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HEADER AMINOPEPTIDASE 22-NOV-97 1AZW
TITLE PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV.
TITLE 2 CITRI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE IMINOPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.11.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOMONAS CAMPESTRIS PV. CITRI;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 4 EXPRESSION_SYSTEM_STRAIN: HB101
KEYWDS AMINOPEPTIDASE, PROLINE IMINOPEPTIDASE, SERINE PROTEASE,
KEYWDS 2 XANTHOMONAS CAMPESTRIS
EXPDTA X-RAY DIFFRACTION
AUTHOR F.J.MEDRANO,J.ALONSO,J.L.GARCIA,A.ROMERO,W.BODE,
AUTHOR 2 F.X.GOMIS-RUTH
REVDAT 1 13-JAN-99 1AZW 0
JRNL AUTH F.J.MEDRANO,J.ALONSO,J.L.GARCIA,A.ROMERO,W.BODE,
JRNL AUTH 2 F.X.GOMIS-RUTH
JRNL TITL STRUCTURE OF PROLINE IMINOPEPTIDASE FROM
JRNL TITL 2 XANTHOMONAS CAMPESTRIS PV. CITRI: A PROTOTYPE FOR
JRNL TITL 3 THE PROLYL OLIGOPEPTIDASE FAMILY
JRNL REF EMBO J. V. 17 1 1998
JRNL REFN ASTM EMJODG UK ISSN 0261-4189 0897
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.J.MEDRANO,J.ALONSO,J.L.GARCIA,W.BODE,
REMARK 1 AUTH 2 F.X.GOMIS-RUTH
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION
REMARK 1 TITL 2 ANALYSIS OF PROLINE IMINOPEPTIDASE FROM XANTHOMONAS
REMARK 1 TITL 3 CAMPESTRIS PV. CITRI
REMARK 1 REF FEBS LETT. V. 400 91 1997
REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 0165
REMARK 2
REMARK 2 RESOLUTION. 2.7 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.7
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.001
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 26672
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.0
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 : 6140
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 199
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 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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.53
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AZW COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 6
REMARK 6 SER 110 IS ARRANGED IN A SHARP GAMMA-TURN AND EXHIBITS AN
REMARK 6 ENERGETICALLY UNFAVORABLE CONFORMATION, IN THE
REMARK 6 RAMACHANDRAN PLOT THIS CORRESPONDS TO ONLY A GENEROUSLY
REMARK 6 ALLOWED REGION, BUT IS DEFINED BY CLEAR DENSITY.
REMARK 7
REMARK 7 PRO 44 AND PRO 76 EXHIBIT A CIS CONFORMATION.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : SEP-1996
REMARK 200 TEMPERATURE (KELVIN) : 260
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : ROTAVATA/AGROVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29854
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.7
REMARK 200 RESOLUTION RANGE LOW (A) : INFINITY
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 3.1
REMARK 200 R MERGE (I) : 0.096
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) : 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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIPLE
REMARK 200 ISOMORPHOUS REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.6
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM
REMARK 280 4.0 M NACL, 0.1 M SODIUM CITRATE, PH 6.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,Z
REMARK 290 6555 1/2-X,1/2-Y,Z
REMARK 290 7555 1/2-X,1/2+Y,-Z
REMARK 290 8555 1/2+X,1/2-Y,-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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 73.60518
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 83.90670
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 73.60518
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 83.90670
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 73.60518
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 83.90670
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 73.60518
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 83.90670
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 B 1 .. 313 A 1 .. 313 0.151
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: TAKEN FROM RELEASED PDB ENTRY
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AS
REMARK 800 SITE_DESCRIPTION: ACTIVE-SITE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1AZW GLN A 121 - GLN A 121 - INSERTED
REMARK 999 1AZW VAL A 127 - GLU A 129 - INSERTED
REMARK 999 1AZW GLN B 121 - GLN B 121 - INSERTED
REMARK 999 1AZW VAL B 127 - GLU B 129 - INSERTED
DBREF 1AZW A 1 120 SWS P52279 PIP_XANCI 1 120
DBREF 1AZW A 121 121 PDB 1AZW 1AZW 121 121
DBREF 1AZW A 122 124 SWS P52279 PIP_XANCI 121 123
DBREF 1AZW A 125 126 SWS P52279 PIP_XANCI 128 129
DBREF 1AZW A 127 129 PDB 1AZW 1AZW 127 129
DBREF 1AZW A 130 313 SWS P52279 PIP_XANCI 130 313
DBREF 1AZW B 1 120 SWS P52279 PIP_XANCI 1 120
DBREF 1AZW B 121 121 PDB 1AZW 1AZW 121 121
DBREF 1AZW B 122 124 SWS P52279 PIP_XANCI 121 123
DBREF 1AZW B 125 126 SWS P52279 PIP_XANCI 128 129
DBREF 1AZW B 127 129 PDB 1AZW 1AZW 127 129
DBREF 1AZW B 130 313 SWS P52279 PIP_XANCI 130 313
SEQADV 1AZW THR A 122 SWS P52279 ALA 121 CONFLICT
SEQADV 1AZW HIS A 123 SWS P52279 ASP 122 CONFLICT
SEQADV 1AZW A SWS P52279 SER 124 GAP IN PDB ENTRY
SEQADV 1AZW A SWS P52279 ALA 125 GAP IN PDB ENTRY
SEQADV 1AZW A SWS P52279 ALA 126 GAP IN PDB ENTRY
SEQADV 1AZW A SWS P52279 GLY 127 GAP IN PDB ENTRY
SEQADV 1AZW GLN A 125 SWS P52279 HIS 128 CONFLICT
SEQADV 1AZW THR B 122 SWS P52279 ALA 121 CONFLICT
SEQADV 1AZW HIS B 123 SWS P52279 ASP 122 CONFLICT
SEQADV 1AZW B SWS P52279 SER 124 GAP IN PDB ENTRY
SEQADV 1AZW B SWS P52279 ALA 125 GAP IN PDB ENTRY
SEQADV 1AZW B SWS P52279 ALA 126 GAP IN PDB ENTRY
SEQADV 1AZW B SWS P52279 GLY 127 GAP IN PDB ENTRY
SEQADV 1AZW GLN B 125 SWS P52279 HIS 128 CONFLICT
SEQRES 1 A 313 MET ARG THR LEU TYR PRO GLU ILE THR PRO TYR GLN GLN
SEQRES 2 A 313 GLY SER LEU LYS VAL ASP ASP ARG HIS THR LEU TYR PHE
SEQRES 3 A 313 GLU GLN CYS GLY ASN PRO HIS GLY LYS PRO VAL VAL MET
SEQRES 4 A 313 LEU HIS GLY GLY PRO GLY GLY GLY CYS ASN ASP LYS MET
SEQRES 5 A 313 ARG ARG PHE HIS ASP PRO ALA LYS TYR ARG ILE VAL LEU
SEQRES 6 A 313 PHE ASP GLN ARG GLY SER GLY ARG SER THR PRO HIS ALA
SEQRES 7 A 313 ASP LEU VAL ASP ASN THR THR TRP ASP LEU VAL ALA ASP
SEQRES 8 A 313 ILE GLU ARG LEU ARG THR HIS LEU GLY VAL ASP ARG TRP
SEQRES 9 A 313 GLN VAL PHE GLY GLY SER TRP GLY SER THR LEU ALA LEU
SEQRES 10 A 313 ALA TYR ALA GLN THR HIS PRO GLN GLN VAL THR GLU LEU
SEQRES 11 A 313 VAL LEU ARG GLY ILE PHE LEU LEU ARG ARG PHE GLU LEU
SEQRES 12 A 313 GLU TRP PHE TYR GLN GLU GLY ALA SER ARG LEU PHE PRO
SEQRES 13 A 313 ASP ALA TRP GLU HIS TYR LEU ASN ALA ILE PRO PRO VAL
SEQRES 14 A 313 GLU ARG ALA ASP LEU MET SER ALA PHE HIS ARG ARG LEU
SEQRES 15 A 313 THR SER ASP ASP GLU ALA THR ARG LEU ALA ALA ALA LYS
SEQRES 16 A 313 ALA TRP SER VAL TRP GLU GLY ALA THR SER PHE LEU HIS
SEQRES 17 A 313 VAL ASP GLU ASP PHE VAL THR GLY HIS GLU ASP ALA HIS
SEQRES 18 A 313 PHE ALA LEU ALA PHE ALA ARG ILE GLU ASN HIS TYR PHE
SEQRES 19 A 313 VAL ASN GLY GLY PHE PHE GLU VAL GLU ASP GLN LEU LEU
SEQRES 20 A 313 ARG ASP ALA HIS ARG ILE ALA ASP ILE PRO GLY VAL ILE
SEQRES 21 A 313 VAL HIS GLY ARG TYR ASP VAL VAL CYS PRO LEU GLN SER
SEQRES 22 A 313 ALA TRP ASP LEU HIS LYS ALA TRP PRO LYS ALA GLN LEU
SEQRES 23 A 313 GLN ILE SER PRO ALA SER GLY HIS SER ALA PHE GLU PRO
SEQRES 24 A 313 GLU ASN VAL ASP ALA LEU VAL ARG ALA THR ASP GLY PHE
SEQRES 25 A 313 ALA
SEQRES 1 B 313 MET ARG THR LEU TYR PRO GLU ILE THR PRO TYR GLN GLN
SEQRES 2 B 313 GLY SER LEU LYS VAL ASP ASP ARG HIS THR LEU TYR PHE
SEQRES 3 B 313 GLU GLN CYS GLY ASN PRO HIS GLY LYS PRO VAL VAL MET
SEQRES 4 B 313 LEU HIS GLY GLY PRO GLY GLY GLY CYS ASN ASP LYS MET
SEQRES 5 B 313 ARG ARG PHE HIS ASP PRO ALA LYS TYR ARG ILE VAL LEU
SEQRES 6 B 313 PHE ASP GLN ARG GLY SER GLY ARG SER THR PRO HIS ALA
SEQRES 7 B 313 ASP LEU VAL ASP ASN THR THR TRP ASP LEU VAL ALA ASP
SEQRES 8 B 313 ILE GLU ARG LEU ARG THR HIS LEU GLY VAL ASP ARG TRP
SEQRES 9 B 313 GLN VAL PHE GLY GLY SER TRP GLY SER THR LEU ALA LEU
SEQRES 10 B 313 ALA TYR ALA GLN THR HIS PRO GLN GLN VAL THR GLU LEU
SEQRES 11 B 313 VAL LEU ARG GLY ILE PHE LEU LEU ARG ARG PHE GLU LEU
SEQRES 12 B 313 GLU TRP PHE TYR GLN GLU GLY ALA SER ARG LEU PHE PRO
SEQRES 13 B 313 ASP ALA TRP GLU HIS TYR LEU ASN ALA ILE PRO PRO VAL
SEQRES 14 B 313 GLU ARG ALA ASP LEU MET SER ALA PHE HIS ARG ARG LEU
SEQRES 15 B 313 THR SER ASP ASP GLU ALA THR ARG LEU ALA ALA ALA LYS
SEQRES 16 B 313 ALA TRP SER VAL TRP GLU GLY ALA THR SER PHE LEU HIS
SEQRES 17 B 313 VAL ASP GLU ASP PHE VAL THR GLY HIS GLU ASP ALA HIS
SEQRES 18 B 313 PHE ALA LEU ALA PHE ALA ARG ILE GLU ASN HIS TYR PHE
SEQRES 19 B 313 VAL ASN GLY GLY PHE PHE GLU VAL GLU ASP GLN LEU LEU
SEQRES 20 B 313 ARG ASP ALA HIS ARG ILE ALA ASP ILE PRO GLY VAL ILE
SEQRES 21 B 313 VAL HIS GLY ARG TYR ASP VAL VAL CYS PRO LEU GLN SER
SEQRES 22 B 313 ALA TRP ASP LEU HIS LYS ALA TRP PRO LYS ALA GLN LEU
SEQRES 23 B 313 GLN ILE SER PRO ALA SER GLY HIS SER ALA PHE GLU PRO
SEQRES 24 B 313 GLU ASN VAL ASP ALA LEU VAL ARG ALA THR ASP GLY PHE
SEQRES 25 B 313 ALA
FORMUL 3 HOH *199(H2 O1)
HELIX 1 1 ASP A 50 PHE A 55 5 6
HELIX 2 2 THR A 85 HIS A 98 1 14
HELIX 3 3 SER A 110 THR A 122 5 13
HELIX 4 4 PRO A 124 GLN A 126 5 3
HELIX 5 5 ARG A 140 TYR A 147 1 8
HELIX 6 6 ALA A 151 LEU A 154 1 4
HELIX 7 7 PRO A 156 ALA A 165 1 10
HELIX 8 8 PRO A 168 GLU A 170 5 3
HELIX 9 9 LEU A 174 LEU A 182 1 9
HELIX 10 10 GLU A 187 GLY A 202 1 16
HELIX 11 11 GLU A 211 GLU A 218 1 8
HELIX 12 12 ALA A 220 VAL A 235 1 16
HELIX 13 13 GLY A 237 PHE A 239 5 3
HELIX 14 14 GLN A 245 ARG A 248 1 4
HELIX 15 15 ALA A 250 ILE A 253 5 4
HELIX 16 16 LEU A 271 ALA A 280 1 10
HELIX 17 17 PRO A 299 GLY A 311 1 13
HELIX 18 18 LYS B 51 PHE B 55 5 5
HELIX 19 19 THR B 85 HIS B 98 1 14
HELIX 20 20 SER B 110 THR B 122 5 13
HELIX 21 21 PRO B 124 GLN B 126 5 3
HELIX 22 22 ARG B 140 TYR B 147 1 8
HELIX 23 23 ALA B 151 ARG B 153 5 3
HELIX 24 24 PRO B 156 ALA B 165 1 10
HELIX 25 25 PRO B 168 GLU B 170 5 3
HELIX 26 26 LEU B 174 LEU B 182 1 9
HELIX 27 27 GLU B 187 THR B 204 1 18
HELIX 28 28 GLU B 211 HIS B 217 1 7
HELIX 29 29 ALA B 220 VAL B 235 1 16
HELIX 30 30 GLY B 237 PHE B 239 5 3
HELIX 31 31 GLN B 245 ARG B 248 1 4
HELIX 32 32 ALA B 250 ILE B 253 5 4
HELIX 33 33 LEU B 271 ALA B 280 1 10
HELIX 34 34 PRO B 299 GLY B 311 1 13
SHEET 1 A 8 GLN A 12 LYS A 17 0
SHEET 2 A 8 THR A 23 GLY A 30 -1 N GLN A 28 O GLN A 12
SHEET 3 A 8 TYR A 61 PHE A 66 -1 N LEU A 65 O GLU A 27
SHEET 4 A 8 LYS A 35 LEU A 40 1 N LYS A 35 O ARG A 62
SHEET 5 A 8 GLN A 105 GLY A 109 1 N GLN A 105 O VAL A 38
SHEET 6 A 8 GLU A 129 ARG A 133 1 N VAL A 131 O VAL A 106
SHEET 7 A 8 PRO A 257 GLY A 263 1 N PRO A 257 O LEU A 130
SHEET 8 A 8 GLN A 285 SER A 289 1 N GLN A 285 O ILE A 260
SHEET 1 B 8 GLN B 12 LYS B 17 0
SHEET 2 B 8 THR B 23 GLY B 30 -1 N GLN B 28 O GLN B 12
SHEET 3 B 8 TYR B 61 PHE B 66 -1 N LEU B 65 O GLU B 27
SHEET 4 B 8 LYS B 35 LEU B 40 1 N LYS B 35 O ARG B 62
SHEET 5 B 8 GLN B 105 GLY B 109 1 N GLN B 105 O VAL B 38
SHEET 6 B 8 GLU B 129 ARG B 133 1 N VAL B 131 O VAL B 106
SHEET 7 B 8 PRO B 257 GLY B 263 1 N PRO B 257 O LEU B 130
SHEET 8 B 8 GLN B 285 SER B 289 1 N GLN B 285 O ILE B 260
CISPEP 1 GLY A 43 PRO A 44 0 0.06
CISPEP 2 THR A 75 PRO A 76 0 -0.17
CISPEP 3 GLY B 43 PRO B 44 0 -0.12
CISPEP 4 THR B 75 PRO B 76 0 -0.12
SITE 1 AS 3 GLY A 100 ASP A 266 HIS A 294
CRYST1 147.200 167.800 85.600 90.00 90.00 90.00 C 2 2 2 16
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 0.006793 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005959 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011682 0.00000
MTRIX1 1 -0.735159 -0.677868 -0.006000 92.45860 1
MTRIX2 1 -0.677881 0.735171 0.000290 36.07255 1
MTRIX3 1 0.004214 0.004281 -0.999982 114.15431 1 |