HEADER ISOMERASE 29-DEC-09 3L7O
TITLE CRYSTAL STRUCTURE OF RIBOSE-5-PHOSPHATE ISOMERASE A FROM STREPTOCOCCUS
TITLE 2 MUTANS UA159
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSE-5-PHOSPHATE ISOMERASE A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHORIBOISOMERASE A, PRI;
COMPND 5 EC: 5.3.1.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS MUTANS;
SOURCE 3 ORGANISM_TAXID: 210007;
SOURCE 4 STRAIN: UA159;
SOURCE 5 GENE: RPIA, SMU_1234;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS RIBOSE-5-PHOSPHATE ISOMERASE A, RPIA, STREPTOCOCCUS MUTANS, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.X.FAN,K.T.WANG,X.D.SU
REVDAT 4 01-NOV-23 3L7O 1 REMARK
REVDAT 3 25-JUL-18 3L7O 1 REMARK
REVDAT 2 26-JAN-11 3L7O 1 CRYST1
REVDAT 1 05-JAN-11 3L7O 0
JRNL AUTH X.X.FAN,K.T.WANG,X.D.SU
JRNL TITL CRYSTAL STRUCTURE OF RIBOSE-5-PHOSPHATE ISOMERASE A FROM
JRNL TITL 2 STREPTOCOCCUS MUTANS UA159
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 95877
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5033
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6436
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE SET COUNT : 312
REMARK 3 BIN FREE R VALUE : 0.3680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3412
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 611
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : -0.01000
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): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.733
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3463 ; 0.038 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4677 ; 2.536 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 442 ; 6.384 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 159 ;36.541 ;24.717
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 600 ;13.774 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;19.463 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 532 ; 0.223 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2610 ; 0.016 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2181 ; 1.636 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3506 ; 2.503 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1282 ; 4.039 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1171 ; 6.258 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 225
REMARK 3 ORIGIN FOR THE GROUP (A): 40.6686 5.3333 3.6938
REMARK 3 T TENSOR
REMARK 3 T11: 0.0130 T22: 0.0240
REMARK 3 T33: 0.0418 T12: 0.0001
REMARK 3 T13: 0.0070 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0853 L22: 0.2677
REMARK 3 L33: 0.5092 L12: -0.0226
REMARK 3 L13: -0.0077 L23: 0.2044
REMARK 3 S TENSOR
REMARK 3 S11: -0.0059 S12: -0.0050 S13: -0.0093
REMARK 3 S21: -0.0067 S22: 0.0004 S23: -0.0137
REMARK 3 S31: 0.0239 S32: 0.0035 S33: 0.0055
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 225
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4078 23.0210 22.5033
REMARK 3 T TENSOR
REMARK 3 T11: 0.0176 T22: 0.0222
REMARK 3 T33: 0.0326 T12: 0.0138
REMARK 3 T13: 0.0036 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.0621 L22: 0.6999
REMARK 3 L33: 0.3158 L12: 0.0163
REMARK 3 L13: 0.0093 L23: 0.0999
REMARK 3 S TENSOR
REMARK 3 S11: -0.0101 S12: 0.0118 S13: -0.0038
REMARK 3 S21: 0.0623 S22: 0.0326 S23: 0.0176
REMARK 3 S31: -0.0191 S32: -0.0157 S33: -0.0225
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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. THE FILE CONTAINS FRIEDEL PAIRS.
REMARK 4
REMARK 4 3L7O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000056936.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 MICROMAX-002
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106808
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
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) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
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: NULL
REMARK 200 STARTING MODEL: 1UJ4
REMARK 200
REMARK 200 REMARK: THE FILE CONTAINS FRIEDEL PAIRS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG4000, 0.1M NAAC, PH 4.7, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 24.48450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.13350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.54450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.13350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.48450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.54450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
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. (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 GLY A 214
REMARK 465 LYS A 215
REMARK 465 ASP A 216
REMARK 465 MET B 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 76 OG
REMARK 470 LYS B 215 CG CD CE NZ
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 O HOH A 264 O HOH A 665 1.67
REMARK 500 O HOH A 321 O HOH A 673 1.68
REMARK 500 O HOH A 565 O HOH A 665 1.69
REMARK 500 O HOH A 293 O HOH A 596 1.70
REMARK 500 O HOH A 339 O HOH A 636 1.77
REMARK 500 O HOH A 658 O HOH B 294 1.77
REMARK 500 O HOH A 369 O HOH A 596 1.82
REMARK 500 O HOH B 649 O HOH B 689 1.91
REMARK 500 CD ARG B 164 O HOH B 686 1.91
REMARK 500 O HOH A 418 O HOH A 624 1.93
REMARK 500 CD ARG B 56 O HOH B 603 1.94
REMARK 500 CG ARG B 164 O HOH B 686 1.95
REMARK 500 O HOH A 259 O HOH A 665 1.95
REMARK 500 O HOH A 658 O HOH B 573 1.97
REMARK 500 CG GLU B 142 O HOH B 662 1.98
REMARK 500 CA VAL A 41 O HOH A 664 1.99
REMARK 500 OE2 GLU B 36 O HOH B 683 2.01
REMARK 500 O HOH A 375 O HOH A 595 2.02
REMARK 500 CD GLU B 36 O HOH B 683 2.05
REMARK 500 OD2 ASP A 72 O HOH A 570 2.06
REMARK 500 O HOH A 546 O HOH A 636 2.11
REMARK 500 O ASP B 75 O HOH B 679 2.12
REMARK 500 O HOH B 523 O HOH B 693 2.12
REMARK 500 CB LEU A 46 O HOH A 664 2.15
REMARK 500 O HOH A 324 O HOH A 374 2.16
REMARK 500 CG2 VAL B 137 O HOH B 687 2.18
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 CA LYS A 225 O HOH B 341 3645 1.94
REMARK 500 O HOH A 255 O HOH B 556 4555 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 44 CD GLU A 44 OE1 0.069
REMARK 500 PHE A 130 CE1 PHE A 130 CZ 0.137
REMARK 500 VAL A 137 CB VAL A 137 CG2 0.131
REMARK 500 ARG A 143 CB ARG A 143 CG -0.176
REMARK 500 PHE A 157 CG PHE A 157 CD2 0.092
REMARK 500 PHE A 165 CD1 PHE A 165 CE1 0.137
REMARK 500 GLU B 2 N GLU B 2 CA 0.138
REMARK 500 GLU B 3 CG GLU B 3 CD 0.110
REMARK 500 ARG B 11 CG ARG B 11 CD 0.156
REMARK 500 ALA B 13 CA ALA B 13 CB -0.138
REMARK 500 SER B 54 CB SER B 54 OG 0.079
REMARK 500 GLU B 73 CG GLU B 73 CD 0.115
REMARK 500 ASP B 75 CB ASP B 75 CG 0.135
REMARK 500 PHE B 91 CE1 PHE B 91 CZ 0.157
REMARK 500 GLU B 120 CG GLU B 120 CD 0.116
REMARK 500 TYR B 139 CE2 TYR B 139 CD2 0.099
REMARK 500 ARG B 143 CB ARG B 143 CG 0.192
REMARK 500 TYR B 153 CD1 TYR B 153 CE1 0.152
REMARK 500 TYR B 160 CE1 TYR B 160 CZ 0.083
REMARK 500 GLN B 194 CG GLN B 194 CD 0.163
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 B 11 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP B 72 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP B 72 CB - CG - OD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP B 75 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU B 101 CB - CG - CD2 ANGL. DEV. = 11.0 DEGREES
REMARK 500 LEU B 102 CB - CG - CD2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 ARG B 131 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG B 131 NE - CZ - NH2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG B 143 CG - CD - NE ANGL. DEV. = 14.8 DEGREES
REMARK 500 ARG B 143 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG B 146 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 164 NE - CZ - NH1 ANGL. DEV. = 3.1 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 LYS A 170 41.09 76.56
REMARK 500 ASN A 224 -84.90 -57.69
REMARK 500 LYS B 154 60.73 61.30
REMARK 500 LYS B 170 36.50 73.84
REMARK 500 ASN B 224 72.10 41.23
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3L7O A 1 225 UNP Q8DTT9 RPIA_STRMU 1 225
DBREF 3L7O B 1 225 UNP Q8DTT9 RPIA_STRMU 1 225
SEQRES 1 A 225 MET GLU GLU LEU LYS LYS ILE ALA GLY VAL ARG ALA ALA
SEQRES 2 A 225 GLN TYR VAL GLU ASP GLY MET ILE VAL GLY LEU GLY THR
SEQRES 3 A 225 GLY SER THR ALA TYR TYR PHE VAL GLU GLU VAL GLY ARG
SEQRES 4 A 225 ARG VAL GLN GLU GLU GLY LEU GLN VAL ILE GLY VAL THR
SEQRES 5 A 225 THR SER SER ARG THR THR ALA GLN ALA GLN ALA LEU GLY
SEQRES 6 A 225 ILE PRO LEU LYS SER ILE ASP GLU VAL ASP SER VAL ASP
SEQRES 7 A 225 VAL THR VAL ASP GLY ALA ASP GLU VAL ASP PRO ASN PHE
SEQRES 8 A 225 ASN GLY ILE LYS GLY GLY GLY GLY ALA LEU LEU MET GLU
SEQRES 9 A 225 LYS ILE VAL GLY THR LEU THR LYS ASP TYR ILE TRP VAL
SEQRES 10 A 225 VAL ASP GLU SER LYS MET VAL ASP THR LEU GLY ALA PHE
SEQRES 11 A 225 ARG LEU PRO VAL GLU VAL VAL GLN TYR GLY ALA GLU ARG
SEQRES 12 A 225 LEU PHE ARG GLU PHE GLU LYS LYS GLY TYR LYS PRO SER
SEQRES 13 A 225 PHE ARG GLU TYR ASP GLY VAL ARG PHE VAL THR ASP MET
SEQRES 14 A 225 LYS ASN PHE ILE ILE ASP LEU ASP LEU GLY SER ILE PRO
SEQRES 15 A 225 ASP PRO ILE ALA PHE GLY ASN MET LEU ASP HIS GLN VAL
SEQRES 16 A 225 GLY VAL VAL GLU HIS GLY LEU PHE ASN GLY MET VAL ASN
SEQRES 17 A 225 ARG VAL ILE VAL ALA GLY LYS ASP GLY VAL ARG ILE LEU
SEQRES 18 A 225 GLU ALA ASN LYS
SEQRES 1 B 225 MET GLU GLU LEU LYS LYS ILE ALA GLY VAL ARG ALA ALA
SEQRES 2 B 225 GLN TYR VAL GLU ASP GLY MET ILE VAL GLY LEU GLY THR
SEQRES 3 B 225 GLY SER THR ALA TYR TYR PHE VAL GLU GLU VAL GLY ARG
SEQRES 4 B 225 ARG VAL GLN GLU GLU GLY LEU GLN VAL ILE GLY VAL THR
SEQRES 5 B 225 THR SER SER ARG THR THR ALA GLN ALA GLN ALA LEU GLY
SEQRES 6 B 225 ILE PRO LEU LYS SER ILE ASP GLU VAL ASP SER VAL ASP
SEQRES 7 B 225 VAL THR VAL ASP GLY ALA ASP GLU VAL ASP PRO ASN PHE
SEQRES 8 B 225 ASN GLY ILE LYS GLY GLY GLY GLY ALA LEU LEU MET GLU
SEQRES 9 B 225 LYS ILE VAL GLY THR LEU THR LYS ASP TYR ILE TRP VAL
SEQRES 10 B 225 VAL ASP GLU SER LYS MET VAL ASP THR LEU GLY ALA PHE
SEQRES 11 B 225 ARG LEU PRO VAL GLU VAL VAL GLN TYR GLY ALA GLU ARG
SEQRES 12 B 225 LEU PHE ARG GLU PHE GLU LYS LYS GLY TYR LYS PRO SER
SEQRES 13 B 225 PHE ARG GLU TYR ASP GLY VAL ARG PHE VAL THR ASP MET
SEQRES 14 B 225 LYS ASN PHE ILE ILE ASP LEU ASP LEU GLY SER ILE PRO
SEQRES 15 B 225 ASP PRO ILE ALA PHE GLY ASN MET LEU ASP HIS GLN VAL
SEQRES 16 B 225 GLY VAL VAL GLU HIS GLY LEU PHE ASN GLY MET VAL ASN
SEQRES 17 B 225 ARG VAL ILE VAL ALA GLY LYS ASP GLY VAL ARG ILE LEU
SEQRES 18 B 225 GLU ALA ASN LYS
FORMUL 3 HOH *611(H2 O)
HELIX 1 1 GLU A 2 GLN A 14 1 13
HELIX 2 2 THR A 29 GLY A 45 1 17
HELIX 3 3 SER A 54 GLY A 65 1 12
HELIX 4 4 SER A 70 VAL A 74 5 5
HELIX 5 5 ALA A 100 LEU A 110 1 11
HELIX 6 6 SER A 121 MET A 123 5 3
HELIX 7 7 GLY A 140 LYS A 151 1 12
HELIX 8 8 ASP A 183 HIS A 193 1 11
HELIX 9 9 GLU B 2 ALA B 13 1 12
HELIX 10 10 GLN B 14 VAL B 16 5 3
HELIX 11 11 THR B 29 GLY B 45 1 17
HELIX 12 12 SER B 54 GLY B 65 1 12
HELIX 13 13 SER B 70 VAL B 74 5 5
HELIX 14 14 ALA B 100 LEU B 110 1 11
HELIX 15 15 SER B 121 MET B 123 5 3
HELIX 16 16 GLY B 140 LYS B 151 1 12
HELIX 17 17 ASP B 183 ASP B 192 1 10
SHEET 1 A 6 ILE A 49 THR A 52 0
SHEET 2 A 6 ILE A 21 LEU A 24 1 N VAL A 22 O ILE A 49
SHEET 3 A 6 VAL A 77 ASP A 82 1 O VAL A 79 N GLY A 23
SHEET 4 A 6 THR A 111 ASP A 119 1 O ILE A 115 N THR A 80
SHEET 5 A 6 ARG A 209 ALA A 213 1 O ILE A 211 N TRP A 116
SHEET 6 A 6 ARG A 219 GLU A 222 -1 O ARG A 219 N VAL A 212
SHEET 1 B 3 GLU A 86 VAL A 87 0
SHEET 2 B 3 GLY A 93 ILE A 94 -1 O ILE A 94 N GLU A 86
SHEET 3 B 3 LEU A 202 PHE A 203 -1 O PHE A 203 N GLY A 93
SHEET 1 C 4 PRO A 155 PHE A 157 0
SHEET 2 C 4 PHE A 172 LEU A 176 -1 O ASP A 175 N SER A 156
SHEET 3 C 4 LEU A 132 VAL A 136 -1 N VAL A 134 O ILE A 174
SHEET 4 C 4 VAL A 197 HIS A 200 -1 O VAL A 198 N GLU A 135
SHEET 1 D 2 GLU A 159 TYR A 160 0
SHEET 2 D 2 VAL A 163 ARG A 164 -1 O VAL A 163 N TYR A 160
SHEET 1 E 6 VAL B 48 THR B 52 0
SHEET 2 E 6 MET B 20 LEU B 24 1 N VAL B 22 O ILE B 49
SHEET 3 E 6 VAL B 77 ASP B 82 1 O VAL B 79 N GLY B 23
SHEET 4 E 6 THR B 111 ASP B 119 1 O ILE B 115 N THR B 80
SHEET 5 E 6 ARG B 209 GLY B 214 1 O ILE B 211 N TRP B 116
SHEET 6 E 6 GLY B 217 GLU B 222 -1 O LEU B 221 N VAL B 210
SHEET 1 F 3 GLU B 86 VAL B 87 0
SHEET 2 F 3 GLY B 93 ILE B 94 -1 O ILE B 94 N GLU B 86
SHEET 3 F 3 LEU B 202 PHE B 203 -1 O PHE B 203 N GLY B 93
SHEET 1 G 4 PRO B 155 PHE B 157 0
SHEET 2 G 4 PHE B 172 LEU B 176 -1 O ASP B 175 N SER B 156
SHEET 3 G 4 LEU B 132 VAL B 136 -1 N VAL B 134 O ILE B 174
SHEET 4 G 4 VAL B 197 HIS B 200 -1 O VAL B 198 N GLU B 135
SHEET 1 H 2 GLU B 159 TYR B 160 0
SHEET 2 H 2 VAL B 163 ARG B 164 -1 O VAL B 163 N TYR B 160
CISPEP 1 GLY A 217 VAL A 218 0 7.59
CRYST1 48.969 101.089 98.267 90.00 90.00 90.00 P 21 21 21 8
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 0.020421 0.000000 0.000016 0.00000
SCALE2 0.000000 0.009892 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010176 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
