130
SHEET 3 W 4 TYR D 182 VAL D 190 -1 O TYR D 182 N TYR D 151
SHEET 4 W 4 VAL D 175 LEU D 176 -1 N VAL D 175 O SER D 183
SHEET 1 X 3 THR D 157 TRP D 160 0
SHEET 2 X 3 ILE D 201 HIS D 206 -1 O ASN D 203 N SER D 159
SHEET 3 X 3 THR D 211 ARG D 216 -1 O VAL D 213 N VAL D 204
SSBOND 1 CYS A 7 CYS A 34 1555 1555 2.03
SSBOND 2 CYS A 133 CYS A 163 1555 1555 2.03
SSBOND 3 CYS A 166 CYS A 175 1555 1555 2.04
SSBOND 4 CYS A 170 CYS A 183 1555 1555 2.03
SSBOND 5 CYS A 208 CYS A 216 1555 1555 2.03
SSBOND 6 CYS A 212 CYS A 224 1555 1555 2.03
SSBOND 7 CYS A 227 CYS A 236 1555 1555 2.03
SSBOND 8 CYS A 240 CYS A 267 1555 1555 2.04
SSBOND 9 CYS A 271 CYS A 283 1555 1555 2.04
SSBOND 10 CYS A 287 CYS A 302 1555 1555 2.04
SSBOND 11 CYS A 305 CYS A 309 1555 1555 2.04
SSBOND 12 CYS A 313 CYS A 338 1555 1555 2.04
SSBOND 13 CYS A 446 CYS A 475 1555 1555 2.05
SSBOND 14 CYS A 482 CYS A 491 1555 1555 2.05
SSBOND 15 CYS A 486 CYS A 499 1555 1555 2.03
SSBOND 16 CYS A 502 CYS A 511 1555 1555 2.04
SSBOND 17 CYS A 515 CYS A 531 1555 1555 2.03
SSBOND 18 CYS A 534 CYS A 547 1555 1555 2.04
SSBOND 19 CYS A 538 CYS A 555 1555 1555 2.04
SSBOND 20 CYS A 558 CYS A 567 1555 1555 2.03
SSBOND 21 CYS A 571 CYS A 593 1555 1555 2.05
SSBOND 22 CYS A 596 CYS A 604 1555 1555 2.04
SSBOND 23 CYS B 22 CYS B 96 1555 1555 2.03
SSBOND 24 CYS C 23 CYS C 88 1555 1555 2.06
SSBOND 25 CYS C 134 CYS C 194 1555 1555 2.03
SSBOND 26 CYS D 22 CYS D 95 1555 1555 2.07
SSBOND 27 CYS D 146 CYS D 202 1555 1555 2.03
LINK ND2 ASN A 328 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN A 337 C1 NAG A 703 1555 1555 1.45
LINK ND2 ASN A 389 C1 NAG A 704 1555 1555 1.45
LINK ND2 ASN A 420 C1 NAG F 1 1555 1555 1.43
LINK ND2 ASN D 88 C1 NAG D 301 1555 1555 1.36
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.43
CISPEP 1 LYS B 76 THR B 77 0 0.10
CISPEP 2 SER C 7 PRO C 8 0 -2.47
CISPEP 3 TRP C 94 PRO C 95 0 -0.93
CISPEP 4 TYR C 140 PRO C 141 0 -2.56
CISPEP 5 PHE D 152 PRO D 153 0 -0.71
CISPEP 6 GLU D 154 PRO D 155 0 -3.68
CRYST1 66.207 96.288 128.097 90.00 100.68 90.00 P 1 21 1 2
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 0.015104 0.000000 0.002848 0.00000
SCALE2 0.000000 0.010386 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007944 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
