HEADER TRANSPORT PROTEIN 07-OCT-16 5H0X
TITLE CRYSTAL STRUCTURE OF H88S MUTATED HUMAN TRANSTHYRETIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSTHYRETIN;
COMPND 3 CHAIN: B, A;
COMPND 4 FRAGMENT: UNP RESIDUES 31-147;
COMPND 5 SYNONYM: ATTR,PREALBUMIN,TBPA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TTR, PALB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSTHHYRETIN, AMYLOIDOSIS, TRANSPORTER, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.YOKOYAMA,Y.HANAWA,T.OBITA,M.MIZUGUCHI
REVDAT 3 20-MAR-24 5H0X 1 REMARK
REVDAT 2 26-JUL-17 5H0X 1 JRNL
REVDAT 1 14-JUN-17 5H0X 0
JRNL AUTH T.YOKOYAMA,Y.HANAWA,T.OBITA,M.MIZUGUCHI
JRNL TITL STABILITY AND CRYSTAL STRUCTURES OF HIS88 MUTANT HUMAN
JRNL TITL 2 TRANSTHYRETINS
JRNL REF FEBS LETT. V. 591 1862 2017
JRNL REFN ISSN 1873-3468
JRNL PMID 28563699
JRNL DOI 10.1002/1873-3468.12704
REMARK 2
REMARK 2 RESOLUTION. 1.57 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1-2155_1069: ???)
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) : 1.57
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 32901
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1665
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 37.9446 - 3.6004 0.97 2718 148 0.2261 0.2187
REMARK 3 2 3.6004 - 2.8580 0.99 2631 151 0.2195 0.2378
REMARK 3 3 2.8580 - 2.4968 1.00 2645 118 0.2391 0.2807
REMARK 3 4 2.4968 - 2.2686 1.00 2614 149 0.2322 0.2143
REMARK 3 5 2.2686 - 2.1060 1.00 2606 143 0.2343 0.2824
REMARK 3 6 2.1060 - 1.9818 1.00 2565 156 0.2467 0.2595
REMARK 3 7 1.9818 - 1.8826 1.00 2604 125 0.2592 0.2779
REMARK 3 8 1.8826 - 1.8006 1.00 2574 138 0.2634 0.3008
REMARK 3 9 1.8006 - 1.7313 1.00 2575 146 0.2790 0.3199
REMARK 3 10 1.7313 - 1.6716 1.00 2578 138 0.2929 0.3270
REMARK 3 11 1.6716 - 1.6193 1.00 2563 143 0.2889 0.3002
REMARK 3 12 1.6193 - 1.5730 0.99 2563 110 0.2992 0.3215
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.850
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 1814
REMARK 3 ANGLE : 0.851 2474
REMARK 3 CHIRALITY : 0.092 284
REMARK 3 PLANARITY : 0.007 314
REMARK 3 DIHEDRAL : 21.419 636
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 5H0X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1300001811.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32905
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570
REMARK 200 RESOLUTION RANGE LOW (A) : 38.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE, 25% GLYCEROL,
REMARK 280 0.1 M SODIUM ACETATE, PH 4.8, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 21.16500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.74000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.16500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.74000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 B 224 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 242 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 ALA B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 MET B 9
REMARK 465 PRO B 125
REMARK 465 LYS B 126
REMARK 465 GLU B 127
REMARK 465 ALA A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 MET A 9
REMARK 465 PRO A 125
REMARK 465 LYS A 126
REMARK 465 GLU A 127
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 GLU B 63 CD GLU B 63 OE2 0.069
REMARK 500 GLU A 63 CD GLU A 63 OE2 0.083
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 B 39 -2.12 83.14
REMARK 500 PHE B 44 -56.65 -123.03
REMARK 500 THR B 75 -50.81 -129.38
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 ASP B 74 THR B 75 -144.59
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 B 290 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH B 291 DISTANCE = 6.81 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5H0V RELATED DB: PDB
REMARK 900 RELATED ID: 5H0W RELATED DB: PDB
REMARK 900 RELATED ID: 5H0Y RELATED DB: PDB
REMARK 900 RELATED ID: 5H0Z RELATED DB: PDB
DBREF 5H0X B 11 127 UNP P02766 TTHY_HUMAN 31 147
DBREF 5H0X A 11 127 UNP P02766 TTHY_HUMAN 31 147
SEQADV 5H0X ALA B 2 UNP P02766 EXPRESSION TAG
SEQADV 5H0X HIS B 3 UNP P02766 EXPRESSION TAG
SEQADV 5H0X HIS B 4 UNP P02766 EXPRESSION TAG
SEQADV 5H0X HIS B 5 UNP P02766 EXPRESSION TAG
SEQADV 5H0X HIS B 6 UNP P02766 EXPRESSION TAG
SEQADV 5H0X HIS B 7 UNP P02766 EXPRESSION TAG
SEQADV 5H0X HIS B 8 UNP P02766 EXPRESSION TAG
SEQADV 5H0X MET B 9 UNP P02766 EXPRESSION TAG
SEQADV 5H0X SER B 10 UNP P02766 EXPRESSION TAG
SEQADV 5H0X SER B 88 UNP P02766 HIS 108 ENGINEERED MUTATION
SEQADV 5H0X ALA A 2 UNP P02766 EXPRESSION TAG
SEQADV 5H0X HIS A 3 UNP P02766 EXPRESSION TAG
SEQADV 5H0X HIS A 4 UNP P02766 EXPRESSION TAG
SEQADV 5H0X HIS A 5 UNP P02766 EXPRESSION TAG
SEQADV 5H0X HIS A 6 UNP P02766 EXPRESSION TAG
SEQADV 5H0X HIS A 7 UNP P02766 EXPRESSION TAG
SEQADV 5H0X HIS A 8 UNP P02766 EXPRESSION TAG
SEQADV 5H0X MET A 9 UNP P02766 EXPRESSION TAG
SEQADV 5H0X SER A 10 UNP P02766 EXPRESSION TAG
SEQADV 5H0X SER A 88 UNP P02766 HIS 108 ENGINEERED MUTATION
SEQRES 1 B 126 ALA HIS HIS HIS HIS HIS HIS MET SER PRO LEU MET VAL
SEQRES 2 B 126 LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE ASN
SEQRES 3 B 126 VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP THR
SEQRES 4 B 126 TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER GLY
SEQRES 5 B 126 GLU LEU HIS GLY LEU THR THR GLU GLU GLU PHE VAL GLU
SEQRES 6 B 126 GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR TRP
SEQRES 7 B 126 LYS ALA LEU GLY ILE SER PRO PHE SER GLU HIS ALA GLU
SEQRES 8 B 126 VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG TYR
SEQRES 9 B 126 THR ILE ALA ALA LEU LEU SER PRO TYR SER TYR SER THR
SEQRES 10 B 126 THR ALA VAL VAL THR ASN PRO LYS GLU
SEQRES 1 A 126 ALA HIS HIS HIS HIS HIS HIS MET SER PRO LEU MET VAL
SEQRES 2 A 126 LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE ASN
SEQRES 3 A 126 VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP THR
SEQRES 4 A 126 TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER GLY
SEQRES 5 A 126 GLU LEU HIS GLY LEU THR THR GLU GLU GLU PHE VAL GLU
SEQRES 6 A 126 GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR TRP
SEQRES 7 A 126 LYS ALA LEU GLY ILE SER PRO PHE SER GLU HIS ALA GLU
SEQRES 8 A 126 VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG TYR
SEQRES 9 A 126 THR ILE ALA ALA LEU LEU SER PRO TYR SER TYR SER THR
SEQRES 10 A 126 THR ALA VAL VAL THR ASN PRO LYS GLU
FORMUL 3 HOH *182(H2 O)
HELIX 1 AA1 THR B 75 LEU B 82 1 8
HELIX 2 AA2 ASP A 74 GLY A 83 1 10
SHEET 1 AA1 8 SER B 23 PRO B 24 0
SHEET 2 AA1 8 LEU B 12 ASP B 18 -1 N ASP B 18 O SER B 23
SHEET 3 AA1 8 ARG B 104 SER B 112 1 O LEU B 111 N LEU B 17
SHEET 4 AA1 8 SER B 115 THR B 123 -1 O THR B 119 N ALA B 108
SHEET 5 AA1 8 SER A 115 THR A 123 -1 O TYR A 116 N THR B 118
SHEET 6 AA1 8 ARG A 104 SER A 112 -1 N ARG A 104 O THR A 123
SHEET 7 AA1 8 LEU A 12 ASP A 18 1 N LYS A 15 O ILE A 107
SHEET 8 AA1 8 SER A 23 PRO A 24 -1 O SER A 23 N ASP A 18
SHEET 1 AA2 8 GLU B 54 LEU B 55 0
SHEET 2 AA2 8 LEU B 12 ASP B 18 -1 N VAL B 14 O LEU B 55
SHEET 3 AA2 8 ARG B 104 SER B 112 1 O LEU B 111 N LEU B 17
SHEET 4 AA2 8 SER B 115 THR B 123 -1 O THR B 119 N ALA B 108
SHEET 5 AA2 8 SER A 115 THR A 123 -1 O TYR A 116 N THR B 118
SHEET 6 AA2 8 ARG A 104 SER A 112 -1 N ARG A 104 O THR A 123
SHEET 7 AA2 8 LEU A 12 ASP A 18 1 N LYS A 15 O ILE A 107
SHEET 8 AA2 8 GLU A 54 LEU A 55 -1 O LEU A 55 N VAL A 14
SHEET 1 AA3 8 TRP B 41 LYS B 48 0
SHEET 2 AA3 8 ALA B 29 LYS B 35 -1 N VAL B 32 O ALA B 45
SHEET 3 AA3 8 GLY B 67 ASP B 74 -1 O GLU B 72 N HIS B 31
SHEET 4 AA3 8 SER B 88 ALA B 97 -1 O VAL B 93 N VAL B 71
SHEET 5 AA3 8 SER A 88 ALA A 97 -1 O GLU A 89 N VAL B 94
SHEET 6 AA3 8 GLY A 67 ILE A 73 -1 N TYR A 69 O PHE A 95
SHEET 7 AA3 8 ALA A 29 LYS A 35 -1 N HIS A 31 O GLU A 72
SHEET 8 AA3 8 TRP A 41 LYS A 48 -1 O ALA A 45 N VAL A 32
CRYST1 42.330 85.480 64.060 90.00 90.00 90.00 P 21 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 0.023624 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011699 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015610 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
