HEADER IMMUNE SYSTEM 29-SEP-10 3P0Y
TITLE ANTI-EGFR/HER3 FAB DL11 IN COMPLEX WITH DOMAIN III OF EGFR
TITLE 2 EXTRACELLULAR REGION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN III, UNP RESIDUES 334-540;
COMPND 5 SYNONYM: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-1, PROTO-ONCOGENE C-
COMPND 6 ERBB-1;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: FAB DL11 HEAVY CHAIN;
COMPND 11 CHAIN: H;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: FAB DL11 LIGHT CHAIN;
COMPND 15 CHAIN: L;
COMPND 16 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, ERBB1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PW0579-3;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 24 EXPRESSION_SYSTEM_PLASMID: PW0579-3
KEYWDS BETA-SANDWICH, ANTIGENS EGFR, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR C.EIGENBROT,S.SHIA
REVDAT 3 29-JUL-20 3P0Y 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 21-MAR-12 3P0Y 1 JRNL
REVDAT 1 26-OCT-11 3P0Y 0
JRNL AUTH G.SCHAEFER,L.HABER,L.M.CROCKER,S.SHIA,L.SHAO,D.DOWBENKO,
JRNL AUTH 2 K.TOTPAL,A.WONG,C.V.LEE,S.STAWICKI,R.CLARK,C.FIELDS,
JRNL AUTH 3 G.D.LEWIS PHILLIPS,R.A.PRELL,D.M.DANILENKO,Y.FRANKE,
JRNL AUTH 4 J.P.STEPHAN,J.HWANG,Y.WU,J.BOSTROM,M.X.SLIWKOWSKI,G.FUH,
JRNL AUTH 5 C.EIGENBROT
JRNL TITL A TWO-IN-ONE ANTIBODY AGAINST HER3 AND EGFR HAS SUPERIOR
JRNL TITL 2 INHIBITORY ACTIVITY COMPARED WITH MONOSPECIFIC ANTIBODIES.
JRNL REF CANCER CELL V. 20 472 2011
JRNL REFN ISSN 1535-6108
JRNL PMID 22014573
JRNL DOI 10.1016/J.CCR.2011.09.003
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 73362
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1507
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9534
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 189
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4747
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 100
REMARK 3 SOLVENT ATOMS : 650
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.52000
REMARK 3 B22 (A**2) : -0.76000
REMARK 3 B33 (A**2) : 0.24000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.108
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.433
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5067 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6906 ; 1.240 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 642 ; 6.227 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 201 ;32.510 ;24.428
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 818 ;11.926 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;17.155 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 791 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3775 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2184 ; 0.191 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3448 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 543 ; 0.118 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 62 ; 0.157 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 32 ; 0.152 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3260 ; 2.400 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5128 ; 3.507 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2057 ; 3.636 ; 3.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1778 ; 5.426 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3P0Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000061819.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .9774
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : SI
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74875
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 <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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE/PEG3350/SODIUM
REMARK 280 DEXTRAN SULFATE, PH 8, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 286K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 40.96700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 100.33850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.96700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 100.33850
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350 APPLY THE FOLLOWING TO CHAINS: H, L
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 49.42600
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH H 659 LIES ON A SPECIAL POSITION.
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 ASN A 504
REMARK 465 VAL A 505
REMARK 465 SER A 506
REMARK 465 ARG A 507
REMARK 465 GLY A 508
REMARK 465 ARG A 509
REMARK 465 GLU A 510
REMARK 465 CYS A 511
REMARK 465 VAL A 512
REMARK 465 ASP A 513
REMARK 465 LYS A 514
REMARK 465 GLY A 515
REMARK 465 ASN A 516
REMARK 465 SER A 517
REMARK 465 HIS A 518
REMARK 465 HIS A 519
REMARK 465 HIS A 520
REMARK 465 HIS A 521
REMARK 465 HIS A 522
REMARK 465 HIS A 523
REMARK 465 LYS H 129
REMARK 465 SER H 130
REMARK 465 THR H 131
REMARK 465 SER H 132
REMARK 465 GLY H 133
REMARK 465 CYS H 216
REMARK 465 ASP H 217
REMARK 465 LYS H 218
REMARK 465 THR H 219
REMARK 465 HIS H 220
REMARK 465 CYS L 214
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 A 389 C2 NAG C 1 2.12
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 TYR A 447 -23.49 76.22
REMARK 500 ASN A 469 -156.52 -97.86
REMARK 500 SER H 127 81.65 52.05
REMARK 500 ALA L 30 -116.13 54.62
REMARK 500 ALA L 51 -35.11 70.52
REMARK 500 ASN L 152 -2.88 70.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P0V RELATED DB: PDB
REMARK 900 FAB DL11 ALONE
REMARK 900 RELATED ID: 3P11 RELATED DB: PDB
REMARK 900 FAB DL11 WITH HER3
DBREF 3P0Y A 310 514 UNP P00533 EGFR_HUMAN 334 538
DBREF 3P0Y L 1 214 PDB 3P0Y 3P0Y 1 214
DBREF 3P0Y H 1 220 PDB 3P0Y 3P0Y 1 220
SEQADV 3P0Y GLY A 515 UNP P00533 EXPRESSION TAG
SEQADV 3P0Y ASN A 516 UNP P00533 EXPRESSION TAG
SEQADV 3P0Y SER A 517 UNP P00533 EXPRESSION TAG
SEQADV 3P0Y HIS A 518 UNP P00533 EXPRESSION TAG
SEQADV 3P0Y HIS A 519 UNP P00533 EXPRESSION TAG
SEQADV 3P0Y HIS A 520 UNP P00533 EXPRESSION TAG
SEQADV 3P0Y HIS A 521 UNP P00533 EXPRESSION TAG
SEQADV 3P0Y HIS A 522 UNP P00533 EXPRESSION TAG
SEQADV 3P0Y HIS A 523 UNP P00533 EXPRESSION TAG
SEQRES 1 A 214 ARG LYS VAL CYS ASN GLY ILE GLY ILE GLY GLU PHE LYS
SEQRES 2 A 214 ASP SER LEU SER ILE ASN ALA THR ASN ILE LYS HIS PHE
SEQRES 3 A 214 LYS ASN CYS THR SER ILE SER GLY ASP LEU HIS ILE LEU
SEQRES 4 A 214 PRO VAL ALA PHE ARG GLY ASP SER PHE THR HIS THR PRO
SEQRES 5 A 214 PRO LEU ASP PRO GLN GLU LEU ASP ILE LEU LYS THR VAL
SEQRES 6 A 214 LYS GLU ILE THR GLY PHE LEU LEU ILE GLN ALA TRP PRO
SEQRES 7 A 214 GLU ASN ARG THR ASP LEU HIS ALA PHE GLU ASN LEU GLU
SEQRES 8 A 214 ILE ILE ARG GLY ARG THR LYS GLN HIS GLY GLN PHE SER
SEQRES 9 A 214 LEU ALA VAL VAL SER LEU ASN ILE THR SER LEU GLY LEU
SEQRES 10 A 214 ARG SER LEU LYS GLU ILE SER ASP GLY ASP VAL ILE ILE
SEQRES 11 A 214 SER GLY ASN LYS ASN LEU CYS TYR ALA ASN THR ILE ASN
SEQRES 12 A 214 TRP LYS LYS LEU PHE GLY THR SER GLY GLN LYS THR LYS
SEQRES 13 A 214 ILE ILE SER ASN ARG GLY GLU ASN SER CYS LYS ALA THR
SEQRES 14 A 214 GLY GLN VAL CYS HIS ALA LEU CYS SER PRO GLU GLY CYS
SEQRES 15 A 214 TRP GLY PRO GLU PRO ARG ASP CYS VAL SER CYS ARG ASN
SEQRES 16 A 214 VAL SER ARG GLY ARG GLU CYS VAL ASP LYS GLY ASN SER
SEQRES 17 A 214 HIS HIS HIS HIS HIS HIS
SEQRES 1 H 228 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 H 228 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 228 PHE THR LEU SER GLY ASP TRP ILE HIS TRP VAL ARG GLN
SEQRES 4 H 228 ALA PRO GLY LYS GLY LEU GLU TRP LEU GLY GLU ILE SER
SEQRES 5 H 228 ALA ALA GLY GLY TYR THR ASP TYR ALA ASP SER VAL LYS
SEQRES 6 H 228 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR
SEQRES 7 H 228 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 H 228 ALA VAL TYR TYR CYS ALA ARG GLU SER ARG VAL SER PHE
SEQRES 9 H 228 GLU ALA ALA MET ASP TYR TRP GLY GLN GLY THR LEU VAL
SEQRES 10 H 228 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE
SEQRES 11 H 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR
SEQRES 12 H 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU
SEQRES 13 H 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER
SEQRES 14 H 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY
SEQRES 15 H 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER
SEQRES 16 H 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS
SEQRES 17 H 228 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO
SEQRES 18 H 228 LYS SER CYS ASP LYS THR HIS
SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 L 214 GLN ASP LEU ALA THR ASP VAL ALA TRP TYR GLN GLN LYS
SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER
SEQRES 5 L 214 PHE LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU
SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER
SEQRES 8 L 214 GLU PRO GLU PRO TYR THR PHE GLY GLN GLY THR LYS VAL
SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS
MODRES 3P0Y ASN A 389 ASN GLYCOSYLATION SITE
MODRES 3P0Y ASN A 328 ASN GLYCOSYLATION SITE
MODRES 3P0Y ASN A 420 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET NAG C 1 14
HET NAG C 2 14
HET FUL C 3 10
HET NAG D 1 14
HET NAG D 2 14
HET GOL H 401 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUL BETA-L-FUCOPYRANOSE
HETNAM GOL GLYCEROL
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 NAG 6(C8 H15 N O6)
FORMUL 5 FUL C6 H12 O5
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *650(H2 O)
HELIX 1 1 ILE A 318 LYS A 322 5 5
HELIX 2 2 ASN A 331 LYS A 336 5 6
HELIX 3 3 LEU A 348 GLY A 354 1 7
HELIX 4 4 ASP A 364 VAL A 374 5 11
HELIX 5 5 LEU A 393 GLU A 397 5 5
HELIX 6 6 LYS A 407 GLY A 410 5 4
HELIX 7 7 TYR A 447 ILE A 451 5 5
HELIX 8 8 ASN A 452 PHE A 457 1 6
HELIX 9 9 GLY A 471 THR A 478 1 8
HELIX 10 10 GLU A 495 CYS A 499 5 5
HELIX 11 11 ARG H 83 THR H 87 5 5
HELIX 12 12 SER H 156 ALA H 158 5 3
HELIX 13 13 SER H 187 LEU H 189 5 3
HELIX 14 14 LYS H 201 ASN H 204 5 4
HELIX 15 15 GLN L 79 PHE L 83 5 5
HELIX 16 16 SER L 121 LYS L 126 1 6
HELIX 17 17 LYS L 183 LYS L 188 1 6
SHEET 1 A 5 VAL A 312 ASN A 314 0
SHEET 2 A 5 SER A 340 SER A 342 1 O SER A 342 N CYS A 313
SHEET 3 A 5 GLU A 376 ILE A 377 1 O GLU A 376 N ILE A 341
SHEET 4 A 5 ILE A 401 ILE A 402 1 O ILE A 401 N ILE A 377
SHEET 5 A 5 GLU A 431 ILE A 432 1 O GLU A 431 N ILE A 402
SHEET 1 B 5 LEU A 345 ILE A 347 0
SHEET 2 B 5 LEU A 381 ILE A 383 1 O LEU A 382 N LEU A 345
SHEET 3 B 5 PHE A 412 VAL A 417 1 O ALA A 415 N ILE A 383
SHEET 4 B 5 ASP A 436 SER A 440 1 O ILE A 438 N LEU A 414
SHEET 5 B 5 THR A 464 ILE A 467 1 O LYS A 465 N ILE A 439
SHEET 1 C 4 GLN H 3 SER H 7 0
SHEET 2 C 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5
SHEET 3 C 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18
SHEET 4 C 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81
SHEET 1 D 6 LEU H 11 VAL H 12 0
SHEET 2 D 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 D 6 ALA H 88 GLU H 95 -1 N TYR H 90 O THR H 107
SHEET 4 D 6 TRP H 33 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 D 6 LEU H 45 SER H 52 -1 O LEU H 48 N TRP H 36
SHEET 6 D 6 TYR H 56 TYR H 59 -1 O ASP H 58 N GLU H 50
SHEET 1 E 4 LEU H 11 VAL H 12 0
SHEET 2 E 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 E 4 ALA H 88 GLU H 95 -1 N TYR H 90 O THR H 107
SHEET 4 E 4 MET H 100D TRP H 103 -1 O TYR H 102 N ARG H 94
SHEET 1 F 4 SER H 120 LEU H 124 0
SHEET 2 F 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120
SHEET 3 F 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142
SHEET 4 F 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 G 4 SER H 120 LEU H 124 0
SHEET 2 G 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120
SHEET 3 G 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142
SHEET 4 G 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177
SHEET 1 H 3 THR H 151 TRP H 154 0
SHEET 2 H 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153
SHEET 3 H 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198
SHEET 1 I 4 MET L 4 SER L 7 0
SHEET 2 I 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7
SHEET 3 I 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23
SHEET 4 I 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 J 6 SER L 10 SER L 14 0
SHEET 2 J 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11
SHEET 3 J 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104
SHEET 4 J 6 VAL L 33 GLN L 38 -1 N GLN L 38 O THR L 85
SHEET 5 J 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35
SHEET 6 J 6 PHE L 53 LEU L 54 -1 O PHE L 53 N TYR L 49
SHEET 1 K 4 SER L 114 PHE L 118 0
SHEET 2 K 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114
SHEET 3 K 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130
SHEET 4 K 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176
SHEET 1 L 4 ALA L 153 LEU L 154 0
SHEET 2 L 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 L 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147
SHEET 4 L 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196
SSBOND 1 CYS A 313 CYS A 338 1555 1555 2.00
SSBOND 2 CYS A 446 CYS A 475 1555 1555 2.06
SSBOND 3 CYS A 482 CYS A 491 1555 1555 2.07
SSBOND 4 CYS A 486 CYS A 499 1555 1555 2.03
SSBOND 5 CYS H 22 CYS H 92 1555 1555 2.03
SSBOND 6 CYS H 140 CYS H 196 1555 1555 2.05
SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.08
SSBOND 8 CYS L 134 CYS L 194 1555 1555 2.04
LINK ND2 ASN A 328 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN A 389 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 420 C1 NAG D 1 1555 1555 1.46
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O3 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O6 NAG C 1 C1 FUL C 3 1555 1555 1.42
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.46
CISPEP 1 PHE H 146 PRO H 147 0 -5.70
CISPEP 2 GLU H 148 PRO H 149 0 -2.88
CISPEP 3 SER L 7 PRO L 8 0 -4.39
CISPEP 4 GLU L 92 PRO L 93 0 -8.76
CISPEP 5 GLU L 94 PRO L 95 0 2.62
CISPEP 6 TYR L 140 PRO L 141 0 2.83
CRYST1 81.934 200.677 49.426 90.00 90.00 90.00 P 21 21 2 4
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 0.012205 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004983 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020232 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
