HEADER LIGASE 11-MAR-10 3M4Q
TITLE ENTAMOEBA HISTOLYTICA ASPARAGINYL-TRNA SYNTHETASE (ASNRS)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARAGINYL-TRNA SYNTHETASE, PUTATIVE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: EHASNRS;
COMPND 5 EC: 6.1.1.22;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTAMOEBA HISTOLYTICA;
SOURCE 3 ORGANISM_TAXID: 5759;
SOURCE 4 GENE: 159.M00096, EHI_126920;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS AMINOACYL-TRNA SYNTHETASE, TRNA LIGASE, AARS, ASNRS, TRANSLATION,
KEYWDS 2 ATP-BINDING, NUCLEOTIDE-BINDING, STRUCTURAL GENOMICS, MEDICAL
KEYWDS 3 STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA, MSGPP, LIGASE, PROTEIN
KEYWDS 4 BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR E.T.LARSON,E.A.MERRITT,MEDICAL STRUCTURAL GENOMICS OF PATHOGENIC
AUTHOR 2 PROTOZOA (MSGPP)
REVDAT 3 06-SEP-23 3M4Q 1 SEQADV
REVDAT 2 08-NOV-17 3M4Q 1 REMARK
REVDAT 1 23-MAR-10 3M4Q 0
JRNL AUTH E.T.LARSON,J.E.KIM,L.ZHANG,A.NAPULI,A.KELLEY,L.CASTANEDA,
JRNL AUTH 2 C.L.M.J.VERLINDE,W.C.VAN VOORHIS,F.S.BUCKNER,E.FAN,
JRNL AUTH 3 W.G.J.HOL,E.A.MERRITT
JRNL TITL X-RAY CRYSTAL STRUCTURE OF ASPARAGINYL-TRNA SYNTHETASE FROM
JRNL TITL 2 THE EUKARYOTIC HUMAN PATHOGEN ENTAMOEBA HISTOLYTICA.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.5.0106
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 22380
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) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1144
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1507
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE SET COUNT : 73
REMARK 3 BIN FREE R VALUE : 0.3490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6742
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 76.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.41000
REMARK 3 B22 (A**2) : 3.41000
REMARK 3 B33 (A**2) : -6.82000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.459
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.395
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 48.301
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6919 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4617 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9406 ; 0.958 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11236 ; 0.765 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 861 ; 5.494 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 307 ;33.966 ;23.681
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1092 ;13.930 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;17.304 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1019 ; 0.056 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7763 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1422 ; 0.001 ; 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): 4323 ; 0.754 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1737 ; 0.200 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6917 ; 1.349 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2596 ; 1.475 ; 6.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2489 ; 2.376 ;10.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 124 2
REMARK 3 1 A 1 A 124 2
REMARK 3 2 B 132 B 500 2
REMARK 3 2 A 132 A 500 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 B (A): 2474 ; 0.270 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2916 ; 0.340 ; 0.500
REMARK 3 TIGHT THERMAL 1 B (A**2): 2474 ; 0.280 ; 0.500
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2916 ; 0.270 ; 2.000
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 1 A 500
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0987 47.1844 -11.9581
REMARK 3 T TENSOR
REMARK 3 T11: 0.3765 T22: 0.3382
REMARK 3 T33: 0.1132 T12: 0.1105
REMARK 3 T13: 0.0195 T23: 0.0777
REMARK 3 L TENSOR
REMARK 3 L11: 2.7791 L22: 2.1449
REMARK 3 L33: 2.7053 L12: 1.0445
REMARK 3 L13: 0.6983 L23: 0.5744
REMARK 3 S TENSOR
REMARK 3 S11: 0.0705 S12: -0.1071 S13: -0.3025
REMARK 3 S21: 0.0963 S22: 0.0776 S23: -0.2334
REMARK 3 S31: 0.9183 S32: 0.3081 S33: -0.1481
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 1 B 500
REMARK 3 ORIGIN FOR THE GROUP (A): -1.7287 67.3660 -5.5985
REMARK 3 T TENSOR
REMARK 3 T11: 0.1623 T22: 0.3979
REMARK 3 T33: 0.3198 T12: 0.0333
REMARK 3 T13: 0.1015 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 3.4548 L22: 1.2100
REMARK 3 L33: 2.8908 L12: 0.1475
REMARK 3 L13: 1.2978 L23: 0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.0524 S12: -0.4090 S13: 0.4997
REMARK 3 S21: 0.2530 S22: -0.0944 S23: 0.3539
REMARK 3 S31: -0.2949 S32: -0.4116 S33: 0.0420
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. U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3M4Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058105.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22471
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.90
REMARK 200 R MERGE (I) : 0.12100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 10.80
REMARK 200 R MERGE FOR SHELL (I) : 0.76200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.750
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: 3M4P; A CHAIN, PROTEIN ONLY MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 UL 29 MG/ML PROTEIN IN SGPP BUFFER
REMARK 280 MIXED WITH 0.2 UL WELL SOLN. (100 MM HEPES PH 7.6, 25% PEG 3350,
REMARK 280 200 MM MGCL2); CRYOPROTECTED BY SOAKING ~1 MIN. IN WELL SOLN
REMARK 280 SUPPLEMENTED WITH 10% PEG 200, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 102.50750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 51.02350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 51.02350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 51.25375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 51.02350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 51.02350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 153.76125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 51.02350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.02350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 51.25375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 51.02350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.02350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 153.76125
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 102.50750
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: 7770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 GLY A -4
REMARK 465 PRO A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 MET A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 GLU A 3
REMARK 465 ALA A 4
REMARK 465 THR A 5
REMARK 465 THR A 6
REMARK 465 THR A 7
REMARK 465 PRO A 8
REMARK 465 VAL A 9
REMARK 465 GLU A 10
REMARK 465 GLN A 182
REMARK 465 CYS A 183
REMARK 465 GLU A 184
REMARK 465 GLY A 185
REMARK 465 GLY A 186
REMARK 465 SER A 187
REMARK 465 GLN A 230
REMARK 465 SER A 231
REMARK 465 ARG A 232
REMARK 465 THR A 233
REMARK 465 VAL A 234
REMARK 465 ARG A 235
REMARK 465 GLY B -4
REMARK 465 PRO B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 MET B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 GLU B 3
REMARK 465 ALA B 4
REMARK 465 THR B 5
REMARK 465 THR B 6
REMARK 465 THR B 7
REMARK 465 PRO B 8
REMARK 465 VAL B 9
REMARK 465 GLU B 10
REMARK 465 THR B 11
REMARK 465 GLU B 184
REMARK 465 GLY B 185
REMARK 465 GLY B 186
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 ILE A 17 CG1 CG2 CD1
REMARK 470 ARG A 18 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 26 CG CD CE NZ
REMARK 470 ARG A 41 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 48 CG CD OE1 OE2
REMARK 470 ILE A 60 CG1 CG2 CD1
REMARK 470 LYS A 63 CG CD CE NZ
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 LEU A 73 CG CD1 CD2
REMARK 470 LEU A 80 CG CD1 CD2
REMARK 470 ILE A 82 CG1 CG2 CD1
REMARK 470 ASN A 93 CG OD1 ND2
REMARK 470 GLU A 97 CG CD OE1 OE2
REMARK 470 ILE A 98 CG1 CG2 CD1
REMARK 470 ILE A 101 CG1 CG2 CD1
REMARK 470 ASN A 103 CG OD1 ND2
REMARK 470 LEU A 121 CG CD1 CD2
REMARK 470 LYS A 127 CG CD CE NZ
REMARK 470 ASP A 128 CG OD1 OD2
REMARK 470 SER A 130 OG
REMARK 470 GLN A 133 CG CD OE1 NE2
REMARK 470 LYS A 134 CG CD CE NZ
REMARK 470 ILE A 140 CG1 CG2 CD1
REMARK 470 THR A 188 OG1 CG2
REMARK 470 LEU A 189 CG CD1 CD2
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 ASN A 196 CG OD1 ND2
REMARK 470 GLU A 229 CG CD OE1 OE2
REMARK 470 HIS A 236 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 302 CG CD CE NZ
REMARK 470 ILE A 309 CG1 CG2 CD1
REMARK 470 LYS A 312 CG CD CE NZ
REMARK 470 ASP A 313 CG OD1 OD2
REMARK 470 LYS A 314 CG CD CE NZ
REMARK 470 GLU A 320 CG CD OE1 OE2
REMARK 470 ASP A 321 CG OD1 OD2
REMARK 470 SER A 323 OG
REMARK 470 LYS A 325 CG CD CE NZ
REMARK 470 ARG A 328 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 354 CG CD CE NZ
REMARK 470 LEU A 397 CG CD1 CD2
REMARK 470 LYS A 410 CG CD CE NZ
REMARK 470 GLU A 447 CG CD OE1 OE2
REMARK 470 LYS B 26 CG CD CE NZ
REMARK 470 LEU B 27 CG CD1 CD2
REMARK 470 ARG B 38 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 44 CG CD1 CD2
REMARK 470 LYS B 63 CG CD CE NZ
REMARK 470 GLU B 64 CG CD OE1 OE2
REMARK 470 GLU B 67 CG CD OE1 OE2
REMARK 470 GLU B 69 CG CD OE1 OE2
REMARK 470 LYS B 70 CG CD CE NZ
REMARK 470 LYS B 72 CG CD CE NZ
REMARK 470 LEU B 73 CG CD1 CD2
REMARK 470 LYS B 92 CG CD CE NZ
REMARK 470 GLU B 97 CG CD OE1 OE2
REMARK 470 GLN B 107 CG CD OE1 NE2
REMARK 470 GLU B 116 CG CD OE1 OE2
REMARK 470 LEU B 121 CG CD1 CD2
REMARK 470 LYS B 127 CG CD CE NZ
REMARK 470 ASP B 128 CG OD1 OD2
REMARK 470 ILE B 140 CG1 CG2 CD1
REMARK 470 THR B 181 OG1 CG2
REMARK 470 GLN B 182 CG CD OE1 NE2
REMARK 470 SER B 187 OG
REMARK 470 THR B 188 OG1 CG2
REMARK 470 LEU B 189 CG CD1 CD2
REMARK 470 LYS B 191 CG CD CE NZ
REMARK 470 ARG B 232 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 235 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 286 CG CD CE NZ
REMARK 470 LEU B 310 CG CD1 CD2
REMARK 470 LYS B 312 CG CD CE NZ
REMARK 470 ASP B 313 CG OD1 OD2
REMARK 470 GLU B 317 CG CD OE1 OE2
REMARK 470 GLU B 320 CG CD OE1 OE2
REMARK 470 ASP B 321 CG OD1 OD2
REMARK 470 GLU B 324 CG CD OE1 OE2
REMARK 470 LYS B 325 CG CD CE NZ
REMARK 470 ARG B 328 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 346 CG CD CE NZ
REMARK 470 HIS B 358 CG ND1 CD2 CE1 NE2
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 ALA A 40 -111.10 35.89
REMARK 500 ASP A 51 27.27 -141.98
REMARK 500 ASN A 103 17.80 -67.50
REMARK 500 SER A 117 90.16 -161.29
REMARK 500 ASN A 126 -103.32 -116.28
REMARK 500 ASN A 137 43.11 -103.88
REMARK 500 PHE A 195 -118.93 60.30
REMARK 500 PHE A 249 70.59 49.83
REMARK 500 ASP A 313 3.67 88.52
REMARK 500 SER A 323 -178.80 -67.16
REMARK 500 PRO A 370 109.03 -53.00
REMARK 500 VAL A 372 -19.67 -143.09
REMARK 500 ALA B 40 -93.93 61.60
REMARK 500 CYS B 66 50.71 -116.49
REMARK 500 GLU B 97 78.15 -69.57
REMARK 500 ASN B 103 32.56 -77.99
REMARK 500 ILE B 114 -62.29 -104.19
REMARK 500 ASN B 137 34.91 -94.05
REMARK 500 GLN B 182 -76.42 -119.08
REMARK 500 THR B 188 64.77 -106.18
REMARK 500 PHE B 195 -82.48 65.01
REMARK 500 SER B 204 147.55 -170.58
REMARK 500 VAL B 234 36.39 -77.15
REMARK 500 ASP B 313 -55.26 124.22
REMARK 500 TYR B 318 106.50 -46.72
REMARK 500 TYR B 402 33.04 -99.97
REMARK 500 LEU B 441 -78.58 -65.38
REMARK 500 CYS B 449 24.34 -142.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3M4P RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH ASPARAGINYL-ADENYLATE
DBREF 3M4Q A 1 451 UNP C4LWW8 C4LWW8_ENTHI 1 451
DBREF 3M4Q B 1 451 UNP C4LWW8 C4LWW8_ENTHI 1 451
SEQADV 3M4Q GLY A -4 UNP C4LWW8 EXPRESSION TAG
SEQADV 3M4Q PRO A -3 UNP C4LWW8 EXPRESSION TAG
SEQADV 3M4Q GLY A -2 UNP C4LWW8 EXPRESSION TAG
SEQADV 3M4Q SER A -1 UNP C4LWW8 EXPRESSION TAG
SEQADV 3M4Q MET A 0 UNP C4LWW8 EXPRESSION TAG
SEQADV 3M4Q GLY B -4 UNP C4LWW8 EXPRESSION TAG
SEQADV 3M4Q PRO B -3 UNP C4LWW8 EXPRESSION TAG
SEQADV 3M4Q GLY B -2 UNP C4LWW8 EXPRESSION TAG
SEQADV 3M4Q SER B -1 UNP C4LWW8 EXPRESSION TAG
SEQADV 3M4Q MET B 0 UNP C4LWW8 EXPRESSION TAG
SEQRES 1 A 456 GLY PRO GLY SER MET MET THR GLU ALA THR THR THR PRO
SEQRES 2 A 456 VAL GLU THR PRO ILE VAL CYS ASN ILE ARG ASP ALA ALA
SEQRES 3 A 456 GLY LEU GLU GLY LYS LEU VAL THR PHE LYS GLY TRP ALA
SEQRES 4 A 456 TYR HIS ILE ARG LYS ALA ARG LYS THR LEU ILE PHE VAL
SEQRES 5 A 456 GLU LEU ARG ASP GLY SER GLY TYR CYS GLN CYS VAL ILE
SEQRES 6 A 456 PHE GLY LYS GLU LEU CYS GLU PRO GLU LYS VAL LYS LEU
SEQRES 7 A 456 LEU THR ARG GLU CYS SER LEU GLU ILE THR GLY ARG LEU
SEQRES 8 A 456 ASN ALA TYR ALA GLY LYS ASN HIS PRO PRO GLU ILE ALA
SEQRES 9 A 456 ASP ILE LEU ASN LEU GLU MET GLN VAL THR GLU TRP LYS
SEQRES 10 A 456 VAL ILE GLY GLU SER PRO ILE ASP LEU GLU ASN ILE ILE
SEQRES 11 A 456 ASN LYS ASP SER SER ILE PRO GLN LYS MET GLN ASN ARG
SEQRES 12 A 456 HIS ILE VAL ILE ARG SER GLU HIS THR GLN GLN VAL LEU
SEQRES 13 A 456 GLN LEU ARG SER GLU ILE GLN TRP TYR PHE ARG LYS TYR
SEQRES 14 A 456 TYR HIS ASP ASN HIS PHE THR GLU ILE GLN PRO PRO THR
SEQRES 15 A 456 ILE VAL LYS THR GLN CYS GLU GLY GLY SER THR LEU PHE
SEQRES 16 A 456 LYS LEU GLN TYR PHE ASN GLU PRO ALA TYR LEU THR GLN
SEQRES 17 A 456 SER SER GLN LEU TYR LEU GLU SER VAL ILE ALA SER LEU
SEQRES 18 A 456 GLY LYS SER PHE CYS MET LEU SER SER TYR ARG ALA GLU
SEQRES 19 A 456 GLN SER ARG THR VAL ARG HIS LEU ALA GLU TYR LEU HIS
SEQRES 20 A 456 LEU GLU ALA GLU LEU PRO PHE ILE SER PHE GLU ASP LEU
SEQRES 21 A 456 LEU ASN HIS LEU GLU ASP LEU VAL CYS THR VAL ILE ASP
SEQRES 22 A 456 ASN VAL MET ALA VAL HIS GLY ASP LYS ILE ARG LYS MET
SEQRES 23 A 456 ASN PRO HIS LEU LYS LEU PRO THR ARG PRO PHE LYS ARG
SEQRES 24 A 456 MET THR TYR ALA ASP ALA ILE LYS TYR CYS ASN ASP HIS
SEQRES 25 A 456 GLY ILE LEU ASN LYS ASP LYS PRO PHE GLU TYR GLY GLU
SEQRES 26 A 456 ASP ILE SER GLU LYS PRO GLU ARG GLN MET THR ASP GLU
SEQRES 27 A 456 ILE GLY CYS PRO ILE PHE MET ILE HIS PHE PRO SER LYS
SEQRES 28 A 456 MET LYS ALA PHE TYR MET SER LYS VAL PRO GLY HIS PRO
SEQRES 29 A 456 ASP LEU THR GLU SER VAL ASP LEU LEU MET PRO GLY VAL
SEQRES 30 A 456 GLY GLU ILE VAL GLY GLY SER MET ARG ILE TRP ASN TYR
SEQRES 31 A 456 ASP GLU LEU MET GLY ALA TYR LYS ALA ASN GLY LEU ASN
SEQRES 32 A 456 PRO ASP PRO TYR TYR TRP TYR THR GLN GLN ARG LYS TYR
SEQRES 33 A 456 GLY SER CYS PRO HIS GLY GLY TYR GLY LEU GLY VAL GLU
SEQRES 34 A 456 ARG LEU VAL MET TRP LEU LEU GLY GLU ASP HIS ILE ARG
SEQRES 35 A 456 LYS VAL CYS LEU TYR PRO ARG TYR LEU GLU ARG CYS GLU
SEQRES 36 A 456 PRO
SEQRES 1 B 456 GLY PRO GLY SER MET MET THR GLU ALA THR THR THR PRO
SEQRES 2 B 456 VAL GLU THR PRO ILE VAL CYS ASN ILE ARG ASP ALA ALA
SEQRES 3 B 456 GLY LEU GLU GLY LYS LEU VAL THR PHE LYS GLY TRP ALA
SEQRES 4 B 456 TYR HIS ILE ARG LYS ALA ARG LYS THR LEU ILE PHE VAL
SEQRES 5 B 456 GLU LEU ARG ASP GLY SER GLY TYR CYS GLN CYS VAL ILE
SEQRES 6 B 456 PHE GLY LYS GLU LEU CYS GLU PRO GLU LYS VAL LYS LEU
SEQRES 7 B 456 LEU THR ARG GLU CYS SER LEU GLU ILE THR GLY ARG LEU
SEQRES 8 B 456 ASN ALA TYR ALA GLY LYS ASN HIS PRO PRO GLU ILE ALA
SEQRES 9 B 456 ASP ILE LEU ASN LEU GLU MET GLN VAL THR GLU TRP LYS
SEQRES 10 B 456 VAL ILE GLY GLU SER PRO ILE ASP LEU GLU ASN ILE ILE
SEQRES 11 B 456 ASN LYS ASP SER SER ILE PRO GLN LYS MET GLN ASN ARG
SEQRES 12 B 456 HIS ILE VAL ILE ARG SER GLU HIS THR GLN GLN VAL LEU
SEQRES 13 B 456 GLN LEU ARG SER GLU ILE GLN TRP TYR PHE ARG LYS TYR
SEQRES 14 B 456 TYR HIS ASP ASN HIS PHE THR GLU ILE GLN PRO PRO THR
SEQRES 15 B 456 ILE VAL LYS THR GLN CYS GLU GLY GLY SER THR LEU PHE
SEQRES 16 B 456 LYS LEU GLN TYR PHE ASN GLU PRO ALA TYR LEU THR GLN
SEQRES 17 B 456 SER SER GLN LEU TYR LEU GLU SER VAL ILE ALA SER LEU
SEQRES 18 B 456 GLY LYS SER PHE CYS MET LEU SER SER TYR ARG ALA GLU
SEQRES 19 B 456 GLN SER ARG THR VAL ARG HIS LEU ALA GLU TYR LEU HIS
SEQRES 20 B 456 LEU GLU ALA GLU LEU PRO PHE ILE SER PHE GLU ASP LEU
SEQRES 21 B 456 LEU ASN HIS LEU GLU ASP LEU VAL CYS THR VAL ILE ASP
SEQRES 22 B 456 ASN VAL MET ALA VAL HIS GLY ASP LYS ILE ARG LYS MET
SEQRES 23 B 456 ASN PRO HIS LEU LYS LEU PRO THR ARG PRO PHE LYS ARG
SEQRES 24 B 456 MET THR TYR ALA ASP ALA ILE LYS TYR CYS ASN ASP HIS
SEQRES 25 B 456 GLY ILE LEU ASN LYS ASP LYS PRO PHE GLU TYR GLY GLU
SEQRES 26 B 456 ASP ILE SER GLU LYS PRO GLU ARG GLN MET THR ASP GLU
SEQRES 27 B 456 ILE GLY CYS PRO ILE PHE MET ILE HIS PHE PRO SER LYS
SEQRES 28 B 456 MET LYS ALA PHE TYR MET SER LYS VAL PRO GLY HIS PRO
SEQRES 29 B 456 ASP LEU THR GLU SER VAL ASP LEU LEU MET PRO GLY VAL
SEQRES 30 B 456 GLY GLU ILE VAL GLY GLY SER MET ARG ILE TRP ASN TYR
SEQRES 31 B 456 ASP GLU LEU MET GLY ALA TYR LYS ALA ASN GLY LEU ASN
SEQRES 32 B 456 PRO ASP PRO TYR TYR TRP TYR THR GLN GLN ARG LYS TYR
SEQRES 33 B 456 GLY SER CYS PRO HIS GLY GLY TYR GLY LEU GLY VAL GLU
SEQRES 34 B 456 ARG LEU VAL MET TRP LEU LEU GLY GLU ASP HIS ILE ARG
SEQRES 35 B 456 LYS VAL CYS LEU TYR PRO ARG TYR LEU GLU ARG CYS GLU
SEQRES 36 B 456 PRO
HELIX 1 1 GLU A 67 LEU A 74 1 8
HELIX 2 2 ASP A 120 ILE A 125 1 6
HELIX 3 3 SER A 130 ASN A 137 1 8
HELIX 4 4 ASN A 137 ILE A 142 1 6
HELIX 5 5 SER A 144 ASN A 168 1 25
HELIX 6 6 SER A 205 GLY A 217 1 13
HELIX 7 7 SER A 251 ASN A 282 1 32
HELIX 8 8 TYR A 297 GLY A 308 1 12
HELIX 9 9 SER A 323 GLY A 335 1 13
HELIX 10 10 PRO A 344 LYS A 348 5 5
HELIX 11 11 ASN A 384 ASN A 395 1 12
HELIX 12 12 PRO A 399 PRO A 401 5 3
HELIX 13 13 TYR A 402 TYR A 411 1 10
HELIX 14 14 VAL A 423 GLY A 432 1 10
HELIX 15 15 HIS A 435 CYS A 440 5 6
HELIX 16 16 GLU B 67 LYS B 72 1 6
HELIX 17 17 PRO B 118 GLU B 122 5 5
HELIX 18 18 SER B 130 ASN B 137 1 8
HELIX 19 19 ASN B 137 ILE B 142 1 6
HELIX 20 20 SER B 144 ASN B 168 1 25
HELIX 21 21 SER B 205 SER B 211 1 7
HELIX 22 22 SER B 251 ASN B 282 1 32
HELIX 23 23 TYR B 297 GLY B 308 1 12
HELIX 24 24 SER B 323 GLY B 335 1 13
HELIX 25 25 PRO B 344 LYS B 348 5 5
HELIX 26 26 ASN B 384 ASN B 395 1 12
HELIX 27 27 PRO B 399 PRO B 401 5 3
HELIX 28 28 TYR B 402 TYR B 411 1 10
HELIX 29 29 VAL B 423 GLY B 432 1 10
HELIX 30 30 HIS B 435 CYS B 440 5 6
SHEET 1 A 7 CYS A 15 ASN A 16 0
SHEET 2 A 7 LEU A 27 ARG A 41 1 O LEU A 27 N CYS A 15
SHEET 3 A 7 SER A 79 ALA A 88 -1 O GLY A 84 N VAL A 28
SHEET 4 A 7 LEU A 104 GLY A 115 -1 O GLU A 110 N THR A 83
SHEET 5 A 7 TYR A 55 PHE A 61 1 N VAL A 59 O MET A 106
SHEET 6 A 7 LEU A 44 ARG A 50 -1 N VAL A 47 O CYS A 58
SHEET 7 A 7 LEU A 27 ARG A 41 -1 N TRP A 33 O ARG A 50
SHEET 1 B 8 THR A 171 GLU A 172 0
SHEET 2 B 8 SER A 219 TYR A 226 1 O PHE A 220 N THR A 171
SHEET 3 B 8 GLU A 239 PRO A 248 -1 O GLU A 244 N CYS A 221
SHEET 4 B 8 HIS A 416 GLY A 422 -1 O GLY A 417 N LEU A 247
SHEET 5 B 8 GLY A 373 ARG A 381 -1 N ARG A 381 O HIS A 416
SHEET 6 B 8 SER A 364 MET A 369 -1 N VAL A 365 O GLY A 378
SHEET 7 B 8 ILE A 338 ILE A 341 -1 N ILE A 338 O LEU A 368
SHEET 8 B 8 LYS A 293 THR A 296 1 N MET A 295 O ILE A 341
SHEET 1 C 6 ILE A 178 VAL A 179 0
SHEET 2 C 6 GLU A 197 LEU A 201 -1 O TYR A 200 N VAL A 179
SHEET 3 C 6 LYS A 191 TYR A 194 -1 N LEU A 192 O ALA A 199
SHEET 4 C 6 LYS B 191 TYR B 194 -1 O GLN B 193 N LYS A 191
SHEET 5 C 6 GLU B 197 LEU B 201 -1 O GLU B 197 N TYR B 194
SHEET 6 C 6 ILE B 178 VAL B 179 -1 N VAL B 179 O TYR B 200
SHEET 1 D 2 LYS A 354 VAL A 355 0
SHEET 2 D 2 HIS A 358 THR A 362 -1 O HIS A 358 N VAL A 355
SHEET 1 E 7 CYS B 15 ASN B 16 0
SHEET 2 E 7 LEU B 27 ARG B 38 1 O THR B 29 N CYS B 15
SHEET 3 E 7 SER B 79 ALA B 88 -1 O ILE B 82 N PHE B 30
SHEET 4 E 7 LEU B 104 GLY B 115 -1 O THR B 109 N THR B 83
SHEET 5 E 7 TYR B 55 PHE B 61 1 N VAL B 59 O MET B 106
SHEET 6 E 7 LEU B 44 ARG B 50 -1 N VAL B 47 O CYS B 58
SHEET 7 E 7 LEU B 27 ARG B 38 -1 N HIS B 36 O GLU B 48
SHEET 1 F 8 THR B 171 GLU B 172 0
SHEET 2 F 8 SER B 219 TYR B 226 1 O PHE B 220 N THR B 171
SHEET 3 F 8 GLU B 239 PRO B 248 -1 O HIS B 242 N LEU B 223
SHEET 4 F 8 HIS B 416 GLY B 422 -1 O GLY B 417 N LEU B 247
SHEET 5 F 8 GLY B 373 ARG B 381 -1 N ARG B 381 O HIS B 416
SHEET 6 F 8 SER B 364 MET B 369 -1 N VAL B 365 O GLY B 378
SHEET 7 F 8 ILE B 338 ILE B 341 -1 N ILE B 338 O LEU B 368
SHEET 8 F 8 LYS B 293 THR B 296 1 N LYS B 293 O PHE B 339
CISPEP 1 ARG A 290 PRO A 291 0 -3.69
CISPEP 2 GLU A 450 PRO A 451 0 -4.32
CISPEP 3 ARG B 290 PRO B 291 0 -1.24
CISPEP 4 GLU B 450 PRO B 451 0 -2.05
CRYST1 102.047 102.047 205.015 90.00 90.00 90.00 P 41 21 2 16
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 0.009799 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009799 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004878 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
