HEADER IMMUNE SYSTEM 04-MAY-18 6DC8
TITLE FAB/EPITOPE COMPLEX OF MOUSE MONOCLONAL ANTIBODY 8B2 TARGETING A NON-
TITLE 2 PHOSPHORYLATED TAU EPITOPE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGG LIGHT CHAIN;
COMPND 3 CHAIN: L;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: IGG HEAVY CHAIN;
COMPND 6 CHAIN: H;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: MICROTUBULE-ASSOCIATED PROTEIN TAU;
COMPND 9 CHAIN: P;
COMPND 10 SYNONYM: NEUROFIBRILLARY TANGLE PROTEIN,PAIRED HELICAL FILAMENT-TAU,
COMPND 11 PHF-TAU;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 MOL_ID: 3;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS MONOCLONAL ANTIBODY, FAB, TAU, PHOSPHORYLATION STATE -SPECIFIC
KEYWDS 2 ANTIBODY, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.E.CHUKWU,X.-P.KONG
REVDAT 3 18-DEC-19 6DC8 1 REMARK
REVDAT 2 03-APR-19 6DC8 1 JRNL
REVDAT 1 20-MAR-19 6DC8 0
JRNL AUTH J.E.CHUKWU,E.E.CONGDON,E.M.SIGURDSSON,X.P.KONG
JRNL TITL STRUCTURAL CHARACTERIZATION OF MONOCLONAL ANTIBODIES
JRNL TITL 2 TARGETING C-TERMINAL SER404REGION OF PHOSPHORYLATED TAU
JRNL TITL 3 PROTEIN.
JRNL REF MABS V. 11 477 2019
JRNL REFN ESSN 1942-0870
JRNL PMID 30794086
JRNL DOI 10.1080/19420862.2019.1574530
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 45380
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 2252
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 40.3120 - 4.5318 1.00 2957 152 0.1638 0.1937
REMARK 3 2 4.5318 - 3.5977 1.00 2765 170 0.1449 0.1914
REMARK 3 3 3.5977 - 3.1432 1.00 2738 131 0.1698 0.1856
REMARK 3 4 3.1432 - 2.8559 1.00 2723 147 0.1873 0.2280
REMARK 3 5 2.8559 - 2.6512 1.00 2694 137 0.1949 0.2435
REMARK 3 6 2.6512 - 2.4949 1.00 2700 146 0.2037 0.2292
REMARK 3 7 2.4949 - 2.3700 1.00 2657 133 0.1949 0.2376
REMARK 3 8 2.3700 - 2.2668 1.00 2673 152 0.1920 0.2366
REMARK 3 9 2.2668 - 2.1796 1.00 2654 174 0.1874 0.2457
REMARK 3 10 2.1796 - 2.1044 1.00 2642 133 0.1855 0.2656
REMARK 3 11 2.1044 - 2.0386 1.00 2661 135 0.1907 0.2381
REMARK 3 12 2.0386 - 1.9803 1.00 2652 144 0.1881 0.2534
REMARK 3 13 1.9803 - 1.9282 1.00 2658 128 0.1980 0.2237
REMARK 3 14 1.9282 - 1.8811 1.00 2641 137 0.2058 0.2185
REMARK 3 15 1.8811 - 1.8384 1.00 2664 121 0.2154 0.2834
REMARK 3 16 1.8384 - 1.7992 1.00 2649 112 0.2340 0.3100
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.320
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 : 0.006 3506
REMARK 3 ANGLE : 0.912 4778
REMARK 3 CHIRALITY : 0.059 535
REMARK 3 PLANARITY : 0.005 603
REMARK 3 DIHEDRAL : 13.883 2076
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6DC8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1000234348.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45390
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 40.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 1.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 46.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% POLYETHYLENE GLYCOL 8000, 0.17 M
REMARK 280 AMMONIUM ACETATE, AND 0.085 M SODIUM CACODYLATE TRIHYDRATE PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 99.42650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.41800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.41800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 149.13975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.41800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.41800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 49.71325
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.41800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.41800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 149.13975
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.41800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.41800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 49.71325
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 99.42650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, P
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH H 635 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ARG P 379
REMARK 465 GLU P 380
REMARK 465 ASN P 381
REMARK 465 ALA P 382
REMARK 465 LYS P 383
REMARK 465 ALA P 384
REMARK 465 LYS P 385
REMARK 465 THR P 386
REMARK 465 ASP P 387
REMARK 465 HIS P 388
REMARK 465 GLY P 389
REMARK 465 ALA P 390
REMARK 465 GLU P 391
REMARK 465 ILE P 392
REMARK 465 VAL P 393
REMARK 465 TYR P 394
REMARK 465 LYS P 395
REMARK 465 SER P 396
REMARK 465 PRO P 397
REMARK 465 VAL P 398
REMARK 465 VAL P 399
REMARK 465 SER P 400
REMARK 465 GLY P 401
REMARK 465 ASP P 402
REMARK 465 THR P 403
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 HOH H 444 O HOH H 646 2.11
REMARK 500 O HOH H 481 O HOH H 504 2.15
REMARK 500 O HOH H 567 O HOH H 639 2.16
REMARK 500 O HOH H 652 O HOH H 674 2.17
REMARK 500 NZ LYS L 199 O HOH L 401 2.17
REMARK 500 O HOH L 414 O HOH L 553 2.19
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 VAL L 51 -46.63 72.75
REMARK 500 LYS H 66 -50.33 -122.05
REMARK 500 ASP H 97 -164.13 -120.79
REMARK 500 ASP H 130 163.28 178.40
REMARK 500 THR H 131 -149.24 53.81
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 H 686 DISTANCE = 5.87 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL L 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 P 501
DBREF 6DC8 L 1 213 PDB 6DC8 6DC8 1 213
DBREF 6DC8 H 1 213 PDB 6DC8 6DC8 1 213
DBREF 6DC8 P 379 408 UNP P10636 TAU_HUMAN 696 725
SEQADV 6DC8 NH2 P 409 UNP P10636 AMIDATION
SEQRES 1 L 218 ASP VAL LEU LEU THR GLN THR PRO LEU SER LEU PRO VAL
SEQRES 2 L 218 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER
SEQRES 3 L 218 GLN SER ILE VAL HIS SER ASN GLY ASN THR TYR LEU GLU
SEQRES 4 L 218 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLU LEU LEU
SEQRES 5 L 218 ILE TYR LYS VAL SER ASN ARG PHE TYR GLY VAL PRO ASP
SEQRES 6 L 218 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU
SEQRES 7 L 218 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR
SEQRES 8 L 218 TYR CYS PHE GLN ASP SER HIS ILE PRO TYR THR PHE GLY
SEQRES 9 L 218 GLY GLY THR ARG LEU GLU ILE LYS ARG ALA ASP ALA ALA
SEQRES 10 L 218 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU
SEQRES 11 L 218 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN
SEQRES 12 L 218 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP
SEQRES 13 L 218 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR
SEQRES 14 L 218 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER
SEQRES 15 L 218 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN
SEQRES 16 L 218 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER
SEQRES 17 L 218 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU
SEQRES 1 H 217 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 H 217 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY
SEQRES 3 H 217 TYR THR PHE THR SER TYR VAL ILE HIS TRP VAL LYS GLN
SEQRES 4 H 217 LYS PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR ILE TYR
SEQRES 5 H 217 PRO TYR ASN ASP GLY THR ILE TYR ASN GLU LYS PHE LYS
SEQRES 6 H 217 GLY LYS ALA THR LEU THR SER ASP THR SER SER SER THR
SEQRES 7 H 217 VAL TYR MET GLU LEU ILE SER LEU THR ALA GLU ASP SER
SEQRES 8 H 217 ALA VAL TYR TRP CYS VAL ARG GLU ARG ASP ASN TYR GLY
SEQRES 9 H 217 VAL TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER
SEQRES 10 H 217 ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO
SEQRES 11 H 217 GLY THR GLY ASP THR GLY SER SER MET VAL THR LEU GLY
SEQRES 12 H 217 CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL
SEQRES 13 H 217 THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR
SEQRES 14 H 217 PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER
SEQRES 15 H 217 SER SER VAL THR VAL THR SER SER THR TRP PRO SER GLN
SEQRES 16 H 217 THR ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER THR
SEQRES 17 H 217 LYS VAL ASP LYS LYS ILE VAL PRO GLU
SEQRES 1 P 31 ARG GLU ASN ALA LYS ALA LYS THR ASP HIS GLY ALA GLU
SEQRES 2 P 31 ILE VAL TYR LYS SER PRO VAL VAL SER GLY ASP THR SER
SEQRES 3 P 31 PRO ARG HIS LEU NH2
HET NH2 P 409 1
HET GOL L 301 6
HET GOL H 301 6
HET GOL H 302 6
HET PO4 P 501 5
HETNAM NH2 AMINO GROUP
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NH2 H2 N
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 7 PO4 O4 P 3-
FORMUL 8 HOH *569(H2 O)
HELIX 1 AA1 GLU L 79 LEU L 83 5 5
HELIX 2 AA2 SER L 121 SER L 127 1 7
HELIX 3 AA3 LYS L 183 GLU L 187 1 5
HELIX 4 AA4 THR H 28 TYR H 32 5 5
HELIX 5 AA5 GLU H 61 LYS H 64 5 4
HELIX 6 AA6 THR H 73 SER H 75 5 3
HELIX 7 AA7 THR H 83 SER H 87 5 5
HELIX 8 AA8 SER H 156 SER H 158 5 3
HELIX 9 AA9 PRO H 200 SER H 203 5 4
SHEET 1 AA1 4 LEU L 4 THR L 7 0
SHEET 2 AA1 4 ALA L 19 SER L 25 -1 O ARG L 24 N THR L 5
SHEET 3 AA1 4 ASP L 70 ILE L 75 -1 O ILE L 75 N ALA L 19
SHEET 4 AA1 4 PHE L 62 SER L 67 -1 N SER L 63 O LYS L 74
SHEET 1 AA2 6 SER L 10 VAL L 13 0
SHEET 2 AA2 6 THR L 102 ILE L 106 1 O ARG L 103 N LEU L 11
SHEET 3 AA2 6 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104
SHEET 4 AA2 6 LEU L 33 GLN L 38 -1 N GLU L 34 O PHE L 89
SHEET 5 AA2 6 GLU L 45 TYR L 49 -1 O LEU L 47 N TRP L 35
SHEET 6 AA2 6 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49
SHEET 1 AA3 4 SER L 10 VAL L 13 0
SHEET 2 AA3 4 THR L 102 ILE L 106 1 O ARG L 103 N LEU L 11
SHEET 3 AA3 4 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104
SHEET 4 AA3 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 AA4 4 THR L 114 PHE L 118 0
SHEET 2 AA4 4 GLY L 129 PHE L 139 -1 O ASN L 137 N THR L 114
SHEET 3 AA4 4 TYR L 173 THR L 182 -1 O LEU L 181 N ALA L 130
SHEET 4 AA4 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176
SHEET 1 AA5 4 SER L 153 ARG L 155 0
SHEET 2 AA5 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153
SHEET 3 AA5 4 SER L 191 HIS L 198 -1 O THR L 197 N ASN L 145
SHEET 4 AA5 4 SER L 201 ASN L 210 -1 O ILE L 205 N ALA L 196
SHEET 1 AA6 4 GLN H 3 GLN H 6 0
SHEET 2 AA6 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5
SHEET 3 AA6 4 THR H 77 LEU H 82 -1 O MET H 80 N MET H 20
SHEET 4 AA6 4 ALA H 67 ASP H 72 -1 N THR H 68 O GLU H 81
SHEET 1 AA7 6 GLU H 10 VAL H 12 0
SHEET 2 AA7 6 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10
SHEET 3 AA7 6 ALA H 88 ARG H 94 -1 N ALA H 88 O LEU H 109
SHEET 4 AA7 6 ILE H 34 GLN H 39 -1 N HIS H 35 O VAL H 93
SHEET 5 AA7 6 GLU H 46 ILE H 51 -1 O GLU H 46 N LYS H 38
SHEET 6 AA7 6 THR H 57 TYR H 59 -1 O ILE H 58 N TYR H 50
SHEET 1 AA8 4 GLU H 10 VAL H 12 0
SHEET 2 AA8 4 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10
SHEET 3 AA8 4 ALA H 88 ARG H 94 -1 N ALA H 88 O LEU H 109
SHEET 4 AA8 4 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94
SHEET 1 AA9 4 SER H 120 LEU H 124 0
SHEET 2 AA9 4 MET H 135 TYR H 145 -1 O LEU H 141 N TYR H 122
SHEET 3 AA9 4 LEU H 174 THR H 184 -1 O LEU H 177 N VAL H 142
SHEET 4 AA9 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180
SHEET 1 AB1 4 SER H 120 LEU H 124 0
SHEET 2 AB1 4 MET H 135 TYR H 145 -1 O LEU H 141 N TYR H 122
SHEET 3 AB1 4 LEU H 174 THR H 184 -1 O LEU H 177 N VAL H 142
SHEET 4 AB1 4 VAL H 169 GLN H 171 -1 N GLN H 171 O LEU H 174
SHEET 1 AB2 3 THR H 151 TRP H 154 0
SHEET 2 AB2 3 THR H 194 HIS H 199 -1 O ASN H 196 N THR H 153
SHEET 3 AB2 3 THR H 204 LYS H 209 -1 O VAL H 206 N VAL H 197
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.06
SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.03
SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.06
SSBOND 4 CYS H 140 CYS H 195 1555 1555 2.02
LINK C LEU P 408 N NH2 P 409 1555 1555 1.33
CISPEP 1 THR L 7 PRO L 8 0 -3.51
CISPEP 2 ILE L 94 PRO L 95 0 3.07
CISPEP 3 TYR L 140 PRO L 141 0 1.43
CISPEP 4 SER H 133 SER H 134 0 -1.41
CISPEP 5 PHE H 146 PRO H 147 0 -4.71
CISPEP 6 GLU H 148 PRO H 149 0 1.20
CISPEP 7 TRP H 188 PRO H 189 0 2.37
SITE 1 AC1 7 LEU L 37 LYS L 39 GLU L 45 GLU L 81
SITE 2 AC1 7 ASP L 82 HOH L 403 HOH L 526
SITE 1 AC2 8 ARG H 96 ASP H 97 ASN H 98 HOH H 486
SITE 2 AC2 8 TYR L 49 PHE L 55 ASP L 151 PO4 P 501
SITE 1 AC3 4 PRO H 119 VAL H 121 THR H 204 LYS H 208
SITE 1 AC4 8 GOL H 301 TYR L 32 LYS L 50 HIS L 189
SITE 2 AC4 8 HOH L 412 SER P 404 HIS P 407 HOH P 601
CRYST1 68.836 68.836 198.853 90.00 90.00 90.00 P 43 21 2 8
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 0.014527 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014527 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005029 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
