HEADER LIPID TRANSPORT 28-DEC-15 5H9H
TITLE HOLO ACYL CARRIER PROTEIN (HOLO-ACP) FROM HELICOBACTER PYLORI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL CARRIER PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: ACP;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI P12;
SOURCE 3 ORGANISM_TAXID: 570508;
SOURCE 4 STRAIN: P12;
SOURCE 5 GENE: ACPP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ACYL CARRIER PROTEIN, FATTY ACID BIOSYNTHESIS, HELICOBACTER PYLORI,
KEYWDS 2 LIPID TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR L.ZHANG,L.ZHANG,X.SHEN,H.JIANG
REVDAT 2 08-NOV-23 5H9H 1 HETNAM HETSYN
REVDAT 1 28-DEC-16 5H9H 0
JRNL AUTH L.ZHANG,L.ZHANG,X.SHEN,H.JIANG
JRNL TITL HOLO ACYL CARRIER PROTEIN (HOLO-ACP) FROM HELICOBACTER
JRNL TITL 2 PYLORI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 6736
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 326
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 491
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE SET COUNT : 31
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1782
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 20
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.40000
REMARK 3 B22 (A**2) : 1.40000
REMARK 3 B33 (A**2) : -2.10000
REMARK 3 B12 (A**2) : 0.70000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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): 0.333
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.311
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.328
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1797 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2444 ; 1.484 ; 2.023
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 220 ; 5.979 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 90 ;47.693 ;28.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 307 ;19.380 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 292 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1333 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 862 ; 0.233 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1287 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 53 ; 0.130 ; 0.200
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): 91 ; 0.271 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.254 ; 0.200
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): 1145 ; 0.545 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1793 ; 0.964 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 708 ; 1.510 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 651 ; 2.701 ; 4.500
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5H9H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216703.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-X
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6736
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.27000
REMARK 200 R SYM FOR SHELL (I) : 0.16000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1T8K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M AMMONIUM SULFATE, 0.1 M TRI
REMARK 280 -SODIUM CITRATE DIHYDRATE, 1 M LITHIUM SULFATE MONOHYDRATE, PH
REMARK 280 4.0, EVAPORATION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 24.43333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 48.86667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A -4
REMARK 465 MET A -3
REMARK 465 GLY A -2
REMARK 465 TYR A -1
REMARK 465 LEU A 0
REMARK 465 MET A 1
REMARK 465 LYS A 76
REMARK 465 LEU A 77
REMARK 465 ALA A 78
REMARK 465 ALA B -4
REMARK 465 MET B -3
REMARK 465 GLY B -2
REMARK 465 TYR B -1
REMARK 465 LEU B 0
REMARK 465 MET B 1
REMARK 465 LEU B 77
REMARK 465 ALA B 78
REMARK 465 ALA C -4
REMARK 465 MET C -3
REMARK 465 GLY C -2
REMARK 465 TYR C -1
REMARK 465 LEU C 0
REMARK 465 MET C 1
REMARK 465 LYS C 76
REMARK 465 LEU C 77
REMARK 465 ALA C 78
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 ASN B 16 73.06 55.10
REMARK 500 ASN B 75 29.65 -141.14
REMARK 500 ASP C 74 14.71 -61.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5H9G RELATED DB: PDB
DBREF 5H9H A 1 78 UNP B6JLE2 ACP_HELP2 1 78
DBREF 5H9H B 1 78 UNP B6JLE2 ACP_HELP2 1 78
DBREF 5H9H C 1 78 UNP B6JLE2 ACP_HELP2 1 78
SEQADV 5H9H ALA A -4 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H MET A -3 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H GLY A -2 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H TYR A -1 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H LEU A 0 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H ALA B -4 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H MET B -3 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H GLY B -2 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H TYR B -1 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H LEU B 0 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H ALA C -4 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H MET C -3 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H GLY C -2 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H TYR C -1 UNP B6JLE2 EXPRESSION TAG
SEQADV 5H9H LEU C 0 UNP B6JLE2 EXPRESSION TAG
SEQRES 1 A 83 ALA MET GLY TYR LEU MET ALA LEU PHE GLU ASP ILE GLN
SEQRES 2 A 83 ALA VAL ILE ALA GLU GLN LEU ASN VAL ASP ALA ALA GLN
SEQRES 3 A 83 VAL THR PRO GLU ALA GLU PHE VAL LYS ASP LEU GLY ALA
SEQRES 4 A 83 ASP 4HH LEU ASP VAL VAL GLU LEU ILE MET ALA LEU GLU
SEQRES 5 A 83 GLU LYS PHE GLY ILE GLU ILE PRO ASP GLU GLN ALA GLU
SEQRES 6 A 83 LYS ILE VAL ASN VAL GLY ASP VAL VAL LYS TYR ILE GLU
SEQRES 7 A 83 ASP ASN LYS LEU ALA
SEQRES 1 B 83 ALA MET GLY TYR LEU MET ALA LEU PHE GLU ASP ILE GLN
SEQRES 2 B 83 ALA VAL ILE ALA GLU GLN LEU ASN VAL ASP ALA ALA GLN
SEQRES 3 B 83 VAL THR PRO GLU ALA GLU PHE VAL LYS ASP LEU GLY ALA
SEQRES 4 B 83 ASP 4HH LEU ASP VAL VAL GLU LEU ILE MET ALA LEU GLU
SEQRES 5 B 83 GLU LYS PHE GLY ILE GLU ILE PRO ASP GLU GLN ALA GLU
SEQRES 6 B 83 LYS ILE VAL ASN VAL GLY ASP VAL VAL LYS TYR ILE GLU
SEQRES 7 B 83 ASP ASN LYS LEU ALA
SEQRES 1 C 83 ALA MET GLY TYR LEU MET ALA LEU PHE GLU ASP ILE GLN
SEQRES 2 C 83 ALA VAL ILE ALA GLU GLN LEU ASN VAL ASP ALA ALA GLN
SEQRES 3 C 83 VAL THR PRO GLU ALA GLU PHE VAL LYS ASP LEU GLY ALA
SEQRES 4 C 83 ASP 4HH LEU ASP VAL VAL GLU LEU ILE MET ALA LEU GLU
SEQRES 5 C 83 GLU LYS PHE GLY ILE GLU ILE PRO ASP GLU GLN ALA GLU
SEQRES 6 C 83 LYS ILE VAL ASN VAL GLY ASP VAL VAL LYS TYR ILE GLU
SEQRES 7 C 83 ASP ASN LYS LEU ALA
MODRES 5H9H 4HH A 36 SER MODIFIED RESIDUE
MODRES 5H9H 4HH B 36 SER MODIFIED RESIDUE
MODRES 5H9H 4HH C 36 SER MODIFIED RESIDUE
HET 4HH A 36 27
HET 4HH B 36 27
HET 4HH C 36 27
HETNAM 4HH 4'-PHOSPHOPANTHETHEINE-SERINE
HETSYN 4HH O-[(S)-HYDROXY{[(3R)-3-HYDROXY-2,2-DIMETHYL-4-OXO-4-
HETSYN 2 4HH ({3-OXO-3-[(2-SULFANYLETHYL)AMINO]PROPYL}AMINO)
HETSYN 3 4HH BUTYL]OXY}PHOSPHORYL]-L-SERINE
FORMUL 1 4HH 3(C14 H28 N3 O9 P S)
FORMUL 4 HOH *20(H2 O)
HELIX 1 AA1 ALA A 2 LEU A 15 1 14
HELIX 2 AA2 ASP A 18 VAL A 22 5 5
HELIX 3 AA3 ASP A 35 GLY A 51 1 17
HELIX 4 AA4 PRO A 55 ILE A 62 1 8
HELIX 5 AA5 ASN A 64 ASN A 75 1 12
HELIX 6 AA6 LEU B 3 ASN B 16 1 14
HELIX 7 AA7 ASP B 18 VAL B 22 5 5
HELIX 8 AA8 ASP B 35 GLY B 51 1 17
HELIX 9 AA9 PRO B 55 GLU B 60 1 6
HELIX 10 AB1 ASN B 64 ASP B 74 1 11
HELIX 11 AB2 LEU C 3 ASN C 16 1 14
HELIX 12 AB3 GLU C 27 GLY C 33 1 7
HELIX 13 AB4 ASP C 35 GLY C 51 1 17
HELIX 14 AB5 PRO C 55 LYS C 61 1 7
HELIX 15 AB6 ASN C 64 ASP C 74 1 11
LINK C ASP A 35 N 4HH A 36 1555 1555 1.32
LINK C 4HH A 36 N LEU A 37 1555 1555 1.33
LINK C ASP B 35 N 4HH B 36 1555 1555 1.32
LINK C 4HH B 36 N LEU B 37 1555 1555 1.34
LINK C ASP C 35 N 4HH C 36 1555 1555 1.33
LINK C 4HH C 36 N LEU C 37 1555 1555 1.33
CRYST1 50.344 50.344 73.300 90.00 90.00 120.00 P 31 9
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 0.019863 0.011468 0.000000 0.00000
SCALE2 0.000000 0.022936 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013643 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
