HEADER TRANSFERASE/IMMUNE SYSTEM 20-MAR-14 3WSQ
TITLE STRUCTURE OF HER2 WITH AN FAB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 23-586;
COMPND 5 SYNONYM: METASTATIC LYMPH NODE GENE 19 PROTEIN, MLN 19, PROTO-
COMPND 6 ONCOGENE NEU, PROTO-ONCOGENE C-ERBB-2, TYROSINE KINASE-TYPE CELL
COMPND 7 SURFACE RECEPTOR HER2, P185ERBB2;
COMPND 8 EC: 2.7.10.1;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: ANTIBODY LIGHT CHAIN;
COMPND 12 CHAIN: L;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: ANTIBODY HEAVY CHAIN;
COMPND 16 CHAIN: H;
COMPND 17 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: ERBB2;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PLASMID;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PLASMID;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PLASMID
KEYWDS KINASE, TRANSFERASE-IMMUNE SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR W.Y.FU,Y.X.WANG,L.J.ZHOU
REVDAT 2 22-NOV-17 3WSQ 1 REMARK
REVDAT 1 25-MAR-15 3WSQ 0
JRNL AUTH W.FU,Y.WANG,Y.ZHANG,L.XIONG,H.TAKEDA,L.DING,Q.XU,L.HE,W.TAN,
JRNL AUTH 2 A.N.BETHUNE,L.ZHOU
JRNL TITL INSIGHTS INTO HER2 SIGNALING FROM STEP-BY-STEP OPTIMIZATION
JRNL TITL 2 OF ANTI-HER2 ANTIBODIES.
JRNL REF MABS V. 6 978 2014
JRNL REFN ISSN 1942-0862
JRNL PMID 24838231
JRNL DOI 10.4161/MABS.28786
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 18180
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 : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 930
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 38.5323 - 6.3702 1.00 2669 139 0.2515 0.3022
REMARK 3 2 6.3702 - 5.0598 1.00 2616 136 0.2106 0.2978
REMARK 3 3 5.0598 - 4.4213 1.00 2580 154 0.2189 0.2734
REMARK 3 4 4.4213 - 4.0175 1.00 2590 146 0.2171 0.2356
REMARK 3 5 4.0175 - 3.6598 0.99 2561 127 0.2280 0.2795
REMARK 3 6 3.6598 - 3.4901 0.98 2562 134 0.2191 0.2896
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) : 0.590
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.840
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 : 0.008 7670
REMARK 3 ANGLE : 1.363 10414
REMARK 3 CHIRALITY : 0.090 1171
REMARK 3 PLANARITY : 0.006 1369
REMARK 3 DIHEDRAL : 18.817 2757
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): 166.1588 2.7872 30.5975
REMARK 3 T TENSOR
REMARK 3 T11: 0.4724 T22: 0.3614
REMARK 3 T33: 0.2309 T12: 0.1573
REMARK 3 T13: 0.0357 T23: -0.0562
REMARK 3 L TENSOR
REMARK 3 L11: 1.1780 L22: 1.3916
REMARK 3 L33: 0.7640 L12: -0.4635
REMARK 3 L13: 0.1720 L23: -0.1456
REMARK 3 S TENSOR
REMARK 3 S11: 0.3114 S12: 0.4496 S13: 0.0757
REMARK 3 S21: -0.5427 S22: -0.3205 S23: -0.0274
REMARK 3 S31: -0.0852 S32: 0.0875 S33: -0.0059
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 3WSQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000096744.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
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 : 18262
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 38.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.13600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.47300
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: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1M SODIUM MALONATE PH 7.0, 0.1M
REMARK 280 HEPES 7.0, 0.5% V/V JEFFAMINE ED-2001, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298.0K
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 41.23000
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, H
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 ASN A 102
REMARK 465 ASN A 103
REMARK 465 THR A 104
REMARK 465 THR A 105
REMARK 465 PRO A 106
REMARK 465 VAL A 107
REMARK 465 THR A 108
REMARK 465 GLY A 109
REMARK 465 ALA A 110
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 L 191 CG CD CE NZ
REMARK 470 LYS H 215 CG CD CE NZ
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 A 293 CB CYS A 309 1.63
REMARK 500 SG CYS A 233 CB CYS A 242 1.98
REMARK 500 O THR L 51 CD PRO L 53 2.03
REMARK 500 SG CYS A 541 CB CYS A 554 2.06
REMARK 500 SG CYS A 545 CB CYS A 562 2.09
REMARK 500 OE2 GLU A 39 OH TYR A 61 2.13
REMARK 500 O LYS A 148 NH2 ARG A 195 2.18
REMARK 500 OD2 ASP L 152 ND1 HIS L 190 2.18
REMARK 500 O ASP H 50 CE MET H 70 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 478 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO L 53 CA - N - CD ANGL. DEV. = -13.1 DEGREES
REMARK 500 PRO L 60 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 PRO L 96 CA - N - CD ANGL. DEV. = -11.9 DEGREES
REMARK 500 TYR H 103 N - CA - C ANGL. DEV. = 16.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 7 -162.80 -106.64
REMARK 500 ASP A 8 38.08 -173.49
REMARK 500 LYS A 10 -128.50 56.02
REMARK 500 GLN A 29 95.60 -59.61
REMARK 500 GLN A 32 -73.80 -111.26
REMARK 500 GLN A 35 78.78 -53.94
REMARK 500 ASN A 37 90.89 -35.92
REMARK 500 LEU A 38 102.13 -59.48
REMARK 500 TYR A 42 -8.76 60.84
REMARK 500 ASN A 46 38.97 -77.66
REMARK 500 SER A 50 25.12 -72.64
REMARK 500 GLN A 53 -1.76 -43.05
REMARK 500 GLN A 56 -95.13 -90.77
REMARK 500 HIS A 66 18.21 43.73
REMARK 500 ASN A 67 -151.01 -69.48
REMARK 500 GLN A 68 -17.85 -168.51
REMARK 500 LEU A 74 48.42 -93.76
REMARK 500 LEU A 77 91.94 -52.81
REMARK 500 ARG A 78 -84.39 -60.41
REMARK 500 ASN A 89 -60.83 -133.64
REMARK 500 ASP A 96 53.00 -2.70
REMARK 500 GLN A 119 25.38 45.23
REMARK 500 LEU A 120 26.57 -75.39
REMARK 500 ARG A 121 43.77 -48.72
REMARK 500 SER A 122 -15.03 -164.04
REMARK 500 LEU A 123 89.30 -59.28
REMARK 500 PRO A 137 37.79 -52.08
REMARK 500 GLN A 138 -2.33 -153.24
REMARK 500 THR A 144 15.13 -60.68
REMARK 500 LYS A 153 -77.12 -55.50
REMARK 500 ASN A 154 46.00 -66.76
REMARK 500 LEU A 157 40.41 -109.38
REMARK 500 CYS A 173 -158.61 -69.14
REMARK 500 MET A 176 5.09 -59.55
REMARK 500 LYS A 178 -85.78 -53.67
REMARK 500 ASP A 189 20.49 -77.13
REMARK 500 THR A 194 -6.08 -157.50
REMARK 500 ALA A 199 77.44 -102.21
REMARK 500 CYS A 202 102.03 -11.66
REMARK 500 ALA A 219 72.79 -170.07
REMARK 500 ALA A 220 25.35 167.59
REMARK 500 SER A 228 33.93 -92.08
REMARK 500 ASP A 229 17.50 -144.70
REMARK 500 HIS A 235 -64.59 -126.71
REMARK 500 ASN A 237 67.84 -61.52
REMARK 500 HIS A 238 77.86 -62.28
REMARK 500 CYS A 242 103.23 -21.17
REMARK 500 THR A 254 -31.60 67.94
REMARK 500 ASP A 255 -82.47 -94.46
REMARK 500 THR A 256 -82.90 -64.58
REMARK 500
REMARK 500 THIS ENTRY HAS 140 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 TYR H 102 TYR H 103 -142.33
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3WSQ A 1 564 UNP P04626 ERBB2_HUMAN 23 586
DBREF 3WSQ L 1 215 PDB 3WSQ 3WSQ 1 215
DBREF 3WSQ H 1 218 PDB 3WSQ 3WSQ 1 218
SEQRES 1 A 564 THR GLN VAL CYS THR GLY THR ASP MET LYS LEU ARG LEU
SEQRES 2 A 564 PRO ALA SER PRO GLU THR HIS LEU ASP MET LEU ARG HIS
SEQRES 3 A 564 LEU TYR GLN GLY CYS GLN VAL VAL GLN GLY ASN LEU GLU
SEQRES 4 A 564 LEU THR TYR LEU PRO THR ASN ALA SER LEU SER PHE LEU
SEQRES 5 A 564 GLN ASP ILE GLN GLU VAL GLN GLY TYR VAL LEU ILE ALA
SEQRES 6 A 564 HIS ASN GLN VAL ARG GLN VAL PRO LEU GLN ARG LEU ARG
SEQRES 7 A 564 ILE VAL ARG GLY THR GLN LEU PHE GLU ASP ASN TYR ALA
SEQRES 8 A 564 LEU ALA VAL LEU ASP ASN GLY ASP PRO LEU ASN ASN THR
SEQRES 9 A 564 THR PRO VAL THR GLY ALA SER PRO GLY GLY LEU ARG GLU
SEQRES 10 A 564 LEU GLN LEU ARG SER LEU THR GLU ILE LEU LYS GLY GLY
SEQRES 11 A 564 VAL LEU ILE GLN ARG ASN PRO GLN LEU CYS TYR GLN ASP
SEQRES 12 A 564 THR ILE LEU TRP LYS ASP ILE PHE HIS LYS ASN ASN GLN
SEQRES 13 A 564 LEU ALA LEU THR LEU ILE ASP THR ASN ARG SER ARG ALA
SEQRES 14 A 564 CYS HIS PRO CYS SER PRO MET CYS LYS GLY SER ARG CYS
SEQRES 15 A 564 TRP GLY GLU SER SER GLU ASP CYS GLN SER LEU THR ARG
SEQRES 16 A 564 THR VAL CYS ALA GLY GLY CYS ALA ARG CYS LYS GLY PRO
SEQRES 17 A 564 LEU PRO THR ASP CYS CYS HIS GLU GLN CYS ALA ALA GLY
SEQRES 18 A 564 CYS THR GLY PRO LYS HIS SER ASP CYS LEU ALA CYS LEU
SEQRES 19 A 564 HIS PHE ASN HIS SER GLY ILE CYS GLU LEU HIS CYS PRO
SEQRES 20 A 564 ALA LEU VAL THR TYR ASN THR ASP THR PHE GLU SER MET
SEQRES 21 A 564 PRO ASN PRO GLU GLY ARG TYR THR PHE GLY ALA SER CYS
SEQRES 22 A 564 VAL THR ALA CYS PRO TYR ASN TYR LEU SER THR ASP VAL
SEQRES 23 A 564 GLY SER CYS THR LEU VAL CYS PRO LEU HIS ASN GLN GLU
SEQRES 24 A 564 VAL THR ALA GLU ASP GLY THR GLN ARG CYS GLU LYS CYS
SEQRES 25 A 564 SER LYS PRO CYS ALA ARG VAL CYS TYR GLY LEU GLY MET
SEQRES 26 A 564 GLU HIS LEU ARG GLU VAL ARG ALA VAL THR SER ALA ASN
SEQRES 27 A 564 ILE GLN GLU PHE ALA GLY CYS LYS LYS ILE PHE GLY SER
SEQRES 28 A 564 LEU ALA PHE LEU PRO GLU SER PHE ASP GLY ASP PRO ALA
SEQRES 29 A 564 SER ASN THR ALA PRO LEU GLN PRO GLU GLN LEU GLN VAL
SEQRES 30 A 564 PHE GLU THR LEU GLU GLU ILE THR GLY TYR LEU TYR ILE
SEQRES 31 A 564 SER ALA TRP PRO ASP SER LEU PRO ASP LEU SER VAL PHE
SEQRES 32 A 564 GLN ASN LEU GLN VAL ILE ARG GLY ARG ILE LEU HIS ASN
SEQRES 33 A 564 GLY ALA TYR SER LEU THR LEU GLN GLY LEU GLY ILE SER
SEQRES 34 A 564 TRP LEU GLY LEU ARG SER LEU ARG GLU LEU GLY SER GLY
SEQRES 35 A 564 LEU ALA LEU ILE HIS HIS ASN THR HIS LEU CYS PHE VAL
SEQRES 36 A 564 HIS THR VAL PRO TRP ASP GLN LEU PHE ARG ASN PRO HIS
SEQRES 37 A 564 GLN ALA LEU LEU HIS THR ALA ASN ARG PRO GLU ASP GLU
SEQRES 38 A 564 CYS VAL GLY GLU GLY LEU ALA CYS HIS GLN LEU CYS ALA
SEQRES 39 A 564 ARG GLY HIS CYS TRP GLY PRO GLY PRO THR GLN CYS VAL
SEQRES 40 A 564 ASN CYS SER GLN PHE LEU ARG GLY GLN GLU CYS VAL GLU
SEQRES 41 A 564 GLU CYS ARG VAL LEU GLN GLY LEU PRO ARG GLU TYR VAL
SEQRES 42 A 564 ASN ALA ARG HIS CYS LEU PRO CYS HIS PRO GLU CYS GLN
SEQRES 43 A 564 PRO GLN ASN GLY SER VAL THR CYS PHE GLY PRO GLU ALA
SEQRES 44 A 564 ASP GLN CYS VAL ALA
SEQRES 1 L 215 GLN SER VAL LEU THR GLN PRO PRO SER ALA SER GLY THR
SEQRES 2 L 215 PRO GLY GLN THR VAL THR LEU SER CYS SER GLY SER ARG
SEQRES 3 L 215 THR ASN ALA GLY ARG ASP PRO VAL SER TRP TYR GLN GLN
SEQRES 4 L 215 LEU PRO GLY THR ALA PRO LYS LEU LEU THR SER THR ALA
SEQRES 5 L 215 PRO GLN GLY PRO SER GLY VAL PRO ASP ARG PHE SER GLY
SEQRES 6 L 215 SER LYS SER GLY THR SER SER SER LEU ALA ILE SER GLY
SEQRES 7 L 215 LEU GLN SER GLY ASP GLU ALA ASP TYR TYR CYS THR VAL
SEQRES 8 L 215 TRP ASP SER VAL PRO GLY ALA SER VAL PHE GLY SER GLY
SEQRES 9 L 215 THR PHE LEU THR VAL THR VAL ALA ALA PRO SER VAL PHE
SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR
SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG
SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN
SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER
SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU
SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS
SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS
SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS
SEQRES 1 H 218 GLU VAL GLN LEU VAL GLN SER GLY GLY GLY LEU LYS VAL
SEQRES 2 H 218 PRO GLY GLY SER VAL LYS VAL SER CYS LYS ALA SER SER
SEQRES 3 H 218 TYR THR PHE THR SER TYR GLY ILE SER TRP VAL ARG GLN
SEQRES 4 H 218 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY ASP VAL ASN
SEQRES 5 H 218 THR TYR ALA GLY ASN THR ASN TYR ALA GLN LYS LEU GLN
SEQRES 6 H 218 GLY ARG VAL THR MET THR THR ASP THR GLY THR SER THR
SEQRES 7 H 218 ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP ALA
SEQRES 8 H 218 ALA VAL TYR TYR CYS ALA ARG ASP ARG GLY TYR TYR ALA
SEQRES 9 H 218 PHE ASP ILE TRP GLY GLN GLY THR MET VAL THR VAL SER
SEQRES 10 H 218 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA
SEQRES 11 H 218 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU
SEQRES 12 H 218 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR
SEQRES 13 H 218 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS
SEQRES 14 H 218 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER
SEQRES 15 H 218 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY
SEQRES 16 H 218 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER
SEQRES 17 H 218 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO
HELIX 1 1 SER A 16 TYR A 28 1 13
HELIX 2 2 PHE A 51 ILE A 55 5 5
HELIX 3 3 LEU A 85 ASP A 88 5 4
HELIX 4 4 LEU A 146 PHE A 151 1 6
HELIX 5 5 LYS A 226 CYS A 230 5 5
HELIX 6 6 MET A 325 ARG A 329 5 5
HELIX 7 7 ASN A 338 ALA A 343 5 6
HELIX 8 8 ASP A 362 ASN A 366 5 5
HELIX 9 9 VAL A 377 LEU A 381 5 5
HELIX 10 10 LEU A 414 GLY A 417 5 4
HELIX 11 11 PRO A 459 LEU A 463 5 5
HELIX 12 12 CYS A 493 HIS A 497 5 5
HELIX 13 13 GLN L 125 SER L 128 5 4
HELIX 14 14 LYS L 184 GLU L 188 1 5
HELIX 15 15 THR H 28 TYR H 32 5 5
HELIX 16 16 ALA H 61 GLN H 65 5 5
HELIX 17 17 ARG H 87 ALA H 91 5 5
HELIX 18 18 SER H 161 ALA H 163 5 3
SHEET 1 A 2 CYS A 4 THR A 5 0
SHEET 2 A 2 VAL A 34 GLN A 35 1 O GLN A 35 N CYS A 4
SHEET 1 B 5 LEU A 38 THR A 41 0
SHEET 2 B 5 VAL A 62 ALA A 65 1 O LEU A 63 N LEU A 40
SHEET 3 B 5 TYR A 90 VAL A 94 1 O ALA A 93 N ILE A 64
SHEET 4 B 5 GLY A 130 ILE A 133 1 O LEU A 132 N LEU A 92
SHEET 5 B 5 THR A 160 ILE A 162 1 O LEU A 161 N VAL A 131
SHEET 1 C 4 CYS A 289 THR A 290 0
SHEET 2 C 4 LEU A 282 THR A 284 -1 N LEU A 282 O THR A 290
SHEET 3 C 4 ARG A 308 GLU A 310 1 O CYS A 309 N SER A 283
SHEET 4 C 4 GLN A 298 VAL A 300 -1 N GLN A 298 O GLU A 310
SHEET 1 D 4 CYS A 320 TYR A 321 0
SHEET 2 D 4 LYS A 347 PHE A 349 1 O PHE A 349 N CYS A 320
SHEET 3 D 4 GLU A 383 ILE A 384 1 O GLU A 383 N ILE A 348
SHEET 4 D 4 VAL A 408 ILE A 409 1 O VAL A 408 N ILE A 384
SHEET 1 E 5 LEU A 352 PHE A 354 0
SHEET 2 E 5 LEU A 388 ILE A 390 1 O TYR A 389 N PHE A 354
SHEET 3 E 5 TYR A 419 GLN A 424 1 O THR A 422 N LEU A 388
SHEET 4 E 5 LEU A 443 HIS A 447 1 O LEU A 445 N LEU A 421
SHEET 5 E 5 LEU A 471 THR A 474 1 O LEU A 472 N ALA A 444
SHEET 1 F 2 PHE A 512 ARG A 514 0
SHEET 2 F 2 GLU A 517 VAL A 519 -1 O GLU A 517 N ARG A 514
SHEET 1 G 2 GLU A 531 ASN A 534 0
SHEET 2 G 2 HIS A 537 PRO A 540 -1 O LEU A 539 N TYR A 532
SHEET 1 H 5 SER L 11 GLY L 12 0
SHEET 2 H 5 SER L 103 LEU L 107 1 O PHE L 106 N GLY L 12
SHEET 3 H 5 ALA L 85 THR L 90 -1 N TYR L 87 O SER L 103
SHEET 4 H 5 SER L 35 GLN L 39 -1 N TYR L 37 O TYR L 88
SHEET 5 H 5 LYS L 46 SER L 50 -1 O LEU L 48 N TRP L 36
SHEET 1 I 3 VAL L 18 SER L 23 0
SHEET 2 I 3 SER L 71 ILE L 76 -1 O SER L 72 N CYS L 22
SHEET 3 I 3 PHE L 63 SER L 64 -1 N SER L 64 O ALA L 75
SHEET 1 J 4 SER L 115 VAL L 116 0
SHEET 2 J 4 THR L 130 ASN L 138 -1 O ASN L 138 N SER L 115
SHEET 3 J 4 SER L 175 SER L 183 -1 O LEU L 176 N LEU L 137
SHEET 4 J 4 SER L 160 GLN L 161 -1 N GLN L 161 O THR L 179
SHEET 1 K 4 ALA L 145 VAL L 147 0
SHEET 2 K 4 VAL L 192 HIS L 199 -1 O THR L 198 N LYS L 146
SHEET 3 K 4 LYS L 150 VAL L 151 -1 N LYS L 150 O ALA L 194
SHEET 4 K 4 ALA L 154 LEU L 155 -1 O ALA L 154 N VAL L 151
SHEET 1 L 3 ALA L 145 VAL L 147 0
SHEET 2 L 3 VAL L 192 HIS L 199 -1 O THR L 198 N LYS L 146
SHEET 3 L 3 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197
SHEET 1 M 4 GLN H 3 SER H 7 0
SHEET 2 M 4 VAL H 18 SER H 25 -1 O SER H 25 N GLN H 3
SHEET 3 M 4 TYR H 80 LEU H 83 -1 O LEU H 83 N VAL H 18
SHEET 4 M 4 VAL H 68 THR H 71 -1 N THR H 69 O GLU H 82
SHEET 1 N 5 GLY H 10 LYS H 12 0
SHEET 2 N 5 MET H 113 VAL H 116 1 O THR H 115 N LYS H 12
SHEET 3 N 5 ALA H 92 ALA H 97 -1 N ALA H 92 O VAL H 114
SHEET 4 N 5 SER H 35 ARG H 38 -1 N SER H 35 O ALA H 97
SHEET 5 N 5 TRP H 47 GLY H 49 -1 O MET H 48 N TRP H 36
SHEET 1 O 4 SER H 125 LEU H 129 0
SHEET 2 O 4 THR H 140 TYR H 150 -1 O LEU H 146 N PHE H 127
SHEET 3 O 4 SER H 185 PRO H 190 -1 O VAL H 189 N ALA H 141
SHEET 4 O 4 HIS H 169 THR H 170 -1 N HIS H 169 O VAL H 186
SHEET 1 P 3 THR H 136 SER H 137 0
SHEET 2 P 3 THR H 140 TYR H 150 -1 O THR H 140 N SER H 137
SHEET 3 P 3 TYR H 181 LEU H 183 -1 O LEU H 183 N VAL H 147
SHEET 1 Q 3 SER H 158 TRP H 159 0
SHEET 2 Q 3 TYR H 199 ASN H 202 -1 O ASN H 202 N SER H 158
SHEET 3 Q 3 ASP H 213 VAL H 216 -1 O VAL H 216 N TYR H 199
SSBOND 1 CYS A 4 CYS A 31 1555 1555 2.03
SSBOND 2 CYS A 140 CYS A 170 1555 1555 2.03
SSBOND 3 CYS A 173 CYS A 182 1555 1555 2.05
SSBOND 4 CYS A 177 CYS A 190 1555 1555 2.03
SSBOND 5 CYS A 198 CYS A 205 1555 1555 2.03
SSBOND 6 CYS A 202 CYS A 213 1555 1555 2.03
SSBOND 7 CYS A 214 CYS A 222 1555 1555 2.04
SSBOND 8 CYS A 218 CYS A 230 1555 1555 2.03
SSBOND 9 CYS A 233 CYS A 242 1555 1555 2.03
SSBOND 10 CYS A 246 CYS A 273 1555 1555 2.05
SSBOND 11 CYS A 277 CYS A 289 1555 1555 2.04
SSBOND 12 CYS A 293 CYS A 309 1555 1555 2.02
SSBOND 13 CYS A 312 CYS A 316 1555 1555 2.04
SSBOND 14 CYS A 320 CYS A 345 1555 1555 2.03
SSBOND 15 CYS A 453 CYS A 482 1555 1555 2.03
SSBOND 16 CYS A 489 CYS A 498 1555 1555 2.04
SSBOND 17 CYS A 493 CYS A 506 1555 1555 2.04
SSBOND 18 CYS A 509 CYS A 518 1555 1555 2.04
SSBOND 19 CYS A 522 CYS A 538 1555 1555 2.03
SSBOND 20 CYS A 541 CYS A 554 1555 1555 2.03
SSBOND 21 CYS A 545 CYS A 562 1555 1555 2.02
SSBOND 22 CYS L 22 CYS L 89 1555 1555 2.03
SSBOND 23 CYS L 135 CYS L 195 1555 1555 2.03
SSBOND 24 CYS H 22 CYS H 96 1555 1555 2.03
SSBOND 25 CYS H 145 CYS H 201 1555 1555 2.03
CISPEP 1 GLN L 6 PRO L 7 0 -1.66
CISPEP 2 ALA L 29 GLY L 30 0 22.36
CISPEP 3 GLY L 30 ARG L 31 0 1.00
CISPEP 4 VAL L 95 PRO L 96 0 2.86
CISPEP 5 TYR L 141 PRO L 142 0 1.25
CISPEP 6 GLY H 101 TYR H 102 0 -4.45
CISPEP 7 PHE H 151 PRO H 152 0 -1.83
CISPEP 8 GLU H 153 PRO H 154 0 3.66
CRYST1 72.562 82.460 110.339 90.00 90.91 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 0.013781 0.000000 0.000219 0.00000
SCALE2 0.000000 0.012127 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009064 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
