HEADER TRANSFERASE 11-MAR-03 1O2F
TITLE COMPLEX OF ENZYME IIAGLC AND IIBGLC PHOSPHOCARRIER PROTEIN HPR FROM
TITLE 2 ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PTS SYSTEM, GLUCOSE-SPECIFIC IIA COMPONENT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: IIAGLC, EIIA-GLC, GLUCOSE-PERMEASE IIA COMPONENT,
COMPND 5 PHOSPHOTRANSFERASE ENZYME II, A COMPONENT, EIII-GLC;
COMPND 6 EC: 2.7.1.69;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PTS SYSTEM, GLUCOSE-SPECIFIC IIBC COMPONENT;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: IIBGLC, EIIBC-GLC, GLUCOSE-PERMEASE IIBC COMPONENT,
COMPND 12 PHOSPHOTRANSFERASE ENZYME II, BC COMPONENT, EII-GLC;
COMPND 13 EC: 2.7.1.69;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 8 ORGANISM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHOTRANSFERASE, TRANSFERASE, KINASE, SUGAR TRANSPORT, COMPLEX
KEYWDS 2 (TRANSFERASE-PHOSPHOCARRIER)
EXPDTA SOLUTION NMR
NUMMDL 3
AUTHOR G.M.CLORE,M.CAI,D.C.WILLIAMS
REVDAT 5 27-DEC-23 1O2F 1 REMARK
REVDAT 4 30-JUN-21 1O2F 1 REMARK ATOM
REVDAT 3 24-FEB-09 1O2F 1 VERSN
REVDAT 2 08-JUL-03 1O2F 1 JRNL AUTHOR
REVDAT 1 13-MAY-03 1O2F 0
JRNL AUTH M.CAI,D.C.WILLIAMS JR.,G.WANG,B.R.LEE,A.PETERKOFSKY,
JRNL AUTH 2 G.M.CLORE
JRNL TITL SOLUTION STRUCTURE OF THE PHOSPHORYL TRANSFER COMPLEX
JRNL TITL 2 BETWEEN THE SIGNAL-TRANSDUCING PROTEIN IIAGLUCOSE AND THE
JRNL TITL 3 CYTOPLASMIC DOMAIN OF THE GLUCOSE TRANSPORTER IICBGLUCOSE OF
JRNL TITL 4 THE ESCHERICHIA COLI GLUCOSE PHOSPHOTRANSFERASE SYSTEM.
JRNL REF J.BIOL.CHEM. V. 278 25191 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12716891
JRNL DOI 10.1074/JBC.M302677200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH (HTTP://NMR.CIT.NIH.GOV/XPLOR_NIH)
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA, CLORE
REMARK 3 J.MAGN.RESON. 160, 66-73 (2003)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED BY CONJOINED RIGID BODY/TORSION
REMARK 3 ANGLE DYNAMICS (SCHWIETERS & CLORE (2001) J.MAGN.RESON 152, 288-
REMARK 3 302). THE TARGET FUNCTIONS COMPRISES TERMS FOR THE NOE-DERIVED
REMARK 3 TERMS FOR THE NOE RESTRAINTS (INTRA AND INTERMOLECULAR), THE
REMARK 3 INTERFACIAL SIDECHAIN TORSION ANGLE RESTRAINTS FOR IIAGLC, THE
REMARK 3 BACKBONE AND SIDE CHAIN TORSION ANGLE RESTRAINTS FOR IIBGLC, THE
REMARK 3 DIPOLAR COUPLING RESTRAINTS FOR IIBGL (CLORE ET AL. J.MAGN.RESON.
REMARK 3 131, 159-162 (1998); J.MAGN.RESON. 133, 216-221(1998)), THE RADIUS
REMARK 3 OF GYRATION (KUSZEWSKI ET AL. (1999), A QUARTIC VAN DER WAALS
REMARK 3 REPULSION TERM (NILGES ET AL. (1988) FEBS LETT. 229, 129- 136),
REMARK 3 AND A TORSION ANGLE DATABASE POTENTIAL OF MEAN FORCE (CLORE &
REMARK 3 KUSZEWSKI (2002) J.AM.CHEM.SOC 121, 2337-2338). THE STARTING
REMARK 3 COORDINATES FOR IIAGLC ARE FROM THE 2.1 ANGSTROM RESOLUTION X-RAY
REMARK 3 STRUCTURE (WITH PROTONS ADDED) OF E. COLI IIAGLC (MOLECULE 2 OF
REMARK 3 2F3G; FEESE ET AL. BIOCHEMISTRY 36, 16087-16096 (1997)). THE
REMARK 3 BACKBONE COORDINATES AND NON- INTERFACIAL SIDECHAINS OF IIAGLC ARE
REMARK 3 TREATED AS A RIGID BODY.
REMARK 3
REMARK 3 IN THIS ENTRY THE LAST COLUMN REPRESENTS THE AVERAGE RMS
REMARK 3 DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED ANNEALING
REMARK 3 STRUCTURES AND THE MEAN COORDINATE POSITIONS. IT IS
REMARK 3 IMPORTANT TO NOTE THAT THE VALUES GIVEN FOR THE BACKBONE
REMARK 3 ATOMS AND NON-INTERFACIAL SIDECHAINS OF IIAGLC
REMARK 3 PROVIDE ONLY A MEASURE OF THE PRECISION WITH WHICH THE
REMARK 3 RELATIVE ORIENTATION OF IIAGLC IN THE COMPLEX
REMARK 3 HAS BEEN DETERMINED AND DOES NOT TAKE INTO ACCOUNT THE
REMARK 3 THE ERRORS IN THE X-RAY COORDINATES OF IIAGLC
REMARK 3
REMARK 3 RESIDUE NUMBERING:
REMARK 3 IIAGLC: 19-168 (RESIDUES 1-18 ARE DISORDERED
REMARK 3 IN SOLUTION AND NOT VISIBLE IN THE ELECTRON DENSITY
REMARK 3 MAP OF THE CRYSTAL STRUCTURE OF THE FREE PROTEIN).
REMARK 3 IIBGLC: 314-390 (CORRESPONDING TO RESIDUES 400-476 OF
REMARK 3 INTACT IIBCGLC. RESIDUES 301-314 ARE DISORDERED IN
REMARK 3 SOLUTION.
REMARK 3 PRO317 HAS BEEN MUTATED TO ALA TO REMOVE HETEROGENEITY
REMARK 3 ARISING FROM CIS-TRANS PROLINE ISOMERIZATION.
REMARK 3 PHOSPHATE: RESIDUE 200
REMARK 3
REMARK 3 EXPERIMENTAL RESTRAINTS:
REMARK 3 INTRAMOLECULAR INTERPROTON DISTANCE RESTRAINTS:
REMARK 3 IIBGLC: 987 (189 INTRARESIDUE, 273 SEQUENTIAL,
REMARK 3 (218 MEDIUM RANGE (1 < |I-J|<=5,
REMARK 3 307 LONG RANGE (|I-J>5)
REMARK 3 IIAGLC INTERFACIAL SIDE CHAINS: 30
REMARK 3 INTERMOLECULAR INTERPROTON DISTANCE RESTRAINTS: 113
REMARK 3 BACKBONE H-BOND RESTRAINTS FOR IIBGLC (2 PER H-BOND): 72
REMARK 3 TORSION ANGLE RESTRAINTS:
REMARK 3 IIBGLC: 221
REMARK 3 IIAGLC INTERFACIAL SIDE CHAINS: 34
REMARK 3 RESIDUAL DIPOLAR COUPLINGS FOR IIBGLC: 174
REMARK 3 (58 N-H, 58 N-C', 58 HN-C')
REMARK 3 13CALPHA/BETA SHIFTS FOR IIBGLC: 138
REMARK 3
REMARK 3 THREE SETS OF COORDINATES ARE GIVEN:
REMARK 3
REMARK 3 MODEL 3: RESTRAINED REGULARIZED MEAN
REMARK 3 COORDINATES OF THE UNPHOSPHORYLATED IIAGLC-IIBGLC COMPLEX
REMARK 3 OVERALL BACKBONE COORDINATE PRECISION (IIAGLC+IIBGLC): 0.31A
REMARK 3 HEAVY ATOM INTERFACE SIDECHAIN COORDINATE PRECISION
REMARK 3 (IIAGLC+IIBGLC): 0.67A
REMARK 3 BACKBONE COORDINATE PRECISION FOR IIBGLC: 0.21 A
REMARK 3 ALL HEAVY ATOM COORDINATE PRECISION FOR IIBGLC; 0.71 A
REMARK 3
REMARK 3 MODEL 2: RESTRAINED REGULARIZED MEAN COORDINATES FOR THE
REMARK 3 MODEL OF THE DISSOCIATIVE PHOSPHORYL TRANSITION STATE
REMARK 3 IIAGLC-IIBGLC. EXPERIMENTAL RESTRAINTS ARE
REMARK 3 IDENTICAL TO THOSE USED FOR MODEL 3, BUT COVALENT
REMARK 3 GEOMETRY RESTRAINTS ARE INCLUDED RELATING TO THE
REMARK 3 PENTACOORDINATE PHOSPHORYL GROUP IN A TRIGONAL BIPYRAMIDAL
REMARK 3 GEOMETRY. THE STRUCTURE IS DERIVED FROM
REMARK 3 MODEL 3 BY RESTRAINED CONJOINED
REMARK 3 TORSION ANGLE/RIGID BODY MINIMIZATION. NO RESTRAINTS
REMARK 3 WERE EMPLOYED FOR THE NE2(HIS90/IIAGLC)-P
REMARK 3 AND SG(CYS35/IIBGLC)-P DISTANCES. THERE IS NO CHANGE
REMARK 3 IN BACKBONE RELATIVE TO MODEL 3 BUT THE NE2(HIS90/IIAGLC-
REMARK 3 SG(CYS35/IIBGLC) DISTANCE IS REDUCED FROM 5.75 A IN
REMARK 3 MODEL 3 TO 5.3 A IN MODEL 2.
REMARK 3
REMARK 3 MODEL 1: RESTRAINED REGULARIZED MEAN COORDINATES FOR THE
REMARK 3 MODEL OF THE ASSOCIATIVE PHOSPHORYL TRANSITION STATE
REMARK 3 HPR-IIAGLC COMPLEX. CALCULATED LIKE MODEL 2 BUT
REMARK 3 WITH THE NE2(HIS90/IIAGLC)-P
REMARK 3 AND SG(CYS35/IIBGLC)-P DISTANCES RESTRAINED TO 2 A.
REMARK 3 THE STRUCTURE IS DERIVED FROM
REMARK 3 MODEL 3 BY RESTRAINED CONJOINED
REMARK 3 TORSION ANGLE/RIGID BODY MINIMIZATION.
REMARK 3 THE RMS DIFFERENCE BETWEEN THE MEAN
REMARK 3 STRUCTURES OF THE UNPHOSPHORYLATED COMPLEX (MODEL 3)
REMARK 3 AND THE TRANSITION STATE COMPLEX (MODEL 1) IS ONLY 0.1 A
REMARK 3 FOR BACKBONE COORDINATES IMMEDIATELY ADJACENT TO THE ACTIVE
REMARK 3 SITE HIS AND CYS (RESIDUES 89-91 OF IIAGLC AND
REMARK 3 334-336 OF IIBGLC). THE REMAINING BACKBONE
REMARK 3 COORDINATES DO NOT SHIFT.
REMARK 4
REMARK 4 1O2F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000001719.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308.00
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 10 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1) TRIPLE RESONANCE FOR
REMARK 210 ASSIGNMENT OF PROTEIN; (2)
REMARK 210 QUANTITATIVE J CORRELATION FOR
REMARK 210 COUPLING CONSTANTS; (3) 3D; 4D
REMARK 210 HETERONUCLEAR SEPARATED;
REMARK 210 FILTERED NOE EXPTS; (4) IPAP
REMARK 210 EXPERIMENTS FOR DIPOLAR
REMARK 210 COUPLINGS. DIPOLAR COUPLINGS
REMARK 210 WERE MEASURED IN PHAGE PF1
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ; 800
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE DMX; AVANCE DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : CONJOINED RIGID BODY/TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 3
REMARK 210 CONFORMERS, SELECTION CRITERIA : REGULARIZED MEAN STRUCTURES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-3
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 LEU A 2
REMARK 465 PHE A 3
REMARK 465 ASP A 4
REMARK 465 LYS A 5
REMARK 465 LEU A 6
REMARK 465 LYS A 7
REMARK 465 SER A 8
REMARK 465 LEU A 9
REMARK 465 VAL A 10
REMARK 465 SER A 11
REMARK 465 ASP A 12
REMARK 465 ASP A 13
REMARK 465 LYS A 14
REMARK 465 LYS A 15
REMARK 465 ASP A 16
REMARK 465 THR A 17
REMARK 465 GLY A 18
REMARK 465 GLU B 301
REMARK 465 ASP B 302
REMARK 465 ALA B 303
REMARK 465 THR B 304
REMARK 465 GLU B 305
REMARK 465 ASP B 306
REMARK 465 ALA B 307
REMARK 465 LYS B 308
REMARK 465 ALA B 309
REMARK 465 THR B 310
REMARK 465 GLY B 311
REMARK 465 THR B 312
REMARK 465 SER B 313
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-3
REMARK 470 RES CSSEQI ATOMS
REMARK 470 LYS A 168 O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 OE2 GLU A 97 HH12 ARG B 340 1.39
REMARK 500 OD1 ASP A 64 H VAL A 115 1.48
REMARK 500 H GLY A 68 O SER A 78 1.51
REMARK 500 O GLY A 102 HZ1 LYS A 104 1.53
REMARK 500 O PHE A 91 HG1 THR A 95 1.56
REMARK 500 SG CYS B 335 P PO3 B 200 2.07
REMARK 500 NE2 HIS A 90 P PO3 B 200 2.09
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 1 PRO A 37 47.65 -73.02
REMARK 500 1 ASN A 57 17.08 -142.21
REMARK 500 1 VAL A 158 131.51 -37.35
REMARK 500 1 GLU A 160 -51.54 -144.33
REMARK 500 1 CYS B 335 -131.27 -135.25
REMARK 500 2 PRO A 37 47.69 -73.19
REMARK 500 2 ASN A 57 17.99 -141.91
REMARK 500 2 VAL A 158 131.53 -39.10
REMARK 500 2 GLU A 160 -52.54 -141.02
REMARK 500 2 CYS B 335 -130.20 -144.38
REMARK 500 3 PRO A 37 48.81 -75.15
REMARK 500 3 ASN A 57 17.06 -142.88
REMARK 500 3 GLU A 160 -55.08 -136.26
REMARK 500 3 ALA B 334 -168.38 -161.08
REMARK 500 3 CYS B 335 -130.92 -135.19
REMARK 500 3 LYS B 376 4.09 -69.92
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 1 ARG A 105 0.14 SIDE CHAIN
REMARK 500 1 ARG A 112 0.31 SIDE CHAIN
REMARK 500 1 ARG A 165 0.10 SIDE CHAIN
REMARK 500 2 ARG A 105 0.14 SIDE CHAIN
REMARK 500 2 ARG A 112 0.31 SIDE CHAIN
REMARK 500 2 ARG A 165 0.09 SIDE CHAIN
REMARK 500 3 ARG A 105 0.14 SIDE CHAIN
REMARK 500 3 ARG A 112 0.31 SIDE CHAIN
REMARK 500 3 ARG A 165 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1O2F A 1 168 UNP P69783 PTGA_ECOLI 1 168
DBREF 1O2F B 301 390 UNP P69786 PTGCB_ECOLI 387 476
SEQADV 1O2F ALA B 317 UNP P69786 PRO 403 SEE REMARK 999
SEQRES 1 A 168 GLY LEU PHE ASP LYS LEU LYS SER LEU VAL SER ASP ASP
SEQRES 2 A 168 LYS LYS ASP THR GLY THR ILE GLU ILE ILE ALA PRO LEU
SEQRES 3 A 168 SER GLY GLU ILE VAL ASN ILE GLU ASP VAL PRO ASP VAL
SEQRES 4 A 168 VAL PHE ALA GLU LYS ILE VAL GLY ASP GLY ILE ALA ILE
SEQRES 5 A 168 LYS PRO THR GLY ASN LYS MET VAL ALA PRO VAL ASP GLY
SEQRES 6 A 168 THR ILE GLY LYS ILE PHE GLU THR ASN HIS ALA PHE SER
SEQRES 7 A 168 ILE GLU SER ASP SER GLY VAL GLU LEU PHE VAL HIS PHE
SEQRES 8 A 168 GLY ILE ASP THR VAL GLU LEU LYS GLY GLU GLY PHE LYS
SEQRES 9 A 168 ARG ILE ALA GLU GLU GLY GLN ARG VAL LYS VAL GLY ASP
SEQRES 10 A 168 THR VAL ILE GLU PHE ASP LEU PRO LEU LEU GLU GLU LYS
SEQRES 11 A 168 ALA LYS SER THR LEU THR PRO VAL VAL ILE SER ASN MET
SEQRES 12 A 168 ASP GLU ILE LYS GLU LEU ILE LYS LEU SER GLY SER VAL
SEQRES 13 A 168 THR VAL GLY GLU THR PRO VAL ILE ARG ILE LYS LYS
SEQRES 1 B 90 GLU ASP ALA THR GLU ASP ALA LYS ALA THR GLY THR SER
SEQRES 2 B 90 GLU MET ALA ALA ALA LEU VAL ALA ALA PHE GLY GLY LYS
SEQRES 3 B 90 GLU ASN ILE THR ASN LEU ASP ALA CYS ILE THR ARG LEU
SEQRES 4 B 90 ARG VAL SER VAL ALA ASP VAL SER LYS VAL ASP GLN ALA
SEQRES 5 B 90 GLY LEU LYS LYS LEU GLY ALA ALA GLY VAL VAL VAL ALA
SEQRES 6 B 90 GLY SER GLY VAL GLN ALA ILE PHE GLY THR LYS SER ASP
SEQRES 7 B 90 ASN LEU LYS THR GLU MET ASP GLU TYR ILE ARG ASN
HET PO3 B 200 4
HETNAM PO3 PHOSPHITE ION
FORMUL 3 PO3 O3 P 3-
HELIX 1 1 ASN A 32 VAL A 36 5 5
HELIX 2 2 ASP A 38 GLU A 43 1 6
HELIX 3 3 ASP A 94 LYS A 99 5 6
HELIX 4 4 ASP A 123 ALA A 131 1 9
HELIX 5 5 ASN A 142 ILE A 146 5 5
HELIX 6 6 GLU B 314 GLY B 324 1 11
HELIX 7 7 ASP B 345 VAL B 349 5 5
HELIX 8 8 ASP B 350 LEU B 357 1 8
HELIX 9 9 LYS B 376 ARG B 389 1 14
SHEET 1 A 3 ILE A 20 ILE A 23 0
SHEET 2 A 3 PRO A 162 LYS A 167 -1 O VAL A 163 N ILE A 22
SHEET 3 A 3 GLU A 148 LYS A 151 -1 N ILE A 150 O ARG A 165
SHEET 1 B 8 ARG A 112 VAL A 113 0
SHEET 2 B 8 GLY A 65 ILE A 70 -1 N GLY A 65 O VAL A 113
SHEET 3 B 8 ALA A 76 SER A 81 -1 O SER A 78 N LYS A 69
SHEET 4 B 8 GLU A 86 HIS A 90 -1 O LEU A 87 N ILE A 79
SHEET 5 B 8 THR A 136 ILE A 140 -1 O VAL A 139 N PHE A 88
SHEET 6 B 8 ASP A 48 PRO A 54 -1 N ILE A 50 O VAL A 138
SHEET 7 B 8 GLY A 28 VAL A 31 -1 N VAL A 31 O ALA A 51
SHEET 8 B 8 SER A 155 VAL A 156 -1 O VAL A 156 N GLY A 28
SHEET 1 C 3 LYS A 58 VAL A 60 0
SHEET 2 C 3 THR A 118 PHE A 122 -1 O ILE A 120 N MET A 59
SHEET 3 C 3 PHE A 103 ARG A 105 -1 N LYS A 104 O GLU A 121
SHEET 1 D 4 ILE B 329 ALA B 334 0
SHEET 2 D 4 LEU B 339 VAL B 343 -1 O ARG B 340 N ASP B 333
SHEET 3 D 4 GLY B 368 ILE B 372 -1 O VAL B 369 N VAL B 341
SHEET 4 D 4 GLY B 361 ALA B 365 -1 N VAL B 363 O GLN B 370
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
