HEADER PROTEIN TRANSPORT 21-MAR-12 4E9J
TITLE CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF THE SECRETIN XCPQ FROM
TITLE 2 PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENERAL SECRETION PATHWAY PROTEIN D;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 35-277;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: ATCC 15692/PAO1/1C/PRS 101/LMG 12228;
SOURCE 5 GENE: XCPQ, PA3105;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HOMODIMER, XCPQ, PERIPLASMIC DOMAIN, STRUCTURAL PROTEIN, PERIPLASMIC
KEYWDS 2 SPACE, OUTER MEMBRANE, PROTEIN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR R.VAN DER MEEREN
REVDAT 5 28-FEB-24 4E9J 1 REMARK SEQADV LINK
REVDAT 4 06-FEB-13 4E9J 1 JRNL
REVDAT 3 16-JAN-13 4E9J 1 JRNL
REVDAT 2 02-JAN-13 4E9J 1 JRNL
REVDAT 1 05-DEC-12 4E9J 0
JRNL AUTH R.VAN DER MEEREN,Y.WEN,P.VAN GELDER,J.TOMMASSEN,B.DEVREESE,
JRNL AUTH 2 S.N.SAVVIDES
JRNL TITL NEW INSIGHTS INTO THE ASSEMBLY OF BACTERIAL SECRETINS:
JRNL TITL 2 STRUCTURAL STUDIES OF THE PERIPLASMIC DOMAIN OF XCPQ FROM
JRNL TITL 3 PSEUDOMONAS AERUGINOSA.
JRNL REF J.BIOL.CHEM. V. 288 1214 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23188826
JRNL DOI 10.1074/JBC.M112.432096
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX + BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 27839
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 1382
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 2.1100 - 2.0300 0.98 2772 144 0.2077 0.2329
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.68390
REMARK 3 B22 (A**2) : -1.66240
REMARK 3 B33 (A**2) : -1.02150
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.30400
REMARK 3 B23 (A**2) : 0.00000
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 : 0.010 6175
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL 1339
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 4E9J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071339.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9193
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28407
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030
REMARK 200 RESOLUTION RANGE LOW (A) : 39.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 40.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MGCL2, 0.1M TRIS PH 8.5, 25%
REMARK 280 PEG3350, EVAPORATION, TEMPERATURE 293.15K
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 59.75000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.86000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.75000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.86000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 MG MG B 301 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 377 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 457 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 SER A 32
REMARK 465 HIS A 33
REMARK 465 MET A 34
REMARK 465 GLU A 35
REMARK 465 ASN A 36
REMARK 465 SER A 37
REMARK 465 GLY A 38
REMARK 465 GLY A 39
REMARK 465 ASN A 40
REMARK 465 GLY A 46
REMARK 465 ASN A 47
REMARK 465 GLN A 48
REMARK 465 GLN A 49
REMARK 465 GLU A 50
REMARK 465 GLU A 129
REMARK 465 ALA A 130
REMARK 465 LYS A 131
REMARK 465 THR A 132
REMARK 465 GLU A 133
REMARK 465 ALA A 134
REMARK 465 GLY A 135
REMARK 465 GLY A 136
REMARK 465 GLY A 137
REMARK 465 GLN A 138
REMARK 465 SER A 139
REMARK 465 PRO A 274
REMARK 465 THR A 275
REMARK 465 ALA A 276
REMARK 465 ARG A 277
REMARK 465 SER B 32
REMARK 465 HIS B 33
REMARK 465 MET B 34
REMARK 465 GLU B 35
REMARK 465 ASN B 36
REMARK 465 SER B 37
REMARK 465 GLY B 38
REMARK 465 GLY B 39
REMARK 465 ASN B 40
REMARK 465 ALA B 41
REMARK 465 PHE B 42
REMARK 465 VAL B 43
REMARK 465 PRO B 44
REMARK 465 ALA B 45
REMARK 465 GLY B 46
REMARK 465 ASN B 47
REMARK 465 GLN B 48
REMARK 465 GLN B 49
REMARK 465 GLU B 50
REMARK 465 ALA B 128
REMARK 465 GLU B 129
REMARK 465 ALA B 130
REMARK 465 LYS B 131
REMARK 465 THR B 132
REMARK 465 GLU B 133
REMARK 465 ALA B 134
REMARK 465 GLY B 135
REMARK 465 GLY B 136
REMARK 465 GLY B 137
REMARK 465 GLN B 138
REMARK 465 SER B 139
REMARK 465 ALA B 140
REMARK 465 PRO B 141
REMARK 465 ASP B 142
REMARK 465 PRO B 274
REMARK 465 THR B 275
REMARK 465 ALA B 276
REMARK 465 ARG B 277
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 GLU A 71 CG CD OE1 OE2
REMARK 470 GLU A 75 CG CD OE1 OE2
REMARK 470 LYS A 84 CG CD CE NZ
REMARK 470 LYS A 92 CG CD CE NZ
REMARK 470 ASP A 120 CG OD1 OD2
REMARK 470 GLN A 121 CG CD OE1 NE2
REMARK 470 ASP A 142 CG OD1 OD2
REMARK 470 ARG A 143 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 152 CG CD OE1 NE2
REMARK 470 GLN A 169 CG CD OE1 NE2
REMARK 470 ARG A 187 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 190 CG OD1 ND2
REMARK 470 ARG A 193 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 196 CG OD1 OD2
REMARK 470 ARG A 199 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 200 CG CD OE1 NE2
REMARK 470 GLN A 203 CG CD OE1 NE2
REMARK 470 LYS A 204 CG CD CE NZ
REMARK 470 LYS A 236 CG CD CE NZ
REMARK 470 ARG A 248 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 263 CG CD CE NZ
REMARK 470 GLN A 266 CG CD OE1 NE2
REMARK 470 GLU B 75 CG CD OE1 OE2
REMARK 470 ARG B 82 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 84 CG CD CE NZ
REMARK 470 LEU B 97 CG CD1 CD2
REMARK 470 GLN B 102 CG CD OE1 NE2
REMARK 470 GLN B 118 CG CD OE1 NE2
REMARK 470 ASP B 120 CG OD1 OD2
REMARK 470 GLN B 121 CG CD OE1 NE2
REMARK 470 ARG B 143 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 145 CG CD OE1 OE2
REMARK 470 GLN B 169 CG CD OE1 NE2
REMARK 470 ARG B 187 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 193 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 232 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 236 CG CD CE NZ
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 HD22 ASN B 56 HZ2 LYS B 58 1.18
REMARK 500 OG1 THR A 110 HG SER A 185 1.58
REMARK 500 HG SER B 106 O HOH B 504 1.58
REMARK 500 HZ3 LYS B 263 O HOH B 517 1.60
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 ASN A 56 74.24 -151.31
REMARK 500 ASP A 186 -177.17 -171.12
REMARK 500 ASP B 186 -179.30 -170.27
REMARK 500 ASP B 272 47.98 -102.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 67 OD1
REMARK 620 2 HOH B 503 O 89.3
REMARK 620 3 HOH B 520 O 94.9 79.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EC5 RELATED DB: PDB
DBREF 4E9J A 35 277 UNP P35818 GSPD_PSEAE 35 277
DBREF 4E9J B 35 277 UNP P35818 GSPD_PSEAE 35 277
SEQADV 4E9J SER A 32 UNP P35818 EXPRESSION TAG
SEQADV 4E9J HIS A 33 UNP P35818 EXPRESSION TAG
SEQADV 4E9J MET A 34 UNP P35818 EXPRESSION TAG
SEQADV 4E9J SER B 32 UNP P35818 EXPRESSION TAG
SEQADV 4E9J HIS B 33 UNP P35818 EXPRESSION TAG
SEQADV 4E9J MET B 34 UNP P35818 EXPRESSION TAG
SEQRES 1 A 246 SER HIS MET GLU ASN SER GLY GLY ASN ALA PHE VAL PRO
SEQRES 2 A 246 ALA GLY ASN GLN GLN GLU ALA HIS TRP THR ILE ASN LEU
SEQRES 3 A 246 LYS ASP ALA ASP ILE ARG GLU PHE ILE ASP GLN ILE SER
SEQRES 4 A 246 GLU ILE THR GLY GLU THR PHE VAL VAL ASP PRO ARG VAL
SEQRES 5 A 246 LYS GLY GLN VAL SER VAL VAL SER LYS ALA GLN LEU SER
SEQRES 6 A 246 LEU SER GLU VAL TYR GLN LEU PHE LEU SER VAL MET SER
SEQRES 7 A 246 THR HIS GLY PHE THR VAL VAL ALA GLN GLY ASP GLN ALA
SEQRES 8 A 246 ARG ILE VAL PRO ASN ALA GLU ALA LYS THR GLU ALA GLY
SEQRES 9 A 246 GLY GLY GLN SER ALA PRO ASP ARG LEU GLU THR ARG VAL
SEQRES 10 A 246 ILE GLN VAL GLN GLN SER PRO VAL SER GLU LEU ILE PRO
SEQRES 11 A 246 LEU ILE ARG PRO LEU VAL PRO GLN TYR GLY HIS LEU ALA
SEQRES 12 A 246 ALA VAL PRO SER ALA ASN ALA LEU ILE ILE SER ASP ARG
SEQRES 13 A 246 SER ALA ASN ILE ALA ARG ILE GLU ASP VAL ILE ARG GLN
SEQRES 14 A 246 LEU ASP GLN LYS GLY SER HIS ASP TYR SER VAL ILE ASN
SEQRES 15 A 246 LEU ARG TYR GLY TRP VAL MET ASP ALA ALA GLU VAL LEU
SEQRES 16 A 246 ASN ASN ALA MET SER ARG GLY GLN ALA LYS GLY ALA ALA
SEQRES 17 A 246 GLY ALA GLN VAL ILE ALA ASP ALA ARG THR ASN ARG LEU
SEQRES 18 A 246 ILE ILE LEU GLY PRO PRO GLN ALA ARG ALA LYS LEU VAL
SEQRES 19 A 246 GLN LEU ALA GLN SER LEU ASP THR PRO THR ALA ARG
SEQRES 1 B 246 SER HIS MET GLU ASN SER GLY GLY ASN ALA PHE VAL PRO
SEQRES 2 B 246 ALA GLY ASN GLN GLN GLU ALA HIS TRP THR ILE ASN LEU
SEQRES 3 B 246 LYS ASP ALA ASP ILE ARG GLU PHE ILE ASP GLN ILE SER
SEQRES 4 B 246 GLU ILE THR GLY GLU THR PHE VAL VAL ASP PRO ARG VAL
SEQRES 5 B 246 LYS GLY GLN VAL SER VAL VAL SER LYS ALA GLN LEU SER
SEQRES 6 B 246 LEU SER GLU VAL TYR GLN LEU PHE LEU SER VAL MET SER
SEQRES 7 B 246 THR HIS GLY PHE THR VAL VAL ALA GLN GLY ASP GLN ALA
SEQRES 8 B 246 ARG ILE VAL PRO ASN ALA GLU ALA LYS THR GLU ALA GLY
SEQRES 9 B 246 GLY GLY GLN SER ALA PRO ASP ARG LEU GLU THR ARG VAL
SEQRES 10 B 246 ILE GLN VAL GLN GLN SER PRO VAL SER GLU LEU ILE PRO
SEQRES 11 B 246 LEU ILE ARG PRO LEU VAL PRO GLN TYR GLY HIS LEU ALA
SEQRES 12 B 246 ALA VAL PRO SER ALA ASN ALA LEU ILE ILE SER ASP ARG
SEQRES 13 B 246 SER ALA ASN ILE ALA ARG ILE GLU ASP VAL ILE ARG GLN
SEQRES 14 B 246 LEU ASP GLN LYS GLY SER HIS ASP TYR SER VAL ILE ASN
SEQRES 15 B 246 LEU ARG TYR GLY TRP VAL MET ASP ALA ALA GLU VAL LEU
SEQRES 16 B 246 ASN ASN ALA MET SER ARG GLY GLN ALA LYS GLY ALA ALA
SEQRES 17 B 246 GLY ALA GLN VAL ILE ALA ASP ALA ARG THR ASN ARG LEU
SEQRES 18 B 246 ILE ILE LEU GLY PRO PRO GLN ALA ARG ALA LYS LEU VAL
SEQRES 19 B 246 GLN LEU ALA GLN SER LEU ASP THR PRO THR ALA ARG
HET MG B 301 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG MG 2+
FORMUL 4 HOH *203(H2 O)
HELIX 1 1 ILE A 62 GLY A 74 1 13
HELIX 2 2 LEU A 97 HIS A 111 1 15
HELIX 3 3 PRO A 155 ARG A 164 1 10
HELIX 4 4 PRO A 165 VAL A 167 5 3
HELIX 5 5 PRO A 177 ALA A 179 5 3
HELIX 6 6 ARG A 187 GLN A 203 1 17
HELIX 7 7 TRP A 218 ARG A 232 1 15
HELIX 8 8 ALA A 247 THR A 249 5 3
HELIX 9 9 PRO A 257 ASP A 272 1 16
HELIX 10 10 ILE B 62 GLY B 74 1 13
HELIX 11 11 SER B 96 HIS B 111 1 16
HELIX 12 12 PRO B 155 ARG B 164 1 10
HELIX 13 13 PRO B 165 VAL B 167 5 3
HELIX 14 14 PRO B 177 ALA B 179 5 3
HELIX 15 15 ARG B 187 ASP B 202 1 16
HELIX 16 16 TRP B 218 ARG B 232 1 15
HELIX 17 17 PRO B 257 ASP B 272 1 16
SHEET 1 A 6 PHE A 42 PRO A 44 0
SHEET 2 A 6 HIS A 52 ASP A 61 -1 O THR A 54 N VAL A 43
SHEET 3 A 6 GLN A 86 SER A 96 -1 O VAL A 87 N ALA A 60
SHEET 4 A 6 GLU A 145 GLN A 150 1 O THR A 146 N SER A 88
SHEET 5 A 6 ALA A 181 ASP A 186 -1 O ASP A 186 N GLU A 145
SHEET 6 A 6 HIS A 172 VAL A 176 -1 N ALA A 174 O ILE A 183
SHEET 1 B 3 PHE A 77 VAL A 79 0
SHEET 2 B 3 ALA A 122 PRO A 126 1 O ALA A 122 N VAL A 78
SHEET 3 B 3 PHE A 113 ALA A 117 -1 N VAL A 116 O ARG A 123
SHEET 1 C 6 GLN A 242 ASP A 246 0
SHEET 2 C 6 ARG A 251 LEU A 255 -1 O LEU A 255 N GLN A 242
SHEET 3 C 6 TYR A 209 ASN A 213 -1 N SER A 210 O ILE A 254
SHEET 4 C 6 TYR B 209 ASN B 213 -1 O VAL B 211 N TYR A 209
SHEET 5 C 6 ARG B 251 LEU B 255 -1 O ILE B 254 N SER B 210
SHEET 6 C 6 GLN B 242 ASP B 246 -1 N GLN B 242 O LEU B 255
SHEET 1 D 5 TRP B 53 ASP B 61 0
SHEET 2 D 5 GLN B 86 LEU B 95 -1 O VAL B 87 N ALA B 60
SHEET 3 D 5 GLU B 145 GLN B 150 1 O THR B 146 N SER B 88
SHEET 4 D 5 ALA B 181 ASP B 186 -1 O LEU B 182 N ILE B 149
SHEET 5 D 5 HIS B 172 VAL B 176 -1 N ALA B 174 O ILE B 183
SHEET 1 E 3 PHE B 77 VAL B 79 0
SHEET 2 E 3 GLN B 121 PRO B 126 1 O ILE B 124 N VAL B 78
SHEET 3 E 3 PHE B 113 GLN B 118 -1 N THR B 114 O VAL B 125
LINK OD1 ASP B 67 MG MG B 301 1555 1555 2.00
LINK MG MG B 301 O HOH B 503 1555 1555 2.20
LINK MG MG B 301 O HOH B 520 1555 1555 2.03
SITE 1 AC1 3 ASP B 67 HOH B 503 HOH B 520
CRYST1 119.500 39.720 93.300 90.00 99.84 90.00 C 1 2 1 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 0.008368 0.000000 0.001451 0.00000
SCALE2 0.000000 0.025176 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010878 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
