HEADER TRANSFERASE 11-DEC-97 1GUK
TITLE CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE A4-4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MGSTA4-4, GST5.7;
COMPND 5 EC: 2.5.1.18;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 ORGAN: LUNG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLUTATHIONE S-TRANSFERASE, GST, CRYSTAL STRUCTURE,
KEYWDS 2 OXIDATIVE STRESS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR U.KRENGEL,K.H.SCHROTER,H.HOIER,B.W.DIJKSTRA
REVDAT 2 24-FEB-09 1GUK 1 VERSN
REVDAT 1 08-APR-98 1GUK 0
JRNL AUTH U.KRENGEL,K.H.SCHROTER,H.HOIER,A.ARKEMA,K.H.KALK,
JRNL AUTH 2 P.ZIMNIAK,B.W.DIJKSTRA
JRNL TITL CRYSTAL STRUCTURE OF A MURINE ALPHA-CLASS
JRNL TITL 2 GLUTATHIONE S-TRANSFERASE INVOLVED IN CELLULAR
JRNL TITL 3 DEFENSE AGAINST OXIDATIVE STRESS.
JRNL REF FEBS LETT. V. 422 285 1998
JRNL REFN ISSN 0014-5793
JRNL PMID 9498801
JRNL DOI 10.1016/S0014-5793(98)00026-X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 5.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 77.8
REMARK 3 NUMBER OF REFLECTIONS : 9798
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1089
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3432
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.60
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.71
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.23
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.91
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : TOPHCSDX.PRO
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DURING THE REFINEMENT, 10% OF THE
REMARK 3 REFLECTIONS WERE SET ASIDE TO CALCULATE THE FREE R-FACTOR. THE
REMARK 3 LAST CYCLE, WHICH RESULTED IN AN R-FACTOR OF 22.9% AND A FREE
REMARK 3 R-FACTOR OF 30.3%, WAS THEN REPEATED USING ALL THE REFLECTIONS
REMARK 3 FOR THE FINAL RESULTS.
REMARK 4
REMARK 4 1GUK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-94
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 8.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.04
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 180 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10477
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 42.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.0
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
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 (%) : 75.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.31900
REMARK 200 R SYM FOR SHELL (I) : 0.31900
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.843
REMARK 200 STARTING MODEL: HGSTA1-1 DIMER (1GUH)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION BY HANGING DROP
REMARK 280 VAPOR DIFFUSION RESERVOIR: 9% PEG 8000, 0.1 M TRIS/HCL PH 8.1,
REMARK 280 5% MPD PROTEIN: 10 MG/ML DISSOLVED IN H20 DROP: 5 + 5
REMARK 280 MICROLITER, VAPOR DIFFUSION - HANGING DROP
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 57.15000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 57.15000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.95000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 LYS A 4
REMARK 465 LEU A 220
REMARK 465 LYS A 221
REMARK 465 PHE A 222
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 LYS B 4
REMARK 465 PRO B 114
REMARK 465 LYS B 115
REMARK 465 GLU B 116
REMARK 465 LYS B 117
REMARK 465 GLU B 118
REMARK 465 GLU B 119
REMARK 465 LEU B 220
REMARK 465 LYS B 221
REMARK 465 PHE B 222
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 TYR A 9 -178.48 171.76
REMARK 500 ARG A 13 -76.58 -80.02
REMARK 500 GLU A 33 108.22 -168.35
REMARK 500 GLU A 36 -78.90 -86.92
REMARK 500 ARG A 38 -48.20 -7.27
REMARK 500 LEU A 51 -71.65 -47.05
REMARK 500 MET A 64 79.69 -103.69
REMARK 500 THR A 66 -15.13 -142.39
REMARK 500 THR A 68 -78.01 -41.62
REMARK 500 ASN A 80 64.00 -45.53
REMARK 500 GLU A 145 154.05 -15.33
REMARK 500 PRO A 173 -77.54 -57.04
REMARK 500 VAL A 174 -27.20 57.04
REMARK 500 LEU A 175 -10.40 -153.55
REMARK 500 PHE A 178 74.77 -112.56
REMARK 500 TYR B 9 -178.55 171.65
REMARK 500 ARG B 13 -75.85 -79.79
REMARK 500 GLU B 33 109.00 -168.28
REMARK 500 GLU B 36 -78.83 -87.24
REMARK 500 ARG B 38 -47.94 -6.92
REMARK 500 PRO B 56 157.50 -49.81
REMARK 500 THR B 66 -21.79 -144.59
REMARK 500 THR B 68 -74.88 -45.40
REMARK 500 ASN B 80 64.99 -46.61
REMARK 500 ARG B 131 -60.75 -97.72
REMARK 500 GLU B 145 157.30 -13.41
REMARK 500 PRO B 173 -76.73 -53.27
REMARK 500 VAL B 174 -19.88 55.00
REMARK 500 LEU B 175 -14.98 -156.32
REMARK 500 ASP B 209 -75.75 -130.72
REMARK 500 PRO B 211 47.28 -67.35
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 VAL A 174 LEU A 175 -147.11
REMARK 500 PRO B 211 TYR B 212 131.96
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 PHE A 178 0.09 SIDE_CHAIN
REMARK 500 PHE A 184 0.08 SIDE_CHAIN
REMARK 500 TYR A 212 0.07 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PRO A 173 12.57
REMARK 500 PRO B 173 13.20
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GUK A 1 222 UNP P24472 GSTA4_MOUSE 1 222
DBREF 1GUK B 1 222 UNP P24472 GSTA4_MOUSE 1 222
SEQRES 1 A 222 MET ALA ALA LYS PRO LYS LEU TYR TYR PHE ASN GLY ARG
SEQRES 2 A 222 GLY ARG MET GLU SER ILE ARG TRP LEU LEU ALA ALA ALA
SEQRES 3 A 222 GLY VAL GLU PHE GLU GLU GLU PHE LEU GLU THR ARG GLU
SEQRES 4 A 222 GLN TYR GLU LYS MET GLN LYS ASP GLY HIS LEU LEU PHE
SEQRES 5 A 222 GLY GLN VAL PRO LEU VAL GLU ILE ASP GLY MET MET LEU
SEQRES 6 A 222 THR GLN THR ARG ALA ILE LEU SER TYR LEU ALA ALA LYS
SEQRES 7 A 222 TYR ASN LEU TYR GLY LYS ASP LEU LYS GLU ARG VAL ARG
SEQRES 8 A 222 ILE ASP MET TYR ALA ASP GLY THR GLN ASP LEU MET MET
SEQRES 9 A 222 MET ILE ALA VAL ALA PRO PHE LYS THR PRO LYS GLU LYS
SEQRES 10 A 222 GLU GLU SER TYR ASP LEU ILE LEU SER ARG ALA LYS THR
SEQRES 11 A 222 ARG TYR PHE PRO VAL PHE GLU LYS ILE LEU LYS ASP HIS
SEQRES 12 A 222 GLY GLU ALA PHE LEU VAL GLY ASN GLN LEU SER TRP ALA
SEQRES 13 A 222 ASP ILE GLN LEU LEU GLU ALA ILE LEU MET VAL GLU GLU
SEQRES 14 A 222 LEU SER ALA PRO VAL LEU SER ASP PHE PRO LEU LEU GLN
SEQRES 15 A 222 ALA PHE LYS THR ARG ILE SER ASN ILE PRO THR ILE LYS
SEQRES 16 A 222 LYS PHE LEU GLN PRO GLY SER GLN ARG LYS PRO PRO PRO
SEQRES 17 A 222 ASP GLY PRO TYR VAL GLU VAL VAL ARG ILE VAL LEU LYS
SEQRES 18 A 222 PHE
SEQRES 1 B 222 MET ALA ALA LYS PRO LYS LEU TYR TYR PHE ASN GLY ARG
SEQRES 2 B 222 GLY ARG MET GLU SER ILE ARG TRP LEU LEU ALA ALA ALA
SEQRES 3 B 222 GLY VAL GLU PHE GLU GLU GLU PHE LEU GLU THR ARG GLU
SEQRES 4 B 222 GLN TYR GLU LYS MET GLN LYS ASP GLY HIS LEU LEU PHE
SEQRES 5 B 222 GLY GLN VAL PRO LEU VAL GLU ILE ASP GLY MET MET LEU
SEQRES 6 B 222 THR GLN THR ARG ALA ILE LEU SER TYR LEU ALA ALA LYS
SEQRES 7 B 222 TYR ASN LEU TYR GLY LYS ASP LEU LYS GLU ARG VAL ARG
SEQRES 8 B 222 ILE ASP MET TYR ALA ASP GLY THR GLN ASP LEU MET MET
SEQRES 9 B 222 MET ILE ALA VAL ALA PRO PHE LYS THR PRO LYS GLU LYS
SEQRES 10 B 222 GLU GLU SER TYR ASP LEU ILE LEU SER ARG ALA LYS THR
SEQRES 11 B 222 ARG TYR PHE PRO VAL PHE GLU LYS ILE LEU LYS ASP HIS
SEQRES 12 B 222 GLY GLU ALA PHE LEU VAL GLY ASN GLN LEU SER TRP ALA
SEQRES 13 B 222 ASP ILE GLN LEU LEU GLU ALA ILE LEU MET VAL GLU GLU
SEQRES 14 B 222 LEU SER ALA PRO VAL LEU SER ASP PHE PRO LEU LEU GLN
SEQRES 15 B 222 ALA PHE LYS THR ARG ILE SER ASN ILE PRO THR ILE LYS
SEQRES 16 B 222 LYS PHE LEU GLN PRO GLY SER GLN ARG LYS PRO PRO PRO
SEQRES 17 B 222 ASP GLY PRO TYR VAL GLU VAL VAL ARG ILE VAL LEU LYS
SEQRES 18 B 222 PHE
HELIX 1 1 GLU A 17 ALA A 26 1 10
HELIX 2 2 GLU A 39 LYS A 46 1 8
HELIX 3 3 THR A 68 LYS A 78 1 11
HELIX 4 4 LEU A 86 PHE A 111 1 26
HELIX 5 5 PRO A 114 THR A 130 1 17
HELIX 6 6 PHE A 133 HIS A 143 1 11
HELIX 7 7 ASP A 157 GLU A 168 1 12
HELIX 8 8 PRO A 179 SER A 189 1 11
HELIX 9 9 PRO A 192 PHE A 197 1 6
HELIX 10 10 GLY A 210 ILE A 218 1 9
HELIX 11 11 GLU B 17 ALA B 26 1 10
HELIX 12 12 GLU B 39 LYS B 46 1 8
HELIX 13 13 THR B 68 LYS B 78 1 11
HELIX 14 14 LEU B 86 PHE B 111 1 26
HELIX 15 15 TYR B 121 THR B 130 1 10
HELIX 16 16 PHE B 133 HIS B 143 1 11
HELIX 17 17 ASP B 157 GLU B 168 1 12
HELIX 18 18 PRO B 179 SER B 189 1 11
HELIX 19 19 PRO B 192 LEU B 198 1 7
HELIX 20 20 VAL B 213 ILE B 218 1 6
SHEET 1 A 4 GLU A 31 PHE A 34 0
SHEET 2 A 4 LYS A 6 TYR A 9 1 N LEU A 7 O GLU A 31
SHEET 3 A 4 LEU A 57 ILE A 60 -1 N GLU A 59 O LYS A 6
SHEET 4 A 4 MET A 63 LEU A 65 -1 N LEU A 65 O VAL A 58
SHEET 1 B 4 GLU B 31 PHE B 34 0
SHEET 2 B 4 LYS B 6 TYR B 9 1 N LEU B 7 O GLU B 31
SHEET 3 B 4 LEU B 57 ILE B 60 -1 N GLU B 59 O LYS B 6
SHEET 4 B 4 MET B 63 LEU B 65 -1 N LEU B 65 O VAL B 58
CISPEP 1 VAL A 55 PRO A 56 0 11.96
CISPEP 2 VAL B 55 PRO B 56 0 11.22
CRYST1 114.300 95.900 50.800 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 0.008749 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010428 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019685 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
