HEADER TRANSFERASE 15-NOV-07 3BE1
TITLE DUAL SPECIFIC BH1 FAB IN COMPLEX WITH THE EXTRACELLULAR DOMAIN OF
TITLE 2 HER2/ERBB-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 23-646;
COMPND 5 SYNONYM: P185ERBB2, C-ERBB-2, NEU PROTO-ONCOGENE, TYROSINE KINASE-
COMPND 6 TYPE CELL SURFACE RECEPTOR HER2, MLN 19, CD340 ANTIGEN;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: FAB FRAGMENT-HEAVY CHAIN;
COMPND 11 CHAIN: H;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: FAB FRAGMENT-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: ERBB2, HER2, NEU, NGL;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: CHINESE HAMSTER OVARY;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 MOL_ID: 3;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FAB COMPLEX, ATP-BINDING, GLYCOPROTEIN, KINASE, MEMBRANE, NUCLEOTIDE-
KEYWDS 2 BINDING, PHOSPHORYLATION, RECEPTOR, TRANSFERASE, TRANSMEMBRANE,
KEYWDS 3 TYROSINE-PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.BOSTROM,C.WIESMANN,B.A.APPLETON
REVDAT 7 30-AUG-23 3BE1 1 HETSYN
REVDAT 6 29-JUL-20 3BE1 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE
REVDAT 5 25-OCT-17 3BE1 1 REMARK
REVDAT 4 13-JUL-11 3BE1 1 VERSN
REVDAT 3 31-MAR-09 3BE1 1 JRNL
REVDAT 2 24-FEB-09 3BE1 1 VERSN
REVDAT 1 18-NOV-08 3BE1 0
JRNL AUTH J.BOSTROM,S.F.YU,D.KAN,B.A.APPLETON,C.V.LEE,K.BILLECI,W.MAN,
JRNL AUTH 2 F.PEALE,S.ROSS,C.WIESMANN,G.FUH
JRNL TITL VARIANTS OF THE ANTIBODY HERCEPTIN THAT INTERACT WITH HER2
JRNL TITL 2 AND VEGF AT THE ANTIGEN BINDING SITE
JRNL REF SCIENCE V. 323 1610 2009
JRNL REFN ISSN 0036-8075
JRNL PMID 19299620
JRNL DOI 10.1126/SCIENCE.1165480
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 33988
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) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1711
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 25
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.96
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1850
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.3760
REMARK 3 BIN FREE R VALUE SET COUNT : 102
REMARK 3 BIN FREE R VALUE : 0.4050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7770
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.48000
REMARK 3 B22 (A**2) : -4.19000
REMARK 3 B33 (A**2) : 4.67000
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): 1.776
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.407
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.304
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.265
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.886
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8024 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5412 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10937 ; 1.210 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13133 ; 0.846 ; 3.008
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1005 ; 6.756 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 348 ;36.357 ;24.138
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1253 ;15.444 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;14.469 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1208 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8949 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1568 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1530 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5586 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3800 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 4331 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 149 ; 0.138 ; 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): 9 ; 0.189 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 15 ; 0.164 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.296 ; 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): 5401 ; 2.728 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2052 ; 0.464 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8131 ; 4.227 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3291 ; 2.402 ; 2.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2806 ; 3.741 ; 5.000
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 : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 114
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7944 -19.4991 86.4199
REMARK 3 T TENSOR
REMARK 3 T11: 0.2173 T22: -0.0205
REMARK 3 T33: -0.1547 T12: 0.0147
REMARK 3 T13: -0.0039 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 3.1396 L22: 1.2177
REMARK 3 L33: 3.0757 L12: -0.4194
REMARK 3 L13: 2.1476 L23: 0.3570
REMARK 3 S TENSOR
REMARK 3 S11: -0.2968 S12: 0.2112 S13: 0.1829
REMARK 3 S21: -0.2307 S22: 0.1503 S23: 0.1922
REMARK 3 S31: -0.3832 S32: 0.0143 S33: 0.1465
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 115 H 215
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9774 11.1172 96.6333
REMARK 3 T TENSOR
REMARK 3 T11: 0.6142 T22: -0.4985
REMARK 3 T33: 0.5217 T12: 0.1456
REMARK 3 T13: -0.4472 T23: -0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 5.3815 L22: 3.3279
REMARK 3 L33: 1.2477 L12: 4.2304
REMARK 3 L13: 1.4682 L23: 1.1094
REMARK 3 S TENSOR
REMARK 3 S11: -0.6556 S12: -0.2077 S13: 0.9928
REMARK 3 S21: -0.3479 S22: -0.0627 S23: 0.7108
REMARK 3 S31: -0.9371 S32: 0.0292 S33: 0.7184
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 109
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8698 -21.1832 103.6787
REMARK 3 T TENSOR
REMARK 3 T11: 0.1548 T22: 0.0196
REMARK 3 T33: -0.1747 T12: -0.0009
REMARK 3 T13: 0.0723 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 2.1178 L22: 2.8866
REMARK 3 L33: 3.2055 L12: 0.9418
REMARK 3 L13: 2.0106 L23: 1.8968
REMARK 3 S TENSOR
REMARK 3 S11: 0.1894 S12: 0.0139 S13: -0.0446
REMARK 3 S21: 0.0792 S22: 0.0134 S23: 0.0244
REMARK 3 S31: -0.1064 S32: 0.1430 S33: -0.2028
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 110 L 212
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7138 12.3864 113.4280
REMARK 3 T TENSOR
REMARK 3 T11: 0.5511 T22: -0.1081
REMARK 3 T33: 0.5100 T12: 0.3969
REMARK 3 T13: -0.2773 T23: -0.5922
REMARK 3 L TENSOR
REMARK 3 L11: 0.3428 L22: 3.3432
REMARK 3 L33: 1.0378 L12: -1.0705
REMARK 3 L13: 0.5964 L23: -1.8627
REMARK 3 S TENSOR
REMARK 3 S11: -0.2965 S12: -0.1750 S13: 0.3310
REMARK 3 S21: 0.2064 S22: -0.0493 S23: 0.6930
REMARK 3 S31: -0.4743 S32: -0.1829 S33: 0.3458
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 195
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0268 -24.8261 39.5992
REMARK 3 T TENSOR
REMARK 3 T11: -0.0267 T22: 0.0288
REMARK 3 T33: 0.0788 T12: -0.0207
REMARK 3 T13: -0.0119 T23: 0.0310
REMARK 3 L TENSOR
REMARK 3 L11: 2.0876 L22: 1.0365
REMARK 3 L33: 0.1507 L12: 0.0911
REMARK 3 L13: 0.3419 L23: 0.0411
REMARK 3 S TENSOR
REMARK 3 S11: -0.0603 S12: 0.2082 S13: -0.0122
REMARK 3 S21: -0.0185 S22: 0.0617 S23: -0.0109
REMARK 3 S31: -0.0251 S32: 0.0205 S33: -0.0014
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 196 A 320
REMARK 3 RESIDUE RANGE : A 1001 A 1001
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9660 -7.3859 57.0914
REMARK 3 T TENSOR
REMARK 3 T11: -0.0197 T22: -0.0150
REMARK 3 T33: 0.1375 T12: 0.0231
REMARK 3 T13: 0.0062 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.3893 L22: 2.0757
REMARK 3 L33: 0.2710 L12: -0.1593
REMARK 3 L13: 0.2549 L23: 0.3531
REMARK 3 S TENSOR
REMARK 3 S11: -0.0912 S12: 0.0055 S13: 0.0691
REMARK 3 S21: 0.2203 S22: 0.0844 S23: 0.0127
REMARK 3 S31: -0.0053 S32: -0.0222 S33: 0.0068
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 321 A 488
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0973 -38.7217 51.6103
REMARK 3 T TENSOR
REMARK 3 T11: -0.0124 T22: -0.0328
REMARK 3 T33: 0.1244 T12: 0.0100
REMARK 3 T13: -0.0567 T23: -0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 1.3097 L22: 1.1772
REMARK 3 L33: 0.5752 L12: 0.3309
REMARK 3 L13: -0.1491 L23: -0.1827
REMARK 3 S TENSOR
REMARK 3 S11: -0.0255 S12: 0.0520 S13: -0.0633
REMARK 3 S21: 0.1222 S22: 0.0517 S23: -0.0810
REMARK 3 S31: 0.0235 S32: -0.0049 S33: -0.0262
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 489 A 607
REMARK 3 RESIDUE RANGE : A 1002 A 1002
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3618 -45.0651 82.0399
REMARK 3 T TENSOR
REMARK 3 T11: 0.1732 T22: 0.0523
REMARK 3 T33: -0.0850 T12: 0.1355
REMARK 3 T13: -0.0948 T23: -0.1061
REMARK 3 L TENSOR
REMARK 3 L11: 2.5972 L22: 0.7191
REMARK 3 L33: 2.4049 L12: 0.7931
REMARK 3 L13: 2.4935 L23: 0.8339
REMARK 3 S TENSOR
REMARK 3 S11: 0.1291 S12: 0.2237 S13: -0.1703
REMARK 3 S21: 0.2505 S22: 0.2294 S23: 0.0561
REMARK 3 S31: 0.2136 S32: 0.2414 S33: -0.3585
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 3BE1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045402.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34149
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.65800
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 3BDY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF THE FAB/HER2 COMPLEX WERE
REMARK 280 OBTAINED BY MIXING PROTEIN SOLUTION (11 MG/ML PROTEIN, 25 MM
REMARK 280 TRIS-HCL PH 8 AND 150 MM SODIUM CHLORIDE) WITH CRYSTALLIZATION
REMARK 280 BUFFER CONTAINING 25% W/V PEG2000, 0.1M MES PH 6.5. BEFORE DATA
REMARK 280 COLLECTION THE CRYSTALS WERE FLASH FROZEN IN LIQUID NITROGEN
REMARK 280 WITH 20% ETHYLENE GLYCOL AS CRYO-PROTECTANT, PH 8.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 31.16200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.08550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.52800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.08550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.16200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.52800
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 APPLY THE FOLLOWING TO CHAINS: A, H, L
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 101
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 465 ASP A 362
REMARK 465 PRO A 363
REMARK 465 ALA A 364
REMARK 465 SER A 365
REMARK 465 GLY A 581
REMARK 465 VAL A 582
REMARK 465 LYS A 583
REMARK 465 PRO A 584
REMARK 465 ASP A 585
REMARK 465 LEU A 586
REMARK 465 SER A 587
REMARK 465 TYR A 588
REMARK 465 MET A 589
REMARK 465 PRO A 590
REMARK 465 CYS A 608
REMARK 465 THR A 609
REMARK 465 HIS A 610
REMARK 465 SER A 611
REMARK 465 CYS A 612
REMARK 465 VAL A 613
REMARK 465 ASP A 614
REMARK 465 LEU A 615
REMARK 465 ASP A 616
REMARK 465 ASP A 617
REMARK 465 LYS A 618
REMARK 465 GLY A 619
REMARK 465 CYS A 620
REMARK 465 PRO A 621
REMARK 465 ALA A 622
REMARK 465 GLU A 623
REMARK 465 GLN A 624
REMARK 465 GLU H -2
REMARK 465 ILE H -1
REMARK 465 SER H 0
REMARK 465 SER H 129
REMARK 465 SER H 130
REMARK 465 LYS H 131
REMARK 465 SER H 132
REMARK 465 THR H 133
REMARK 465 SER H 134
REMARK 465 GLY H 135
REMARK 465 LYS H 216
REMARK 465 SER H 217
REMARK 465 CYS H 218
REMARK 465 ASP H 219
REMARK 465 LYS H 220
REMARK 465 THR H 221
REMARK 465 HIS H 222
REMARK 465 GLU L 213
REMARK 465 CYS L 214
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 ARG L 27D 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 OE1 GLU A 125 O ALA A 219 1.96
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 ASP A 8 78.23 -156.16
REMARK 500 LYS A 10 -123.99 49.30
REMARK 500 THR A 45 -50.61 -19.58
REMARK 500 LEU A 74 40.42 -106.15
REMARK 500 ASN A 89 -40.80 -155.87
REMARK 500 TYR A 141 -12.57 72.13
REMARK 500 LYS A 178 -84.17 -10.74
REMARK 500 ARG A 195 -47.02 -132.33
REMARK 500 CYS A 213 125.85 -6.13
REMARK 500 HIS A 215 154.92 -31.94
REMARK 500 HIS A 235 -76.36 -137.06
REMARK 500 VAL A 286 -8.19 -58.86
REMARK 500 VAL A 292 128.08 -179.66
REMARK 500 LEU A 295 153.91 -45.20
REMARK 500 GLU A 326 -122.12 38.67
REMARK 500 ALA A 343 115.48 -39.49
REMARK 500 PHE A 359 -93.75 -93.12
REMARK 500 ASP A 360 77.28 -41.37
REMARK 500 LEU A 400 42.43 -106.31
REMARK 500 ALA A 418 -51.09 -121.47
REMARK 500 ARG A 495 -2.17 61.16
REMARK 500 GLN A 511 -99.10 -101.34
REMARK 500 HIS A 567 -101.66 -126.03
REMARK 500 GLU A 598 34.28 -87.76
REMARK 500 SER H 25 137.36 -174.23
REMARK 500 ARG H 66 -46.28 -148.03
REMARK 500 ASP H 146 78.73 62.06
REMARK 500 PRO H 151 -159.67 -101.84
REMARK 500 SER H 155 111.52 -164.03
REMARK 500 ASN H 157 -161.96 72.88
REMARK 500 SER H 158 -78.72 -66.23
REMARK 500 SER H 190 -59.08 -164.36
REMARK 500 LEU H 191 -84.41 22.73
REMARK 500 THR H 193 -58.03 -142.56
REMARK 500 GLN H 194 -87.28 -85.85
REMARK 500 THR H 195 145.01 165.52
REMARK 500 ASN H 206 5.00 56.52
REMARK 500 PRO L 27C -78.51 -72.59
REMARK 500 ARG L 27D -113.38 62.57
REMARK 500 SER L 28 95.76 -164.41
REMARK 500 SER L 30 -68.84 -18.68
REMARK 500 SER L 77 76.23 -151.16
REMARK 500 ALA L 84 -179.94 178.77
REMARK 500 THR L 109 127.33 -39.17
REMARK 500 SER L 127 -60.65 -160.73
REMARK 500 ASN L 138 67.57 34.56
REMARK 500 ASP L 151 -80.04 60.87
REMARK 500 LYS L 169 -67.14 -108.66
REMARK 500 SER L 182 -161.20 -75.85
REMARK 500 ALA L 184 -71.20 -58.41
REMARK 500
REMARK 500 THIS ENTRY HAS 52 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 GLY A 427 ILE A 428 144.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BDY RELATED DB: PDB
REMARK 900 RELATED ID: 2JPA RELATED DB: PDB
REMARK 900 RELATED ID: 2JP9 RELATED DB: PDB
DBREF 3BE1 A 1 624 UNP P04626 ERBB2_HUMAN 23 646
DBREF 3BE1 H -2 222 PDB 3BDY 3BDY -2 222
DBREF 3BE1 L 1 214 PDB 3BDY 3BDY 1 214
SEQRES 1 A 624 THR GLN VAL CYS THR GLY THR ASP MET LYS LEU ARG LEU
SEQRES 2 A 624 PRO ALA SER PRO GLU THR HIS LEU ASP MET LEU ARG HIS
SEQRES 3 A 624 LEU TYR GLN GLY CYS GLN VAL VAL GLN GLY ASN LEU GLU
SEQRES 4 A 624 LEU THR TYR LEU PRO THR ASN ALA SER LEU SER PHE LEU
SEQRES 5 A 624 GLN ASP ILE GLN GLU VAL GLN GLY TYR VAL LEU ILE ALA
SEQRES 6 A 624 HIS ASN GLN VAL ARG GLN VAL PRO LEU GLN ARG LEU ARG
SEQRES 7 A 624 ILE VAL ARG GLY THR GLN LEU PHE GLU ASP ASN TYR ALA
SEQRES 8 A 624 LEU ALA VAL LEU ASP ASN GLY ASP PRO LEU ASN ASN THR
SEQRES 9 A 624 THR PRO VAL THR GLY ALA SER PRO GLY GLY LEU ARG GLU
SEQRES 10 A 624 LEU GLN LEU ARG SER LEU THR GLU ILE LEU LYS GLY GLY
SEQRES 11 A 624 VAL LEU ILE GLN ARG ASN PRO GLN LEU CYS TYR GLN ASP
SEQRES 12 A 624 THR ILE LEU TRP LYS ASP ILE PHE HIS LYS ASN ASN GLN
SEQRES 13 A 624 LEU ALA LEU THR LEU ILE ASP THR ASN ARG SER ARG ALA
SEQRES 14 A 624 CYS HIS PRO CYS SER PRO MET CYS LYS GLY SER ARG CYS
SEQRES 15 A 624 TRP GLY GLU SER SER GLU ASP CYS GLN SER LEU THR ARG
SEQRES 16 A 624 THR VAL CYS ALA GLY GLY CYS ALA ARG CYS LYS GLY PRO
SEQRES 17 A 624 LEU PRO THR ASP CYS CYS HIS GLU GLN CYS ALA ALA GLY
SEQRES 18 A 624 CYS THR GLY PRO LYS HIS SER ASP CYS LEU ALA CYS LEU
SEQRES 19 A 624 HIS PHE ASN HIS SER GLY ILE CYS GLU LEU HIS CYS PRO
SEQRES 20 A 624 ALA LEU VAL THR TYR ASN THR ASP THR PHE GLU SER MET
SEQRES 21 A 624 PRO ASN PRO GLU GLY ARG TYR THR PHE GLY ALA SER CYS
SEQRES 22 A 624 VAL THR ALA CYS PRO TYR ASN TYR LEU SER THR ASP VAL
SEQRES 23 A 624 GLY SER CYS THR LEU VAL CYS PRO LEU HIS ASN GLN GLU
SEQRES 24 A 624 VAL THR ALA GLU ASP GLY THR GLN ARG CYS GLU LYS CYS
SEQRES 25 A 624 SER LYS PRO CYS ALA ARG VAL CYS TYR GLY LEU GLY MET
SEQRES 26 A 624 GLU HIS LEU ARG GLU VAL ARG ALA VAL THR SER ALA ASN
SEQRES 27 A 624 ILE GLN GLU PHE ALA GLY CYS LYS LYS ILE PHE GLY SER
SEQRES 28 A 624 LEU ALA PHE LEU PRO GLU SER PHE ASP GLY ASP PRO ALA
SEQRES 29 A 624 SER ASN THR ALA PRO LEU GLN PRO GLU GLN LEU GLN VAL
SEQRES 30 A 624 PHE GLU THR LEU GLU GLU ILE THR GLY TYR LEU TYR ILE
SEQRES 31 A 624 SER ALA TRP PRO ASP SER LEU PRO ASP LEU SER VAL PHE
SEQRES 32 A 624 GLN ASN LEU GLN VAL ILE ARG GLY ARG ILE LEU HIS ASN
SEQRES 33 A 624 GLY ALA TYR SER LEU THR LEU GLN GLY LEU GLY ILE SER
SEQRES 34 A 624 TRP LEU GLY LEU ARG SER LEU ARG GLU LEU GLY SER GLY
SEQRES 35 A 624 LEU ALA LEU ILE HIS HIS ASN THR HIS LEU CYS PHE VAL
SEQRES 36 A 624 HIS THR VAL PRO TRP ASP GLN LEU PHE ARG ASN PRO HIS
SEQRES 37 A 624 GLN ALA LEU LEU HIS THR ALA ASN ARG PRO GLU ASP GLU
SEQRES 38 A 624 CYS VAL GLY GLU GLY LEU ALA CYS HIS GLN LEU CYS ALA
SEQRES 39 A 624 ARG GLY HIS CYS TRP GLY PRO GLY PRO THR GLN CYS VAL
SEQRES 40 A 624 ASN CYS SER GLN PHE LEU ARG GLY GLN GLU CYS VAL GLU
SEQRES 41 A 624 GLU CYS ARG VAL LEU GLN GLY LEU PRO ARG GLU TYR VAL
SEQRES 42 A 624 ASN ALA ARG HIS CYS LEU PRO CYS HIS PRO GLU CYS GLN
SEQRES 43 A 624 PRO GLN ASN GLY SER VAL THR CYS PHE GLY PRO GLU ALA
SEQRES 44 A 624 ASP GLN CYS VAL ALA CYS ALA HIS TYR LYS ASP PRO PRO
SEQRES 45 A 624 PHE CYS VAL ALA ARG CYS PRO SER GLY VAL LYS PRO ASP
SEQRES 46 A 624 LEU SER TYR MET PRO ILE TRP LYS PHE PRO ASP GLU GLU
SEQRES 47 A 624 GLY ALA CYS GLN PRO CYS PRO ILE ASN CYS THR HIS SER
SEQRES 48 A 624 CYS VAL ASP LEU ASP ASP LYS GLY CYS PRO ALA GLU GLN
SEQRES 1 H 230 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY
SEQRES 2 H 230 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA
SEQRES 3 H 230 ALA SER GLY PHE ASN ILE LYS ASP THR TYR ILE HIS TRP
SEQRES 4 H 230 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA
SEQRES 5 H 230 ARG ILE TYR PRO THR ASN GLY TYR THR ARG TYR ALA ASP
SEQRES 6 H 230 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER
SEQRES 7 H 230 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA
SEQRES 8 H 230 GLU ASP THR ALA VAL TYR TYR CYS SER ARG TRP GLY GLY
SEQRES 9 H 230 ASP GLY PHE TYR ALA MET ASP TYR TRP GLY GLN GLY THR
SEQRES 10 H 230 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER
SEQRES 11 H 230 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY
SEQRES 12 H 230 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE
SEQRES 13 H 230 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU
SEQRES 14 H 230 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER
SEQRES 15 H 230 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO
SEQRES 16 H 230 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL
SEQRES 17 H 230 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL
SEQRES 18 H 230 GLU PRO LYS SER CYS ASP LYS THR HIS
SEQRES 1 L 218 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 L 218 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 L 218 GLN ASP ILE PRO ARG SER ILE SER GLY TYR VAL ALA TRP
SEQRES 4 L 218 TYR GLN GLN LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE
SEQRES 5 L 218 TYR TRP GLY SER TYR LEU TYR SER GLY VAL PRO SER ARG
SEQRES 6 L 218 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU THR
SEQRES 7 L 218 ILE SER SER LEU GLN PRO GLU ASP PHE ALA THR TYR TYR
SEQRES 8 L 218 CYS GLN GLN HIS TYR THR THR PRO PRO THR PHE GLY GLN
SEQRES 9 L 218 GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO
SEQRES 10 L 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS
SEQRES 11 L 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE
SEQRES 12 L 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN
SEQRES 13 L 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU
SEQRES 14 L 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR
SEQRES 15 L 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL
SEQRES 16 L 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO
SEQRES 17 L 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS
MODRES 3BE1 ASN A 237 ASN GLYCOSYLATION SITE
MODRES 3BE1 ASN A 508 ASN GLYCOSYLATION SITE
HET NAG A1001 14
HET NAG A1002 14
HET MES L 215 12
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
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 4 NAG 2(C8 H15 N O6)
FORMUL 6 MES C6 H13 N O4 S
HELIX 1 1 SER A 16 GLN A 29 1 14
HELIX 2 2 LEU A 49 ILE A 55 5 7
HELIX 3 3 LEU A 85 ASP A 88 5 4
HELIX 4 4 TYR A 141 ILE A 145 5 5
HELIX 5 5 LEU A 146 PHE A 151 1 6
HELIX 6 6 HIS A 152 GLN A 156 5 5
HELIX 7 7 MET A 325 ARG A 329 5 5
HELIX 8 8 THR A 335 ALA A 343 5 9
HELIX 9 9 LEU A 355 PHE A 359 5 5
HELIX 10 10 GLN A 371 LEU A 381 5 11
HELIX 11 11 LEU A 400 GLN A 404 5 5
HELIX 12 12 LEU A 414 GLY A 417 5 4
HELIX 13 13 PRO A 459 PHE A 464 1 6
HELIX 14 14 PRO A 478 GLY A 484 1 7
HELIX 15 15 CYS A 493 HIS A 497 5 5
HELIX 16 16 ASN H 28 THR H 32 5 5
HELIX 17 17 ARG H 83 THR H 87 5 5
HELIX 18 18 LYS H 203 ASN H 206 5 4
HELIX 19 19 ILE L 29 GLY L 31 5 3
HELIX 20 20 GLN L 79 PHE L 83 5 5
HELIX 21 21 SER L 121 LYS L 126 1 6
SHEET 1 A 5 VAL A 3 THR A 5 0
SHEET 2 A 5 VAL A 33 GLN A 35 1 O GLN A 35 N CYS A 4
SHEET 3 A 5 GLU A 57 VAL A 58 1 O GLU A 57 N VAL A 34
SHEET 4 A 5 ILE A 79 VAL A 80 1 O ILE A 79 N VAL A 58
SHEET 5 A 5 GLU A 125 ILE A 126 1 O GLU A 125 N VAL A 80
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 LEU A 95 1 O ALA A 91 N VAL A 62
SHEET 4 B 5 GLY A 130 GLN A 134 1 O LEU A 132 N VAL A 94
SHEET 5 B 5 THR A 160 ILE A 162 1 O LEU A 161 N ILE A 133
SHEET 1 C 2 PHE A 236 HIS A 238 0
SHEET 2 C 2 ILE A 241 GLU A 243 -1 O ILE A 241 N HIS A 238
SHEET 1 D 2 VAL A 250 TYR A 252 0
SHEET 2 D 2 SER A 259 PRO A 261 -1 O MET A 260 N THR A 251
SHEET 1 E 2 TYR A 267 PHE A 269 0
SHEET 2 E 2 SER A 272 VAL A 274 -1 O VAL A 274 N TYR A 267
SHEET 1 F 4 CYS A 289 THR A 290 0
SHEET 2 F 4 LEU A 282 THR A 284 -1 N LEU A 282 O THR A 290
SHEET 3 F 4 GLN A 307 LYS A 311 1 O CYS A 309 N SER A 283
SHEET 4 F 4 ASN A 297 THR A 301 -1 N VAL A 300 O ARG A 308
SHEET 1 G 5 CYS A 320 TYR A 321 0
SHEET 2 G 5 LYS A 347 PHE A 349 1 O PHE A 349 N CYS A 320
SHEET 3 G 5 GLU A 383 ILE A 384 1 O GLU A 383 N ILE A 348
SHEET 4 G 5 VAL A 408 ILE A 409 1 O VAL A 408 N ILE A 384
SHEET 5 G 5 GLU A 438 LEU A 439 1 O GLU A 438 N ILE A 409
SHEET 1 H 5 LEU A 352 PHE A 354 0
SHEET 2 H 5 LEU A 388 ILE A 390 1 O TYR A 389 N PHE A 354
SHEET 3 H 5 TYR A 419 GLN A 424 1 O THR A 422 N ILE A 390
SHEET 4 H 5 LEU A 443 HIS A 447 1 O LEU A 445 N LEU A 421
SHEET 5 H 5 LEU A 471 THR A 474 1 O LEU A 472 N ALA A 444
SHEET 1 I 2 PHE A 512 ARG A 514 0
SHEET 2 I 2 GLU A 517 VAL A 519 -1 O GLU A 517 N ARG A 514
SHEET 1 J 2 GLU A 531 VAL A 533 0
SHEET 2 J 2 CYS A 538 PRO A 540 -1 O LEU A 539 N TYR A 532
SHEET 1 K 2 TYR A 568 ASP A 570 0
SHEET 2 K 2 PHE A 573 VAL A 575 -1 O PHE A 573 N ASP A 570
SHEET 1 L 2 LYS A 593 PRO A 595 0
SHEET 2 L 2 CYS A 601 PRO A 603 -1 O GLN A 602 N PHE A 594
SHEET 1 M 4 GLN H 3 SER H 7 0
SHEET 2 M 4 SER H 17 SER H 25 -1 O ALA H 23 N VAL H 5
SHEET 3 M 4 THR H 77 ASN H 82A-1 O ALA H 78 N CYS H 22
SHEET 4 M 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79
SHEET 1 N 6 LEU H 11 VAL H 12 0
SHEET 2 N 6 THR H 109 VAL H 113 1 O THR H 112 N VAL H 12
SHEET 3 N 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 109
SHEET 4 N 6 ILE H 34 GLN H 39 -1 N HIS H 35 O SER H 93
SHEET 5 N 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 N 6 THR H 57 TYR H 59 -1 O ARG H 58 N ARG H 50
SHEET 1 O 4 LEU H 11 VAL H 12 0
SHEET 2 O 4 THR H 109 VAL H 113 1 O THR H 112 N VAL H 12
SHEET 3 O 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 109
SHEET 4 O 4 TYR H 104 TRP H 105 -1 O TYR H 104 N ARG H 94
SHEET 1 P 4 SER H 122 PHE H 124 0
SHEET 2 P 4 THR H 137 TYR H 147 -1 O LEU H 143 N PHE H 124
SHEET 3 P 4 SER H 182 PRO H 187 -1 O VAL H 186 N ALA H 138
SHEET 4 P 4 VAL H 165 THR H 167 -1 N HIS H 166 O VAL H 183
SHEET 1 Q 3 SER H 122 PHE H 124 0
SHEET 2 Q 3 THR H 137 TYR H 147 -1 O LEU H 143 N PHE H 124
SHEET 3 Q 3 TYR H 178 SER H 179 -1 O TYR H 178 N TYR H 147
SHEET 1 R 3 SER H 155 TRP H 156 0
SHEET 2 R 3 CYS H 198 HIS H 202 -1 O ASN H 199 N SER H 155
SHEET 3 R 3 THR H 207 VAL H 209 -1 O VAL H 209 N VAL H 200
SHEET 1 S 4 GLN L 3 SER L 7 0
SHEET 2 S 4 VAL L 19 SER L 26 -1 O THR L 22 N SER L 7
SHEET 3 S 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23
SHEET 4 S 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72
SHEET 1 T 6 SER L 10 ALA L 13 0
SHEET 2 T 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11
SHEET 3 T 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104
SHEET 4 T 6 VAL L 33 GLN L 38 -1 N TYR L 36 O TYR L 87
SHEET 5 T 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37
SHEET 6 T 6 TYR L 53 LEU L 54 -1 O TYR L 53 N TYR L 49
SHEET 1 U 4 SER L 10 ALA L 13 0
SHEET 2 U 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11
SHEET 3 U 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104
SHEET 4 U 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 V 4 PHE L 116 PHE L 118 0
SHEET 2 V 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 V 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139
SHEET 4 V 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176
SHEET 1 W 4 ALA L 153 LEU L 154 0
SHEET 2 W 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 W 4 TYR L 192 THR L 197 -1 O GLU L 195 N GLN L 147
SHEET 4 W 4 VAL L 205 THR L 206 -1 O VAL L 205 N VAL L 196
SSBOND 1 CYS A 4 CYS A 31 1555 1555 2.04
SSBOND 2 CYS A 140 CYS A 170 1555 1555 2.05
SSBOND 3 CYS A 173 CYS A 182 1555 1555 2.03
SSBOND 4 CYS A 177 CYS A 190 1555 1555 2.04
SSBOND 5 CYS A 198 CYS A 205 1555 1555 2.04
SSBOND 6 CYS A 202 CYS A 213 1555 1555 2.03
SSBOND 7 CYS A 214 CYS A 222 1555 1555 2.05
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 2.03
SSBOND 12 CYS A 293 CYS A 309 1555 1555 2.05
SSBOND 13 CYS A 312 CYS A 316 1555 1555 2.03
SSBOND 14 CYS A 320 CYS A 345 1555 1555 2.03
SSBOND 15 CYS A 453 CYS A 482 1555 1555 2.02
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 2.02
SSBOND 20 CYS A 541 CYS A 554 1555 1555 2.04
SSBOND 21 CYS A 545 CYS A 562 1555 1555 2.03
SSBOND 22 CYS A 565 CYS A 574 1555 1555 2.03
SSBOND 23 CYS A 578 CYS A 601 1555 1555 2.79
SSBOND 24 CYS H 22 CYS H 92 1555 1555 2.03
SSBOND 25 CYS H 142 CYS H 198 1555 1555 2.04
SSBOND 26 CYS L 23 CYS L 88 1555 1555 2.05
SSBOND 27 CYS L 134 CYS L 194 1555 1555 2.04
LINK ND2 ASN A 237 C1 NAG A1001 1555 1555 2.00
LINK ND2 ASN A 508 C1 NAG A1002 1555 1555 2.00
CISPEP 1 SER A 111 PRO A 112 0 -15.48
CISPEP 2 PRO A 571 PRO A 572 0 9.52
CISPEP 3 PHE H 148 PRO H 149 0 -9.13
CISPEP 4 GLU H 150 PRO H 151 0 -3.20
CISPEP 5 SER L 7 PRO L 8 0 -1.71
CISPEP 6 THR L 94 PRO L 95 0 5.10
CISPEP 7 TYR L 140 PRO L 141 0 1.06
CRYST1 62.324 115.056 208.171 90.00 90.00 90.00 P 21 21 21 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 0.016045 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008691 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004804 0.00000
(ATOM LINES ARE NOT SHOWN.)
END