Header list of 1j6t.pdb file
Complete list - 21 20 Bytes
HEADER TRANSFERASE 14-AUG-02 1J6T TITLE COMPLEX OF ENZYME IIAMTL 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, MANNITOL-SPECIFIC IIABC COMPONENT; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: EIIA DOMAIN; COMPND 5 SYNONYM: IIAMTL, EIIA-MTL, PHOSPHOTRANSFERASE ENZYME II, A DOMAIN COMPND 6 COMPONENT; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: PHOSPHOCARRIER PROTEIN HPR; COMPND 10 CHAIN: B; COMPND 11 SYNONYM: HPR, HISTIDINE-CONTAINING PROTEIN; COMPND 12 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,G.CORNILESCU REVDAT 4 21-DEC-22 1J6T 1 SEQADV REVDAT 3 30-JUN-21 1J6T 1 REMARK ATOM REVDAT 2 24-FEB-09 1J6T 1 VERSN REVDAT 1 13-NOV-02 1J6T 0 JRNL AUTH G.CORNILESCU,B.R.LEE,C.C.CORNILESCU,G.WANG,A.PETERKOSFKY, JRNL AUTH 2 G.M.CLORE JRNL TITL SOLUTION STRUCTURE OF THE PHOSPHORYL TRANSFER COMPLEX JRNL TITL 2 BETWEEN THE CYTOPLASMIC A DOMAIN OF THE MANNITOL TRANSPORTER JRNL TITL 3 IIMANNITOL AND HPR OF THE ESCHERICHIA COLI JRNL TITL 4 PHOSPHOTRANSFERASE SYSTEM JRNL REF J.BIOL.CHEM. V. 277 42289 2002 JRNL REFN ISSN 0021-9258 JRNL PMID 12202490 JRNL DOI 10.1074/JBC.M207314200 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: 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; (CLORE & BEWLEY (2002) J.MAGN.RESON. 154, 329-335) THE TARGET REMARK 3 FUNCTIONS COMPRISES TERMS FOR THE NOE RESTRAINTS, THE SIDECHAIN REMARK 3 TORSION ANGLE RESTRAINTS, THE BACKBONE TORSION ANGLE RESTRAINTS REMARK 3 FOR 4 VARIABLE REGIONS OF IIAMTL, 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 REMARK 3 X-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 IIAMTL (MOLECULE D OF 1A3A, VAN MONTFORT ET AL. STRUCTURE 5, 217- REMARK 3 225 (1998); RESOLUTION 1.8A). SEVERAL DIFFERENT INITIAL REMARK 3 ORIENTATIONS OF THE TWO PROTEINS WERE EMPLOYED WITH THE CA-CA REMARK 3 DISTANCE BETWEEN THE ACTIVE SITE HISTIDINES RANGING FROM 28 TO 95 REMARK 3 A, INCLUDING ORIENTATIONS WHERE THE TWO ACTIVE SITE HISTIDINES ARE REMARK 3 NOT OPPOSED AND WHERE HPR IS DIRECTED TOWARDS THE FACE OF IIAMTL REMARK 3 OPPOSITE TO THE IIAMTL ACTIVE SITE. THE BACKBONE COORDINATES AND REMARK 3 NON-INTERFACIAL SIDECHAINS (EXCLUDING THE FOUR VARIABLE REGIONS OF REMARK 3 IIAMTL: RESIDUES 51-54, 66-78, 91-96 AND 104-110) ARE TREATED AS REMARK 3 RIGID BODIES THROUGHOUT WITH IIAMTL HELD FIXED, HPR ALLOWED TO REMARK 3 ROTATE AND TRANSLATE, AND THE AXIS OF THE DIPOLAR COUPLING REMARK 3 ALIGNMENT TENSOR FREE TO ROTATE. THE INTERFACIAL SIDECHAINS, AS REMARK 3 WELL AS THE BACKBONE AND SIDECHAINS OF THE FOUR VARIABLE REGIONS REMARK 3 OF IIAMTL, ARE GIVEN FULL TORSIONAL DEGREES OF FREEDOM. ALSO NOTE REMARK 3 THAT GLU59 AND HIS111 ARE REFINED IN TWO ALTERNATE CONFORMATIONS. 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 (EXCLUDING REMARK 3 THE FOUR VARIABLE REGIONS OF IIAMTL) PROVIDE ONLY A REMARK 3 MEASURE OF THE PRECISION WITH WHICH THE RELATIVE REMARK 3 ORIENTATION OF THE TWO PROTEINS HAVE BEEN DETERMINED AND REMARK 3 DOES NOT TAKE INTO ACCOUNT THE ERRORS IN THE X-RAY REMARK 3 COORDINATES OF HPR AND IIAMTL. REMARK 3 REMARK 3 RESIDUE NUMBERING: REMARK 3 IIAMTL: 4-147 (RESIDUES 1-3 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 HPR: 301-385 (CORRESPONDING TO RESIDUES 1-85). REMARK 3 PHOSPHATE: RESIDUE 200 REMARK 3 REMARK 3 THREE SETS OF COORDINATES ARE GIVEN: REMARK 3 REMARK 3 MODEL 1: RESTRAINED REGULARIZED MEAN REMARK 3 COORDINATES OF THE UNPHOSPHORYLATED HPR-IIAGLC COMPLEX REMARK 3 SOLVED ON THE BASIS OF 107 INTERMOLECULAR REMARK 3 INTERPROTON DISTANCE DISTANCE RESTRAINTS, 105 INTRAMOLECULAR REMARK 3 DISTANCE RESTRAINTS (RELATING TO INTERFACIAL SIDECHAINS, AS REMARK 3 WELL AS THE FOUR VARIABLE REGIONS OF IIAMTL), 70 INTERFACIAL REMARK 3 SIDECHAIN TORSION ANGLE RESTRAINTS, 62 TORSION ANGLE REMARK 3 RESTRAINTS FOR THE VARIABLE REGIONS OF IIAMTL, AND 528 REMARK 3 RESIDUAL DIPOLAR COUPLINGS. REMARK 3 REMARK 3 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 REGULARIZED MEAN COORDINATES FOR THE REMARK 3 MODEL OF THE DISSOCIATIVE PHOSPHORYL TRANSITION STATE REMARK 3 HPR-IIAMTL COMPLEX. 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 MINIMIZATION. THE N-P BOND LENGTHS REMARK 3 ARE RESTRAINED TO 3 A. THE CA-CA DISTANCE BETWEEN HIS315 REMARK 3 (HPR) AND HIS65 (IIAMTL) REMAINS ESSENTIALLY UNCHANGED REMARK 3 FROM MODEL 3, BUT THE ND1-NE2 DISTANCE BETWEEN HIS315 AND REMARK 3 HIS65 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 STRUCTURE OF THE UNPHOSPHORYLATED COMPLEX (MODEL 3) REMARK 3 AND THE TRANSITION STATE COMPLEX IS 0.2 A FOR REMARK 3 BACKBONE COORDINATES IMMEDIATELY ADJACENT TO THE ACTIVE REMARK 3 SITE HISTIDINES (RESIDUES 64-66 AND RESIDUES 316-317). REMARK 3 THE REMAINING BACKBONE COORDINATES DO NOT SHIFT. REMARK 3 REMARK 3 MODEL 3: 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 N-P BOND LENGTHS RESTRAINED TO 2A. REMARK 3 THE STRUCTURE IS DERIVED FROM REMARK 3 MODEL 1 BY RESTRAINED MINIMIZATION. REMARK 3 THE RMS DIFFERENCE BETWEEN THE MEAN REMARK 3 STRUCTURES OF THE UNPHOSPHORYLATED COMPLEX (MODEL 1) REMARK 3 AND THE TRANSITION STATE COMPLEX IS 0.4 A FOR REMARK 3 BACKBONE COORDINATES IMMEDIATELY ADJACENT TO THE ACTIVE REMARK 3 SITE HISTIDINES (RESIDUES 64-66 AND RESIDUES 316-317). REMARK 3 THE REMAINING BACKBONE COORDINATES DO NOT SHIFT. REMARK 3 REMARK 3 HPR-IIAMTL COMPLEX REMARK 3 DEVIATIONS FROM IDEALIZED GEOMETRY: REMARK 3 BONDS 0.006 A, ANGLES 0.82 DEG, IMPROPER TORSIONS 0.97 DEG REMARK 3 RMS DEVIATIONS FROM NOE DISTANCE RESTRAINTS: 0.007 A REMARK 3 RMS DEVIATIONS FROM SIDECHAIN TORSION ANGLE RESTRAINTS: REMARK 3 0.26 DEG. REMARK 3 RMS DEVIATIONS FROM BACKBONE TORSION ANGLE RESTRAINTS: REMARK 3 1.2 DEG. REMARK 3 DIPOLAR COUPLING R-FACTORS (CLORE AND GARRETT (1999) REMARK 3 J. AM. CHEM. SOC. 121, 9008-9012): REMARK 3 HPR IIAMTL REMARK 3 NH 19.1% 19.2% REMARK 3 CAH 25.9% 18.7% REMARK 3 NC' 34.0% 32.1% REMARK 3 REMARK 3 [NOTE ONE ALIGNMENT TENSOR IS USED FOR THE REMARK 3 NH DIPOLAR COUPLINGS (FOR BOTH HPR AND IIAMTL), REMARK 3 AND ANOTHER FOR THE REMARK 3 CAH AND NC' DIPOLAR COUPLINGS (FOR BOTH REMARK 3 HPR AND IIAMTL), SINCE THE LATTER SET OF DIPOLAR REMARK 3 COUPLINGS WERE OBTAINED REMARK 3 FROM A DIFFERENT BATCH OF PEG/HEXANOL REMARK 3 THAN THE FORMER. THE ORIENTATION OF THE REMARK 3 TWO ALIGNMENT TENSORS DIFFERS BY ONLY 1.9 DEG. REMARK 3 NOTE THE ALIGNMENT TENSORS FOR HPR REMARK 3 AND IIAMTL ARE THE SAME. FOR REFERENCE REMARK 3 THE DIPOLAR COUPLING R-FACTORS FOR THE FREE STRUCTURES REMARK 3 (USING INDIVIDUAL ALIGNMENT TENSORS FOR THE TWO PROTEINS) REMARK 3 ARE 21.3% (NH), 21.1% (CAH), 33.6% (NC') FOR REMARK 3 THE X-RAY STRUCTURE OF HPR, AND REMARK 3 19.2% (NH), 18.0% (CAH) AND 32.0% (NC') FOR THE RESTRAINED REMARK 3 REGULARIZED MEAN STRUCTURE OF IIAMTL IN THE COMPLEX]. REMARK 4 REMARK 4 1J6T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-02. REMARK 100 THE DEPOSITION ID IS D_1000001659. 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 : TRIPLE RESONANCE FOR ASSIGNMENT REMARK 210 OF PROTEIN; QUANTITATIVE J REMARK 210 CORRELATION FOR COUPLING REMARK 210 CONSTANTS; 3D, 4D HETERONUCLEAR REMARK 210 SEPARATED, FILTERED NOE EXPTS; REMARK 210 IPAP EXPERIMENTS FOR DIPOLAR REMARK 210 COUPLINGS 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 : 200 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 MET A 1 REMARK 465 ALA A 2 REMARK 465 ASN A 3 REMARK 465 LYS A 148 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 ARG A 147 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 HA LEU A 7 HD22 ASN A 11 1.14 REMARK 500 HH TYR A 42 H GLY A 66 1.17 REMARK 500 HG1 THR A 134 H SER A 136 1.30 REMARK 500 HG SER B 343 H LYS B 345 1.33 REMARK 500 HH22 ARG A 99 OE2 GLU A 129 1.41 REMARK 500 O ILE B 308 H GLY B 358 1.58 REMARK 500 NE2 HIS A 65 P PO3 B 200 2.16 REMARK 500 ND1 HIS B 315 P PO3 B 200 2.18 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 B 315 -159.83 -80.85 REMARK 500 3 HIS B 315 -179.71 -69.41 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 B 317 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1J6T A 2 148 UNP P00550 PTM3C_ECOLI 491 637 DBREF 1J6T B 301 385 UNP P0AA04 PTHP_ECOLI 1 85 SEQADV 1J6T MET A 1 UNP P00550 INITIATING METHIONINE SEQRES 1 A 148 MET ALA ASN LEU PHE LYS LEU GLY ALA GLU ASN ILE PHE SEQRES 2 A 148 LEU GLY ARG LYS ALA ALA THR LYS GLU GLU ALA ILE ARG SEQRES 3 A 148 PHE ALA GLY GLU GLN LEU VAL LYS GLY GLY TYR VAL GLU SEQRES 4 A 148 PRO GLU TYR VAL GLN ALA MET LEU ASP ARG GLU LYS LEU SEQRES 5 A 148 THR PRO THR TYR LEU GLY GLU SER ILE ALA VAL PRO HIS SEQRES 6 A 148 GLY THR VAL GLU ALA LYS ASP ARG VAL LEU LYS THR GLY SEQRES 7 A 148 VAL VAL PHE CYS GLN TYR PRO GLU GLY VAL ARG PHE GLY SEQRES 8 A 148 GLU GLU GLU ASP ASP ILE ALA ARG LEU VAL ILE GLY ILE SEQRES 9 A 148 ALA ALA ARG ASN ASN GLU HIS ILE GLN VAL ILE THR SER SEQRES 10 A 148 LEU THR ASN ALA LEU ASP ASP GLU SER VAL ILE GLU ARG SEQRES 11 A 148 LEU ALA HIS THR THR SER VAL ASP GLU VAL LEU GLU LEU SEQRES 12 A 148 LEU ALA GLY ARG 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 GLY A 8 GLU A 10 5 3 HELIX 2 2 THR A 20 GLY A 35 1 16 HELIX 3 3 GLU A 41 THR A 53 1 13 HELIX 4 4 THR A 67 VAL A 74 5 8 HELIX 5 5 ALA A 106 ASN A 109 5 4 HELIX 6 6 GLU A 110 LEU A 122 1 13 HELIX 7 7 ASP A 124 THR A 134 1 11 HELIX 8 8 SER A 136 ALA A 145 1 10 HELIX 9 9 HIS B 315 GLY B 328 1 14 HELIX 10 10 SER B 346 GLN B 351 1 6 HELIX 11 11 ASP B 369 LEU B 384 1 16 SHEET 1 A 4 ILE A 12 PHE A 13 0 SHEET 2 A 4 GLY A 78 ARG A 89 1 O GLN A 83 N PHE A 13 SHEET 3 A 4 ILE A 97 ALA A 105 -1 O VAL A 101 N CYS A 82 SHEET 4 A 4 ILE A 61 ALA A 62 1 N ALA A 62 O ILE A 102 SHEET 1 B 4 PHE B 302 THR B 307 0 SHEET 2 B 4 VAL B 360 GLU B 366 -1 O VAL B 361 N VAL B 306 SHEET 3 B 4 GLU B 332 SER B 337 -1 N THR B 334 O SER B 364 SHEET 4 B 4 LYS B 340 SER B 343 -1 O ALA B 342 N VAL B 335 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
Complete list - 21 20 Bytes