HEADER ONCOPROTEIN 21-JAN-22 7QVK TITLE NM-02 IN COMPLEX WITH HER2-ECD COMPND MOL_ID: 1; COMPND 2 MOLECULE: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2; COMPND 3 CHAIN: AAA; COMPND 4 SYNONYM: METASTATIC LYMPH NODE GENE 19 PROTEIN,MLN 19,PROTO-ONCOGENE COMPND 5 NEU,PROTO-ONCOGENE C-ERBB-2,TYROSINE KINASE-TYPE CELL SURFACE COMPND 6 RECEPTOR HER2,P185ERBB2; COMPND 7 EC: 2.7.10.1; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: NM-02; COMPND 11 CHAIN: BBB; COMPND 12 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, MLN19, NEU, NGL; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: CAMELUS BACTRIANUS; SOURCE 11 ORGANISM_TAXID: 9837; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: EXPICHO-S KEYWDS RECEPTOR TYROSINE PROTEIN KINASE, ONCOPROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR R.COWAN,G.HALL,M.CARR JRNL AUTH G.HALL,N.WONG,S.DAVIES,R.COWAN,R.BROWN,D.TANG,M.HENRY, JRNL AUTH 2 D.TICKLE,D.MATTHEWS,M.CARR,P.BAKRANIA,H.H.TING,K.SAWMYNADEN JRNL TITL CO-CRYSTALLISATION AND HUMANISATION OF AN ANTI-HER2 JRNL TITL 2 SINGLE-DOMAIN ANTIBODY WITH POTENTIAL AS A THERANOSTIC TOOL JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.32 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 22447 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM SELECTION REMARK 3 R VALUE (WORKING + TEST SET) : 0.275 REMARK 3 R VALUE (WORKING SET) : 0.275 REMARK 3 FREE R VALUE : 0.330 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.284 REMARK 3 FREE R VALUE TEST SET COUNT : 1186 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1538 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.56 REMARK 3 BIN R VALUE (WORKING SET) : 0.4470 REMARK 3 BIN FREE R VALUE SET COUNT : 57 REMARK 3 BIN FREE R VALUE : 0.3990 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4783 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 53 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 101.2 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 105.6 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.44100 REMARK 3 B22 (A**2) : -3.44100 REMARK 3 B33 (A**2) : 11.16300 REMARK 3 B12 (A**2) : -1.72100 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): 1.380 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.497 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.851 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.777 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4963 ; 0.004 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 4457 ; 0.036 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6767 ; 1.406 ; 1.658 REMARK 3 BOND ANGLES OTHERS (DEGREES): 10284 ; 2.586 ; 1.586 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 623 ; 6.404 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 255 ;34.735 ;22.627 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 764 ;17.891 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;12.787 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 651 ; 0.050 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5706 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1139 ; 0.004 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1145 ; 0.223 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 40 ; 0.192 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2367 ; 0.161 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 125 ; 0.193 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.142 ; 0.200 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): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL 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): 2504 ; 5.052 ;11.337 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2503 ; 5.053 ;11.335 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3123 ; 8.358 ;16.983 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3124 ; 8.357 ;16.985 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2459 ; 4.345 ;11.630 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2459 ; 4.345 ;11.630 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3644 ; 7.346 ;17.355 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3645 ; 7.345 ;17.356 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 BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 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 THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 7QVK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292120441. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-JUN-19 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 : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.96872 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22490 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 65.324 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 19.20 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 19.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.700 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: 5MY6 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.65 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG6000 (W/V), 0.1 M MES PH 6.5, REMARK 280 7% 2-METHYL-2,4-PENTANEDIOL, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 123.92133 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 61.96067 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 61.96067 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 123.92133 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2060 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29150 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAA, BBB, AbA 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 THR A 23 REMARK 465 LEU A 123 REMARK 465 ASN A 124 REMARK 465 ASN A 125 REMARK 465 THR A 126 REMARK 465 THR A 127 REMARK 465 PRO A 128 REMARK 465 VAL A 129 REMARK 465 THR A 130 REMARK 465 GLY A 131 REMARK 465 ALA A 132 REMARK 465 SER A 335 REMARK 465 LYS A 336 REMARK 465 GLU A 542 REMARK 465 GLU A 543 REMARK 465 CYS A 544 REMARK 465 ARG A 545 REMARK 465 VAL A 546 REMARK 465 LEU A 547 REMARK 465 GLN A 548 REMARK 465 GLY A 549 REMARK 465 LEU A 550 REMARK 465 PRO A 551 REMARK 465 ARG A 552 REMARK 465 GLU A 553 REMARK 465 TYR A 554 REMARK 465 VAL A 555 REMARK 465 ASN A 556 REMARK 465 ALA A 557 REMARK 465 ARG A 558 REMARK 465 HIS A 559 REMARK 465 CYS A 560 REMARK 465 LEU A 561 REMARK 465 PRO A 562 REMARK 465 CYS A 563 REMARK 465 HIS A 564 REMARK 465 PRO A 565 REMARK 465 GLU A 566 REMARK 465 CYS A 567 REMARK 465 GLN A 568 REMARK 465 PRO A 569 REMARK 465 GLN A 570 REMARK 465 ASN A 571 REMARK 465 GLY A 572 REMARK 465 SER A 573 REMARK 465 VAL A 574 REMARK 465 THR A 575 REMARK 465 CYS A 576 REMARK 465 PHE A 577 REMARK 465 GLY A 578 REMARK 465 PRO A 579 REMARK 465 GLU A 580 REMARK 465 ALA A 581 REMARK 465 ASP A 582 REMARK 465 GLN A 583 REMARK 465 CYS A 584 REMARK 465 VAL A 585 REMARK 465 ALA A 586 REMARK 465 CYS A 587 REMARK 465 ALA A 588 REMARK 465 HIS A 589 REMARK 465 TYR A 590 REMARK 465 LYS A 591 REMARK 465 ASP A 592 REMARK 465 PRO A 593 REMARK 465 PRO A 594 REMARK 465 PHE A 595 REMARK 465 CYS A 596 REMARK 465 VAL A 597 REMARK 465 ALA A 598 REMARK 465 ARG A 599 REMARK 465 CYS A 600 REMARK 465 PRO A 601 REMARK 465 SER A 602 REMARK 465 GLY A 603 REMARK 465 VAL A 604 REMARK 465 LYS A 605 REMARK 465 PRO A 606 REMARK 465 ASP A 607 REMARK 465 LEU A 608 REMARK 465 SER A 609 REMARK 465 TYR A 610 REMARK 465 MET A 611 REMARK 465 PRO A 612 REMARK 465 ILE A 613 REMARK 465 TRP A 614 REMARK 465 LYS A 615 REMARK 465 PHE A 616 REMARK 465 PRO A 617 REMARK 465 ASP A 618 REMARK 465 GLU A 619 REMARK 465 GLU A 620 REMARK 465 GLY A 621 REMARK 465 ALA A 622 REMARK 465 CYS A 623 REMARK 465 GLN A 624 REMARK 465 PRO A 625 REMARK 465 CYS A 626 REMARK 465 PRO A 627 REMARK 465 ILE A 628 REMARK 465 ASN A 629 REMARK 465 CYS A 630 REMARK 465 THR A 631 REMARK 465 HIS A 632 REMARK 465 SER A 633 REMARK 465 CYS A 634 REMARK 465 VAL A 635 REMARK 465 ASP A 636 REMARK 465 LEU A 637 REMARK 465 ASP A 638 REMARK 465 ASP A 639 REMARK 465 LYS A 640 REMARK 465 GLY A 641 REMARK 465 CYS A 642 REMARK 465 PRO A 643 REMARK 465 ALA A 644 REMARK 465 GLU A 645 REMARK 465 GLN A 646 REMARK 465 HIS A 647 REMARK 465 HIS A 648 REMARK 465 HIS A 649 REMARK 465 HIS A 650 REMARK 465 HIS A 651 REMARK 465 HIS A 652 REMARK 465 GLN B 1 REMARK 465 VAL B 2 REMARK 465 GLY B 124 REMARK 465 SER B 125 REMARK 465 GLY B 126 REMARK 465 HIS B 127 REMARK 465 HIS B 128 REMARK 465 HIS B 129 REMARK 465 HIS B 130 REMARK 465 HIS B 131 REMARK 465 HIS B 132 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 200 CG CD CE NZ REMARK 470 HIS A 318 CG ND1 CD2 CE1 NE2 REMARK 470 GLN A 320 CG CD OE1 NE2 REMARK 470 GLU A 325 CG CD OE1 OE2 REMARK 470 LYS A 333 CG CD CE NZ REMARK 470 ARG A 351 NE CZ NH1 NH2 REMARK 470 GLU B 98 CG CD OE1 OE2 REMARK 470 ARG B 101 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 O4 NAGbA 2 H1 BMAbA 3 1.15 REMARK 500 O4 NAGbA 1 H1 NAGbA 2 1.23 REMARK 500 H LEUAA 168 HE21 GLNAA 213 1.29 REMARK 500 HE2 TYRAA 343 OE1 GLUAA 348 1.39 REMARK 500 HD2 TYRAA 343 OE1 GLUAA 348 1.43 REMARK 500 H GLYAA 346 O LEUAA 350 1.49 REMARK 500 O3 NAGbA 2 HO2 BMAbA 3 1.54 REMARK 500 C4 NAGbA 1 H1 NAGbA 2 1.55 REMARK 500 O GLNAA 24 H GLNAA 54 1.55 REMARK 500 H TYRBB 37 O TYRBB 94 1.55 REMARK 500 ND2 ASNAA 59 HE1 TYRAA 83 1.56 REMARK 500 H ARGAA 487 OE1 GLNAA 491 1.59 REMARK 500 CE2 TYRAA 343 OE1 GLUAA 348 1.65 REMARK 500 CD2 TYRAA 343 OE1 GLUAA 348 1.68 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 HH21 ARGAA 340 O THRBB 17 3665 1.48 REMARK 500 NH2 ARGAA 340 O THRBB 17 3665 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 ASNAA 158 C PROAA 159 N 0.165 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 PROAA 159 C - N - CA ANGL. DEV. = 16.9 DEGREES REMARK 500 PROAA 159 C - N - CD ANGL. DEV. = -16.4 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 ASPAA 30 60.66 -161.02 REMARK 500 LYSAA 32 -141.82 68.44 REMARK 500 SERAA 38 72.04 -116.14 REMARK 500 GLNAA 78 -37.35 -134.55 REMARK 500 ASPAA 118 76.64 49.79 REMARK 500 ASPAA 121 161.37 81.22 REMARK 500 ASNAA 158 100.39 -163.02 REMARK 500 ASNAA 187 114.13 -34.92 REMARK 500 SERAA 189 49.87 -140.28 REMARK 500 HISAA 193 107.86 -43.29 REMARK 500 ARGAA 217 -66.25 -125.86 REMARK 500 ALAAA 242 -4.69 79.20 REMARK 500 LYSAA 248 173.15 -57.44 REMARK 500 HISAA 257 -70.74 -122.55 REMARK 500 PHEAA 279 25.47 87.75 REMARK 500 PROAA 316 170.74 -54.42 REMARK 500 ARGAA 330 -154.67 -121.96 REMARK 500 CYSAA 331 94.66 -162.16 REMARK 500 GLUAA 348 -130.70 53.50 REMARK 500 ASNAA 388 19.33 81.97 REMARK 500 ASNAA 438 15.37 55.86 REMARK 500 LEUAA 453 -72.89 -102.17 REMARK 500 LEUAA 458 98.84 -59.38 REMARK 500 VALAA 529 -70.32 -79.57 REMARK 500 ARGAA 536 50.16 -156.70 REMARK 500 CYSBB 22 79.83 -105.49 REMARK 500 PHEBB 27 -178.10 64.90 REMARK 500 SERBB 32 76.70 -164.30 REMARK 500 ALABB 96 130.02 -175.78 REMARK 500 TYRBB 102 -154.61 -85.07 REMARK 500 GLUBB 103 -51.82 -131.76 REMARK 500 REMARK 500 REMARK: NULL DBREF 7QVKAA 23 646 UNP P04626 ERBB2_HUMAN 23 646 DBREF 7QVKBB 1 132 PDB 7QVK 7QVK 1 132 SEQADV 7QVK HISAA 647 UNP P04626 EXPRESSION TAG SEQADV 7QVK HISAA 648 UNP P04626 EXPRESSION TAG SEQADV 7QVK HISAA 649 UNP P04626 EXPRESSION TAG SEQADV 7QVK HISAA 650 UNP P04626 EXPRESSION TAG SEQADV 7QVK HISAA 651 UNP P04626 EXPRESSION TAG SEQADV 7QVK HISAA 652 UNP P04626 EXPRESSION TAG SEQRES 1AA 630 THR GLN VAL CYS THR GLY THR ASP MET LYS LEU ARG LEU SEQRES 2AA 630 PRO ALA SER PRO GLU THR HIS LEU ASP MET LEU ARG HIS SEQRES 3AA 630 LEU TYR GLN GLY CYS GLN VAL VAL GLN GLY ASN LEU GLU SEQRES 4AA 630 LEU THR TYR LEU PRO THR ASN ALA SER LEU SER PHE LEU SEQRES 5AA 630 GLN ASP ILE GLN GLU VAL GLN GLY TYR VAL LEU ILE ALA SEQRES 6AA 630 HIS ASN GLN VAL ARG GLN VAL PRO LEU GLN ARG LEU ARG SEQRES 7AA 630 ILE VAL ARG GLY THR GLN LEU PHE GLU ASP ASN TYR ALA SEQRES 8AA 630 LEU ALA VAL LEU ASP ASN GLY ASP PRO LEU ASN ASN THR SEQRES 9AA 630 THR PRO VAL THR GLY ALA SER PRO GLY GLY LEU ARG GLU SEQRES 10AA 630 LEU GLN LEU ARG SER LEU THR GLU ILE LEU LYS GLY GLY SEQRES 11AA 630 VAL LEU ILE GLN ARG ASN PRO GLN LEU CYS TYR GLN ASP SEQRES 12AA 630 THR ILE LEU TRP LYS ASP ILE PHE HIS LYS ASN ASN GLN SEQRES 13AA 630 LEU ALA LEU THR LEU ILE ASP THR ASN ARG SER ARG ALA SEQRES 14AA 630 CYS HIS PRO CYS SER PRO MET CYS LYS GLY SER ARG CYS SEQRES 15AA 630 TRP GLY GLU SER SER GLU ASP CYS GLN SER LEU THR ARG SEQRES 16AA 630 THR VAL CYS ALA GLY GLY CYS ALA ARG CYS LYS GLY PRO SEQRES 17AA 630 LEU PRO THR ASP CYS CYS HIS GLU GLN CYS ALA ALA GLY SEQRES 18AA 630 CYS THR GLY PRO LYS HIS SER ASP CYS LEU ALA CYS LEU SEQRES 19AA 630 HIS PHE ASN HIS SER GLY ILE CYS GLU LEU HIS CYS PRO SEQRES 20AA 630 ALA LEU VAL THR TYR ASN THR ASP THR PHE GLU SER MET SEQRES 21AA 630 PRO ASN PRO GLU GLY ARG TYR THR PHE GLY ALA SER CYS SEQRES 22AA 630 VAL THR ALA CYS PRO TYR ASN TYR LEU SER THR ASP VAL SEQRES 23AA 630 GLY SER CYS THR LEU VAL CYS PRO LEU HIS ASN GLN GLU SEQRES 24AA 630 VAL THR ALA GLU ASP GLY THR GLN ARG CYS GLU LYS CYS SEQRES 25AA 630 SER LYS PRO CYS ALA ARG VAL CYS TYR GLY LEU GLY MET SEQRES 26AA 630 GLU HIS LEU ARG GLU VAL ARG ALA VAL THR SER ALA ASN SEQRES 27AA 630 ILE GLN GLU PHE ALA GLY CYS LYS LYS ILE PHE GLY SER SEQRES 28AA 630 LEU ALA PHE LEU PRO GLU SER PHE ASP GLY ASP PRO ALA SEQRES 29AA 630 SER ASN THR ALA PRO LEU GLN PRO GLU GLN LEU GLN VAL SEQRES 30AA 630 PHE GLU THR LEU GLU GLU ILE THR GLY TYR LEU TYR ILE SEQRES 31AA 630 SER ALA TRP PRO ASP SER LEU PRO ASP LEU SER VAL PHE SEQRES 32AA 630 GLN ASN LEU GLN VAL ILE ARG GLY ARG ILE LEU HIS ASN SEQRES 33AA 630 GLY ALA TYR SER LEU THR LEU GLN GLY LEU GLY ILE SER SEQRES 34AA 630 TRP LEU GLY LEU ARG SER LEU ARG GLU LEU GLY SER GLY SEQRES 35AA 630 LEU ALA LEU ILE HIS HIS ASN THR HIS LEU CYS PHE VAL SEQRES 36AA 630 HIS THR VAL PRO TRP ASP GLN LEU PHE ARG ASN PRO HIS SEQRES 37AA 630 GLN ALA LEU LEU HIS THR ALA ASN ARG PRO GLU ASP GLU SEQRES 38AA 630 CYS VAL GLY GLU GLY LEU ALA CYS HIS GLN LEU CYS ALA SEQRES 39AA 630 ARG GLY HIS CYS TRP GLY PRO GLY PRO THR GLN CYS VAL SEQRES 40AA 630 ASN CYS SER GLN PHE LEU ARG GLY GLN GLU CYS VAL GLU SEQRES 41AA 630 GLU CYS ARG VAL LEU GLN GLY LEU PRO ARG GLU TYR VAL SEQRES 42AA 630 ASN ALA ARG HIS CYS LEU PRO CYS HIS PRO GLU CYS GLN SEQRES 43AA 630 PRO GLN ASN GLY SER VAL THR CYS PHE GLY PRO GLU ALA SEQRES 44AA 630 ASP GLN CYS VAL ALA CYS ALA HIS TYR LYS ASP PRO PRO SEQRES 45AA 630 PHE CYS VAL ALA ARG CYS PRO SER GLY VAL LYS PRO ASP SEQRES 46AA 630 LEU SER TYR MET PRO ILE TRP LYS PHE PRO ASP GLU GLU SEQRES 47AA 630 GLY ALA CYS GLN PRO CYS PRO ILE ASN CYS THR HIS SER SEQRES 48AA 630 CYS VAL ASP LEU ASP ASP LYS GLY CYS PRO ALA GLU GLN SEQRES 49AA 630 HIS HIS HIS HIS HIS HIS SEQRES 1BB 132 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL GLN SEQRES 2BB 132 ALA GLY GLU THR LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3BB 132 PHE THR PHE ASP ASP SER ASP MET GLY TRP TYR ARG GLN SEQRES 4BB 132 ALA PRO GLY ASN GLU CYS GLU LEU VAL SER SER ILE SER SEQRES 5BB 132 SER ASP GLY SER THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6BB 132 ARG PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR VAL SEQRES 7BB 132 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR GLY SEQRES 8BB 132 VAL TYR TYR CYS ALA ALA GLU GLY HIS ARG TYR GLU LEU SEQRES 9BB 132 GLY THR CYS ALA ALA LEU ASP TYR TRP GLY ARG GLY THR SEQRES 10BB 132 GLN VAL THR VAL SER SER GLY SER GLY HIS HIS HIS HIS SEQRES 11BB 132 HIS HIS HET NAG AA 700 28 HET NAG bA 1 27 HET NAG bA 2 27 HET BMA bA 3 22 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE FORMUL 3 NAG 3(C8 H15 N O6) FORMUL 4 BMA C6 H12 O6 HELIX 1 AA1 SERAA 38 GLNAA 51 1 14 HELIX 2 AA2 PHEAA 73 ILEAA 77 5 5 HELIX 3 AA3 LEUAA 107 ASPAA 110 5 4 HELIX 4 AA4 LEUAA 168 PHEAA 173 1 6 HELIX 5 AA5 CYSAA 199 ARGAA 203 5 5 HELIX 6 AA6 LEUAA 231 CYSAA 235 5 5 HELIX 7 AA7 METAA 347 GLUAA 352 5 6 HELIX 8 AA8 ASNAA 360 ALAAA 365 5 6 HELIX 9 AA9 LEUAA 377 GLYAA 383 1 7 HELIX 10 AB1 GLUAA 395 THRAA 402 5 8 HELIX 11 AB2 LEUAA 436 GLYAA 439 5 4 HELIX 12 AB3 PROAA 481 LEUAA 485 5 5 HELIX 13 AB4 PROAA 500 GLUAA 507 1 8 HELIX 14 AB5 CYSAA 515 HISAA 519 5 5 HELIX 15 AB6 LYSBB 86 THRBB 90 5 5 HELIX 16 AB7 GLYBB 105 TRPBB 113 1 9 SHEET 1 AA1 5 VALAA 25 THRAA 27 0 SHEET 2 AA1 5 VALAA 55 GLNAA 57 1 O GLNAA 57 N CYSAA 26 SHEET 3 AA1 5 GLUAA 79 VALAA 80 1 O GLUAA 79 N VALAA 56 SHEET 4 AA1 5 ILEAA 101 VALAA 102 1 O ILEAA 101 N VALAA 80 SHEET 5 AA1 5 GLUAA 147 ILEAA 148 1 O GLUAA 147 N VALAA 102 SHEET 1 AA2 5 GLUAA 61 THRAA 63 0 SHEET 2 AA2 5 VALAA 84 ALAAA 87 1 O LEUAA 85 N LEUAA 62 SHEET 3 AA2 5 TYRAA 112 LEUAA 117 1 O ALAAA 115 N VALAA 84 SHEET 4 AA2 5 GLYAA 152 ILEAA 155 1 O GLYAA 152 N ALAAA 113 SHEET 5 AA2 5 THRAA 182 ILEAA 184 1 O LEUAA 183 N VALAA 153 SHEET 1 AA3 2 CYSAA 240 CYSAA 244 0 SHEET 2 AA3 2 CYSAA 252 CYSAA 255 -1 O ALAAA 254 N ALAAA 241 SHEET 1 AA4 2 VALAA 272 TYRAA 274 0 SHEET 2 AA4 2 SERAA 281 PROAA 283 -1 O METAA 282 N THRAA 273 SHEET 1 AA5 2 TYRAA 289 PHEAA 291 0 SHEET 2 AA5 2 SERAA 294 VALAA 296 -1 O VALAA 296 N TYRAA 289 SHEET 1 AA6 2 LEUAA 304 SERAA 305 0 SHEET 2 AA6 2 CYSAA 311 THRAA 312 -1 O THRAA 312 N LEUAA 304 SHEET 1 AA7 2 ASNAA 319 VALAA 322 0 SHEET 2 AA7 2 ARGAA 330 LYSAA 333 -1 O GLUAA 332 N GLNAA 320 SHEET 1 AA8 2 CYSAA 342 TYRAA 343 0 SHEET 2 AA8 2 ILEAA 370 PHEAA 371 1 O PHEAA 371 N CYSAA 342 SHEET 1 AA9 5 LEUAA 374 PHEAA 376 0 SHEET 2 AA9 5 LEUAA 410 ILEAA 412 1 O TYRAA 411 N PHEAA 376 SHEET 3 AA9 5 TYRAA 441 GLNAA 446 1 O THRAA 444 N ILEAA 412 SHEET 4 AA9 5 LEUAA 465 HISAA 469 1 O LEUAA 467 N LEUAA 443 SHEET 5 AA9 5 LEUAA 493 THRAA 496 1 O LEUAA 494 N ALAAA 466 SHEET 1 AB1 3 GLUAA 405 ILEAA 406 0 SHEET 2 AB1 3 VALAA 430 ILEAA 431 1 O VALAA 430 N ILEAA 406 SHEET 3 AB1 3 GLUAA 460 LEUAA 461 1 O GLUAA 460 N ILEAA 431 SHEET 1 AB2 2 LEUAA 535 ARGAA 536 0 SHEET 2 AB2 2 GLUAA 539 CYSAA 540 -1 O GLUAA 539 N ARGAA 536 SHEET 1 AB3 4 GLNBB 5 SERBB 7 0 SHEET 2 AB3 4 LEUBB 18 THRBB 23 -1 O THRBB 23 N GLNBB 5 SHEET 3 AB3 4 THRBB 77 METBB 82 -1 O VALBB 78 N CYSBB 22 SHEET 4 AB3 4 PHEBB 67 ASPBB 72 -1 N SERBB 70 O TYRBB 79 SHEET 1 AB4 6 GLYBB 10 GLNBB 13 0 SHEET 2 AB4 6 THRBB 117 SERBB 122 1 O THRBB 120 N VALBB 12 SHEET 3 AB4 6 GLYBB 91 CYSBB 95 -1 N GLYBB 91 O VALBB 119 SHEET 4 AB4 6 METBB 34 GLNBB 39 -1 N TYRBB 37 O TYRBB 94 SHEET 5 AB4 6 GLUBB 46 ILEBB 51 -1 O GLUBB 46 N ARGBB 38 SHEET 6 AB4 6 TYRBB 58 TYRBB 59 -1 O TYRBB 58 N SERBB 50 SSBOND 1 CYSAA 26 CYSAA 53 1555 1555 2.04 SSBOND 2 CYSAA 162 CYSAA 192 1555 1555 2.05 SSBOND 3 CYSAA 195 CYSAA 204 1555 1555 2.03 SSBOND 4 CYSAA 199 CYSAA 212 1555 1555 2.03 SSBOND 5 CYSAA 220 CYSAA 227 1555 1555 2.01 SSBOND 6 CYSAA 224 CYSAA 235 1555 1555 1.98 SSBOND 7 CYSAA 236 CYSAA 244 1555 1555 2.03 SSBOND 8 CYSAA 240 CYSAA 252 1555 1555 2.03 SSBOND 9 CYSAA 255 CYSAA 264 1555 1555 2.05 SSBOND 10 CYSAA 268 CYSAA 295 1555 1555 2.03 SSBOND 11 CYSAA 299 CYSAA 311 1555 1555 2.03 SSBOND 12 CYSAA 315 CYSAA 331 1555 1555 2.02 SSBOND 13 CYSAA 334 CYSAA 338 1555 1555 2.03 SSBOND 14 CYSAA 342 CYSAA 367 1555 1555 2.00 SSBOND 15 CYSAA 475 CYSAA 504 1555 1555 2.04 SSBOND 16 CYSAA 511 CYSAA 520 1555 1555 2.04 SSBOND 17 CYSAA 515 CYSAA 528 1555 1555 2.04 SSBOND 18 CYSAA 531 CYSAA 540 1555 1555 2.03 SSBOND 19 CYSBB 22 CYSBB 95 1555 1555 2.03 SSBOND 20 CYSBB 45 CYSBB 107 1555 1555 2.04 LINK ND2 ASNAA 68 C1 NAGAA 700 1555 1555 1.47 LINK ND2 ASNAA 259 C1 NAGbA 1 1555 1555 1.43 LINK O4 NAGbA 1 C1 NAGbA 2 1555 1555 1.43 LINK O4 NAGbA 2 C1 BMAbA 3 1555 1555 1.45 CRYST1 105.767 105.767 185.882 90.00 90.00 120.00 P 32 2 1 6 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 0.009455 0.005459 0.000000 0.00000 SCALE2 0.000000 0.010917 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005380 0.00000