HEADER HYDROLASE 18-JUN-13 4L8Y
TITLE CRYSTAL STRUCTURE OF GAMMA-GLUTAMYL HYDROLASE (C108A) FROM ZEBRAFISH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAMMA-GLUTAMYL HYDROLASE;
COMPND 3 CHAIN: C, D, A, B;
COMPND 4 EC: 3.4.19.9;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DANIO RERIO;
SOURCE 3 ORGANISM_COMMON: ZEBRA FISH;
SOURCE 4 ORGANISM_TAXID: 7955;
SOURCE 5 GENE: GGH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SANDWICHED-LIKE DOMAIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.CHUANKHAYAN,T.-T.KAO,C.-J.CHEN,T.-F.FU
REVDAT 2 08-NOV-23 4L8Y 1 SEQADV
REVDAT 1 14-MAY-14 4L8Y 0
JRNL AUTH P.CHUANKHAYAN,T.-T.KAO,C.-C.LIN,H.-H.GUAN,A.NAKAGAWA,
JRNL AUTH 2 T.-F.FU,C.-J.CHEN
JRNL TITL STRUCTURAL INSIGHTS INTO THE HYDROLYSIS AND POLYMORPHISM OF
JRNL TITL 2 METHOTREXATE POLYGLUTAMATE BY ZEBRAFISH GAMMA-GLUTAMYL
JRNL TITL 3 HYDROLASE
JRNL REF J.MED.CHEM. V. 56 7625 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 24028568
JRNL DOI 10.1021/JM401013E
REMARK 2
REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 82658
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4361
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) : 1.97
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5847
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 306
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9232
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 864
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.72000
REMARK 3 B22 (A**2) : 0.45000
REMARK 3 B33 (A**2) : -1.59000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.52000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.195
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.181
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.134
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.696
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.887
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9492 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12887 ; 2.081 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1144 ; 6.917 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 450 ;39.357 ;24.222
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1543 ;18.252 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;23.205 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1380 ; 0.179 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7325 ; 0.011 ; 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): 5736 ; 1.221 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9273 ; 2.081 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3756 ; 3.253 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3614 ; 4.962 ; 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 : 1.40
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 4L8Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000080330.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87110
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
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) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: X-PLOR
REMARK 200 STARTING MODEL: 1L9X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V) PEG 8000, 0.2M MAGNESIUM
REMARK 280 CHLORIDE, 0.1M TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 103.25250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 C -20
REMARK 465 ILE C -19
REMARK 465 HIS C -18
REMARK 465 ILE C -17
REMARK 465 PHE C -16
REMARK 465 LEU C -15
REMARK 465 LEU C -14
REMARK 465 CYS C -13
REMARK 465 LEU C -12
REMARK 465 PHE C -11
REMARK 465 THR C -10
REMARK 465 VAL C -9
REMARK 465 ALA C -8
REMARK 465 ASN C -7
REMARK 465 ALA C -6
REMARK 465 VAL C -5
REMARK 465 SER C -4
REMARK 465 ILE C -3
REMARK 465 TYR C -2
REMARK 465 ASN C -1
REMARK 465 PHE C 0
REMARK 465 GLY C 1
REMARK 465 PRO C 2
REMARK 465 LEU C 3
REMARK 465 ILE C 4
REMARK 465 MET D -20
REMARK 465 ILE D -19
REMARK 465 HIS D -18
REMARK 465 ILE D -17
REMARK 465 PHE D -16
REMARK 465 LEU D -15
REMARK 465 LEU D -14
REMARK 465 CYS D -13
REMARK 465 LEU D -12
REMARK 465 PHE D -11
REMARK 465 THR D -10
REMARK 465 VAL D -9
REMARK 465 ALA D -8
REMARK 465 ASN D -7
REMARK 465 ALA D -6
REMARK 465 VAL D -5
REMARK 465 SER D -4
REMARK 465 ILE D -3
REMARK 465 TYR D -2
REMARK 465 ASN D -1
REMARK 465 PHE D 0
REMARK 465 GLY D 1
REMARK 465 PRO D 2
REMARK 465 LEU D 3
REMARK 465 ILE D 4
REMARK 465 MET A -20
REMARK 465 ILE A -19
REMARK 465 HIS A -18
REMARK 465 ILE A -17
REMARK 465 PHE A -16
REMARK 465 LEU A -15
REMARK 465 LEU A -14
REMARK 465 CYS A -13
REMARK 465 LEU A -12
REMARK 465 PHE A -11
REMARK 465 THR A -10
REMARK 465 VAL A -9
REMARK 465 ALA A -8
REMARK 465 ASN A -7
REMARK 465 ALA A -6
REMARK 465 VAL A -5
REMARK 465 SER A -4
REMARK 465 ILE A -3
REMARK 465 TYR A -2
REMARK 465 ASN A -1
REMARK 465 PHE A 0
REMARK 465 GLY A 1
REMARK 465 PRO A 2
REMARK 465 LEU A 3
REMARK 465 ILE A 4
REMARK 465 MET B -20
REMARK 465 ILE B -19
REMARK 465 HIS B -18
REMARK 465 ILE B -17
REMARK 465 PHE B -16
REMARK 465 LEU B -15
REMARK 465 LEU B -14
REMARK 465 CYS B -13
REMARK 465 LEU B -12
REMARK 465 PHE B -11
REMARK 465 THR B -10
REMARK 465 VAL B -9
REMARK 465 ALA B -8
REMARK 465 ASN B -7
REMARK 465 ALA B -6
REMARK 465 VAL B -5
REMARK 465 SER B -4
REMARK 465 ILE B -3
REMARK 465 TYR B -2
REMARK 465 ASN B -1
REMARK 465 PHE B 0
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 LEU B 3
REMARK 465 ILE B 4
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 CD ARG D 90 O HOH D 312 1.91
REMARK 500 N ASN A 51 O HOH A 471 1.93
REMARK 500 OH TYR D 230 ND2 ASN A 128 1.94
REMARK 500 OE2 GLU A 54 O HOH A 467 1.99
REMARK 500 OE1 GLU C 94 O HOH C 365 2.08
REMARK 500 NZ LYS C 83 O HOH C 508 2.14
REMARK 500 NH2 ARG D 90 O HOH D 545 2.14
REMARK 500 OXT ASN D 291 O HOH D 532 2.17
REMARK 500 OG SER A 28 O HOH A 475 2.18
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 C 150 CD GLU C 150 OE1 0.105
REMARK 500 TRP C 226 CZ3 TRP C 226 CH2 0.108
REMARK 500 VAL D 74 CB VAL D 74 CG1 -0.145
REMARK 500 TYR D 208 CE2 TYR D 208 CD2 0.096
REMARK 500 GLU A 150 CD GLU A 150 OE1 0.073
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 C 44 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG C 44 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASN C 51 C - N - CA ANGL. DEV. = -20.1 DEGREES
REMARK 500 ILE C 173 CB - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 ARG D 44 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ASN D 51 C - N - CA ANGL. DEV. = -15.7 DEGREES
REMARK 500 VAL D 67 CB - CA - C ANGL. DEV. = -11.4 DEGREES
REMARK 500 VAL D 67 CG1 - CB - CG2 ANGL. DEV. = 13.4 DEGREES
REMARK 500 ASP D 100 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ILE D 173 CB - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 VAL A 67 CG1 - CB - CG2 ANGL. DEV. = -12.1 DEGREES
REMARK 500 LEU B 116 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 ILE B 132 CB - CA - C ANGL. DEV. = -17.0 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 ASP C 25 10.69 58.70
REMARK 500 ASN C 51 47.59 -109.34
REMARK 500 ALA C 108 -103.74 56.78
REMARK 500 ASP D 21 76.12 -115.70
REMARK 500 ASP D 25 -2.89 71.99
REMARK 500 ARG D 26 52.51 -140.48
REMARK 500 ASN D 51 65.03 -116.47
REMARK 500 ALA D 108 -113.71 58.37
REMARK 500 SER D 168 59.74 -145.00
REMARK 500 TYR D 198 -42.58 -134.36
REMARK 500 GLN D 281 -75.81 -69.33
REMARK 500 ASP A 25 9.18 58.54
REMARK 500 ARG A 26 43.06 -146.85
REMARK 500 ASN A 51 60.80 -110.80
REMARK 500 ALA A 108 -111.10 50.07
REMARK 500 PRO A 135 -169.55 -77.67
REMARK 500 TYR A 198 -48.28 -136.66
REMARK 500 ASP B 25 15.03 53.48
REMARK 500 ARG B 26 60.95 -152.79
REMARK 500 ALA B 108 -105.55 62.03
REMARK 500 PRO B 163 75.48 -68.50
REMARK 500 SER B 168 59.36 -146.14
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 C 144 SER C 145 -148.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4L7Q RELATED DB: PDB
REMARK 900 WILD-TYPE PROTEIN
REMARK 900 RELATED ID: 4L8F RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH MTX
REMARK 900 RELATED ID: 4L8W RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH MTX POLYGLUTAMATE
REMARK 900 RELATED ID: 4L95 RELATED DB: PDB
REMARK 900 H218N MUTANT
DBREF 4L8Y C -20 291 UNP Q6NY42 Q6NY42_DANRE 1 312
DBREF 4L8Y D -20 291 UNP Q6NY42 Q6NY42_DANRE 1 312
DBREF 4L8Y A -20 291 UNP Q6NY42 Q6NY42_DANRE 1 312
DBREF 4L8Y B -20 291 UNP Q6NY42 Q6NY42_DANRE 1 312
SEQADV 4L8Y ALA C 108 UNP Q6NY42 CYS 129 ENGINEERED MUTATION
SEQADV 4L8Y ALA D 108 UNP Q6NY42 CYS 129 ENGINEERED MUTATION
SEQADV 4L8Y ALA A 108 UNP Q6NY42 CYS 129 ENGINEERED MUTATION
SEQADV 4L8Y ALA B 108 UNP Q6NY42 CYS 129 ENGINEERED MUTATION
SEQRES 1 C 312 MET ILE HIS ILE PHE LEU LEU CYS LEU PHE THR VAL ALA
SEQRES 2 C 312 ASN ALA VAL SER ILE TYR ASN PHE GLY PRO LEU ILE LYS
SEQRES 3 C 312 THR ASN GLU ARG PRO ILE ILE GLY VAL LEU ALA GLN ASP
SEQRES 4 C 312 VAL PHE ASP PRO LYS PRO ASP ARG ASN SER TYR ILE ALA
SEQRES 5 C 312 ALA SER TYR VAL LYS PHE LEU GLU SER ALA GLY ALA ARG
SEQRES 6 C 312 VAL VAL PRO VAL MET ILE ASN LYS SER GLU ASP GLU TYR
SEQRES 7 C 312 SER ARG LEU PHE LYS SER ILE ASN GLY VAL LEU PHE PRO
SEQRES 8 C 312 GLY GLY GLY VAL SER LEU GLU SER SER GLY TYR SER LYS
SEQRES 9 C 312 ALA ALA GLY ILE PHE TYR ARG LEU ALA LEU GLU ALA ASN
SEQRES 10 C 312 SER ASN GLY ASP TYR PHE PRO VAL TRP GLY THR ALA LEU
SEQRES 11 C 312 GLY PHE GLU LEU LEU THR LEU LEU THR SER GLY GLU LEU
SEQRES 12 C 312 LEU LEU SER HIS THR ASN THR SER GLY ILE ALA LEU PRO
SEQRES 13 C 312 LEU ASP PHE THR GLU ASP VAL LYS GLY SER ARG LEU PHE
SEQRES 14 C 312 LYS GLU PHE PRO GLU GLU LEU MET LYS SER LEU ALA THR
SEQRES 15 C 312 GLU PRO LEU THR GLU ASN SER HIS GLN TRP SER ILE THR
SEQRES 16 C 312 THR GLU ASN PHE THR ALA ASN LYS LYS LEU LYS LYS PHE
SEQRES 17 C 312 TYR ARG VAL LEU SER THR ASN THR ASP GLY TYR ASN LYS
SEQRES 18 C 312 PHE VAL SER THR MET GLU ALA TYR ASP PHE PRO ILE TYR
SEQRES 19 C 312 ALA THR GLN TRP HIS PRO GLU LYS ASN ALA PHE GLU TRP
SEQRES 20 C 312 THR ARG PRO TYR ILE PRO HIS THR PRO SER ALA ILE LYS
SEQRES 21 C 312 THR THR PHE TYR MET ALA ASN PHE PHE VAL ASN GLU ALA
SEQRES 22 C 312 ARG LYS ASN LEU HIS SER PHE ALA SER THR GLU GLU GLU
SEQRES 23 C 312 GLU LYS ALA LEU ILE TYR ASN TYR LYS PRO GLU TYR THR
SEQRES 24 C 312 GLY ILE GLN SER ALA PHE GLU GLN THR TYR PHE PHE ASN
SEQRES 1 D 312 MET ILE HIS ILE PHE LEU LEU CYS LEU PHE THR VAL ALA
SEQRES 2 D 312 ASN ALA VAL SER ILE TYR ASN PHE GLY PRO LEU ILE LYS
SEQRES 3 D 312 THR ASN GLU ARG PRO ILE ILE GLY VAL LEU ALA GLN ASP
SEQRES 4 D 312 VAL PHE ASP PRO LYS PRO ASP ARG ASN SER TYR ILE ALA
SEQRES 5 D 312 ALA SER TYR VAL LYS PHE LEU GLU SER ALA GLY ALA ARG
SEQRES 6 D 312 VAL VAL PRO VAL MET ILE ASN LYS SER GLU ASP GLU TYR
SEQRES 7 D 312 SER ARG LEU PHE LYS SER ILE ASN GLY VAL LEU PHE PRO
SEQRES 8 D 312 GLY GLY GLY VAL SER LEU GLU SER SER GLY TYR SER LYS
SEQRES 9 D 312 ALA ALA GLY ILE PHE TYR ARG LEU ALA LEU GLU ALA ASN
SEQRES 10 D 312 SER ASN GLY ASP TYR PHE PRO VAL TRP GLY THR ALA LEU
SEQRES 11 D 312 GLY PHE GLU LEU LEU THR LEU LEU THR SER GLY GLU LEU
SEQRES 12 D 312 LEU LEU SER HIS THR ASN THR SER GLY ILE ALA LEU PRO
SEQRES 13 D 312 LEU ASP PHE THR GLU ASP VAL LYS GLY SER ARG LEU PHE
SEQRES 14 D 312 LYS GLU PHE PRO GLU GLU LEU MET LYS SER LEU ALA THR
SEQRES 15 D 312 GLU PRO LEU THR GLU ASN SER HIS GLN TRP SER ILE THR
SEQRES 16 D 312 THR GLU ASN PHE THR ALA ASN LYS LYS LEU LYS LYS PHE
SEQRES 17 D 312 TYR ARG VAL LEU SER THR ASN THR ASP GLY TYR ASN LYS
SEQRES 18 D 312 PHE VAL SER THR MET GLU ALA TYR ASP PHE PRO ILE TYR
SEQRES 19 D 312 ALA THR GLN TRP HIS PRO GLU LYS ASN ALA PHE GLU TRP
SEQRES 20 D 312 THR ARG PRO TYR ILE PRO HIS THR PRO SER ALA ILE LYS
SEQRES 21 D 312 THR THR PHE TYR MET ALA ASN PHE PHE VAL ASN GLU ALA
SEQRES 22 D 312 ARG LYS ASN LEU HIS SER PHE ALA SER THR GLU GLU GLU
SEQRES 23 D 312 GLU LYS ALA LEU ILE TYR ASN TYR LYS PRO GLU TYR THR
SEQRES 24 D 312 GLY ILE GLN SER ALA PHE GLU GLN THR TYR PHE PHE ASN
SEQRES 1 A 312 MET ILE HIS ILE PHE LEU LEU CYS LEU PHE THR VAL ALA
SEQRES 2 A 312 ASN ALA VAL SER ILE TYR ASN PHE GLY PRO LEU ILE LYS
SEQRES 3 A 312 THR ASN GLU ARG PRO ILE ILE GLY VAL LEU ALA GLN ASP
SEQRES 4 A 312 VAL PHE ASP PRO LYS PRO ASP ARG ASN SER TYR ILE ALA
SEQRES 5 A 312 ALA SER TYR VAL LYS PHE LEU GLU SER ALA GLY ALA ARG
SEQRES 6 A 312 VAL VAL PRO VAL MET ILE ASN LYS SER GLU ASP GLU TYR
SEQRES 7 A 312 SER ARG LEU PHE LYS SER ILE ASN GLY VAL LEU PHE PRO
SEQRES 8 A 312 GLY GLY GLY VAL SER LEU GLU SER SER GLY TYR SER LYS
SEQRES 9 A 312 ALA ALA GLY ILE PHE TYR ARG LEU ALA LEU GLU ALA ASN
SEQRES 10 A 312 SER ASN GLY ASP TYR PHE PRO VAL TRP GLY THR ALA LEU
SEQRES 11 A 312 GLY PHE GLU LEU LEU THR LEU LEU THR SER GLY GLU LEU
SEQRES 12 A 312 LEU LEU SER HIS THR ASN THR SER GLY ILE ALA LEU PRO
SEQRES 13 A 312 LEU ASP PHE THR GLU ASP VAL LYS GLY SER ARG LEU PHE
SEQRES 14 A 312 LYS GLU PHE PRO GLU GLU LEU MET LYS SER LEU ALA THR
SEQRES 15 A 312 GLU PRO LEU THR GLU ASN SER HIS GLN TRP SER ILE THR
SEQRES 16 A 312 THR GLU ASN PHE THR ALA ASN LYS LYS LEU LYS LYS PHE
SEQRES 17 A 312 TYR ARG VAL LEU SER THR ASN THR ASP GLY TYR ASN LYS
SEQRES 18 A 312 PHE VAL SER THR MET GLU ALA TYR ASP PHE PRO ILE TYR
SEQRES 19 A 312 ALA THR GLN TRP HIS PRO GLU LYS ASN ALA PHE GLU TRP
SEQRES 20 A 312 THR ARG PRO TYR ILE PRO HIS THR PRO SER ALA ILE LYS
SEQRES 21 A 312 THR THR PHE TYR MET ALA ASN PHE PHE VAL ASN GLU ALA
SEQRES 22 A 312 ARG LYS ASN LEU HIS SER PHE ALA SER THR GLU GLU GLU
SEQRES 23 A 312 GLU LYS ALA LEU ILE TYR ASN TYR LYS PRO GLU TYR THR
SEQRES 24 A 312 GLY ILE GLN SER ALA PHE GLU GLN THR TYR PHE PHE ASN
SEQRES 1 B 312 MET ILE HIS ILE PHE LEU LEU CYS LEU PHE THR VAL ALA
SEQRES 2 B 312 ASN ALA VAL SER ILE TYR ASN PHE GLY PRO LEU ILE LYS
SEQRES 3 B 312 THR ASN GLU ARG PRO ILE ILE GLY VAL LEU ALA GLN ASP
SEQRES 4 B 312 VAL PHE ASP PRO LYS PRO ASP ARG ASN SER TYR ILE ALA
SEQRES 5 B 312 ALA SER TYR VAL LYS PHE LEU GLU SER ALA GLY ALA ARG
SEQRES 6 B 312 VAL VAL PRO VAL MET ILE ASN LYS SER GLU ASP GLU TYR
SEQRES 7 B 312 SER ARG LEU PHE LYS SER ILE ASN GLY VAL LEU PHE PRO
SEQRES 8 B 312 GLY GLY GLY VAL SER LEU GLU SER SER GLY TYR SER LYS
SEQRES 9 B 312 ALA ALA GLY ILE PHE TYR ARG LEU ALA LEU GLU ALA ASN
SEQRES 10 B 312 SER ASN GLY ASP TYR PHE PRO VAL TRP GLY THR ALA LEU
SEQRES 11 B 312 GLY PHE GLU LEU LEU THR LEU LEU THR SER GLY GLU LEU
SEQRES 12 B 312 LEU LEU SER HIS THR ASN THR SER GLY ILE ALA LEU PRO
SEQRES 13 B 312 LEU ASP PHE THR GLU ASP VAL LYS GLY SER ARG LEU PHE
SEQRES 14 B 312 LYS GLU PHE PRO GLU GLU LEU MET LYS SER LEU ALA THR
SEQRES 15 B 312 GLU PRO LEU THR GLU ASN SER HIS GLN TRP SER ILE THR
SEQRES 16 B 312 THR GLU ASN PHE THR ALA ASN LYS LYS LEU LYS LYS PHE
SEQRES 17 B 312 TYR ARG VAL LEU SER THR ASN THR ASP GLY TYR ASN LYS
SEQRES 18 B 312 PHE VAL SER THR MET GLU ALA TYR ASP PHE PRO ILE TYR
SEQRES 19 B 312 ALA THR GLN TRP HIS PRO GLU LYS ASN ALA PHE GLU TRP
SEQRES 20 B 312 THR ARG PRO TYR ILE PRO HIS THR PRO SER ALA ILE LYS
SEQRES 21 B 312 THR THR PHE TYR MET ALA ASN PHE PHE VAL ASN GLU ALA
SEQRES 22 B 312 ARG LYS ASN LEU HIS SER PHE ALA SER THR GLU GLU GLU
SEQRES 23 B 312 GLU LYS ALA LEU ILE TYR ASN TYR LYS PRO GLU TYR THR
SEQRES 24 B 312 GLY ILE GLN SER ALA PHE GLU GLN THR TYR PHE PHE ASN
FORMUL 5 HOH *864(H2 O)
HELIX 1 1 ALA C 32 SER C 40 1 9
HELIX 2 2 SER C 53 LYS C 62 1 10
HELIX 3 3 SER C 79 GLY C 99 1 21
HELIX 4 4 ALA C 108 GLY C 120 1 13
HELIX 5 5 GLU C 140 LYS C 143 5 4
HELIX 6 6 PRO C 152 GLU C 162 1 11
HELIX 7 7 THR C 174 ASN C 181 1 8
HELIX 8 8 ASN C 181 PHE C 187 1 7
HELIX 9 9 GLU C 220 GLU C 225 1 6
HELIX 10 10 THR C 234 ARG C 253 1 20
HELIX 11 11 SER C 261 LEU C 269 1 9
HELIX 12 12 ILE C 270 TYR C 273 5 4
HELIX 13 13 ALA D 32 ALA D 41 1 10
HELIX 14 14 SER D 53 ILE D 64 1 12
HELIX 15 15 SER D 79 GLY D 99 1 21
HELIX 16 16 ALA D 108 GLY D 120 1 13
HELIX 17 17 GLU D 140 LYS D 143 5 4
HELIX 18 18 PRO D 152 GLU D 162 1 11
HELIX 19 19 THR D 174 ASN D 181 1 8
HELIX 20 20 ASN D 181 PHE D 187 1 7
HELIX 21 21 GLU D 220 GLU D 225 1 6
HELIX 22 22 THR D 234 ARG D 253 1 20
HELIX 23 23 SER D 261 LEU D 269 1 9
HELIX 24 24 ILE D 270 TYR D 273 5 4
HELIX 25 25 ALA A 32 SER A 40 1 9
HELIX 26 26 SER A 53 ILE A 64 1 12
HELIX 27 27 SER A 79 GLY A 99 1 21
HELIX 28 28 ALA A 108 GLY A 120 1 13
HELIX 29 29 GLU A 140 LYS A 143 5 4
HELIX 30 30 PRO A 152 GLU A 162 1 11
HELIX 31 31 THR A 174 ASN A 181 1 8
HELIX 32 32 ASN A 181 PHE A 187 1 7
HELIX 33 33 GLU A 220 GLU A 225 1 6
HELIX 34 34 THR A 234 LYS A 254 1 21
HELIX 35 35 SER A 261 LEU A 269 1 9
HELIX 36 36 ILE A 270 TYR A 273 5 4
HELIX 37 37 ALA B 32 ALA B 41 1 10
HELIX 38 38 SER B 53 LYS B 62 1 10
HELIX 39 39 SER B 79 GLY B 99 1 21
HELIX 40 40 ALA B 108 GLY B 120 1 13
HELIX 41 41 GLU B 140 SER B 145 5 6
HELIX 42 42 PRO B 152 GLU B 162 1 11
HELIX 43 43 THR B 174 ALA B 180 1 7
HELIX 44 44 ASN B 181 PHE B 187 1 7
HELIX 45 45 GLU B 220 GLU B 225 1 6
HELIX 46 46 THR B 234 ARG B 253 1 20
HELIX 47 47 SER B 261 LEU B 269 1 9
HELIX 48 48 ILE B 270 TYR B 273 5 4
SHEET 1 A 8 ARG C 44 VAL C 48 0
SHEET 2 A 8 ILE C 11 LEU C 15 1 N ILE C 12 O ARG C 44
SHEET 3 A 8 VAL C 67 PHE C 69 1 O LEU C 68 N GLY C 13
SHEET 4 A 8 VAL C 104 THR C 107 1 O TRP C 105 N PHE C 69
SHEET 5 A 8 ILE C 212 THR C 215 1 O TYR C 213 N VAL C 104
SHEET 6 A 8 LYS C 200 ALA C 207 -1 N ALA C 207 O ILE C 212
SHEET 7 A 8 TYR C 188 THR C 195 -1 N ASN C 194 O PHE C 201
SHEET 8 A 8 ASP C 137 PHE C 138 -1 N ASP C 137 O THR C 193
SHEET 1 B 4 GLN C 17 LYS C 23 0
SHEET 2 B 4 ARG C 26 ALA C 31 -1 O ASN C 27 N VAL C 19
SHEET 3 B 4 GLN C 286 PHE C 290 -1 O TYR C 288 N ILE C 30
SHEET 4 B 4 GLU C 276 TYR C 277 -1 N GLU C 276 O THR C 287
SHEET 1 C 2 SER C 125 LEU C 134 0
SHEET 2 C 2 THR C 165 SER C 172 -1 O SER C 172 N SER C 125
SHEET 1 D 8 ARG D 44 VAL D 48 0
SHEET 2 D 8 ILE D 11 LEU D 15 1 N VAL D 14 O VAL D 48
SHEET 3 D 8 GLY D 66 PHE D 69 1 O GLY D 66 N GLY D 13
SHEET 4 D 8 VAL D 104 THR D 107 1 O TRP D 105 N PHE D 69
SHEET 5 D 8 ILE D 212 THR D 215 1 O TYR D 213 N GLY D 106
SHEET 6 D 8 LYS D 200 ALA D 207 -1 N ALA D 207 O ILE D 212
SHEET 7 D 8 TYR D 188 THR D 195 -1 N ARG D 189 O GLU D 206
SHEET 8 D 8 ASP D 137 PHE D 138 -1 N ASP D 137 O THR D 193
SHEET 1 E 4 GLN D 17 LYS D 23 0
SHEET 2 E 4 ARG D 26 ALA D 31 -1 O ARG D 26 N LYS D 23
SHEET 3 E 4 GLN D 286 PHE D 290 -1 O PHE D 290 N ASN D 27
SHEET 4 E 4 GLU D 276 TYR D 277 -1 N GLU D 276 O THR D 287
SHEET 1 F 2 SER D 125 LEU D 134 0
SHEET 2 F 2 THR D 165 SER D 172 -1 O SER D 172 N SER D 125
SHEET 1 G 8 ARG A 44 VAL A 48 0
SHEET 2 G 8 ILE A 11 LEU A 15 1 N VAL A 14 O VAL A 48
SHEET 3 G 8 VAL A 67 PHE A 69 1 O LEU A 68 N LEU A 15
SHEET 4 G 8 VAL A 104 THR A 107 1 O TRP A 105 N PHE A 69
SHEET 5 G 8 ILE A 212 THR A 215 1 O TYR A 213 N VAL A 104
SHEET 6 G 8 LYS A 200 ALA A 207 -1 N ALA A 207 O ILE A 212
SHEET 7 G 8 TYR A 188 THR A 195 -1 N ARG A 189 O GLU A 206
SHEET 8 G 8 ASP A 137 PHE A 138 -1 N ASP A 137 O THR A 193
SHEET 1 H 4 GLN A 17 LYS A 23 0
SHEET 2 H 4 ARG A 26 ALA A 31 -1 O ARG A 26 N LYS A 23
SHEET 3 H 4 GLN A 286 PHE A 290 -1 O TYR A 288 N ILE A 30
SHEET 4 H 4 GLU A 276 TYR A 277 -1 N GLU A 276 O THR A 287
SHEET 1 I 2 SER A 125 LEU A 134 0
SHEET 2 I 2 THR A 165 SER A 172 -1 O SER A 172 N SER A 125
SHEET 1 J 8 ARG B 44 VAL B 48 0
SHEET 2 J 8 ILE B 11 LEU B 15 1 N ILE B 12 O ARG B 44
SHEET 3 J 8 VAL B 67 PHE B 69 1 O LEU B 68 N GLY B 13
SHEET 4 J 8 VAL B 104 THR B 107 1 O TRP B 105 N PHE B 69
SHEET 5 J 8 ILE B 212 THR B 215 1 O TYR B 213 N GLY B 106
SHEET 6 J 8 LYS B 200 ALA B 207 -1 N MET B 205 O ALA B 214
SHEET 7 J 8 TYR B 188 THR B 195 -1 N ARG B 189 O GLU B 206
SHEET 8 J 8 ASP B 137 PHE B 138 -1 N ASP B 137 O THR B 193
SHEET 1 K 4 GLN B 17 LYS B 23 0
SHEET 2 K 4 ARG B 26 ALA B 31 -1 O TYR B 29 N GLN B 17
SHEET 3 K 4 GLN B 286 PHE B 290 -1 O PHE B 290 N ASN B 27
SHEET 4 K 4 GLU B 276 TYR B 277 -1 N GLU B 276 O THR B 287
SHEET 1 L 2 SER B 125 LEU B 134 0
SHEET 2 L 2 THR B 165 SER B 172 -1 O SER B 172 N SER B 125
CRYST1 51.586 206.505 65.198 90.00 113.42 90.00 P 1 21 1 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 0.019385 0.000000 0.008397 0.00000
SCALE2 0.000000 0.004842 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016715 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
