HEADER SERINE PROTEASE INHIBITOR 06-AUG-96 1KCT
TITLE ALPHA1-ANTITRYPSIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA1-ANTITRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA1-PROTEINASE INHIBITOR;
COMPND 5 ENGINEERED: YES;
COMPND 6 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: A1AT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-8C;
SOURCE 10 EXPRESSION_SYSTEM_GENE: A1AT
KEYWDS SERPIN, SERINE PROTEASE INHIBITOR, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.K.SONG,S.W.SUH
REVDAT 5 07-FEB-24 1KCT 1 REMARK
REVDAT 4 03-NOV-21 1KCT 1 SEQADV
REVDAT 3 18-APR-18 1KCT 1 REMARK
REVDAT 2 24-FEB-09 1KCT 1 VERSN
REVDAT 1 11-JAN-97 1KCT 0
JRNL AUTH H.K.SONG,K.N.LEE,K.S.KWON,M.H.YU,S.W.SUH
JRNL TITL CRYSTAL STRUCTURE OF AN UNCLEAVED ALPHA 1-ANTITRYPSIN
JRNL TITL 2 REVEALS THE CONFORMATION OF ITS INHIBITORY REACTIVE LOOP.
JRNL REF FEBS LETT. V. 377 150 1995
JRNL REFN ISSN 0014-5793
JRNL PMID 8543039
JRNL DOI 10.1016/0014-5793(95)01331-8
REMARK 2
REMARK 2 RESOLUTION. 3.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 81.2
REMARK 3 NUMBER OF REFLECTIONS : 4079
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
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 : 2965
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) : 20.00
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) : NULL
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) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 2.440
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.42
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.940
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 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KCT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174406.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-94
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : DIFFRACTOMETER
REMARK 200 DETECTOR MANUFACTURER : ENRAF-NONIUS FAST
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MADNES
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 4380
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.6
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.0
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 57.43500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.99000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.43500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.99000
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLU A 1
REMARK 465 ASP A 2
REMARK 465 PRO A 3
REMARK 465 GLN A 4
REMARK 465 GLY A 5
REMARK 465 ASP A 6
REMARK 465 ALA A 7
REMARK 465 ALA A 8
REMARK 465 GLN A 9
REMARK 465 LYS A 10
REMARK 465 THR A 11
REMARK 465 ASP A 12
REMARK 465 THR A 13
REMARK 465 SER A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 ASP A 17
REMARK 465 GLN A 18
REMARK 465 ASP A 19
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 HIS A 20 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 394 CG CD CE NZ
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 LEU A 126 CA - CB - CG ANGL. DEV. = 18.6 DEGREES
REMARK 500 PRO A 197 C - N - CA ANGL. DEV. = 11.3 DEGREES
REMARK 500 PRO A 255 C - N - CA ANGL. DEV. = 11.3 DEGREES
REMARK 500 LEU A 286 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 PRO A 326 C - N - CA ANGL. DEV. = 12.6 DEGREES
REMARK 500 ILE A 360 N - CA - C ANGL. DEV. = -22.3 DEGREES
REMARK 500 PRO A 361 C - N - CA ANGL. DEV. = -17.4 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 PRO A 21 75.47 -69.30
REMARK 500 LEU A 30 -32.46 174.52
REMARK 500 LEU A 41 -53.93 -140.54
REMARK 500 ALA A 42 32.52 -75.85
REMARK 500 HIS A 43 -42.33 -138.43
REMARK 500 ASN A 46 29.67 173.03
REMARK 500 SER A 47 -42.40 -147.87
REMARK 500 VAL A 55 -50.39 -149.33
REMARK 500 ILE A 57 -65.64 -95.31
REMARK 500 ALA A 59 -68.92 -104.14
REMARK 500 ALA A 62 -22.56 -154.83
REMARK 500 LEU A 64 48.85 -108.95
REMARK 500 LEU A 66 -64.34 -122.56
REMARK 500 ALA A 68 121.45 167.38
REMARK 500 THR A 72 -79.00 -76.35
REMARK 500 HIS A 73 41.09 -69.88
REMARK 500 GLU A 75 -39.05 -172.58
REMARK 500 ILE A 76 -77.56 -72.93
REMARK 500 LEU A 80 42.90 -70.36
REMARK 500 ASN A 81 -58.69 71.53
REMARK 500 LEU A 84 -3.12 -44.00
REMARK 500 GLU A 89 -71.52 -52.10
REMARK 500 ALA A 90 -12.20 -49.89
REMARK 500 GLN A 91 60.76 -112.25
REMARK 500 ILE A 92 -10.07 -165.09
REMARK 500 GLN A 97 35.06 -76.15
REMARK 500 GLU A 98 51.32 -157.32
REMARK 500 LEU A 99 17.79 169.48
REMARK 500 LEU A 100 8.76 -158.68
REMARK 500 ARG A 101 -7.06 -167.76
REMARK 500 ASN A 104 -23.43 -172.84
REMARK 500 PRO A 106 99.93 -27.00
REMARK 500 ASP A 107 -174.47 -55.14
REMARK 500 SER A 108 -56.86 -120.17
REMARK 500 GLN A 109 -51.17 -122.18
REMARK 500 GLN A 111 -108.74 55.89
REMARK 500 LEU A 112 166.29 87.56
REMARK 500 THR A 113 37.12 -151.50
REMARK 500 LEU A 118 146.30 68.10
REMARK 500 LEU A 124 -148.76 -155.91
REMARK 500 LYS A 125 -24.75 -162.33
REMARK 500 LEU A 126 -169.37 29.25
REMARK 500 GLU A 132 56.50 -104.45
REMARK 500 ASP A 133 -66.34 -157.90
REMARK 500 HIS A 139 -22.38 75.11
REMARK 500 SER A 140 101.34 -10.02
REMARK 500 THR A 150 38.77 -78.83
REMARK 500 LYS A 155 27.12 -68.65
REMARK 500 GLN A 156 -21.95 -157.20
REMARK 500 ILE A 157 -68.89 -96.43
REMARK 500
REMARK 500 THIS ENTRY HAS 129 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: P1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: REACTIVE SITE IN INHIBITORY LOOP.
DBREF 1KCT A 1 394 UNP P01009 A1AT_HUMAN 25 418
SEQADV 1KCT ALA A 59 UNP P01009 THR 83 ENGINEERED MUTATION
SEQADV 1KCT ALA A 68 UNP P01009 THR 92 ENGINEERED MUTATION
SEQADV 1KCT GLY A 70 UNP P01009 ALA 94 ENGINEERED MUTATION
SEQRES 1 A 394 GLU ASP PRO GLN GLY ASP ALA ALA GLN LYS THR ASP THR
SEQRES 2 A 394 SER HIS HIS ASP GLN ASP HIS PRO THR PHE ASN LYS ILE
SEQRES 3 A 394 THR PRO ASN LEU ALA GLU PHE ALA PHE SER LEU TYR ARG
SEQRES 4 A 394 GLN LEU ALA HIS GLN SER ASN SER THR ASN ILE PHE PHE
SEQRES 5 A 394 SER PRO VAL SER ILE ALA ALA ALA PHE ALA MET LEU SER
SEQRES 6 A 394 LEU GLY ALA LYS GLY ASP THR HIS ASP GLU ILE LEU GLU
SEQRES 7 A 394 GLY LEU ASN PHE ASN LEU THR GLU ILE PRO GLU ALA GLN
SEQRES 8 A 394 ILE HIS GLU GLY PHE GLN GLU LEU LEU ARG THR LEU ASN
SEQRES 9 A 394 GLN PRO ASP SER GLN LEU GLN LEU THR THR GLY ASN GLY
SEQRES 10 A 394 LEU PHE LEU SER GLU GLY LEU LYS LEU VAL ASP LYS PHE
SEQRES 11 A 394 LEU GLU ASP VAL LYS LYS LEU TYR HIS SER GLU ALA PHE
SEQRES 12 A 394 THR VAL ASN PHE GLY ASP THR GLU GLU ALA LYS LYS GLN
SEQRES 13 A 394 ILE ASN ASP TYR VAL GLU LYS GLY THR GLN GLY LYS ILE
SEQRES 14 A 394 VAL ASP LEU VAL LYS GLU LEU ASP ARG ASP THR VAL PHE
SEQRES 15 A 394 ALA LEU VAL ASN TYR ILE PHE PHE LYS GLY LYS TRP GLU
SEQRES 16 A 394 ARG PRO PHE GLU VAL LYS ASP THR GLU GLU GLU ASP PHE
SEQRES 17 A 394 HIS VAL ASP GLN VAL THR THR VAL LYS VAL PRO MET MET
SEQRES 18 A 394 LYS ARG LEU GLY MET PHE ASN ILE GLN HIS CYS LYS LYS
SEQRES 19 A 394 LEU SER SER TRP VAL LEU LEU MET LYS TYR LEU GLY ASN
SEQRES 20 A 394 ALA THR ALA ILE PHE PHE LEU PRO ASP GLU GLY LYS LEU
SEQRES 21 A 394 GLN HIS LEU GLU ASN GLU LEU THR HIS ASP ILE ILE THR
SEQRES 22 A 394 LYS PHE LEU GLU ASN GLU ASP ARG ARG SER ALA SER LEU
SEQRES 23 A 394 HIS LEU PRO LYS LEU SER ILE THR GLY THR TYR ASP LEU
SEQRES 24 A 394 LYS SER VAL LEU GLY GLN LEU GLY ILE THR LYS VAL PHE
SEQRES 25 A 394 SER ASN GLY ALA ASP LEU SER GLY VAL THR GLU GLU ALA
SEQRES 26 A 394 PRO LEU LYS LEU SER LYS ALA VAL HIS LYS ALA VAL LEU
SEQRES 27 A 394 THR ILE ASP GLU LYS GLY THR GLU ALA ALA GLY ALA MET
SEQRES 28 A 394 PHE LEU GLU ALA ILE PRO MET SER ILE PRO PRO GLU VAL
SEQRES 29 A 394 LYS PHE ASN LYS PRO PHE VAL PHE LEU MET ILE GLU GLN
SEQRES 30 A 394 ASN THR LYS SER PRO LEU PHE MET GLY LYS VAL VAL ASN
SEQRES 31 A 394 PRO THR GLN LYS
HELIX 1 1 ASN A 24 THR A 27 1 4
HELIX 2 2 ALA A 34 TYR A 38 1 5
HELIX 3 3 LEU A 131 LEU A 137 1 7
HELIX 4 4 ASP A 270 THR A 273 1 4
HELIX 5 5 LEU A 303 LEU A 306 1 4
HELIX 6 6 THR A 309 VAL A 311 5 3
SHEET 1 A 2 ILE A 50 PHE A 52 0
SHEET 2 A 2 MET A 385 LYS A 387 -1 N LYS A 387 O ILE A 50
SHEET 1 B 2 ALA A 248 ILE A 251 0
SHEET 2 B 2 LEU A 373 GLU A 376 -1 N ILE A 375 O THR A 249
SITE 1 P1 1 MET A 358
CRYST1 114.870 39.980 92.420 90.00 102.82 90.00 C 1 2 1 4
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 0.008705 0.000000 0.001981 0.00000
SCALE2 0.000000 0.025013 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011097 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
