Header list of 1vrc.pdb file
Complete list - n 30 2 Bytes
HEADER TRANSFERASE 21-FEB-05 1VRC
TITLE COMPLEX OF ENZYME IIAMANNOSE AND THE HISTIDINE-CONTAINING
TITLE 2 PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED
TITLE 3 REGULARIZED MEAN STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PTS SYSTEM, MANNOSE-SPECIFIC IIAB COMPONENT;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: EIIA DOMAIN;
COMPND 5 SYNONYM: EIIAB-MAN, MANNOSE-PERMEASE IIAB COMPONENT,
COMPND 6 PHOSPHOTRANSFERASE ENZYME II, AB COMPONENT, EIII-MAN;
COMPND 7 EC: 2.7.1.69;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PHOSPHOCARRIER PROTEIN HPR;
COMPND 11 CHAIN: C, D;
COMPND 12 SYNONYM: HISTIDINE-CONTAINING PROTEIN;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: MANX, GPTB, PTSL;
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 GENE: PTSH, HPR;
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 2
AUTHOR G.M.CLORE,D.C.WILLIAMS
REVDAT 4 30-JUN-21 1VRC 1 COMPND REMARK SEQADV ATOM
REVDAT 3 24-FEB-09 1VRC 1 VERSN
REVDAT 2 21-JUN-05 1VRC 1 JRNL
REVDAT 1 19-APR-05 1VRC 0
JRNL AUTH D.C.WILLIAMS,M.CAI,J.Y.SUH,A.PETERKOFSKY,G.M.CLORE
JRNL TITL SOLUTION NMR STRUCTURE OF THE 48-KDA IIAMANNOSE-HPR COMPLEX
JRNL TITL 2 OF THE ESCHERICHIA COLI MANNOSE PHOSPHOTRANSFERASE SYSTEM.
JRNL REF J.BIOL.CHEM. V. 280 20775 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15788390
JRNL DOI 10.1074/JBC.M501986200
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 : CLORE, KUSZEWSKI, SCHWIETERS, TJANDRA
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE CALCULATED BY
REMARK 3 CONJOINED RIGID BODY/TORSION ANGLE DYNAMICS (SCHWIETERS & CLORE
REMARK 3 (2001) J.MAGN.RESON 152, 288-302). THE TARGET FUNCTIONS
REMARK 3 COMPRISES TERMS FOR NOE RESTRAINTS, SIDECHAIN TORSION ANGLE
REMARK 3 RESTRAINTS, RESIDUAL DIPOLAR COUPLING RESTRAINTS (CLORE ET AL.
REMARK 3 J.MAGN.RESON. 131, 159-162 (1998); J.MAGN.RESON.133, 216-
REMARK 3 221(1998)), A RADIUS OF GYRATION TERM (KUSZEWSKI ET AL.(1999), A
REMARK 3 QUARTIC VAN DER WAALS REPULSION TERM (NILGES ET AL. (1988) FEBS
REMARK 3 LETT. 229, 129- 136), AND A TORSION ANGLE CONFORMATIONAL
REMARK 3 DATABASE POTENTIAL OF MEAN FORCE (CLORE AND KUSZEWSKI 2002)
REMARK 3 J.AM.CHEM.SOC 124, 2866-2867). THE STARTING COORDINATE COME FROM
REMARK 3 THE X-RAY STRUCTURES (WITH PROTONS ADDED) OF E. COLI HPR (1POH,
REMARK 3 JIA ET AL. (1993) J.BIOL.CHEM. 268, 22940-22501, RESOLUTION 2.0
REMARK 3 A); AND IIAMAN (1PDO, NUNN ET AL. (1996) J.MOL.BI J.MOL.BIOL.
REMARK 3 259, 502-511; RESOLUTION 1.7A). THE BACKBONE COORDINATES AND NON-
REMARK 3 INTERFACIAL SIDECHAINS ARE TREATED AS RIGID BODIES THROUGHOUT
REMARK 3 WITH THE IIAMAN DIMER HELD FIXED, THE TWO HPR MOLECULES ALLOWED
REMARK 3 TO ROTATE AND TRANSLATE, AND THE AXIS OF THE SINGLE DIPOLAR
REMARK 3 COUPLING ALIGNMENT TENSOR FREE TO ROTATE. THE INTERFACIAL
REMARK 3 SIDECHAINS ARE GIVEN FULL TORSIONAL DEGREES OF FREEDOM.
REMARK 4
REMARK 4 1VRC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 7
REMARK 7 IN THIS ENTRY THE LAST COLUMN REPRESENTS THE AVERAGE RMS
REMARK 7 DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED ANNEALING
REMARK 7 STRUCTURES AND THE MEAN COORDINATE POSITIONS. IT IS
REMARK 7 IMPORTANT TO NOTE THAT THE VALUES GIVEN FOR THE BACKBONE
REMARK 7 ATOMS AND NON-INTERFACIAL SIDECHAINS PROVIDE ONLY A
REMARK 7 MEASURE OF THE PRECISION WITH WHICH THE RELATIVE
REMARK 7 ORIENTATION OF THE TWO PROTEINS HAVE BEEN DETERMINED AND
REMARK 7 DOES NOT TAKE INTO ACCOUNT THE ERRORS IN THE X-RAY
REMARK 7 COORDINATES OF HPR AND IIAMAN.
REMARK 7 RESIDUE NUMBERING:
REMARK 7 IIAMAN: 1-136 (THE N-TERMINAL METHIONINE IS CLEAVED AND
REMARK 7 RESIDUES 131-136 WERE DISORDERED. RESIDUES 134-136 ARE
REMARK 7 CLONING ARTIFACTS; SEE REMARKS IN THE
REMARK 7 1PDO CRYSTAL STRUCTURE.)
REMARK 7 HPR: 201-285 (CORRESPONDING TO RESIDUES 1-85).
REMARK 7 PHOSPHATES: RESIDUES 401 AND 402.
REMARK 7 TWO SETS OF COORDINATES ARE GIVEN:
REMARK 7 MODEL 1: RESTRAINED REGULARIZED MEAN COORDINATES FOR THE
REMARK 7 MODEL OF THE ASSOCIATIVE PHOSPHORYL TRANSITION STATE
REMARK 7 HPR-IIAMTL COMPLEX. EXPERIMENTAL RESTRAINTS ARE
REMARK 7 IDENTICAL TO THOSE USED FOR MODEL 2, BUT COVALENT
REMARK 7 GEOMETRY RESTRAINTS ARE INCLUDED RELATING TO THE
REMARK 7 PENTACOORDINATE PHOSPHORYL GROUP IN A TRIGONAL BIPYRAMIDAL
REMARK 7 GEOMETRY. THE STRUCTURE IS DERIVED FROM
REMARK 7 MODEL 2 BY RESTRAINED REGULARIZATION IN WHICH ONLY
REMARK 7 THE ACTIVE SITE HISTIDINES, THE BACKBONE IMMIEDIATELY
REMARK 7 ADJACENT (ONE RESIDUE ON EITHER SIDE) TO THE ACTIVE SITE
REMARK 7 HISTIDINES, AND THE INTERFACIAL SIDECHAINS ARE ALLOWED TO
REMARK 7 MOVE. THE N-P BOND LENGTHS ARE RESTRAINED TO 2 A.
REMARK 7 IIAMAN-HPR COMPLEX
REMARK 7 RMS DEVIATIONS FROM NOE DISTANCE RESTRAINTS: 0.009 A
REMARK 7 RMS DEVIATIONS FROM SIDECHAIN TORSION ANGLE RESTRAINTS:
REMARK 7 0.0 DEG.
REMARK 7 DIPOLAR COUPLING R-FACTORS (CLORE AND GARRETT (1999)
REMARK 7 J. AM. CHEM. SOC. 121, 9008-9012):
REMARK 7 IIAMAN HPR
REMARK 7 NH 11.6 18.5/12.4
REMARK 7 MODEL 2: RESTRAINED REGULARIZED MEAN
REMARK 7 COORDINATES OF THE UNPHOSPHORYLATED IIAMAN-HPR COMPLEX
REMARK 7 SOLVED ON THE BASIS OF 58X2 INTERMOLECULAR
REMARK 7 INTERPROTON DISTANCE DISTANCE RESTRAINTS BETWEEN
REMARK 7 THE TWO MOLECULES OF HPR AND THE IIAMAN DIMER,
REMARK 7 47X2 INTRA AND 16X2 INTER-SUBUNIT IIAMAN
REMARK 7 DISTANCE RESTRAINTS RELATING ONLY TO INTERFACIAL
REMARK 7 SIDECHAINS, 39X2 INTRAMOLECULAR HPR CWDISTANCE
REMARK 7 RESTRAINTS RELATING ONLY TO INTERFACIAL SIDECHAINS,
REMARK 7 29X2 INTERFACIAL SIDECHAIN TORSION ANGLE RESTRAINTS,
REMARK 7 92X2 RESIDUAL DIPOLAR COUPLINGS FOR IIAMAN AND
REMARK 7 66X2 RESIDUAL DIPOLAR COUPLINGS FOR HPR.
REMARK 7 WAS USED FOR THE DIPOLAR COUPLINGS (CLORE AND GARRETT
REMARK 7 (1999) J. AM. CHEM. SOC. 121, 9008-9012).
REMARK 7 NOTE THE NH DIPOLAR COUPLINGS FOR FULLY BOUND HPR
REMARK 7 (I.E. BOTH BIDNING SITES ON IIAMAN FULLY SATURATED)
REMARK 7 ARE BACKCALCULATED FROM THE DIPOLAR COUPLINGS MEASURED
REMARK 7 FOR A SAMPLE WITH A THREE-FOLD MOLAR EXCESS OF HPR
REMARK 7 OVER IIAMAN BINDING SITES AND A SAMPLE OF FREE HPR.
REMARK 7 THE FIRST VALUE OF THE R-FACTOR USES DIPOLAR COUPLINGS
REMARK 7 FOR THE FULLY BOUND STATE BACK-CALCULATED USING THE MEASURED
REMARK 7 VALUES OF THE DIPOLAR OUPLINGS FOR FREE HPR; WHILE
REMARK 7 THE SECOND NUMBER USES THE CALCULATED VALUES OF THE DIPOLAR
REMARK 7 COUPLINGS FOR FREE HPR DERIVED FROM THE MEASURED VALUES
REMARK 7 AND THE CRYSTAL STRUCTURE OF FREE HPR USING SINGULAR VALUE
REMARK 7 DECOMPOSITION. NOTE A SINGLE ALIGNMENT TENSOR IS USED.
REMARK 7 THE DIPOLAR COUPLING R-FACTOR OBTAINED BY SINGULAR VALUE
REMARK 7 DECOMPOSITION AGAINST THE CRYSTAL STRUCTURES OF IIAMAN
REMARK 7 AND HPR INDIVIDUAL ARE THE SAME AS THOSE OBTAINED FOR THE
REMARK 7 COMPLEX AS A WHOLE.
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000002084.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308.00
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 40 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) TRSOE-
REMARK 210 BASED 2D, 3D EXPERIMENTS FOR
REMARK 210 DIPOLAR COUPLINGS. DIPOLAR
REMARK 210 COUPLINGS WERE MEASURED IN A
REMARK 210 NEMATIC PHASE OF A 5% PEG/
REMARK 210 HEXANOL (SURFACTANT TO ALCOHOL
REMARK 210 RATION OF 0.96)
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 : X-PLOR NIH
REMARK 210 METHOD USED : CONJOINED RIGID BODY/TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 2
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 1-2
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 131
REMARK 465 LYS A 132
REMARK 465 PRO A 133
REMARK 465 PHE A 134
REMARK 465 ALA A 135
REMARK 465 GLY A 136
REMARK 465 MET B 1
REMARK 465 ALA B 131
REMARK 465 LYS B 132
REMARK 465 PRO B 133
REMARK 465 PHE B 134
REMARK 465 ALA B 135
REMARK 465 GLY B 136
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 1-2
REMARK 470 RES CSSEQI ATOMS
REMARK 470 LYS A 130 O
REMARK 470 LYS B 130 O
REMARK 470 GLU C 285 O
REMARK 470 GLU D 285 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 HH21 ARG A 123 HH21 ARG B 123 0.79
REMARK 500 HE3 LYS A 130 HG22 VAL B 81 1.29
REMARK 500 NH2 ARG A 123 HH21 ARG B 123 1.42
REMARK 500 HH21 ARG A 123 NH2 ARG B 123 1.43
REMARK 500 O ILE D 208 H GLY D 258 1.54
REMARK 500 O ILE C 208 H GLY C 258 1.55
REMARK 500 NE2 HIS B 10 P PO3 C 401 1.99
REMARK 500 NE2 HIS A 10 P PO3 D 400 1.99
REMARK 500 ND1 HIS D 215 P PO3 D 400 2.00
REMARK 500 ND1 HIS C 215 P PO3 C 401 2.01
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 HIS A 10 84.33 -64.98
REMARK 500 1 VAL A 82 -55.99 -29.34
REMARK 500 1 HIS B 10 84.27 -64.97
REMARK 500 1 VAL B 82 -55.91 -29.38
REMARK 500 1 HIS C 215 -121.11 -64.35
REMARK 500 1 HIS D 215 -121.09 -64.36
REMARK 500 2 VAL A 82 -55.99 -29.34
REMARK 500 2 VAL B 82 -55.91 -29.38
REMARK 500 2 HIS C 215 -179.88 -68.74
REMARK 500 2 HIS D 215 -179.95 -68.67
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1VRC A 2 133 UNP P69797 PTNAB_ECOLI 1 132
DBREF 1VRC B 2 133 UNP P69797 PTNAB_ECOLI 1 132
DBREF 1VRC C 201 285 UNP P0AA04 PTHP_ECOLI 1 85
DBREF 1VRC D 201 285 UNP P0AA04 PTHP_ECOLI 1 85
SEQADV 1VRC MET A 1 UNP P69797 INITIATING METHIONINE
SEQADV 1VRC PHE A 134 UNP P69797 CLONING ARTIFACT
SEQADV 1VRC ALA A 135 UNP P69797 CLONING ARTIFACT
SEQADV 1VRC GLY A 136 UNP P69797 CLONING ARTIFACT
SEQADV 1VRC MET B 1 UNP P69797 INITIATING METHIONINE
SEQADV 1VRC PHE B 134 UNP P69797 CLONING ARTIFACT
SEQADV 1VRC ALA B 135 UNP P69797 CLONING ARTIFACT
SEQADV 1VRC GLY B 136 UNP P69797 CLONING ARTIFACT
SEQRES 1 A 136 MET THR ILE ALA ILE VAL ILE GLY THR HIS GLY TRP ALA
SEQRES 2 A 136 ALA GLU GLN LEU LEU LYS THR ALA GLU MET LEU LEU GLY
SEQRES 3 A 136 GLU GLN GLU ASN VAL GLY TRP ILE ASP PHE VAL PRO GLY
SEQRES 4 A 136 GLU ASN ALA GLU THR LEU ILE GLU LYS TYR ASN ALA GLN
SEQRES 5 A 136 LEU ALA LYS LEU ASP THR THR LYS GLY VAL LEU PHE LEU
SEQRES 6 A 136 VAL ASP THR TRP GLY GLY SER PRO PHE ASN ALA ALA SER
SEQRES 7 A 136 ARG ILE VAL VAL ASP LYS GLU HIS TYR GLU VAL ILE ALA
SEQRES 8 A 136 GLY VAL ASN ILE PRO MET LEU VAL GLU THR LEU MET ALA
SEQRES 9 A 136 ARG ASP ASP ASP PRO SER PHE ASP GLU LEU VAL ALA LEU
SEQRES 10 A 136 ALA VAL GLU THR GLY ARG GLU GLY VAL LYS ALA LEU LYS
SEQRES 11 A 136 ALA LYS PRO PHE ALA GLY
SEQRES 1 B 136 MET THR ILE ALA ILE VAL ILE GLY THR HIS GLY TRP ALA
SEQRES 2 B 136 ALA GLU GLN LEU LEU LYS THR ALA GLU MET LEU LEU GLY
SEQRES 3 B 136 GLU GLN GLU ASN VAL GLY TRP ILE ASP PHE VAL PRO GLY
SEQRES 4 B 136 GLU ASN ALA GLU THR LEU ILE GLU LYS TYR ASN ALA GLN
SEQRES 5 B 136 LEU ALA LYS LEU ASP THR THR LYS GLY VAL LEU PHE LEU
SEQRES 6 B 136 VAL ASP THR TRP GLY GLY SER PRO PHE ASN ALA ALA SER
SEQRES 7 B 136 ARG ILE VAL VAL ASP LYS GLU HIS TYR GLU VAL ILE ALA
SEQRES 8 B 136 GLY VAL ASN ILE PRO MET LEU VAL GLU THR LEU MET ALA
SEQRES 9 B 136 ARG ASP ASP ASP PRO SER PHE ASP GLU LEU VAL ALA LEU
SEQRES 10 B 136 ALA VAL GLU THR GLY ARG GLU GLY VAL LYS ALA LEU LYS
SEQRES 11 B 136 ALA LYS PRO PHE ALA GLY
SEQRES 1 C 85 MET PHE GLN GLN GLU VAL THR ILE THR ALA PRO ASN GLY
SEQRES 2 C 85 LEU HIS THR ARG PRO ALA ALA GLN PHE VAL LYS GLU ALA
SEQRES 3 C 85 LYS GLY PHE THR SER GLU ILE THR VAL THR SER ASN GLY
SEQRES 4 C 85 LYS SER ALA SER ALA LYS SER LEU PHE LYS LEU GLN THR
SEQRES 5 C 85 LEU GLY LEU THR GLN GLY THR VAL VAL THR ILE SER ALA
SEQRES 6 C 85 GLU GLY GLU ASP GLU GLN LYS ALA VAL GLU HIS LEU VAL
SEQRES 7 C 85 LYS LEU MET ALA GLU LEU GLU
SEQRES 1 D 85 MET PHE GLN GLN GLU VAL THR ILE THR ALA PRO ASN GLY
SEQRES 2 D 85 LEU HIS THR ARG PRO ALA ALA GLN PHE VAL LYS GLU ALA
SEQRES 3 D 85 LYS GLY PHE THR SER GLU ILE THR VAL THR SER ASN GLY
SEQRES 4 D 85 LYS SER ALA SER ALA LYS SER LEU PHE LYS LEU GLN THR
SEQRES 5 D 85 LEU GLY LEU THR GLN GLY THR VAL VAL THR ILE SER ALA
SEQRES 6 D 85 GLU GLY GLU ASP GLU GLN LYS ALA VAL GLU HIS LEU VAL
SEQRES 7 D 85 LYS LEU MET ALA GLU LEU GLU
HET PO3 C 401 4
HET PO3 D 400 4
HETNAM PO3 PHOSPHITE ION
FORMUL 5 PO3 2(O3 P 3-)
HELIX 1 1 TRP A 12 GLY A 26 1 15
HELIX 2 2 ASN A 41 ALA A 54 1 14
HELIX 3 3 GLY A 71 VAL A 82 1 12
HELIX 4 4 ASN A 94 ASP A 106 1 13
HELIX 5 5 SER A 110 GLY A 125 1 16
HELIX 6 6 TRP B 12 GLY B 26 1 15
HELIX 7 7 ASN B 41 ALA B 54 1 14
HELIX 8 8 GLY B 71 VAL B 82 1 12
HELIX 9 9 ASN B 94 ASP B 106 1 13
HELIX 10 10 SER B 110 GLY B 125 1 16
HELIX 11 11 HIS C 215 LYS C 227 1 13
HELIX 12 12 SER C 246 GLN C 251 1 6
HELIX 13 13 ASP C 269 LEU C 284 1 16
HELIX 14 14 HIS D 215 LYS D 227 1 13
HELIX 15 15 SER D 246 GLN D 251 1 6
HELIX 16 16 ASP D 269 LEU D 284 1 16
SHEET 1 A 5 VAL A 31 ILE A 34 0
SHEET 2 A 5 ALA A 4 GLY A 8 1 N ILE A 5 O GLY A 32
SHEET 3 A 5 VAL A 62 VAL A 66 1 O LEU A 65 N VAL A 6
SHEET 4 A 5 TYR A 87 ALA A 91 1 O GLU A 88 N PHE A 64
SHEET 5 A 5 LYS B 127 ALA B 128 -1 O LYS B 127 N ALA A 91
SHEET 1 B 5 LYS A 127 ALA A 128 0
SHEET 2 B 5 TYR B 87 ALA B 91 -1 O ALA B 91 N LYS A 127
SHEET 3 B 5 VAL B 62 VAL B 66 1 N PHE B 64 O GLU B 88
SHEET 4 B 5 ALA B 4 GLY B 8 1 N VAL B 6 O LEU B 65
SHEET 5 B 5 VAL B 31 ILE B 34 1 O GLY B 32 N ILE B 5
SHEET 1 C 4 PHE C 202 THR C 207 0
SHEET 2 C 4 VAL C 260 GLU C 266 -1 O ALA C 265 N PHE C 202
SHEET 3 C 4 GLU C 232 SER C 237 -1 N THR C 236 O THR C 262
SHEET 4 C 4 LYS C 240 SER C 243 -1 O LYS C 240 N SER C 237
SHEET 1 D 4 PHE D 202 THR D 207 0
SHEET 2 D 4 VAL D 260 GLU D 266 -1 O ALA D 265 N PHE D 202
SHEET 3 D 4 GLU D 232 SER D 237 -1 N THR D 236 O THR D 262
SHEET 4 D 4 LYS D 240 SER D 243 -1 O LYS D 240 N SER D 237
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
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