HEADER IMMUNE SYSTEM 29-OCT-24 9H8H TITLE STRUCTURE OF DC11 ANTI TAU ANTIBODY FAB FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: DC11; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IGK PROTEIN; COMPND 7 CHAIN: D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS; SOURCE 3 ORGANISM_TAXID: 10088; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS; SOURCE 8 ORGANISM_COMMON: MICE; SOURCE 9 ORGANISM_TAXID: 10088; SOURCE 10 GENE: IGK; SOURCE 11 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS FAB, TAU PROTEIN BINDING, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR O.CEHLAR,S.NJEMOGA REVDAT 1 12-NOV-25 9H8H 0 JRNL AUTH O.CEHLAR,S.NJEMOGA JRNL TITL STRUCTURE OF DC11 ANTI TAU ANTIBODY FAB FRAGMENT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.33 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0425 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) : 1.33 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.07 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 75.4 REMARK 3 NUMBER OF REFLECTIONS : 70143 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 : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.145 REMARK 3 FREE R VALUE : 0.196 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.007 REMARK 3 FREE R VALUE TEST SET COUNT : 3512 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.33 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.37 REMARK 3 REFLECTION IN BIN (WORKING SET) : 394 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 5.95 REMARK 3 BIN R VALUE (WORKING SET) : 0.2840 REMARK 3 BIN FREE R VALUE SET COUNT : 14 REMARK 3 BIN FREE R VALUE : 0.3560 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3318 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 7 REMARK 3 SOLVENT ATOMS : 523 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.22 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.16400 REMARK 3 B22 (A**2) : 0.24400 REMARK 3 B33 (A**2) : -0.07900 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.00400 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.076 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.071 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.973 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3479 ; 0.008 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 3146 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4770 ; 1.706 ; 1.805 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7344 ; 0.621 ; 1.743 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 465 ; 7.073 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 11 ;12.423 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 570 ;11.415 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 546 ; 0.088 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4079 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 745 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 580 ; 0.221 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 75 ; 0.189 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1676 ; 0.176 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 344 ; 0.185 ; 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): 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): 1758 ; 5.680 ; 2.123 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1758 ; 5.678 ; 2.122 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2203 ; 8.279 ; 3.815 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2204 ; 8.278 ; 3.815 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1721 ; 7.070 ; 2.435 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1722 ; 7.069 ; 2.436 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2549 ;10.287 ; 4.318 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2550 ;10.285 ; 4.319 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): 6625 ; 3.557 ; 3.000 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 9H8H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1292142842. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-FEB-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY REMARK 200 BEAMLINE : P13 (MX1) REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70143 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.331 REMARK 200 RESOLUTION RANGE LOW (A) : 48.067 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2 REMARK 200 DATA REDUNDANCY : 6.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.0290 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.33 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43 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 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 (%): 43.91 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1% MIB, 25% W/V PEG 1500, PH 6.0, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 44.22250 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 475 REMARK 475 ZERO OCCUPANCY RESIDUES REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY. REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE) REMARK 475 M RES C SSEQI REMARK 475 ALA A 128 REMARK 475 ALA A 129 REMARK 475 GLN A 130 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 O THR A 131 O MET A 134 2.18 REMARK 500 O HOH A 514 O HOH A 529 2.19 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 SER A 127 O - C - N ANGL. DEV. = 9.7 DEGREES REMARK 500 GLU A 147 CG - CD - OE1 ANGL. DEV. = -13.3 DEGREES REMARK 500 GLU A 147 CG - CD - OE2 ANGL. DEV. = 14.5 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 ASN A 132 -157.05 49.84 REMARK 500 ASP A 172 -7.70 75.85 REMARK 500 VAL D 56 -48.51 72.65 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG D 82 0.18 SIDE CHAIN REMARK 500 ARG D 193 0.15 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 579 DISTANCE = 5.99 ANGSTROMS REMARK 525 HOH A 580 DISTANCE = 6.15 ANGSTROMS REMARK 525 HOH A 581 DISTANCE = 6.58 ANGSTROMS REMARK 525 HOH A 582 DISTANCE = 6.82 ANGSTROMS REMARK 525 HOH A 583 DISTANCE = 7.04 ANGSTROMS REMARK 525 HOH A 584 DISTANCE = 7.34 ANGSTROMS REMARK 525 HOH A 585 DISTANCE = 7.87 ANGSTROMS REMARK 525 HOH A 586 DISTANCE = 9.15 ANGSTROMS REMARK 525 HOH D 634 DISTANCE = 6.10 ANGSTROMS REMARK 525 HOH D 635 DISTANCE = 6.55 ANGSTROMS REMARK 525 HOH D 636 DISTANCE = 6.79 ANGSTROMS REMARK 525 HOH D 637 DISTANCE = 7.38 ANGSTROMS DBREF 9H8H A 1 214 PDB 9H8H 9H8H 1 214 DBREF 9H8H D 1 219 UNP Q58EU8 Q58EU8_MOUSE 21 239 SEQADV 9H8H ASP D 31 UNP Q58EU8 HIS 51 CONFLICT SEQADV 9H8H ASP D 33 UNP Q58EU8 ASN 53 CONFLICT SEQADV 9H8H ARG D 51 UNP Q58EU8 LEU 71 CONFLICT SEQADV 9H8H PHE D 54 UNP Q58EU8 TYR 74 CONFLICT SEQADV 9H8H ASP D 60 UNP Q58EU8 GLU 80 CONFLICT SEQADV 9H8H THR D 68 UNP Q58EU8 SER 88 CONFLICT SEQADV 9H8H TRP D 94 UNP Q58EU8 LEU 114 CONFLICT SEQADV 9H8H LYS D 96 UNP Q58EU8 ALA 116 CONFLICT SEQADV 9H8H GLN D 101 UNP Q58EU8 ARG 121 CONFLICT SEQADV 9H8H ASN D 108 UNP Q58EU8 LYS 128 CONFLICT SEQRES 1 A 214 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 A 214 SER GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY SEQRES 3 A 214 PHE ASN ILE LYS ASP TYR TYR MET HIS TRP VAL LYS GLN SEQRES 4 A 214 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY TRP ILE ASP SEQRES 5 A 214 PRO GLU ASN ALA ASP THR GLU TYR ALA PRO LYS PHE GLN SEQRES 6 A 214 GLY LYS ALA THR MET THR ALA ASP THR SER SER ASN THR SEQRES 7 A 214 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR SEQRES 8 A 214 ALA VAL TYR TYR CYS LYS THR GLY ASP TYR TRP GLY GLN SEQRES 9 A 214 GLY THR THR LEU THR VAL SER SER ALA LYS THR THR PRO SEQRES 10 A 214 PRO SER VAL TYR PRO LEU ALA PRO GLY SER ALA ALA GLN SEQRES 11 A 214 THR ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS GLY SEQRES 12 A 214 TYR PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY SEQRES 13 A 214 SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 14 A 214 GLU SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL SEQRES 15 A 214 PRO SER SER THR TRP PRO SER GLU THR VAL THR CYS ASN SEQRES 16 A 214 VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS SEQRES 17 A 214 ILE VAL PRO ARG ASP CYS SEQRES 1 D 219 ASP VAL VAL MET THR GLN THR PRO LEU THR LEU SER VAL SEQRES 2 D 219 THR ILE GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 D 219 GLN SER LEU LEU ASP SER ASP GLY LYS THR TYR LEU ASN SEQRES 4 D 219 TRP LEU LEU GLN ARG PRO GLY GLN SER PRO LYS ARG LEU SEQRES 5 D 219 ILE PHE LEU VAL SER LYS LEU ASP SER GLY VAL PRO ASP SEQRES 6 D 219 ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 D 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 D 219 TYR CYS TRP GLN LYS THR HIS PHE PRO GLN THR PHE GLY SEQRES 9 D 219 GLY GLY THR ASN LEU GLU ILE LYS ARG ALA ASP ALA ALA SEQRES 10 D 219 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU SEQRES 11 D 219 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN SEQRES 12 D 219 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP SEQRES 13 D 219 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR SEQRES 14 D 219 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER SEQRES 15 D 219 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SEQRES 16 D 219 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER SEQRES 17 D 219 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS HET PEG D 301 7 HETNAM PEG DI(HYDROXYETHYL)ETHER FORMUL 3 PEG C4 H10 O3 FORMUL 4 HOH *523(H2 O) HELIX 1 AA1 ASN A 28 TYR A 32 5 5 HELIX 2 AA2 PRO A 62 GLN A 65 5 4 HELIX 3 AA3 THR A 74 SER A 76 5 3 HELIX 4 AA4 THR A 87 THR A 91 5 5 HELIX 5 AA5 SER A 155 SER A 157 5 3 HELIX 6 AA6 SER A 185 TRP A 187 5 3 HELIX 7 AA7 PRO A 199 SER A 202 5 4 HELIX 8 AA8 GLU D 84 LEU D 88 5 5 HELIX 9 AA9 SER D 126 THR D 131 1 6 HELIX 10 AB1 LYS D 188 GLU D 192 1 5 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O THR A 23 N GLN A 5 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O LEU A 81 N LEU A 20 SHEET 4 AA1 4 ALA A 68 ASP A 73 -1 N ASP A 73 O THR A 78 SHEET 1 AA2 6 GLU A 10 ARG A 13 0 SHEET 2 AA2 6 THR A 106 SER A 111 1 O THR A 109 N VAL A 12 SHEET 3 AA2 6 ALA A 92 THR A 98 -1 N ALA A 92 O LEU A 108 SHEET 4 AA2 6 MET A 34 ARG A 40 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 GLY A 44 ILE A 51 -1 O GLU A 46 N LYS A 38 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O GLU A 59 N TRP A 50 SHEET 1 AA3 4 GLU A 10 ARG A 13 0 SHEET 2 AA3 4 THR A 106 SER A 111 1 O THR A 109 N VAL A 12 SHEET 3 AA3 4 ALA A 92 THR A 98 -1 N ALA A 92 O LEU A 108 SHEET 4 AA3 4 TYR A 101 TRP A 102 -1 O TYR A 101 N THR A 98 SHEET 1 AA4 4 SER A 119 LEU A 123 0 SHEET 2 AA4 4 MET A 134 TYR A 144 -1 O LYS A 142 N SER A 119 SHEET 3 AA4 4 LEU A 173 PRO A 183 -1 O TYR A 174 N TYR A 144 SHEET 4 AA4 4 VAL A 162 THR A 164 -1 N HIS A 163 O SER A 179 SHEET 1 AA5 4 SER A 119 LEU A 123 0 SHEET 2 AA5 4 MET A 134 TYR A 144 -1 O LYS A 142 N SER A 119 SHEET 3 AA5 4 LEU A 173 PRO A 183 -1 O TYR A 174 N TYR A 144 SHEET 4 AA5 4 VAL A 168 GLU A 170 -1 N GLU A 170 O LEU A 173 SHEET 1 AA6 3 THR A 150 TRP A 153 0 SHEET 2 AA6 3 THR A 193 HIS A 198 -1 O ASN A 195 N THR A 152 SHEET 3 AA6 3 THR A 203 LYS A 208 -1 O THR A 203 N HIS A 198 SHEET 1 AA7 4 MET D 4 THR D 7 0 SHEET 2 AA7 4 ALA D 19 SER D 25 -1 O LYS D 24 N THR D 5 SHEET 3 AA7 4 ASP D 75 ILE D 80 -1 O LEU D 78 N ILE D 21 SHEET 4 AA7 4 PHE D 67 SER D 72 -1 N THR D 68 O LYS D 79 SHEET 1 AA8 6 THR D 10 VAL D 13 0 SHEET 2 AA8 6 THR D 107 ILE D 111 1 O GLU D 110 N VAL D 13 SHEET 3 AA8 6 GLY D 89 GLN D 95 -1 N GLY D 89 O LEU D 109 SHEET 4 AA8 6 LEU D 38 GLN D 43 -1 N ASN D 39 O TRP D 94 SHEET 5 AA8 6 LYS D 50 PHE D 54 -1 O LYS D 50 N LEU D 42 SHEET 6 AA8 6 LYS D 58 LEU D 59 -1 O LYS D 58 N PHE D 54 SHEET 1 AA9 4 THR D 10 VAL D 13 0 SHEET 2 AA9 4 THR D 107 ILE D 111 1 O GLU D 110 N VAL D 13 SHEET 3 AA9 4 GLY D 89 GLN D 95 -1 N GLY D 89 O LEU D 109 SHEET 4 AA9 4 THR D 102 PHE D 103 -1 O THR D 102 N GLN D 95 SHEET 1 AB1 4 THR D 119 PHE D 123 0 SHEET 2 AB1 4 GLY D 134 PHE D 144 -1 O ASN D 142 N THR D 119 SHEET 3 AB1 4 TYR D 178 THR D 187 -1 O LEU D 186 N ALA D 135 SHEET 4 AB1 4 VAL D 164 TRP D 168 -1 N SER D 167 O SER D 181 SHEET 1 AB2 4 SER D 158 ARG D 160 0 SHEET 2 AB2 4 ASN D 150 ILE D 155 -1 N TRP D 153 O ARG D 160 SHEET 3 AB2 4 SER D 196 THR D 202 -1 O GLU D 200 N LYS D 152 SHEET 4 AB2 4 ILE D 210 ASN D 215 -1 O ILE D 210 N ALA D 201 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.08 SSBOND 2 CYS A 139 CYS A 194 1555 1555 2.04 SSBOND 3 CYS A 214 CYS D 219 1555 1555 2.35 SSBOND 4 CYS D 23 CYS D 93 1555 1555 2.27 SSBOND 5 CYS D 139 CYS D 199 1555 1555 2.08 CISPEP 1 PHE A 145 PRO A 146 0 -4.83 CISPEP 2 GLU A 147 PRO A 148 0 -4.53 CISPEP 3 GLU A 147 PRO A 148 0 -1.85 CISPEP 4 TRP A 187 PRO A 188 0 3.25 CISPEP 5 THR D 7 PRO D 8 0 -10.56 CISPEP 6 PHE D 99 PRO D 100 0 -5.74 CISPEP 7 TYR D 145 PRO D 146 0 -0.94 CRYST1 40.901 88.445 57.464 90.00 94.80 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 0.024449 0.000000 0.002054 0.00000 SCALE2 0.000000 0.011306 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017464 0.00000