HEADER TRANSFERASE 18-SEP-00 1GGR
TITLE COMPLEX OF ENZYME IIAGLC AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER
TITLE 2 PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN
TITLE 3 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PTS SYSTEM, GLUCOSE-SPECIFIC IIA COMPONENT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EIIA-GLC, PHOSPHOTRANSFERASE ENZYME II, A COMPONENT;
COMPND 5 EC: 2.7.1.69;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PHOSPHOCARRIER PROTEIN HPR;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: HISTIDINE-CONTAINING PROTEIN;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: GI698;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 9 ORGANISM_TAXID: 562;
SOURCE 10 STRAIN: GI698;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHOTRANSFERASE, TRANSFERASE, KINASE, SUGAR TRANSPORT, COMPLEX
KEYWDS 2 (TRANSFERASE-PHOSPHOCARRIER)
EXPDTA SOLUTION NMR
NUMMDL 3
AUTHOR G.M.CLORE,G.WANG
REVDAT 5 27-DEC-23 1GGR 1 REMARK
REVDAT 4 23-FEB-22 1GGR 1 REMARK
REVDAT 3 24-FEB-09 1GGR 1 VERSN
REVDAT 2 01-APR-03 1GGR 1 JRNL
REVDAT 1 15-NOV-00 1GGR 0
JRNL AUTH G.WANG,J.M.LOUIS,M.SONDEJ,Y.J.SEOK,A.PETERKOFSKY,G.M.CLORE
JRNL TITL SOLUTION STRUCTURE OF THE PHOSPHORYL TRANSFER COMPLEX
JRNL TITL 2 BETWEEN THE SIGNAL TRANSDUCING PROTEINS HPR AND IIA(GLUCOSE)
JRNL TITL 3 OF THE ESCHERICHIA COLI PHOSPHOENOLPYRUVATE:SUGAR
JRNL TITL 4 PHOSPHOTRANSFERASE SYSTEM.
JRNL REF EMBO J. V. 19 5635 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 11060015
JRNL DOI 10.1093/EMBOJ/19.21.5635
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED BY RIGID BODY MINIMIZATION (CLORE
REMARK 3 (2000) PROC.NATL.ACAD. SCI. 97, 9021-9025; BEWLEY AND CLORE (2000)
REMARK 3 J.AM.CHEM.SOC. 122, 6009-6016) FOLLOWED BY CONSTRAINED/RESTRAINED
REMARK 3 SIMULATED ANNEALING TO REFINE THE INTERFACIAL SIDECHAIN POSITIONS
REMARK 3 AND FINE TUNE THE RELATIVE ORIENTATION OF THE TWO PROTEINS (WANG
REMARK 3 ET AL. (2000) EMBO J. IN PRESS). THE TARGET FUNCTIONS COMPRISES
REMARK 3 TERMS FOR THE NOE RESTRAINTS, THE DIPOLAR COUPLING RESTRAINTS
REMARK 3 (CLORE ET AL. J.MAGN.RESON. 131, 159-162 (1998); J.MAGN.RESON. 133,
REMARK 3 216-221(1998)), THE RADIUS OF GYRATION (KUSZEWSKI ET AL. (1999),
REMARK 3 AND A QUARTIC VAN DER WAALS REPULSION TERM (NILGES ET AL. (1988)
REMARK 3 FEBS LETT. 229, 129-136). THE STARTING COORDINATES COME FROM THE X-
REMARK 3 RAY STRUCTURES (WITH PROTONS ADDED) OF E. COLI HPR (1POH, JIA ET
REMARK 3 AL. (1993) J.BIOL.CHEM. 268, 22940-22501; RESOLUTION 1.5 A) AND
REMARK 3 IIAGLC (MOLECULE 2 OF 2F3G, FEESE ET AL. BIOCHEMISTRY 36, 16087-
REMARK 3 16096; RESOLUTION 2.0 A) IN SEVERAL DIFFERENT ORIENTATIONS WITH
REMARK 3 THE CA-CA DISTANCE BETWEEN THE ACTIVE SITE HISTIDINES RANGING FROM
REMARK 3 28 TO 95 A, INCLUDING ORIENTATIONS WHERE THE TWO ACTIVE SITE
REMARK 3 HISTIDINES ARE NOT OPPOSED AND WHERE HPR IS DIRECTED TOWARDS THE
REMARK 3 FACE OF IIAGLC OPPOSITE TO THE IIAGLC ACTIVE SITE. ONLY THE
REMARK 3 INTERFACIAL SIDECHAINS ARE ALLOWED TO ALTER THEIR CONFORMATION;
REMARK 3 THE BACKBONE AND NON-INTERFACIAL SIDECHAINS OF ONE MOLECULE
REMARK 3 (IIAGLC) ARE HELD COMPLETELY FIXED; THE SECOND MOLECULE (HPR) CAN
REMARK 3 ROTATE AND TRANSLATE BUT THE RELATIVE COORDINATES OF ITS BACKBONE
REMARK 3 AND NON-INTERFACIAL SIDECHAINS ARE HELD FIXED.
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 PROVIDE ONLY A
REMARK 3 MEASURE OF THE PRECISION WITH WHICH THE RELATIVE
REMARK 3 OF THE TWO PROTEINS HAVE BEEN DETERMINED AND DOES
REMARK 3 NOT TAKE INTO ACCOUNT THE ERRORS IN THE X-RAY COORDINATES
REMARK 3 OF HPR AND IIAGLC.
REMARK 3
REMARK 3 THREE SETS OF COORDINATES ARE GIVEN:
REMARK 3
REMARK 3 MODEL 1: RESTRAINED MINIMIZED MEAN
REMARK 3 COORDINATES OF THE UNPHOSPHORYLATED HPR-IIAGLC COMPLEX
REMARK 3 SOLVED ON THE BASIS OF 82 INTERMOLECULAR DISTANCE
REMARK 3 RESTRAINTS (74 NOE DERIVED INTERPROTON DISTANCE
REMARK 3 AND 8 AMBIGUOUS INTERMOLECULAR SALT BRIDGE RESTRAINTS),
REMARK 3 12 INTRAMOLECULAR INTERPROTON DISTANCE RESTRAINTS
REMARK 3 (RELATED SPECIFICALLY TO NOES INVOLVING RESIDUES
REMARK 3 315 AND 317 OF HPR), 61 NMR DERIVED SIDECHAIN TORSION
REMARK 3 ANGLE RESTRAINTS, AND 195 1DNH DIPOLAR COUPLINGS
REMARK 3 (118 FOR IIAGLC AND 77 FOR HPR). CROSS-VALIDATION
REMARK 3 WAS USED FOR THE DIPOLAR COUPLINGS (CLORE AND GARRETT
REMARK 3 (1999) J. AM. CHEM. SOC. 121, 9008-9012).
REMARK 3
REMARK 3 MODEL 2: RESTRAINED MINIMIZED MEAN COORDINATES FOR THE
REMARK 3 MODEL OF THE DISSOCIATIVE PHOSPHORYL TRANSITION STATE
REMARK 3 HPR-IIAGLC COMPLEX. EXPERIMENTAL RESTRAINTS ARE
REMARK 3 TO THOSE USED FOR MODEL 1, EXCEPT THAT ONE
REMARK 3 INTRAMOLECULAR INTERPROTON DISTANCE RESTRAINT
REMARK 3 INVOLVING HIS15 WAS REMOVED TO PERMIT A TRANSITION STATE
REMARK 3 TO FORM. IN ADDITION, COVALENT GEOMETRY RESTRAINTS
REMARK 3 ARE INCLUDED RELATING TO THE TRIGONAL BIPYRAMIDAL
REMARK 3 AT THE PHOSPHORUS. NO DISTANCE RESTRAINT IS INCLUDED
REMARK 3 FOR THE N-P BOND LENGTHS. THE CA-CA DISTANCE BETWEEN
REMARK 3 HIS315 (HPR) AND HIS90 (IIAGLC) REMAINS UNCHANGED FROM
REMARK 3 MODEL 1, BUT THE ND1-NE2 DISTANCE BETWEEN HIS315 AND
REMARK 3 HIS90 IS REDUCED TO 6 A, WITH ESSENTIALLY IDEALIZED
REMARK 3 GEOMETRY OF THE PHOSPHORYL TRANSITION STATE.
REMARK 3 THE ND1-NE2 DISTANCE CORRESPONDS TO A DISSOCIATIVE
REMARK 3 TRANSITION STATE. THE RMS DIFFERENCE BETWEEN THE MEAN
REMARK 3 STRUCTURES OF THE UNPHOSPHORYLATED COMPLEX (MODEL 1)
REMARK 3 AND THE TRANSITION STATE COMPLEX IS 0.03 A FOR THE
REMARK 3 BACKBONE ATOMS AND 0.2 A FOR THE INTERFACIAL
REMARK 3 SIDECHAINS (EXCLUDING HIS315 AND HIS90).
REMARK 3
REMARK 3 MODEL 3: RESTRAINED MINIMIZED MEAN COORDINATES FOR THE
REMARK 3 MODEL OF THE ASSOCIATIVE PHOSPHORYL TRANSITION STATE
REMARK 3 HPR-IIAGLC COMPLEX. MODEL 3 IS DERIVED FROM MODEL 2
REMARK 3 BY CONSTRAINED/RESTRAINED MINIMIZATION IN WHICH
REMARK 3 THE COORDINATES OF ALL BACKBONE ATOMS, WITH THE
REMARK 3 OF RESIDUES 313-317 OF HPR AND RESIDUES 89-91 OF IIAGLC,
REMARK 3 AND ALL NON-INTERFACIAL SIDECHAINS ARE HELD COMPLETELY
REMARK 3 FIXED, AND IN WHICH THE N-P DISTANCES ARE RESTRAINED
REMARK 3 TO CA. 2 A, CORRESPONDING TO AN SN2 ASSOCIATIVE
REMARK 3 TRANSITION STATE.
REMARK 3
REMARK 3 HPR-IIAGLC COMPLEX
REMARK 3 DEVIATIONS FROM IDEALIZED GEOMETRY:
REMARK 3 BONDS 0.014 A, ANGLES 1.74 A, IMPROPER TORSIONS 1.66 A
REMARK 3 RMS DEVIATIONS FROM NOE DISTANCE RESTRAINTS: 0.057 A
REMARK 3 RMS DEVIATIONS FROM SIDECHAIN TORSION ANGLE RESTRAINTS:
REMARK 3 0.16 DEG.
REMARK 3 DIPOLAR COUPLING R-FACTORS (CLORE AND GARRETT (1999)
REMARK 3 J. AM. CHEM. SOC. 121, 9008-9012):
REMARK 3 16.9% FOR HPR AND 15.2% FOR IIAGLC
REMARK 3 (NOTE ONLY ONE ALIGNMENT TENSOR IS USED FOR BOTH HPR
REMARK 3 AND IIAGLC; FOR REFERENCE THE DIPOLAR COUPLING R-FACTORS
REMARK 3 FOR THE FREE X-RAY STRUCTURES OF HPR AND IIAGLC
REMARK 3 (USING INDIVIDUAL ALIGNMENT TENSORS FOR THE TWO PROTEINS)
REMARK 3 ARE 16.7% AND 15.0%, RESPECTIVELY).
REMARK 4
REMARK 4 1GGR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000001499.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.1
REMARK 210 IONIC STRENGTH : 10 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ; 800
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600; DRX750; DRX800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : RIGID BODY MINIMIZATION AND
REMARK 210 CONSTRAINED/RESTRAINED SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
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: THE FOLLOWING EXPERIMENTS WERE CONDUCTED: (1) TRIPLE
REMARK 210 RESONANCE FOR ASSIGNMENT OF PROTEIN; (2) QUANTITATIVE J
REMARK 210 CORRELATION FOR COUPLING CONSTANTS; (3) 3D AND 4D HETERONUCLEAR
REMARK 210 SEPARATED AND FILTERED NOE EXPERIMENTS; (4) IPAP EXPERIMENTS FOR
REMARK 210 DIPOLAR COUPLINGS. DIPOLAR COUPLINGS WERE MEASURED IN A NEMATIC
REMARK 210 PHASE OF A COLLOIDAL SUSPENSION OF TMV (CLORE ET AL. 1998
REMARK 210 J.AM.CHEM.SOC. 120, 105-106).
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 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 470 GLU B 385 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 O GLY A 102 HZ1 LYS A 104 1.35
REMARK 500 OD1 ASP A 64 H VAL A 115 1.46
REMARK 500 O PHE A 91 HG1 THR A 95 1.53
REMARK 500 OD1 ASP A 38 HH21 ARG B 317 1.57
REMARK 500 O ASN A 142 H GLU A 145 1.58
REMARK 500 O ILE B 308 H GLY B 358 1.58
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 48.01 -70.49
REMARK 500 1 ASN A 57 14.52 -142.97
REMARK 500 1 VAL A 158 123.64 -37.23
REMARK 500 1 GLU A 160 -53.26 -136.42
REMARK 500 1 HIS B 315 -178.06 -69.27
REMARK 500 2 PRO A 37 48.03 -70.46
REMARK 500 2 ASN A 57 14.48 -142.97
REMARK 500 2 VAL A 158 123.68 -37.38
REMARK 500 2 GLU A 160 -53.24 -136.43
REMARK 500 2 HIS B 315 -178.04 -69.24
REMARK 500 3 PRO A 37 48.03 -70.46
REMARK 500 3 ASN A 57 14.48 -142.97
REMARK 500 3 VAL A 158 122.48 -37.07
REMARK 500 3 GLU A 160 -51.40 -137.43
REMARK 500 3 HIS B 315 -141.40 -66.08
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 3 ARG A 112 0.31 SIDE CHAIN
REMARK 500 3 ARG A 165 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EZA RELATED DB: PDB
DBREF 1GGR A 1 168 UNP P69783 PTGA_ECOLI 1 168
DBREF 1GGR B 301 385 UNP P0AA04 PTHP_ECOLI 1 85
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 85 MET PHE GLN GLN GLU VAL THR ILE THR ALA PRO ASN GLY
SEQRES 2 B 85 LEU HIS THR ARG PRO ALA ALA GLN PHE VAL LYS GLU ALA
SEQRES 3 B 85 LYS GLY PHE THR SER GLU ILE THR VAL THR SER ASN GLY
SEQRES 4 B 85 LYS SER ALA SER ALA LYS SER LEU PHE LYS LEU GLN THR
SEQRES 5 B 85 LEU GLY LEU THR GLN GLY THR VAL VAL THR ILE SER ALA
SEQRES 6 B 85 GLU GLY GLU ASP GLU GLN LYS ALA VAL GLU HIS LEU VAL
SEQRES 7 B 85 LYS LEU MET ALA GLU LEU GLU
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 HIS B 315 LYS B 327 1 13
HELIX 7 7 SER B 346 GLN B 351 1 6
HELIX 8 8 ASP B 369 LEU B 384 1 16
SHEET 1 A 3 ILE A 20 ILE A 23 0
SHEET 2 A 3 PRO A 162 LYS A 167 -1 N VAL A 163 O ILE A 22
SHEET 3 A 3 GLU A 148 LYS A 151 -1 O GLU A 148 N LYS A 167
SHEET 1 B 8 ARG A 112 VAL A 113 0
SHEET 2 B 8 GLY A 65 ILE A 70 -1 O GLY A 65 N VAL A 113
SHEET 3 B 8 ALA A 76 SER A 81 -1 O SER A 78 N GLY A 68
SHEET 4 B 8 GLU A 86 HIS A 90 -1 N LEU A 87 O ILE A 79
SHEET 5 B 8 THR A 136 ILE A 140 -1 O PRO A 137 N HIS A 90
SHEET 6 B 8 ASP A 48 PRO A 54 -1 O ASP A 48 N ILE A 140
SHEET 7 B 8 GLY A 28 VAL A 31 -1 O GLU A 29 N LYS A 53
SHEET 8 B 8 SER A 155 VAL A 156 -1 N VAL A 156 O 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 N VAL A 119 O MET A 59
SHEET 3 C 3 PHE A 103 ARG A 105 -1 O LYS A 104 N GLU A 121
SHEET 1 D 4 PHE B 302 THR B 307 0
SHEET 2 D 4 VAL B 360 GLU B 366 -1 N VAL B 361 O VAL B 306
SHEET 3 D 4 GLU B 332 SER B 337 -1 O GLU B 332 N GLU B 366
SHEET 4 D 4 LYS B 340 SER B 343 -1 O LYS B 340 N SER B 337
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
