HEADER HYDROLASE/HYDROLASE INHIBITOR 06-SEP-04 1XDH
TITLE STRUCTURE OF PLASMEPSIN II IN COMPLEX WITH PEPSTATIN A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMEPSIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ASPARTIC HEMOGLOBINASE II, PFAPD;
COMPND 5 EC: 3.4.23.39;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PEPSTATIN;
COMPND 8 CHAIN: C, D;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_COMMON: MALARIA PARASITE P. FALCIPARUM;
SOURCE 4 ORGANISM_TAXID: 5833;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES
KEYWDS HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.PRADE
REVDAT 3 13-JUL-11 1XDH 1 VERSN
REVDAT 2 24-FEB-09 1XDH 1 VERSN
REVDAT 1 23-AUG-05 1XDH 0
JRNL AUTH L.PRADE
JRNL TITL STRUCTURE OF PLASMEPSIN II IN COMPLEX WITH PEPSTATIN A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 119.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 114632
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6068
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.76
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11009
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3580
REMARK 3 BIN FREE R VALUE SET COUNT : 581
REMARK 3 BIN FREE R VALUE : 0.3910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5310
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 736
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.29000
REMARK 3 B22 (A**2) : -0.29000
REMARK 3 B33 (A**2) : 0.43000
REMARK 3 B12 (A**2) : -0.14000
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): 0.096
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.095
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.278
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5446 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4810 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7414 ; 1.276 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11256 ; 0.890 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 656 ; 7.043 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 844 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6022 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1084 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1059 ; 0.186 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6081 ; 0.230 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 3325 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 618 ; 0.126 ; 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): 17 ; 0.118 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 71 ; 0.204 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 50 ; 0.140 ; 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): 3272 ; 1.187 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5330 ; 1.975 ; 4.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2174 ; 1.266 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2084 ; 2.017 ; 4.000
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1XDH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-SEP-04.
REMARK 100 THE RCSB ID CODE IS RCSB030236.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
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 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 32.36733
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 64.73467
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 64.73467
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 32.36733
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1531 LIES ON A SPECIAL POSITION.
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 LEU A -1
REMARK 465 GLY A 0
REMARK 465 LEU B -1
REMARK 465 GLY B 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 THR B 221 CA - CB - CG2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 ASP B 279 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
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 SER A 2 -38.86 179.97
REMARK 500 ASN A 13 -3.95 67.92
REMARK 500 ALA A 38 26.50 -145.02
REMARK 500 ASP A 69 -72.85 -136.49
REMARK 500 LYS A 163 -68.87 -96.15
REMARK 500 LEU A 191 -88.09 -147.99
REMARK 500 VAL A 201 -63.53 -127.73
REMARK 500 ASN A 233 51.95 -118.24
REMARK 500 SER B 2 -23.53 98.69
REMARK 500 GLN B 26 -77.84 -59.73
REMARK 500 GLN B 27 77.68 48.78
REMARK 500 ASP B 69 -60.68 -138.88
REMARK 500 SER B 135 73.00 28.66
REMARK 500 LYS B 163 -63.31 -130.33
REMARK 500 LEU B 191 -86.77 -144.82
REMARK 500 PHE B 241 16.67 55.79
REMARK 500 PRO B 243 46.12 -84.09
REMARK 500 ASN B 251 107.93 -55.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1595 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH A1606 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH A1658 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A1715 DISTANCE = 5.62 ANGSTROMS
REMARK 525 HOH A1727 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH A1733 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH A1754 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH A1768 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH B1565 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH B1567 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH B1632 DISTANCE = 7.43 ANGSTROMS
REMARK 525 HOH B1745 DISTANCE = 5.68 ANGSTROMS
REMARK 525 HOH D1638 DISTANCE = 5.55 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF PEPSTATIN
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF PEPSTATIN
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M43 RELATED DB: PDB
DBREF 1XDH A -1 329 UNP P46925 PLM2_PLAFA 123 453
DBREF 1XDH B -1 329 UNP P46925 PLM2_PLAFA 123 453
DBREF 1XDH C 1347 1352 PDB 1XDH 1XDH 1347 1352
DBREF 1XDH D 1347 1352 PDB 1XDH 1XDH 1347 1352
SEQRES 1 A 331 LEU GLY SER SER ASN ASP ASN ILE GLU LEU VAL ASP PHE
SEQRES 2 A 331 GLN ASN ILE MET PHE TYR GLY ASP ALA GLU VAL GLY ASP
SEQRES 3 A 331 ASN GLN GLN PRO PHE THR PHE ILE LEU ASP THR GLY SER
SEQRES 4 A 331 ALA ASN LEU TRP VAL PRO SER VAL LYS CYS THR THR ALA
SEQRES 5 A 331 GLY CYS LEU THR LYS HIS LEU TYR ASP SER SER LYS SER
SEQRES 6 A 331 ARG THR TYR GLU LYS ASP GLY THR LYS VAL GLU MET ASN
SEQRES 7 A 331 TYR VAL SER GLY THR VAL SER GLY PHE PHE SER LYS ASP
SEQRES 8 A 331 LEU VAL THR VAL GLY ASN LEU SER LEU PRO TYR LYS PHE
SEQRES 9 A 331 ILE GLU VAL ILE ASP THR ASN GLY PHE GLU PRO THR TYR
SEQRES 10 A 331 THR ALA SER THR PHE ASP GLY ILE LEU GLY LEU GLY TRP
SEQRES 11 A 331 LYS ASP LEU SER ILE GLY SER VAL ASP PRO ILE VAL VAL
SEQRES 12 A 331 GLU LEU LYS ASN GLN ASN LYS ILE GLU ASN ALA LEU PHE
SEQRES 13 A 331 THR PHE TYR LEU PRO VAL HIS ASP LYS HIS THR GLY PHE
SEQRES 14 A 331 LEU THR ILE GLY GLY ILE GLU GLU ARG PHE TYR GLU GLY
SEQRES 15 A 331 PRO LEU THR TYR GLU LYS LEU ASN HIS ASP LEU TYR TRP
SEQRES 16 A 331 GLN ILE THR LEU ASP ALA HIS VAL GLY ASN ILE MET LEU
SEQRES 17 A 331 GLU LYS ALA ASN CYS ILE VAL ASP SER GLY THR SER ALA
SEQRES 18 A 331 ILE THR VAL PRO THR ASP PHE LEU ASN LYS MET LEU GLN
SEQRES 19 A 331 ASN LEU ASP VAL ILE LYS VAL PRO PHE LEU PRO PHE TYR
SEQRES 20 A 331 VAL THR LEU CYS ASN ASN SER LYS LEU PRO THR PHE GLU
SEQRES 21 A 331 PHE THR SER GLU ASN GLY LYS TYR THR LEU GLU PRO GLU
SEQRES 22 A 331 TYR TYR LEU GLN HIS ILE GLU ASP VAL GLY PRO GLY LEU
SEQRES 23 A 331 CYS MET LEU ASN ILE ILE GLY LEU ASP PHE PRO VAL PRO
SEQRES 24 A 331 THR PHE ILE LEU GLY ASP PRO PHE MET ARG LYS TYR PHE
SEQRES 25 A 331 THR VAL PHE ASP TYR ASP ASN HIS SER VAL GLY ILE ALA
SEQRES 26 A 331 LEU ALA LYS LYS ASN LEU
SEQRES 1 B 331 LEU GLY SER SER ASN ASP ASN ILE GLU LEU VAL ASP PHE
SEQRES 2 B 331 GLN ASN ILE MET PHE TYR GLY ASP ALA GLU VAL GLY ASP
SEQRES 3 B 331 ASN GLN GLN PRO PHE THR PHE ILE LEU ASP THR GLY SER
SEQRES 4 B 331 ALA ASN LEU TRP VAL PRO SER VAL LYS CYS THR THR ALA
SEQRES 5 B 331 GLY CYS LEU THR LYS HIS LEU TYR ASP SER SER LYS SER
SEQRES 6 B 331 ARG THR TYR GLU LYS ASP GLY THR LYS VAL GLU MET ASN
SEQRES 7 B 331 TYR VAL SER GLY THR VAL SER GLY PHE PHE SER LYS ASP
SEQRES 8 B 331 LEU VAL THR VAL GLY ASN LEU SER LEU PRO TYR LYS PHE
SEQRES 9 B 331 ILE GLU VAL ILE ASP THR ASN GLY PHE GLU PRO THR TYR
SEQRES 10 B 331 THR ALA SER THR PHE ASP GLY ILE LEU GLY LEU GLY TRP
SEQRES 11 B 331 LYS ASP LEU SER ILE GLY SER VAL ASP PRO ILE VAL VAL
SEQRES 12 B 331 GLU LEU LYS ASN GLN ASN LYS ILE GLU ASN ALA LEU PHE
SEQRES 13 B 331 THR PHE TYR LEU PRO VAL HIS ASP LYS HIS THR GLY PHE
SEQRES 14 B 331 LEU THR ILE GLY GLY ILE GLU GLU ARG PHE TYR GLU GLY
SEQRES 15 B 331 PRO LEU THR TYR GLU LYS LEU ASN HIS ASP LEU TYR TRP
SEQRES 16 B 331 GLN ILE THR LEU ASP ALA HIS VAL GLY ASN ILE MET LEU
SEQRES 17 B 331 GLU LYS ALA ASN CYS ILE VAL ASP SER GLY THR SER ALA
SEQRES 18 B 331 ILE THR VAL PRO THR ASP PHE LEU ASN LYS MET LEU GLN
SEQRES 19 B 331 ASN LEU ASP VAL ILE LYS VAL PRO PHE LEU PRO PHE TYR
SEQRES 20 B 331 VAL THR LEU CYS ASN ASN SER LYS LEU PRO THR PHE GLU
SEQRES 21 B 331 PHE THR SER GLU ASN GLY LYS TYR THR LEU GLU PRO GLU
SEQRES 22 B 331 TYR TYR LEU GLN HIS ILE GLU ASP VAL GLY PRO GLY LEU
SEQRES 23 B 331 CYS MET LEU ASN ILE ILE GLY LEU ASP PHE PRO VAL PRO
SEQRES 24 B 331 THR PHE ILE LEU GLY ASP PRO PHE MET ARG LYS TYR PHE
SEQRES 25 B 331 THR VAL PHE ASP TYR ASP ASN HIS SER VAL GLY ILE ALA
SEQRES 26 B 331 LEU ALA LYS LYS ASN LEU
SEQRES 1 C 6 IVA VAL VAL STA ALA STA
SEQRES 1 D 6 IVA VAL VAL STA ALA STA
HET IVA C1347 6
HET STA C1350 11
HET STA C1352 12
HET IVA D1347 6
HET STA D1350 11
HET STA D1352 12
HETNAM IVA ISOVALERIC ACID
HETNAM STA STATINE
FORMUL 3 IVA 2(C5 H10 O2)
FORMUL 3 STA 4(C8 H17 N O3)
FORMUL 5 HOH *736(H2 O)
HELIX 1 1 THR A 49 LYS A 55 5 7
HELIX 2 2 ASP A 59 SER A 63 5 5
HELIX 3 3 THR A 108 GLU A 112 5 5
HELIX 4 4 PRO A 113 SER A 118 1 6
HELIX 5 5 TRP A 128 SER A 132 5 5
HELIX 6 6 PRO A 138 GLN A 146 1 9
HELIX 7 7 GLU A 174 ARG A 176 5 3
HELIX 8 8 PRO A 223 LEU A 231 1 9
HELIX 9 9 GLU A 269 TYR A 273 1 5
HELIX 10 10 GLY A 302 LYS A 308 1 7
HELIX 11 11 GLY B 51 LYS B 55 5 5
HELIX 12 12 ASP B 59 SER B 63 5 5
HELIX 13 13 THR B 108 GLU B 112 5 5
HELIX 14 14 PRO B 113 SER B 118 1 6
HELIX 15 15 TRP B 128 SER B 132 5 5
HELIX 16 16 PRO B 138 GLN B 146 1 9
HELIX 17 17 GLU B 174 ARG B 176 5 3
HELIX 18 18 PRO B 223 ASN B 233 1 11
HELIX 19 19 GLU B 269 LEU B 274 1 6
HELIX 20 20 GLY B 302 LYS B 308 1 7
SHEET 1 A15 GLU A 67 TYR A 77 0
SHEET 2 A15 GLY A 80 VAL A 93 -1 O GLY A 80 N TYR A 77
SHEET 3 A15 MET A 15 VAL A 22 -1 O GLU A 21 N THR A 92
SHEET 4 A15 GLN A 27 ASP A 34 -1 O GLN A 27 N VAL A 22
SHEET 5 A15 GLY A 122 GLY A 125 1 N GLY A 122 O THR A 30
SHEET 6 A15 LEU A 40 PRO A 43 -1 N TRP A 41 O ILE A 123
SHEET 7 A15 LEU A 96 ASP A 107 1 N ILE A 103 O LEU A 40
SHEET 8 A15 GLY A 80 VAL A 93 -1 O SER A 83 N ILE A 106
SHEET 9 A15 MET A 15 VAL A 22 -1 O GLU A 21 N THR A 92
SHEET 10 A15 ASP A 4 PHE A 11 -1 O GLU A 7 N ASP A 19
SHEET 11 A15 GLY A 166 ILE A 170 -1 O GLY A 166 N LEU A 8
SHEET 12 A15 LEU A 153 TYR A 157 -1 O THR A 155 N THR A 169
SHEET 13 A15 TYR A 309 ASP A 314 -1 O THR A 311 N PHE A 156
SHEET 14 A15 SER A 319 ALA A 325 -1 O SER A 319 N ASP A 314
SHEET 15 A15 TYR A 178 LYS A 186 -1 N GLU A 179 O LEU A 324
SHEET 1 B 7 LYS A 265 LEU A 268 0
SHEET 2 B 7 PHE A 257 THR A 260 -1 N PHE A 257 O LEU A 268
SHEET 3 B 7 GLN A 194 HIS A 200 -1 N ASP A 198 O THR A 260
SHEET 4 B 7 MET A 205 VAL A 213 -1 O LEU A 206 N ALA A 199
SHEET 5 B 7 THR A 298 LEU A 301 1 O PHE A 299 N ILE A 212
SHEET 6 B 7 ILE A 220 VAL A 222 -1 N THR A 221 O ILE A 300
SHEET 7 B 7 ILE A 289 GLY A 291 1 O ILE A 290 N VAL A 222
SHEET 1 C 4 ILE A 237 LYS A 238 0
SHEET 2 C 4 TYR A 245 LEU A 248 -1 O VAL A 246 N ILE A 237
SHEET 3 C 4 LEU A 284 LEU A 287 -1 N CYS A 285 O THR A 247
SHEET 4 C 4 LEU A 274 HIS A 276 -1 N GLN A 275 O MET A 286
SHEET 1 D24 GLU B 67 TYR B 77 0
SHEET 2 D24 GLY B 80 VAL B 93 -1 O GLY B 80 N TYR B 77
SHEET 3 D24 MET B 15 VAL B 22 -1 N GLU B 21 O THR B 92
SHEET 4 D24 PRO B 28 ASP B 34 -1 N PHE B 29 O ALA B 20
SHEET 5 D24 GLY B 122 GLY B 125 1 N GLY B 122 O THR B 30
SHEET 6 D24 LEU B 40 PRO B 43 -1 N TRP B 41 O ILE B 123
SHEET 7 D24 LEU B 96 ASP B 107 1 N ILE B 103 O LEU B 40
SHEET 8 D24 GLY B 80 VAL B 93 -1 O SER B 83 N ILE B 106
SHEET 9 D24 MET B 15 VAL B 22 -1 N GLU B 21 O THR B 92
SHEET 10 D24 ASP B 4 PHE B 11 -1 O GLU B 7 N ASP B 19
SHEET 11 D24 GLY B 166 ILE B 170 -1 O GLY B 166 N LEU B 8
SHEET 12 D24 LEU B 153 TYR B 157 -1 N THR B 155 O THR B 169
SHEET 13 D24 TYR B 309 ASP B 314 -1 O THR B 311 N PHE B 156
SHEET 14 D24 SER B 319 ALA B 325 -1 O SER B 319 N ASP B 314
SHEET 15 D24 TYR B 178 HIS B 189 -1 N GLU B 179 O LEU B 324
SHEET 16 D24 GLN B 194 VAL B 201 -1 O GLN B 194 N ASN B 188
SHEET 17 D24 PHE B 257 THR B 260 -1 O GLU B 258 N HIS B 200
SHEET 18 D24 LYS B 265 LEU B 268 -1 O TYR B 266 N PHE B 259
SHEET 19 D24 PHE B 257 THR B 260 -1 N PHE B 257 O LEU B 268
SHEET 20 D24 GLN B 194 VAL B 201 -1 N ASP B 198 O THR B 260
SHEET 21 D24 ILE B 204 VAL B 213 -1 O ILE B 204 N VAL B 201
SHEET 22 D24 THR B 298 LEU B 301 1 N PHE B 299 O ASN B 210
SHEET 23 D24 ILE B 220 VAL B 222 -1 N THR B 221 O ILE B 300
SHEET 24 D24 ILE B 289 GLY B 291 1 O ILE B 290 N VAL B 222
SHEET 1 E 4 ILE B 237 LYS B 238 0
SHEET 2 E 4 TYR B 245 LEU B 248 -1 N VAL B 246 O ILE B 237
SHEET 3 E 4 LEU B 284 MET B 286 -1 N CYS B 285 O THR B 247
SHEET 4 E 4 GLN B 275 HIS B 276 -1 O GLN B 275 N MET B 286
SSBOND 1 CYS A 47 CYS A 52 1555 1555 2.05
SSBOND 2 CYS A 249 CYS A 285 1555 1555 2.08
SSBOND 3 CYS B 47 CYS B 52 1555 1555 2.05
SSBOND 4 CYS B 249 CYS B 285 1555 1555 2.02
LINK C IVA C1347 N VAL C1348 1555 1555 1.33
LINK C VAL C1349 N STA C1350 1555 1555 1.33
LINK C STA C1350 N ALA C1351 1555 1555 1.33
LINK C ALA C1351 N STA C1352 1555 1555 1.33
LINK C IVA D1347 N VAL D1348 1555 1555 1.33
LINK C VAL D1349 N STA D1350 1555 1555 1.33
LINK C STA D1350 N ALA D1351 1555 1555 1.33
LINK C ALA D1351 N STA D1352 1555 1555 1.34
CISPEP 1 GLU A 112 PRO A 113 0 5.69
CISPEP 2 GLU B 112 PRO B 113 0 5.23
SITE 1 AC1 20 ILE A 32 ASP A 34 GLY A 36 SER A 37
SITE 2 AC1 20 ASN A 76 TYR A 77 VAL A 78 SER A 79
SITE 3 AC1 20 LEU A 131 TYR A 192 ASP A 214 GLY A 216
SITE 4 AC1 20 THR A 217 SER A 218 HOH A1482 HOH A1514
SITE 5 AC1 20 PHE B 241 LEU B 242 HOH B1404 HOH C1618
SITE 1 AC2 22 PHE A 241 LEU A 242 HOH A1497 ILE B 32
SITE 2 AC2 22 ASP B 34 GLY B 36 SER B 37 ASN B 76
SITE 3 AC2 22 TYR B 77 VAL B 78 SER B 79 LEU B 131
SITE 4 AC2 22 TYR B 192 ASP B 214 GLY B 216 THR B 217
SITE 5 AC2 22 SER B 218 ILE B 290 HOH D1404 HOH D1508
SITE 6 AC2 22 HOH D1583 HOH D1610
CRYST1 141.111 141.111 97.102 90.00 90.00 120.00 P 31 2 1 12
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 0.007087 0.004091 0.000000 0.00000
SCALE2 0.000000 0.008183 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010298 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
