HEADER TRANSFERASE 16-DEC-16 5MP7
TITLE CRYSTAL STRUCTURE OF PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE FROM
TITLE 2 MYCOBACTERIUM SMEGMATIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSE-PHOSPHATE PYROPHOSPHOKINASE;
COMPND 3 CHAIN: A, C, B;
COMPND 4 SYNONYM: RPPK,5-PHOSPHO-D-RIBOSYL ALPHA-1-DIPHOSPHATE,PHOSPHORIBOSYL
COMPND 5 DIPHOSPHATE SYNTHASE,PHOSPHORIBOSYL PYROPHOSPHATE SYNTHASE;
COMPND 6 EC: 2.7.6.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS (STRAIN ATCC 700084 /
SOURCE 3 MC(2)155);
SOURCE 4 ORGANISM_TAXID: 246196;
SOURCE 5 GENE: PRS, MSMEG_5427, MSMEI_5278;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE, PRPP SYNTHETASE,
KEYWDS 2 MYCOBACTERIUM SMEGMATIS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.DONINI,S.GARAVAGLIA,D.M.FERRARIS,R.MIGGIANO,S.MORI,K.SHIBAYAMA,
AUTHOR 2 M.RIZZI
REVDAT 4 17-JAN-24 5MP7 1 REMARK
REVDAT 3 13-JUL-22 5MP7 1 AUTHOR
REVDAT 2 20-FEB-19 5MP7 1 REMARK LINK
REVDAT 1 26-APR-17 5MP7 0
JRNL AUTH S.DONINI,S.GARAVAGLIA,D.M.FERRARIS,R.MIGGIANO,S.MORI,
JRNL AUTH 2 K.SHIBAYAMA,M.RIZZI
JRNL TITL BIOCHEMICAL AND STRUCTURAL INVESTIGATIONS ON
JRNL TITL 2 PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE FROM MYCOBACTERIUM
JRNL TITL 3 SMEGMATIS.
JRNL REF PLOS ONE V. 12 75815 2017
JRNL REFN ESSN 1932-6203
JRNL PMID 28419153
JRNL DOI 10.1371/JOURNAL.PONE.0175815
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 33860
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1820
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2484
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 117
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6864
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 68
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.53000
REMARK 3 B22 (A**2) : -2.53000
REMARK 3 B33 (A**2) : 5.06000
REMARK 3 B12 (A**2) : 0.00000
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): 0.524
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.253
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.220
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.942
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6990 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6876 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9468 ; 1.650 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15756 ; 1.549 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 888 ; 6.186 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 312 ;38.107 ;23.558
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1188 ;16.216 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 63 ;19.278 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1098 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7914 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1557 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 3573 ; 3.133 ; 3.879
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3569 ; 3.119 ; 3.877
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4452 ; 4.831 ; 5.812
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4453 ; 4.830 ; 5.812
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3417 ; 5.047 ; 4.654
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3418 ; 5.047 ; 4.654
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5017 ; 8.146 ; 6.671
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 27958 ;12.159 ;37.793
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 27955 ;12.159 ;37.794
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 3
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 10 316 C 10 316 35536 0.10 0.05
REMARK 3 2 A 10 316 B 10 316 35386 0.11 0.05
REMARK 3 3 C 10 316 B 10 316 35234 0.11 0.05
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5MP7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1200002791.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35723
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 43.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.34000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.340
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1DKR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NACL, 0.1M SODIUM ACETATE, 30%
REMARK 280 (V/V) 2-METHYL-2,4-PENTANEDIOL, PH 4.6, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 124.89550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 42.64600
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.64600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 62.44775
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.64600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 42.64600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 187.34325
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 42.64600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.64600
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 62.44775
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 42.64600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.64600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 187.34325
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 124.89550
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 69840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
REMARK 465 ASP A 4
REMARK 465 TRP A 5
REMARK 465 THR A 6
REMARK 465 ASP A 7
REMARK 465 ASN A 8
REMARK 465 ARG A 9
REMARK 465 ASP A 205
REMARK 465 PRO A 206
REMARK 465 LEU A 207
REMARK 465 VAL A 208
REMARK 465 PRO A 209
REMARK 465 ASN A 210
REMARK 465 GLN A 211
REMARK 465 VAL A 212
REMARK 465 LYS A 213
REMARK 465 SER A 317
REMARK 465 VAL A 318
REMARK 465 THR A 319
REMARK 465 GLY A 320
REMARK 465 LEU A 321
REMARK 465 PHE A 322
REMARK 465 ASP A 323
REMARK 465 GLY A 324
REMARK 465 SER A 325
REMARK 465 ALA A 326
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 THR C 3
REMARK 465 ASP C 4
REMARK 465 TRP C 5
REMARK 465 THR C 6
REMARK 465 ASP C 7
REMARK 465 ASN C 8
REMARK 465 ARG C 9
REMARK 465 ASP C 205
REMARK 465 PRO C 206
REMARK 465 LEU C 207
REMARK 465 VAL C 208
REMARK 465 PRO C 209
REMARK 465 ASN C 210
REMARK 465 GLN C 211
REMARK 465 VAL C 212
REMARK 465 LYS C 213
REMARK 465 SER C 317
REMARK 465 VAL C 318
REMARK 465 THR C 319
REMARK 465 GLY C 320
REMARK 465 LEU C 321
REMARK 465 PHE C 322
REMARK 465 ASP C 323
REMARK 465 GLY C 324
REMARK 465 SER C 325
REMARK 465 ALA C 326
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 ASP B 4
REMARK 465 TRP B 5
REMARK 465 THR B 6
REMARK 465 ASP B 7
REMARK 465 ASN B 8
REMARK 465 ARG B 9
REMARK 465 ASP B 205
REMARK 465 PRO B 206
REMARK 465 LEU B 207
REMARK 465 VAL B 208
REMARK 465 PRO B 209
REMARK 465 ASN B 210
REMARK 465 GLN B 211
REMARK 465 VAL B 212
REMARK 465 LYS B 213
REMARK 465 SER B 317
REMARK 465 VAL B 318
REMARK 465 THR B 319
REMARK 465 GLY B 320
REMARK 465 LEU B 321
REMARK 465 PHE B 322
REMARK 465 ASP B 323
REMARK 465 GLY B 324
REMARK 465 SER B 325
REMARK 465 ALA B 326
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 NH2 ARG B 181 OD1 ASP B 231 1.36
REMARK 500 CZ ARG B 181 OD1 ASP B 231 1.69
REMARK 500 NH1 ARG B 181 OD1 ASP B 231 1.86
REMARK 500 NH1 ARG B 181 OD1 ASP B 230 1.88
REMARK 500 NE2 GLN A 269 OE2 GLU A 273 1.89
REMARK 500 OD1 ASN B 307 NH2 ARG B 310 2.10
REMARK 500 NH2 ARG B 181 CG ASP B 231 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP C 53 OE2 GLU B 248 7555 1.83
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 181 N - CA - CB ANGL. DEV. = -11.0 DEGREES
REMARK 500 ILE A 200 CG1 - CB - CG2 ANGL. DEV. = -18.6 DEGREES
REMARK 500 ARG C 292 CG - CD - NE ANGL. DEV. = -13.7 DEGREES
REMARK 500 ARG C 310 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP B 42 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 MET B 81 CG - SD - CE ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG B 310 NE - CZ - NH1 ANGL. DEV. = 3.4 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 HIS A 109 -127.05 62.89
REMARK 500 ASP A 234 -83.54 -99.53
REMARK 500 ASP A 265 -120.48 58.98
REMARK 500 ASN A 283 40.85 -102.07
REMARK 500 ASP C 234 -83.90 -98.75
REMARK 500 ASP C 265 -120.75 58.98
REMARK 500 ASN C 283 43.18 -103.08
REMARK 500 ASP B 234 -84.16 -98.43
REMARK 500 ASP B 265 -120.75 58.45
REMARK 500 ASN B 283 40.08 -101.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 111 ARG B 112 -30.51
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 A 526 DISTANCE = 7.78 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG B 181 and ASP B
REMARK 800 231
DBREF 5MP7 A 1 326 UNP A0R3C8 A0R3C8_MYCS2 1 326
DBREF 5MP7 C 1 326 UNP A0R3C8 A0R3C8_MYCS2 1 326
DBREF 5MP7 B 1 326 UNP A0R3C8 A0R3C8_MYCS2 1 326
SEQRES 1 A 326 MET ALA THR ASP TRP THR ASP ASN ARG LYS ASN LEU MET
SEQRES 2 A 326 LEU PHE ALA GLY ARG ALA HIS PRO GLU LEU ALA ASP GLN
SEQRES 3 A 326 VAL ALA LYS GLU LEU ASP VAL ALA VAL THR ALA GLN THR
SEQRES 4 A 326 ALA ARG ASP PHE ALA ASN GLY GLU ILE PHE VAL ARG PHE
SEQRES 5 A 326 ASP GLU SER VAL ARG GLY CYS ASP ALA PHE VAL LEU GLN
SEQRES 6 A 326 SER HIS PRO ALA PRO LEU ASN GLN TRP LEU MET GLU GLN
SEQRES 7 A 326 LEU ILE MET ILE ASP ALA LEU LYS ARG GLY SER ALA LYS
SEQRES 8 A 326 ARG ILE THR ALA ILE LEU PRO PHE TYR PRO TYR ALA ARG
SEQRES 9 A 326 GLN ASP LYS LYS HIS ARG GLY ARG GLU PRO ILE SER ALA
SEQRES 10 A 326 ARG LEU VAL ALA ASP LEU LEU LYS THR ALA GLY ALA ASP
SEQRES 11 A 326 ARG ILE VAL SER VAL ASP LEU HIS THR ASP GLN ILE GLN
SEQRES 12 A 326 GLY PHE PHE ASP GLY PRO VAL ASP HIS MET ARG ALA GLN
SEQRES 13 A 326 LYS LEU LEU THR GLY TYR ILE GLY GLU HIS TYR ALA ASP
SEQRES 14 A 326 GLU ASP MET VAL VAL VAL SER PRO ASP SER GLY ARG VAL
SEQRES 15 A 326 ARG VAL ALA GLU LYS TRP ALA ASP SER LEU GLY GLY VAL
SEQRES 16 A 326 PRO LEU ALA PHE ILE HIS LYS THR ARG ASP PRO LEU VAL
SEQRES 17 A 326 PRO ASN GLN VAL LYS SER ASN ARG VAL VAL GLY ASP VAL
SEQRES 18 A 326 LYS GLY LYS THR CYS ILE LEU THR ASP ASP MET ILE ASP
SEQRES 19 A 326 THR GLY GLY THR ILE ALA GLY ALA VAL ASN LEU LEU ARG
SEQRES 20 A 326 GLU ASP GLY ALA LYS ASP VAL ILE ILE ALA ALA THR HIS
SEQRES 21 A 326 GLY VAL LEU SER ASP PRO ALA PRO GLN ARG LEU ALA GLU
SEQRES 22 A 326 CYS GLY ALA ARG GLU VAL ILE VAL THR ASN THR LEU PRO
SEQRES 23 A 326 ILE THR GLU ASP LYS ARG PHE PRO GLN LEU THR VAL LEU
SEQRES 24 A 326 SER ILE ALA PRO LEU LEU ALA ASN THR ILE ARG ALA VAL
SEQRES 25 A 326 PHE GLU ASN GLY SER VAL THR GLY LEU PHE ASP GLY SER
SEQRES 26 A 326 ALA
SEQRES 1 C 326 MET ALA THR ASP TRP THR ASP ASN ARG LYS ASN LEU MET
SEQRES 2 C 326 LEU PHE ALA GLY ARG ALA HIS PRO GLU LEU ALA ASP GLN
SEQRES 3 C 326 VAL ALA LYS GLU LEU ASP VAL ALA VAL THR ALA GLN THR
SEQRES 4 C 326 ALA ARG ASP PHE ALA ASN GLY GLU ILE PHE VAL ARG PHE
SEQRES 5 C 326 ASP GLU SER VAL ARG GLY CYS ASP ALA PHE VAL LEU GLN
SEQRES 6 C 326 SER HIS PRO ALA PRO LEU ASN GLN TRP LEU MET GLU GLN
SEQRES 7 C 326 LEU ILE MET ILE ASP ALA LEU LYS ARG GLY SER ALA LYS
SEQRES 8 C 326 ARG ILE THR ALA ILE LEU PRO PHE TYR PRO TYR ALA ARG
SEQRES 9 C 326 GLN ASP LYS LYS HIS ARG GLY ARG GLU PRO ILE SER ALA
SEQRES 10 C 326 ARG LEU VAL ALA ASP LEU LEU LYS THR ALA GLY ALA ASP
SEQRES 11 C 326 ARG ILE VAL SER VAL ASP LEU HIS THR ASP GLN ILE GLN
SEQRES 12 C 326 GLY PHE PHE ASP GLY PRO VAL ASP HIS MET ARG ALA GLN
SEQRES 13 C 326 LYS LEU LEU THR GLY TYR ILE GLY GLU HIS TYR ALA ASP
SEQRES 14 C 326 GLU ASP MET VAL VAL VAL SER PRO ASP SER GLY ARG VAL
SEQRES 15 C 326 ARG VAL ALA GLU LYS TRP ALA ASP SER LEU GLY GLY VAL
SEQRES 16 C 326 PRO LEU ALA PHE ILE HIS LYS THR ARG ASP PRO LEU VAL
SEQRES 17 C 326 PRO ASN GLN VAL LYS SER ASN ARG VAL VAL GLY ASP VAL
SEQRES 18 C 326 LYS GLY LYS THR CYS ILE LEU THR ASP ASP MET ILE ASP
SEQRES 19 C 326 THR GLY GLY THR ILE ALA GLY ALA VAL ASN LEU LEU ARG
SEQRES 20 C 326 GLU ASP GLY ALA LYS ASP VAL ILE ILE ALA ALA THR HIS
SEQRES 21 C 326 GLY VAL LEU SER ASP PRO ALA PRO GLN ARG LEU ALA GLU
SEQRES 22 C 326 CYS GLY ALA ARG GLU VAL ILE VAL THR ASN THR LEU PRO
SEQRES 23 C 326 ILE THR GLU ASP LYS ARG PHE PRO GLN LEU THR VAL LEU
SEQRES 24 C 326 SER ILE ALA PRO LEU LEU ALA ASN THR ILE ARG ALA VAL
SEQRES 25 C 326 PHE GLU ASN GLY SER VAL THR GLY LEU PHE ASP GLY SER
SEQRES 26 C 326 ALA
SEQRES 1 B 326 MET ALA THR ASP TRP THR ASP ASN ARG LYS ASN LEU MET
SEQRES 2 B 326 LEU PHE ALA GLY ARG ALA HIS PRO GLU LEU ALA ASP GLN
SEQRES 3 B 326 VAL ALA LYS GLU LEU ASP VAL ALA VAL THR ALA GLN THR
SEQRES 4 B 326 ALA ARG ASP PHE ALA ASN GLY GLU ILE PHE VAL ARG PHE
SEQRES 5 B 326 ASP GLU SER VAL ARG GLY CYS ASP ALA PHE VAL LEU GLN
SEQRES 6 B 326 SER HIS PRO ALA PRO LEU ASN GLN TRP LEU MET GLU GLN
SEQRES 7 B 326 LEU ILE MET ILE ASP ALA LEU LYS ARG GLY SER ALA LYS
SEQRES 8 B 326 ARG ILE THR ALA ILE LEU PRO PHE TYR PRO TYR ALA ARG
SEQRES 9 B 326 GLN ASP LYS LYS HIS ARG GLY ARG GLU PRO ILE SER ALA
SEQRES 10 B 326 ARG LEU VAL ALA ASP LEU LEU LYS THR ALA GLY ALA ASP
SEQRES 11 B 326 ARG ILE VAL SER VAL ASP LEU HIS THR ASP GLN ILE GLN
SEQRES 12 B 326 GLY PHE PHE ASP GLY PRO VAL ASP HIS MET ARG ALA GLN
SEQRES 13 B 326 LYS LEU LEU THR GLY TYR ILE GLY GLU HIS TYR ALA ASP
SEQRES 14 B 326 GLU ASP MET VAL VAL VAL SER PRO ASP SER GLY ARG VAL
SEQRES 15 B 326 ARG VAL ALA GLU LYS TRP ALA ASP SER LEU GLY GLY VAL
SEQRES 16 B 326 PRO LEU ALA PHE ILE HIS LYS THR ARG ASP PRO LEU VAL
SEQRES 17 B 326 PRO ASN GLN VAL LYS SER ASN ARG VAL VAL GLY ASP VAL
SEQRES 18 B 326 LYS GLY LYS THR CYS ILE LEU THR ASP ASP MET ILE ASP
SEQRES 19 B 326 THR GLY GLY THR ILE ALA GLY ALA VAL ASN LEU LEU ARG
SEQRES 20 B 326 GLU ASP GLY ALA LYS ASP VAL ILE ILE ALA ALA THR HIS
SEQRES 21 B 326 GLY VAL LEU SER ASP PRO ALA PRO GLN ARG LEU ALA GLU
SEQRES 22 B 326 CYS GLY ALA ARG GLU VAL ILE VAL THR ASN THR LEU PRO
SEQRES 23 B 326 ILE THR GLU ASP LYS ARG PHE PRO GLN LEU THR VAL LEU
SEQRES 24 B 326 SER ILE ALA PRO LEU LEU ALA ASN THR ILE ARG ALA VAL
SEQRES 25 B 326 PHE GLU ASN GLY SER VAL THR GLY LEU PHE ASP GLY SER
SEQRES 26 B 326 ALA
HET ACT A 401 4
HET ACT C 401 4
HET ACT B 401 4
HETNAM ACT ACETATE ION
FORMUL 4 ACT 3(C2 H3 O2 1-)
FORMUL 7 HOH *68(H2 O)
HELIX 1 AA1 HIS A 20 ASP A 32 1 13
HELIX 2 AA2 PRO A 70 GLY A 88 1 19
HELIX 3 AA3 ILE A 115 GLY A 128 1 14
HELIX 4 AA4 THR A 139 PHE A 146 5 8
HELIX 5 AA5 ALA A 155 ALA A 168 1 14
HELIX 6 AA6 ASP A 178 GLY A 180 5 3
HELIX 7 AA7 ARG A 181 LEU A 192 1 12
HELIX 8 AA8 GLY A 236 ASP A 249 1 14
HELIX 9 AA9 PRO A 266 CYS A 274 1 9
HELIX 10 AB1 THR A 288 ARG A 292 5 5
HELIX 11 AB2 ILE A 301 ASN A 315 1 15
HELIX 12 AB3 HIS C 20 ASP C 32 1 13
HELIX 13 AB4 PRO C 70 GLY C 88 1 19
HELIX 14 AB5 ILE C 115 GLY C 128 1 14
HELIX 15 AB6 THR C 139 PHE C 146 5 8
HELIX 16 AB7 ALA C 155 ALA C 168 1 14
HELIX 17 AB8 ASP C 178 GLY C 180 5 3
HELIX 18 AB9 ARG C 181 LEU C 192 1 12
HELIX 19 AC1 GLY C 236 ASP C 249 1 14
HELIX 20 AC2 PRO C 266 CYS C 274 1 9
HELIX 21 AC3 THR C 288 ARG C 292 5 5
HELIX 22 AC4 ILE C 301 ASN C 315 1 15
HELIX 23 AC5 HIS B 20 ASP B 32 1 13
HELIX 24 AC6 PRO B 70 GLY B 88 1 19
HELIX 25 AC7 ILE B 115 GLY B 128 1 14
HELIX 26 AC8 THR B 139 PHE B 146 5 8
HELIX 27 AC9 ALA B 155 ALA B 168 1 14
HELIX 28 AD1 ASP B 178 GLY B 180 5 3
HELIX 29 AD2 ARG B 181 LEU B 192 1 12
HELIX 30 AD3 GLY B 236 ASP B 249 1 14
HELIX 31 AD4 PRO B 266 CYS B 274 1 9
HELIX 32 AD5 THR B 288 ARG B 292 5 5
HELIX 33 AD6 ILE B 301 GLU B 314 1 14
SHEET 1 AA1 5 LEU A 12 ALA A 16 0
SHEET 2 AA1 5 ASP A 60 LEU A 64 1 O PHE A 62 N PHE A 15
SHEET 3 AA1 5 ARG A 92 LEU A 97 1 O ARG A 92 N ALA A 61
SHEET 4 AA1 5 ARG A 131 VAL A 135 1 O VAL A 133 N LEU A 97
SHEET 5 AA1 5 VAL A 150 MET A 153 1 O MET A 153 N SER A 134
SHEET 1 AA2 2 GLN A 38 ASP A 42 0
SHEET 2 AA2 2 ILE A 48 PHE A 52 -1 O PHE A 49 N ARG A 41
SHEET 1 AA3 7 ASN A 215 VAL A 218 0
SHEET 2 AA3 7 LEU A 197 LYS A 202 -1 N HIS A 201 O ARG A 216
SHEET 3 AA3 7 MET A 172 SER A 176 1 N SER A 176 O ALA A 198
SHEET 4 AA3 7 THR A 225 ILE A 233 1 O ILE A 227 N VAL A 175
SHEET 5 AA3 7 ASP A 253 GLY A 261 1 O ILE A 255 N CYS A 226
SHEET 6 AA3 7 GLU A 278 THR A 282 1 O ILE A 280 N ILE A 256
SHEET 7 AA3 7 LEU A 296 LEU A 299 1 O THR A 297 N VAL A 279
SHEET 1 AA4 5 LEU C 12 ALA C 16 0
SHEET 2 AA4 5 ASP C 60 LEU C 64 1 O PHE C 62 N PHE C 15
SHEET 3 AA4 5 ARG C 92 LEU C 97 1 O ARG C 92 N ALA C 61
SHEET 4 AA4 5 ARG C 131 VAL C 135 1 O VAL C 133 N LEU C 97
SHEET 5 AA4 5 VAL C 150 MET C 153 1 O MET C 153 N SER C 134
SHEET 1 AA5 2 GLN C 38 ASP C 42 0
SHEET 2 AA5 2 ILE C 48 PHE C 52 -1 O PHE C 49 N ARG C 41
SHEET 1 AA6 7 ASN C 215 VAL C 218 0
SHEET 2 AA6 7 LEU C 197 LYS C 202 -1 N HIS C 201 O ARG C 216
SHEET 3 AA6 7 MET C 172 SER C 176 1 N SER C 176 O ALA C 198
SHEET 4 AA6 7 THR C 225 ILE C 233 1 O ILE C 227 N VAL C 175
SHEET 5 AA6 7 ASP C 253 GLY C 261 1 O ILE C 255 N CYS C 226
SHEET 6 AA6 7 GLU C 278 THR C 282 1 O ILE C 280 N ILE C 256
SHEET 7 AA6 7 LEU C 296 LEU C 299 1 O THR C 297 N VAL C 279
SHEET 1 AA7 5 LEU B 12 ALA B 16 0
SHEET 2 AA7 5 ASP B 60 LEU B 64 1 O PHE B 62 N PHE B 15
SHEET 3 AA7 5 ARG B 92 LEU B 97 1 O ARG B 92 N ALA B 61
SHEET 4 AA7 5 ARG B 131 VAL B 135 1 O VAL B 133 N LEU B 97
SHEET 5 AA7 5 VAL B 150 MET B 153 1 O MET B 153 N SER B 134
SHEET 1 AA8 2 GLN B 38 ASP B 42 0
SHEET 2 AA8 2 ILE B 48 PHE B 52 -1 O PHE B 49 N ARG B 41
SHEET 1 AA9 7 ASN B 215 VAL B 218 0
SHEET 2 AA9 7 LEU B 197 LYS B 202 -1 N HIS B 201 O ARG B 216
SHEET 3 AA9 7 MET B 172 SER B 176 1 N SER B 176 O ALA B 198
SHEET 4 AA9 7 THR B 225 ILE B 233 1 O ILE B 227 N VAL B 175
SHEET 5 AA9 7 ASP B 253 GLY B 261 1 O ILE B 255 N CYS B 226
SHEET 6 AA9 7 GLU B 278 THR B 282 1 O ILE B 280 N ILE B 256
SHEET 7 AA9 7 LEU B 296 LEU B 299 1 O LEU B 299 N VAL B 281
CISPEP 1 ALA A 69 PRO A 70 0 -8.19
CISPEP 2 ALA C 69 PRO C 70 0 -5.95
CISPEP 3 GLY C 111 ARG C 112 0 -29.38
CISPEP 4 ALA B 69 PRO B 70 0 -7.92
SITE 1 AC1 5 ASP A 234 THR A 235 GLY A 236 GLY A 237
SITE 2 AC1 5 THR A 238
SITE 1 AC2 5 GLN B 269 ASP C 234 THR C 235 GLY C 236
SITE 2 AC2 5 THR C 238
SITE 1 AC3 3 ASP B 234 THR B 235 THR B 238
SITE 1 AC4 13 HIS B 138 SER B 176 ASP B 178 SER B 179
SITE 2 AC4 13 GLY B 180 VAL B 182 ARG B 183 VAL B 184
SITE 3 AC4 13 ALA B 185 ASP B 230 MET B 232 THR B 259
SITE 4 AC4 13 HIS B 260
CRYST1 85.292 85.292 249.791 90.00 90.00 90.00 P 41 21 2 24
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 0.011724 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011724 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004003 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
