HEADER PROTEIN BINDING 30-OCT-03 1R9Q
TITLE STRUCTURE ANALYSIS OF PROX IN COMPLEX WITH PROLINE BETAINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCINE BETAINE-BINDING PERIPLASMIC PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PERIPLASMIC LIGAND-BINDING PROTEIN PROX;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: PROX;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: PD141;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSK7
KEYWDS PERIPLASMIC BINDING PROTEIN, CATION-PI INTERACTIONS, TRYPTOPHAN BOX,
KEYWDS 2 PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SCHIEFNER,J.BREED,L.BOSSER,S.KNEIP,J.GADE,G.HOLTMANN,K.DIEDERICHS,
AUTHOR 2 W.WELTE,E.BREMER
REVDAT 4 25-OCT-23 1R9Q 1 REMARK
REVDAT 3 11-OCT-17 1R9Q 1 REMARK
REVDAT 2 24-FEB-09 1R9Q 1 VERSN
REVDAT 1 24-FEB-04 1R9Q 0
JRNL AUTH A.SCHIEFNER,J.BREED,L.BOSSER,S.KNEIP,J.GADE,G.HOLTMANN,
JRNL AUTH 2 K.DIEDERICHS,W.WELTE,E.BREMER
JRNL TITL CATION-PI INTERACTIONS AS DETERMINANTS FOR BINDING OF THE
JRNL TITL 2 COMPATIBLE SOLUTES GLYCINE BETAINE AND PROLINE BETAINE BY
JRNL TITL 3 THE PERIPLASMIC LIGAND-BINDING PROTEIN PROX FROM ESCHERICHIA
JRNL TITL 4 COLI
JRNL REF J.BIOL.CHEM. V. 279 5588 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14612446
JRNL DOI 10.1074/JBC.M309771200
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 18626
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 804
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) : 2.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.2000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2381
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 59
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R9Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020612.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JAN-00
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
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) : 1.54179
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19587
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
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) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1R9L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PIPES, PH 6.3, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 23.85500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.86500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.49000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.86500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.85500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.49000
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 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 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 O HOH A 1319 O HOH A 1328 1.20
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 116 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 287 CB - CG - OD2 ANGL. DEV. = 6.8 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 ASP A 274 25.50 -77.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PBE A 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R9L RELATED DB: PDB
REMARK 900 PROX IN COMPLEX WITH GLYCINE BETAINE
DBREF 1R9Q A 1 309 UNP P14177 PROX_ECOLI 22 330
SEQRES 1 A 309 ALA ASP LEU PRO GLY LYS GLY ILE THR VAL ASN PRO VAL
SEQRES 2 A 309 GLN SER THR ILE THR GLU GLU THR PHE GLN THR LEU LEU
SEQRES 3 A 309 VAL SER ARG ALA LEU GLU LYS LEU GLY TYR THR VAL ASN
SEQRES 4 A 309 LYS PRO SER GLU VAL ASP TYR ASN VAL GLY TYR THR SER
SEQRES 5 A 309 LEU ALA SER GLY ASP ALA THR PHE THR ALA VAL ASN TRP
SEQRES 6 A 309 THR PRO LEU HIS ASP ASN MET TYR GLU ALA ALA GLY GLY
SEQRES 7 A 309 ASP LYS LYS PHE TYR ARG GLU GLY VAL PHE VAL ASN GLY
SEQRES 8 A 309 ALA ALA GLN GLY TYR LEU ILE ASP LYS LYS THR ALA ASP
SEQRES 9 A 309 GLN TYR LYS ILE THR ASN ILE ALA GLN LEU LYS ASP PRO
SEQRES 10 A 309 LYS ILE ALA LYS LEU PHE ASP THR ASN GLY ASP GLY LYS
SEQRES 11 A 309 ALA ASP LEU THR GLY CYS ASN PRO GLY TRP GLY CYS GLU
SEQRES 12 A 309 GLY ALA ILE ASN HIS GLN LEU ALA ALA TYR GLU LEU THR
SEQRES 13 A 309 ASN THR VAL THR HIS ASN GLN GLY ASN TYR ALA ALA MET
SEQRES 14 A 309 MET ALA ASP THR ILE SER ARG TYR LYS GLU GLY LYS PRO
SEQRES 15 A 309 VAL PHE TYR TYR THR TRP THR PRO TYR TRP VAL SER ASN
SEQRES 16 A 309 GLU LEU LYS PRO GLY LYS ASP VAL VAL TRP LEU GLN VAL
SEQRES 17 A 309 PRO PHE SER ALA LEU PRO GLY ASP LYS ASN ALA ASP THR
SEQRES 18 A 309 LYS LEU PRO ASN GLY ALA ASN TYR GLY PHE PRO VAL SER
SEQRES 19 A 309 THR MET HIS ILE VAL ALA ASN LYS ALA TRP ALA GLU LYS
SEQRES 20 A 309 ASN PRO ALA ALA ALA LYS LEU PHE ALA ILE MET GLN LEU
SEQRES 21 A 309 PRO VAL ALA ASP ILE ASN ALA GLN ASN ALA ILE MET HIS
SEQRES 22 A 309 ASP GLY LYS ALA SER GLU GLY ASP ILE GLN GLY HIS VAL
SEQRES 23 A 309 ASP GLY TRP ILE LYS ALA HIS GLN GLN GLN PHE ASP GLY
SEQRES 24 A 309 TRP VAL ASN GLU ALA LEU ALA ALA GLN LYS
HET UNX A1310 1
HET PBE A1001 10
HETNAM UNX UNKNOWN ATOM OR ION
HETNAM PBE 1,1-DIMETHYL-PROLINIUM
HETSYN PBE PROLINE BETAINE
FORMUL 2 UNX X
FORMUL 3 PBE C7 H14 N O2 1+
FORMUL 4 HOH *59(H2 O)
HELIX 1 1 ILE A 17 GLU A 19 5 3
HELIX 2 2 GLU A 20 LEU A 34 1 15
HELIX 3 3 ASP A 45 SER A 55 1 11
HELIX 4 4 HIS A 69 ALA A 76 1 8
HELIX 5 5 GLY A 77 LYS A 80 5 4
HELIX 6 6 LYS A 100 LYS A 107 1 8
HELIX 7 7 ASN A 110 LYS A 115 5 6
HELIX 8 8 ASP A 116 LYS A 121 1 6
HELIX 9 9 LEU A 122 ASP A 124 5 3
HELIX 10 10 TRP A 140 TYR A 153 1 14
HELIX 11 11 ASN A 165 GLU A 179 1 15
HELIX 12 12 TRP A 192 LEU A 197 1 6
HELIX 13 13 LYS A 242 ASN A 248 1 7
HELIX 14 14 ASN A 248 MET A 258 1 11
HELIX 15 15 PRO A 261 ASP A 274 1 14
HELIX 16 16 SER A 278 HIS A 293 1 16
HELIX 17 17 HIS A 293 ALA A 306 1 14
SHEET 1 A 2 THR A 9 VAL A 10 0
SHEET 2 A 2 THR A 37 VAL A 38 1 O THR A 37 N VAL A 10
SHEET 1 B 5 SER A 42 GLU A 43 0
SHEET 2 B 5 PRO A 12 GLN A 14 1 N GLN A 14 O SER A 42
SHEET 3 B 5 PHE A 60 THR A 66 1 O PHE A 60 N VAL A 13
SHEET 4 B 5 SER A 234 ASN A 241 -1 O VAL A 239 N THR A 61
SHEET 5 B 5 PHE A 82 TYR A 83 -1 N TYR A 83 O ALA A 240
SHEET 1 C 5 SER A 42 GLU A 43 0
SHEET 2 C 5 PRO A 12 GLN A 14 1 N GLN A 14 O SER A 42
SHEET 3 C 5 PHE A 60 THR A 66 1 O PHE A 60 N VAL A 13
SHEET 4 C 5 SER A 234 ASN A 241 -1 O VAL A 239 N THR A 61
SHEET 5 C 5 VAL A 89 ALA A 92 -1 N VAL A 89 O MET A 236
SHEET 1 D 3 PHE A 184 TRP A 188 0
SHEET 2 D 3 GLN A 94 ASP A 99 -1 N LEU A 97 O TYR A 185
SHEET 3 D 3 VAL A 203 TRP A 205 -1 O VAL A 204 N ILE A 98
SHEET 1 E 2 ALA A 131 THR A 134 0
SHEET 2 E 2 VAL A 159 ASN A 162 1 O THR A 160 N ALA A 131
SSBOND 1 CYS A 136 CYS A 142 1555 1555 2.03
CISPEP 1 THR A 66 PRO A 67 0 3.41
CISPEP 2 THR A 189 PRO A 190 0 -1.81
SITE 1 AC1 6 ASP A 124 ASN A 126 ASP A 128 LYS A 130
SITE 2 AC1 6 ASP A 132 HOH A1338
SITE 1 AC2 8 TYR A 46 TRP A 65 LEU A 68 HIS A 69
SITE 2 AC2 8 TRP A 140 GLY A 141 CYS A 142 TRP A 188
CRYST1 47.710 54.980 115.730 90.00 90.00 90.00 P 21 21 21 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 0.020960 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018188 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008641 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
