HEADER LIGASE 13-MAY-09 3HFZ
TITLE CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS PHENYLALANYL-TRNA SYNTHETASE
TITLE 2 COMPLEXED WITH M-TYROSINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHENYLALANYL-TRNA SYNTHETASE ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PHENYLALANINE--TRNA LIGASE ALPHA CHAIN, PHERS;
COMPND 5 EC: 6.1.1.20;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: PHENYLALANINE--TRNA LIGASE BETA CHAIN, PHERS;
COMPND 10 EC: 6.1.1.20
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 6 ORGANISM_TAXID: 274
KEYWDS HETERODIMER, PHENYLALANYL-TRNA, THERMUS THERMOPHILUS, TRNA, M-
KEYWDS 2 TYROSINE, AMINOACYL-TRNA SYNTHETASE, ATP-BINDING, LIGASE, MAGNESIUM,
KEYWDS 3 METAL-BINDING, NUCLEOTIDE-BINDING, PROTEIN BIOSYNTHESIS, RNA-
KEYWDS 4 BINDING, TRNA-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR L.KLIPCAN,N.MOOR,N.KESSLER,M.G.SAFRO
REVDAT 4 06-SEP-23 3HFZ 1 REMARK
REVDAT 3 14-DEC-16 3HFZ 1 TITLE
REVDAT 2 16-NOV-11 3HFZ 1 VERSN HETATM
REVDAT 1 21-JUL-09 3HFZ 0
JRNL AUTH L.KLIPCAN,N.MOOR,N.KESSLER,M.G.SAFRO
JRNL TITL EUKARYOTIC CYTOSOLIC AND MITOCHONDRIAL PHENYLALANYL-TRNA
JRNL TITL 2 SYNTHETASES CATALYZE THE CHARGING OF TRNA WITH THE
JRNL TITL 3 META-TYROSINE
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 11045 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19549855
JRNL DOI 10.1073/PNAS.0905212106
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0067
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 50474
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) : 0.270
REMARK 3 R VALUE (WORKING SET) : 0.269
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2688
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3671
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.4130
REMARK 3 BIN FREE R VALUE SET COUNT : 211
REMARK 3 BIN FREE R VALUE : 0.4130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8250
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 241
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -0.24000
REMARK 3 B12 (A**2) : 0.08000
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): 0.326
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.342
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.289
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.494
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.912
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.20
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 3HFZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000053086.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 7.8
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) : 0.93
REMARK 200 MONOCHROMATOR : ALUMINIUM OR CARBON FOILS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 3671
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.899
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1PYS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (NH4)2SO4, 0.02M IMIDAZOLE-HCL,
REMARK 280 0.001M MAGNESIUM CHLORIDE, M-TYROSINE, PH 7.8, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 92.56800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.28400
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 46.28400
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 92.56800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 26500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 79590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.0 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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 354 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 874 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 ALA A 5
REMARK 465 LEU A 6
REMARK 465 ALA A 7
REMARK 465 ALA A 8
REMARK 465 ILE A 9
REMARK 465 GLN A 10
REMARK 465 ASN A 11
REMARK 465 ALA A 12
REMARK 465 ARG A 13
REMARK 465 ASP A 14
REMARK 465 LEU A 15
REMARK 465 GLU A 16
REMARK 465 GLU A 17
REMARK 465 LEU A 18
REMARK 465 LYS A 19
REMARK 465 ALA A 20
REMARK 465 LEU A 21
REMARK 465 LYS A 22
REMARK 465 ALA A 23
REMARK 465 ARG A 24
REMARK 465 TYR A 25
REMARK 465 LEU A 26
REMARK 465 GLY A 27
REMARK 465 LYS A 28
REMARK 465 LYS A 29
REMARK 465 GLY A 30
REMARK 465 LEU A 31
REMARK 465 LEU A 32
REMARK 465 THR A 33
REMARK 465 GLN A 34
REMARK 465 GLU A 35
REMARK 465 MET A 36
REMARK 465 LYS A 37
REMARK 465 GLY A 38
REMARK 465 LEU A 39
REMARK 465 SER A 40
REMARK 465 ALA A 41
REMARK 465 LEU A 42
REMARK 465 PRO A 43
REMARK 465 LEU A 44
REMARK 465 GLU A 45
REMARK 465 GLU A 46
REMARK 465 ARG A 47
REMARK 465 ARG A 48
REMARK 465 LYS A 49
REMARK 465 ARG A 50
REMARK 465 GLY A 51
REMARK 465 GLN A 52
REMARK 465 GLU A 53
REMARK 465 LEU A 54
REMARK 465 ASN A 55
REMARK 465 ALA A 56
REMARK 465 ILE A 57
REMARK 465 LYS A 58
REMARK 465 ALA A 59
REMARK 465 ALA A 60
REMARK 465 LEU A 61
REMARK 465 GLU A 62
REMARK 465 ALA A 63
REMARK 465 ALA A 64
REMARK 465 LEU A 65
REMARK 465 GLU A 66
REMARK 465 ALA A 67
REMARK 465 ARG A 68
REMARK 465 GLU A 69
REMARK 465 LYS A 70
REMARK 465 ALA A 71
REMARK 465 LEU A 72
REMARK 465 GLU A 73
REMARK 465 GLU A 74
REMARK 465 ALA A 75
REMARK 465 ALA A 76
REMARK 465 LEU A 77
REMARK 465 LYS A 78
REMARK 465 GLU A 79
REMARK 465 ALA A 80
REMARK 465 LEU A 81
REMARK 465 GLU A 82
REMARK 465 ARG A 83
REMARK 465 GLU A 84
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ARG A 85
REMARK 475 ARG B 780
REMARK 475 GLY B 781
REMARK 475 LEU B 782
REMARK 475 ASP B 783
REMARK 475 THR B 784
REMARK 475 PRO B 785
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 CB GLU B 579 O HOH A 408 1.94
REMARK 500 CG ARG B 407 O HOH B 838 1.95
REMARK 500 CB LEU A 278 O HOH A 376 1.98
REMARK 500 CA LEU B 532 O HOH B 933 2.03
REMARK 500 O GLU A 239 O HOH A 402 2.07
REMARK 500 O ALA B 542 O HOH B 933 2.09
REMARK 500 CA GLY A 284 O HOH A 391 2.09
REMARK 500 CB ASP B 33 O HOH B 843 2.10
REMARK 500 CD PRO A 272 O HOH A 366 2.10
REMARK 500 CB THR B 441 O HOH B 838 2.10
REMARK 500 N ALA A 121 O HOH A 378 2.11
REMARK 500 CG GLU A 112 O HOH A 377 2.11
REMARK 500 CD PRO B 211 O HOH B 879 2.11
REMARK 500 CB MTY A 351 O HOH A 381 2.13
REMARK 500 CE1 HIS B 635 O HOH B 908 2.13
REMARK 500 CD1 LEU B 643 O HOH B 791 2.14
REMARK 500 CG GLN A 254 O HOH A 406 2.14
REMARK 500 O ALA B 389 O HOH B 954 2.15
REMARK 500 O LEU B 713 O HOH B 925 2.15
REMARK 500 CA LEU A 240 O HOH A 402 2.15
REMARK 500 CA PRO B 401 O HOH B 803 2.16
REMARK 500 CB GLU B 438 O HOH B 831 2.16
REMARK 500 CG1 ILE B 56 O HOH B 842 2.16
REMARK 500 OG SER B 6 OE2 GLU B 153 2.16
REMARK 500 CG1 ILE A 237 O HOH A 403 2.16
REMARK 500 CE LYS B 9 O HOH B 951 2.17
REMARK 500 CB ASP A 248 O HOH A 399 2.17
REMARK 500 O ARG B 413 O HOH B 869 2.17
REMARK 500 O GLY A 92 O HOH A 404 2.17
REMARK 500 CG GLU A 279 O HOH A 401 2.17
REMARK 500 ND2 ASN B 243 O HOH B 880 2.18
REMARK 500 CB LEU A 173 O HOH A 414 2.19
REMARK 500 CG ARG A 298 O HOH A 362 2.19
REMARK 500 CA GLY B 776 O HOH B 959 2.19
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 O GLY B 110 O HOH B 808 5565 2.13
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 A 87 163.38 -43.22
REMARK 500 VAL A 88 -8.70 -144.55
REMARK 500 ALA A 93 89.59 -44.80
REMARK 500 SER A 94 78.00 -38.12
REMARK 500 PRO A 102 -36.41 -38.09
REMARK 500 LEU A 105 -78.22 -58.62
REMARK 500 GLU A 130 -21.52 -35.72
REMARK 500 PHE A 134 -43.49 -141.53
REMARK 500 LEU A 137 38.00 -87.34
REMARK 500 ASN A 138 37.32 39.42
REMARK 500 PRO A 164 -84.72 -30.92
REMARK 500 LEU A 165 17.14 -64.97
REMARK 500 PRO A 181 -46.13 -29.75
REMARK 500 ASP A 209 -144.11 -122.19
REMARK 500 ILE A 228 156.35 -47.85
REMARK 500 GLU A 262 117.46 -166.38
REMARK 500 ALA A 265 171.75 178.29
REMARK 500 ALA A 283 -174.41 -179.51
REMARK 500 ARG A 300 -9.13 -57.96
REMARK 500 VAL A 319 -88.17 -60.88
REMARK 500 GLU A 320 -42.36 -14.79
REMARK 500 ARG A 321 -70.28 -57.01
REMARK 500 LEU A 322 -77.34 -41.83
REMARK 500 ALA A 323 -33.34 -31.01
REMARK 500 LYS A 341 -1.08 -54.59
REMARK 500 GLN A 345 -4.35 -53.77
REMARK 500 VAL A 349 90.58 -9.59
REMARK 500 ARG B 2 119.09 -32.07
REMARK 500 ARG B 34 160.47 173.58
REMARK 500 PHE B 39 65.71 -105.87
REMARK 500 PRO B 42 175.07 -50.00
REMARK 500 GLU B 52 122.04 178.88
REMARK 500 ALA B 81 97.42 -57.58
REMARK 500 THR B 94 135.02 -39.47
REMARK 500 LEU B 99 10.24 -146.95
REMARK 500 GLU B 105 79.54 -113.15
REMARK 500 MET B 116 142.57 -179.54
REMARK 500 LEU B 132 175.61 -52.88
REMARK 500 GLU B 148 -0.14 -57.02
REMARK 500 ALA B 149 -7.90 -142.69
REMARK 500 PRO B 162 -36.84 -34.69
REMARK 500 ALA B 174 -6.28 -48.00
REMARK 500 PRO B 199 45.01 -60.49
REMARK 500 ALA B 210 64.24 -169.79
REMARK 500 ARG B 222 68.67 -115.35
REMARK 500 ASN B 243 164.10 178.87
REMARK 500 ASN B 244 -102.12 -17.05
REMARK 500 ARG B 256 28.78 -144.36
REMARK 500 GLN B 258 89.80 -152.16
REMARK 500 ARG B 266 -31.25 -39.20
REMARK 500
REMARK 500 THIS ENTRY HAS 95 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 186 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTY A 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTY B 786
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PYS RELATED DB: PDB
REMARK 900 RELATED ID: 1CMQ RELATED DB: PDB
DBREF 3HFZ A 1 350 UNP P27001 SYFA_THETH 1 350
DBREF 3HFZ B 1 785 UNP P27002 SYFB_THETH 1 785
SEQRES 1 A 350 MET LEU GLU GLU ALA LEU ALA ALA ILE GLN ASN ALA ARG
SEQRES 2 A 350 ASP LEU GLU GLU LEU LYS ALA LEU LYS ALA ARG TYR LEU
SEQRES 3 A 350 GLY LYS LYS GLY LEU LEU THR GLN GLU MET LYS GLY LEU
SEQRES 4 A 350 SER ALA LEU PRO LEU GLU GLU ARG ARG LYS ARG GLY GLN
SEQRES 5 A 350 GLU LEU ASN ALA ILE LYS ALA ALA LEU GLU ALA ALA LEU
SEQRES 6 A 350 GLU ALA ARG GLU LYS ALA LEU GLU GLU ALA ALA LEU LYS
SEQRES 7 A 350 GLU ALA LEU GLU ARG GLU ARG VAL ASP VAL SER LEU PRO
SEQRES 8 A 350 GLY ALA SER LEU PHE SER GLY GLY LEU HIS PRO ILE THR
SEQRES 9 A 350 LEU MET GLU ARG GLU LEU VAL GLU ILE PHE ARG ALA LEU
SEQRES 10 A 350 GLY TYR GLN ALA VAL GLU GLY PRO GLU VAL GLU SER GLU
SEQRES 11 A 350 PHE PHE ASN PHE ASP ALA LEU ASN ILE PRO GLU HIS HIS
SEQRES 12 A 350 PRO ALA ARG ASP MET TRP ASP THR PHE TRP LEU THR GLY
SEQRES 13 A 350 GLU GLY PHE ARG LEU GLU GLY PRO LEU GLY GLU GLU VAL
SEQRES 14 A 350 GLU GLY ARG LEU LEU LEU ARG THR HIS THR SER PRO MET
SEQRES 15 A 350 GLN VAL ARG TYR MET VAL ALA HIS THR PRO PRO PHE ARG
SEQRES 16 A 350 ILE VAL VAL PRO GLY ARG VAL PHE ARG PHE GLU GLN THR
SEQRES 17 A 350 ASP ALA THR HIS GLU ALA VAL PHE HIS GLN LEU GLU GLY
SEQRES 18 A 350 LEU VAL VAL GLY GLU GLY ILE ALA MET ALA HIS LEU LYS
SEQRES 19 A 350 GLY ALA ILE TYR GLU LEU ALA GLN ALA LEU PHE GLY PRO
SEQRES 20 A 350 ASP SER LYS VAL ARG PHE GLN PRO VAL TYR PHE PRO PHE
SEQRES 21 A 350 VAL GLU PRO GLY ALA GLN PHE ALA VAL TRP TRP PRO GLU
SEQRES 22 A 350 GLY GLY LYS TRP LEU GLU LEU GLY GLY ALA GLY MET VAL
SEQRES 23 A 350 HIS PRO LYS VAL PHE GLN ALA VAL ASP ALA TYR ARG GLU
SEQRES 24 A 350 ARG LEU GLY LEU PRO PRO ALA TYR ARG GLY VAL THR GLY
SEQRES 25 A 350 PHE ALA PHE GLY LEU GLY VAL GLU ARG LEU ALA MET LEU
SEQRES 26 A 350 ARG TYR GLY ILE PRO ASP ILE ARG TYR PHE PHE GLY GLY
SEQRES 27 A 350 ARG LEU LYS PHE LEU GLU GLN PHE LYS GLY VAL LEU
SEQRES 1 B 785 MET ARG VAL PRO PHE SER TRP LEU LYS ALA TYR VAL PRO
SEQRES 2 B 785 GLU LEU GLU SER PRO GLU VAL LEU GLU GLU ARG LEU ALA
SEQRES 3 B 785 GLY LEU GLY PHE GLU THR ASP ARG ILE GLU ARG VAL PHE
SEQRES 4 B 785 PRO ILE PRO ARG GLY VAL VAL PHE ALA ARG VAL LEU GLU
SEQRES 5 B 785 ALA HIS PRO ILE PRO GLY THR ARG LEU LYS ARG LEU VAL
SEQRES 6 B 785 LEU ASP ALA GLY ARG THR VAL GLU VAL VAL SER GLY ALA
SEQRES 7 B 785 GLU ASN ALA ARG LYS GLY ILE GLY VAL ALA LEU ALA LEU
SEQRES 8 B 785 PRO GLY THR GLU LEU PRO GLY LEU GLY GLN LYS VAL GLY
SEQRES 9 B 785 GLU ARG VAL ILE GLN GLY VAL ARG SER PHE GLY MET ALA
SEQRES 10 B 785 LEU SER PRO ARG GLU LEU GLY VAL GLY GLU TYR GLY GLY
SEQRES 11 B 785 GLY LEU LEU GLU PHE PRO GLU ASP ALA LEU PRO PRO GLY
SEQRES 12 B 785 THR PRO LEU SER GLU ALA TRP PRO GLU GLU VAL VAL LEU
SEQRES 13 B 785 ASP LEU GLU VAL THR PRO ASN ARG PRO ASP ALA LEU GLY
SEQRES 14 B 785 LEU LEU GLY LEU ALA ARG ASP LEU HIS ALA LEU GLY TYR
SEQRES 15 B 785 ALA LEU VAL GLU PRO GLU ALA ALA LEU LYS ALA GLU ALA
SEQRES 16 B 785 LEU PRO LEU PRO PHE ALA LEU LYS VAL GLU ASP PRO GLU
SEQRES 17 B 785 GLY ALA PRO HIS PHE THR LEU GLY TYR ALA PHE GLY LEU
SEQRES 18 B 785 ARG VAL ALA PRO SER PRO LEU TRP MET GLN ARG ALA LEU
SEQRES 19 B 785 PHE ALA ALA GLY MET ARG PRO ILE ASN ASN VAL VAL ASP
SEQRES 20 B 785 VAL THR ASN TYR VAL MET LEU GLU ARG ALA GLN PRO MET
SEQRES 21 B 785 HIS ALA PHE ASP LEU ARG PHE VAL GLY GLU GLY ILE ALA
SEQRES 22 B 785 VAL ARG ARG ALA ARG GLU GLY GLU ARG LEU LYS THR LEU
SEQRES 23 B 785 ASP GLY VAL GLU ARG THR LEU HIS PRO GLU ASP LEU VAL
SEQRES 24 B 785 ILE ALA GLY TRP ARG GLY GLU GLU SER PHE PRO LEU GLY
SEQRES 25 B 785 LEU ALA GLY VAL MET GLY GLY ALA GLU SER GLU VAL ARG
SEQRES 26 B 785 GLU ASP THR GLU ALA ILE ALA LEU GLU VAL ALA CYS PHE
SEQRES 27 B 785 ASP PRO VAL SER ILE ARG LYS THR ALA ARG ARG HIS GLY
SEQRES 28 B 785 LEU ARG THR GLU ALA SER HIS ARG PHE GLU ARG GLY VAL
SEQRES 29 B 785 ASP PRO LEU GLY GLN VAL PRO ALA GLN ARG ARG ALA LEU
SEQRES 30 B 785 SER LEU LEU GLN ALA LEU ALA GLY ALA ARG VAL ALA GLU
SEQRES 31 B 785 ALA LEU LEU GLU ALA GLY SER PRO LYS PRO PRO GLU ALA
SEQRES 32 B 785 ILE PRO PHE ARG PRO GLU TYR ALA ASN ARG LEU LEU GLY
SEQRES 33 B 785 THR SER TYR PRO GLU ALA GLU GLN ILE ALA ILE LEU LYS
SEQRES 34 B 785 ARG LEU GLY CYS ARG VAL GLU GLY GLU GLY PRO THR TYR
SEQRES 35 B 785 ARG VAL THR PRO PRO SER HIS ARG LEU ASP LEU ARG LEU
SEQRES 36 B 785 GLU GLU ASP LEU VAL GLU GLU VAL ALA ARG ILE GLN GLY
SEQRES 37 B 785 TYR GLU THR ILE PRO LEU ALA LEU PRO ALA PHE PHE PRO
SEQRES 38 B 785 ALA PRO ASP ASN ARG GLY VAL GLU ALA PRO TYR ARG LYS
SEQRES 39 B 785 GLU GLN ARG LEU ARG GLU VAL LEU SER GLY LEU GLY PHE
SEQRES 40 B 785 GLN GLU VAL TYR THR TYR SER PHE MET ASP PRO GLU ASP
SEQRES 41 B 785 ALA ARG ARG PHE ARG LEU ASP PRO PRO ARG LEU LEU LEU
SEQRES 42 B 785 LEU ASN PRO LEU ALA PRO GLU LYS ALA ALA LEU ARG THR
SEQRES 43 B 785 HIS LEU PHE PRO GLY LEU VAL ARG VAL LEU LYS GLU ASN
SEQRES 44 B 785 LEU ASP LEU ASP ARG PRO GLU ARG ALA LEU LEU PHE GLU
SEQRES 45 B 785 VAL GLY ARG VAL PHE ARG GLU ARG GLU GLU THR HIS LEU
SEQRES 46 B 785 ALA GLY LEU LEU PHE GLY GLU GLY VAL GLY LEU PRO TRP
SEQRES 47 B 785 ALA LYS GLU ARG LEU SER GLY TYR PHE LEU LEU LYS GLY
SEQRES 48 B 785 TYR LEU GLU ALA LEU PHE ALA ARG LEU GLY LEU ALA PHE
SEQRES 49 B 785 ARG VAL GLU ALA GLN ALA PHE PRO PHE LEU HIS PRO GLY
SEQRES 50 B 785 VAL SER GLY ARG VAL LEU VAL GLU GLY GLU GLU VAL GLY
SEQRES 51 B 785 PHE LEU GLY ALA LEU HIS PRO GLU ILE ALA GLN GLU LEU
SEQRES 52 B 785 GLU LEU PRO PRO VAL HIS LEU PHE GLU LEU ARG LEU PRO
SEQRES 53 B 785 LEU PRO ASP LYS PRO LEU ALA PHE GLN ASP PRO SER ARG
SEQRES 54 B 785 HIS PRO ALA ALA PHE ARG ASP LEU ALA VAL VAL VAL PRO
SEQRES 55 B 785 ALA PRO THR PRO TYR GLY GLU VAL GLU ALA LEU VAL ARG
SEQRES 56 B 785 GLU ALA ALA GLY PRO TYR LEU GLU SER LEU ALA LEU PHE
SEQRES 57 B 785 ASP LEU TYR GLN GLY PRO PRO LEU PRO GLU GLY HIS LYS
SEQRES 58 B 785 SER LEU ALA PHE HIS LEU ARG PHE ARG HIS PRO LYS ARG
SEQRES 59 B 785 THR LEU ARG ASP GLU GLU VAL GLU GLU ALA VAL SER ARG
SEQRES 60 B 785 VAL ALA GLU ALA LEU ARG ALA ARG GLY PHE GLY LEU ARG
SEQRES 61 B 785 GLY LEU ASP THR PRO
HET MTY A 351 13
HET MTY B 786 13
HETNAM MTY META-TYROSINE
FORMUL 3 MTY 2(C9 H11 N O3)
FORMUL 5 HOH *241(H2 O)
HELIX 1 1 HIS A 101 ALA A 116 1 16
HELIX 2 2 GLU A 130 PHE A 134 1 5
HELIX 3 3 PRO A 144 TRP A 149 5 6
HELIX 4 4 SER A 180 HIS A 190 1 11
HELIX 5 5 ALA A 229 GLY A 246 1 18
HELIX 6 6 HIS A 287 ARG A 300 1 14
HELIX 7 7 GLU A 320 GLY A 328 1 9
HELIX 8 8 ASP A 331 PHE A 336 5 6
HELIX 9 9 ARG A 339 GLU A 344 1 6
HELIX 10 10 GLN A 345 LYS A 347 5 3
HELIX 11 11 PHE B 5 LYS B 9 1 5
HELIX 12 12 SER B 17 GLY B 29 1 13
HELIX 13 13 LEU B 96 GLY B 100 5 5
HELIX 14 14 SER B 119 GLY B 124 1 6
HELIX 15 15 PRO B 145 TRP B 150 5 6
HELIX 16 16 ARG B 164 LEU B 168 5 5
HELIX 17 17 GLY B 169 LEU B 180 1 12
HELIX 18 18 PRO B 227 ALA B 237 1 11
HELIX 19 19 ASN B 243 ALA B 257 1 15
HELIX 20 20 ARG B 266 VAL B 268 5 3
HELIX 21 21 ASP B 339 GLY B 351 1 13
HELIX 22 22 THR B 354 GLY B 363 1 10
HELIX 23 23 GLY B 368 GLY B 385 1 18
HELIX 24 24 ARG B 407 GLY B 416 1 10
HELIX 25 25 PRO B 420 LEU B 431 1 12
HELIX 26 26 LEU B 455 GLY B 468 1 14
HELIX 27 27 TYR B 469 ILE B 472 5 4
HELIX 28 28 ALA B 482 ARG B 486 5 5
HELIX 29 29 GLU B 489 GLY B 506 1 18
HELIX 30 30 GLU B 519 PHE B 524 1 6
HELIX 31 31 ALA B 538 ALA B 542 5 5
HELIX 32 32 LEU B 548 ASP B 563 1 16
HELIX 33 33 SER B 604 GLY B 621 1 18
HELIX 34 34 HIS B 656 GLU B 664 1 9
HELIX 35 35 PRO B 706 ALA B 718 1 13
HELIX 36 36 ARG B 757 ALA B 774 1 18
SHEET 1 A 7 GLN A 120 ALA A 121 0
SHEET 2 A 7 PHE A 194 PHE A 203 1 O VAL A 197 N GLN A 120
SHEET 3 A 7 VAL A 215 GLY A 225 -1 O GLU A 220 N VAL A 198
SHEET 4 A 7 THR A 311 GLY A 318 -1 O THR A 311 N GLY A 225
SHEET 5 A 7 LYS A 276 VAL A 286 -1 N GLY A 284 O ALA A 314
SHEET 6 A 7 VAL A 261 TRP A 271 -1 N VAL A 269 O LEU A 278
SHEET 7 A 7 VAL A 251 PRO A 255 -1 N ARG A 252 O ALA A 268
SHEET 1 B 4 VAL A 127 SER A 129 0
SHEET 2 B 4 LEU A 173 LEU A 175 -1 O LEU A 174 N GLU A 128
SHEET 3 B 4 PHE A 152 THR A 155 -1 N PHE A 152 O LEU A 175
SHEET 4 B 4 LEU B 532 LEU B 533 -1 O LEU B 532 N THR A 155
SHEET 1 C 3 ARG B 2 PRO B 4 0
SHEET 2 C 3 VAL B 154 ASP B 157 -1 O LEU B 156 N VAL B 3
SHEET 3 C 3 ILE B 35 ARG B 37 -1 N GLU B 36 O VAL B 155
SHEET 1 D 5 THR B 71 SER B 76 0
SHEET 2 D 5 LYS B 62 ASP B 67 -1 N LYS B 62 O SER B 76
SHEET 3 D 5 VAL B 45 PRO B 55 -1 N HIS B 54 O ARG B 63
SHEET 4 D 5 GLY B 86 ALA B 90 -1 O VAL B 87 N ALA B 48
SHEET 5 D 5 MET B 116 ALA B 117 -1 O MET B 116 N ALA B 90
SHEET 1 E 2 VAL B 107 ILE B 108 0
SHEET 2 E 2 VAL B 111 ARG B 112 -1 O VAL B 111 N ILE B 108
SHEET 1 F 5 ALA B 193 GLU B 194 0
SHEET 2 F 5 ARG B 387 ALA B 395 1 O VAL B 388 N GLU B 194
SHEET 3 F 5 HIS B 212 PHE B 219 -1 N PHE B 213 O ALA B 395
SHEET 4 F 5 ALA B 330 CYS B 337 -1 O LEU B 333 N GLY B 216
SHEET 5 F 5 HIS B 261 ASP B 264 -1 N HIS B 261 O GLU B 334
SHEET 1 G 5 ALA B 201 VAL B 204 0
SHEET 2 G 5 GLY B 271 ARG B 275 1 O ILE B 272 N ALA B 201
SHEET 3 G 5 VAL B 299 ARG B 304 -1 O ALA B 301 N ALA B 273
SHEET 4 G 5 GLU B 307 LEU B 313 -1 O LEU B 311 N ILE B 300
SHEET 5 G 5 MET B 317 GLY B 318 -1 O MET B 317 N LEU B 313
SHEET 1 H 2 ARG B 282 LYS B 284 0
SHEET 2 H 2 GLU B 290 THR B 292 -1 O ARG B 291 N LEU B 283
SHEET 1 I 3 ILE B 404 PHE B 406 0
SHEET 2 I 3 TYR B 442 THR B 445 -1 O VAL B 444 N ILE B 404
SHEET 3 I 3 ARG B 434 GLU B 436 -1 N GLU B 436 O ARG B 443
SHEET 1 J 7 GLN B 508 VAL B 510 0
SHEET 2 J 7 LEU B 570 PHE B 577 1 O PHE B 571 N VAL B 510
SHEET 3 J 7 GLU B 581 LEU B 588 -1 O ALA B 586 N GLU B 572
SHEET 4 J 7 HIS B 669 ARG B 674 -1 O LEU B 673 N LEU B 585
SHEET 5 J 7 GLU B 647 LEU B 655 -1 N GLY B 653 O LEU B 670
SHEET 6 J 7 LEU B 634 VAL B 644 -1 N VAL B 642 O GLY B 650
SHEET 7 J 7 PHE B 624 ARG B 625 -1 N ARG B 625 O LEU B 643
SHEET 1 K 2 PHE B 515 MET B 516 0
SHEET 2 K 2 ALA B 543 LEU B 544 -1 O ALA B 543 N MET B 516
SHEET 1 L 2 VAL B 594 GLY B 595 0
SHEET 2 L 2 ARG B 602 LEU B 603 -1 O LEU B 603 N VAL B 594
SHEET 1 M 3 ALA B 693 PRO B 702 0
SHEET 2 M 3 HIS B 740 PHE B 749 -1 O PHE B 745 N LEU B 697
SHEET 3 M 3 LEU B 722 TYR B 731 -1 N ASP B 729 O ALA B 744
CISPEP 1 PRO A 192 PRO A 193 0 0.19
CISPEP 2 GLU A 262 PRO A 263 0 -0.23
CISPEP 3 GLY B 439 PRO B 440 0 0.37
CISPEP 4 LEU B 675 PRO B 676 0 0.32
CISPEP 5 PRO B 734 PRO B 735 0 -0.16
SITE 1 AC1 16 HIS A 178 SER A 180 GLN A 183 ARG A 204
SITE 2 AC1 16 GLN A 218 GLU A 220 PHE A 258 PHE A 260
SITE 3 AC1 16 GLY A 282 ALA A 283 ALA A 314 PHE A 315
SITE 4 AC1 16 GLY A 316 HOH A 352 HOH A 381 HOH A 394
SITE 1 AC2 10 PRO B 259 HIS B 261 LEU B 286 LEU B 313
SITE 2 AC2 10 GLY B 315 MET B 317 GLY B 318 GLU B 334
SITE 3 AC2 10 HOH B 824 HOH B 876
CRYST1 173.181 173.181 138.852 90.00 90.00 120.00 P 32 2 1 6
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 0.005774 0.003334 0.000000 0.00000
SCALE2 0.000000 0.006668 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007202 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
