HEADER LIGASE/RNA 21-FEB-05 1WZ2
TITLE THE CRYSTAL STRUCTURE OF LEUCYL-TRNA SYNTHETASE AND TRNA(LEUCINE)
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRNA;
COMPND 3 CHAIN: C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: LEUCYL-TRNA SYNTHETASE;
COMPND 7 CHAIN: A, B;
COMPND 8 SYNONYM: LEUCINE--TRNA LIGASE, LEURS;
COMPND 9 EC: 6.1.1.4;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 5 ORGANISM_TAXID: 70601;
SOURCE 6 STRAIN: OT3;
SOURCE 7 GENE: LEUS;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET16B
KEYWDS LIGASE, TRNA, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 2 STRUCTURAL GENOMICS, LIGASE-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.FUKUNAGA,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR 2 (RSGI)
REVDAT 4 13-MAR-24 1WZ2 1 REMARK
REVDAT 3 13-JUL-11 1WZ2 1 VERSN
REVDAT 2 24-FEB-09 1WZ2 1 VERSN
REVDAT 1 06-SEP-05 1WZ2 0
JRNL AUTH R.FUKUNAGA,S.YOKOYAMA
JRNL TITL THE CRYSTAL STRUCTURE OF LEUCYL-TRNA SYNTHETASE AND
JRNL TITL 2 TRNA(LEUCINE) COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2991506.040
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.7
REMARK 3 NUMBER OF REFLECTIONS : 49242
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 SET) : 0.241
REMARK 3 FREE R VALUE : 0.305
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4960
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5961
REMARK 3 BIN R VALUE (WORKING SET) : 0.3150
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 669
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15818
REMARK 3 NUCLEIC ACID ATOMS : 3760
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.09000
REMARK 3 B22 (A**2) : -6.45000
REMARK 3 B33 (A**2) : 6.35000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM SIGMAA (A) : 0.56
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.53
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.65
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.610
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.310 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.340 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.460 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.440 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.23
REMARK 3 BSOL : 26.55
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : DNA-RNA.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WZ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000024173.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 173
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% ISOPROPANOL, 200MM TRI-SODIUM
REMARK 280 CITRATE, 100MM SODIUM CACODYLATE BUFFER, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 60.27300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 115.56350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.27300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 115.56350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 APPLY THE FOLLOWING TO CHAINS: C, A
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 ALA A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 357
REMARK 465 ASN A 358
REMARK 465 ILE A 359
REMARK 465 THR A 360
REMARK 465 TYR A 361
REMARK 465 ILE A 362
REMARK 465 SER A 363
REMARK 465 LEU A 364
REMARK 465 ILE A 365
REMARK 465 LYS A 366
REMARK 465 LEU A 367
REMARK 465 GLU A 368
REMARK 465 GLY A 369
REMARK 465 TYR A 370
REMARK 465 GLY A 371
REMARK 465 ASP A 372
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 357
REMARK 465 ASN B 358
REMARK 465 ILE B 359
REMARK 465 THR B 360
REMARK 465 TYR B 361
REMARK 465 ILE B 362
REMARK 465 SER B 363
REMARK 465 LEU B 364
REMARK 465 ILE B 365
REMARK 465 LYS B 366
REMARK 465 LEU B 367
REMARK 465 GLU B 368
REMARK 465 GLY B 369
REMARK 465 TYR B 370
REMARK 465 GLY B 371
REMARK 465 ASP B 372
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 ARG A 928 N ALA A 930 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 G C 901 P G C 901 OP3 -0.086
REMARK 500 G D 901 P G D 901 OP3 -0.085
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 G C 907 N9 - C1' - C2' ANGL. DEV. = 9.3 DEGREES
REMARK 500 G C 919 N9 - C1' - C2' ANGL. DEV. = 10.1 DEGREES
REMARK 500 A C 953 C1' - O4' - C4' ANGL. DEV. = -4.4 DEGREES
REMARK 500 A C 953 N9 - C1' - C2' ANGL. DEV. = 8.3 DEGREES
REMARK 500 G D 920 N9 - C1' - C2' ANGL. DEV. = 9.2 DEGREES
REMARK 500 G D 920 O4' - C1' - N9 ANGL. DEV. = 4.4 DEGREES
REMARK 500 A D 953 N9 - C1' - C2' ANGL. DEV. = 9.6 DEGREES
REMARK 500 PRO A 157 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU A 675 CA - CB - CG ANGL. DEV. = 23.7 DEGREES
REMARK 500 VAL A 815 CB - CA - C ANGL. DEV. = -15.2 DEGREES
REMARK 500 PRO B 157 C - N - CA ANGL. DEV. = 9.7 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 ASN A 5 -65.76 -146.02
REMARK 500 PHE A 6 -13.55 65.58
REMARK 500 PRO A 25 152.92 -49.99
REMARK 500 GLU A 33 6.36 -69.06
REMARK 500 PHE A 36 68.35 -155.64
REMARK 500 LEU A 45 89.31 -53.43
REMARK 500 ASN A 73 24.06 -66.32
REMARK 500 VAL A 74 132.59 -15.48
REMARK 500 THR A 83 106.93 -47.27
REMARK 500 ALA A 91 -70.13 -46.58
REMARK 500 ASN A 96 3.57 -57.95
REMARK 500 LYS A 110 99.55 36.77
REMARK 500 PRO A 112 108.58 -45.62
REMARK 500 GLU A 113 -41.41 -24.10
REMARK 500 GLU A 114 -76.34 -64.46
REMARK 500 TRP A 117 -28.12 -39.39
REMARK 500 ALA A 133 -68.50 -90.14
REMARK 500 SER A 143 17.08 -58.81
REMARK 500 THR A 153 -178.68 75.58
REMARK 500 PRO A 157 -54.88 -20.44
REMARK 500 HIS A 181 112.11 171.89
REMARK 500 VAL A 183 125.63 166.46
REMARK 500 PRO A 187 13.59 -65.98
REMARK 500 VAL A 188 -90.90 -52.29
REMARK 500 THR A 191 127.90 173.56
REMARK 500 HIS A 196 -38.51 -133.12
REMARK 500 LYS A 213 88.71 -65.36
REMARK 500 ASN A 219 -143.43 32.86
REMARK 500 GLU A 221 -159.18 -146.64
REMARK 500 VAL A 222 162.37 -49.01
REMARK 500 ILE A 223 133.37 175.95
REMARK 500 TYR A 236 4.88 -64.14
REMARK 500 ASN A 240 168.81 162.65
REMARK 500 ASN A 246 -71.70 -48.60
REMARK 500 ARG A 256 -139.87 -118.31
REMARK 500 ASP A 258 -44.49 -144.31
REMARK 500 TYR A 271 -72.88 -39.54
REMARK 500 GLN A 276 27.58 -56.05
REMARK 500 VAL A 282 171.18 -55.51
REMARK 500 ILE A 283 -44.35 -155.70
REMARK 500 PHE A 286 -158.66 -112.34
REMARK 500 LYS A 294 155.20 -43.12
REMARK 500 SER A 301 -130.35 -76.76
REMARK 500 ASP A 303 178.57 -56.44
REMARK 500 ALA A 318 -137.58 70.50
REMARK 500 HIS A 328 -94.40 -141.64
REMARK 500 ALA A 329 97.35 -29.36
REMARK 500 PRO A 330 -13.00 -46.59
REMARK 500 HIS A 333 1.05 161.99
REMARK 500 GLU A 337 78.90 -64.77
REMARK 500
REMARK 500 THIS ENTRY HAS 366 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 G C 907 0.05 SIDE CHAIN
REMARK 500 G C 919 0.09 SIDE CHAIN
REMARK 500 G C 920 0.06 SIDE CHAIN
REMARK 500 U C 921 0.07 SIDE CHAIN
REMARK 500 G C 926 0.05 SIDE CHAIN
REMARK 500 U C 959 0.09 SIDE CHAIN
REMARK 500 G D 919 0.07 SIDE CHAIN
REMARK 500 G D 920 0.06 SIDE CHAIN
REMARK 500 G D 926 0.05 SIDE CHAIN
REMARK 500 A D 953 0.07 SIDE CHAIN
REMARK 500 U D 959 0.07 SIDE CHAIN
REMARK 500 TYR A 535 0.07 SIDE CHAIN
REMARK 500 TYR A 767 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PHO001000965.2 RELATED DB: TARGETDB
DBREF 1WZ2 A 1 967 UNP O58698 SYL_PYRHO 1 967
DBREF 1WZ2 B 1 967 UNP O58698 SYL_PYRHO 1 967
DBREF 1WZ2 C 901 988 PDB 1WZ2 1WZ2 901 988
DBREF 1WZ2 D 901 988 PDB 1WZ2 1WZ2 901 988
SEQRES 1 C 88 G C G G G G G U U G C C G
SEQRES 2 C 88 A G C C U G G U C A A A G
SEQRES 3 C 88 G C G G G G G A C U C A A
SEQRES 4 C 88 G A U C C C C U C C C G U
SEQRES 5 C 88 A G G G G U U C C G G G G
SEQRES 6 C 88 U U C G A A U C C C C G C
SEQRES 7 C 88 C C C C G C A C C A
SEQRES 1 D 88 G C G G G G G U U G C C G
SEQRES 2 D 88 A G C C U G G U C A A A G
SEQRES 3 D 88 G C G G G G G A C U C A A
SEQRES 4 D 88 G A U C C C C U C C C G U
SEQRES 5 D 88 A G G G G U U C C G G G G
SEQRES 6 D 88 U U C G A A U C C C C G C
SEQRES 7 D 88 C C C C G C A C C A
SEQRES 1 A 967 MET ALA GLU LEU ASN PHE LYS ALA ILE GLU GLU LYS TRP
SEQRES 2 A 967 GLN LYS ARG TRP LEU GLU ALA LYS ILE PHE GLU PRO ASN
SEQRES 3 A 967 ILE ARG ASP LYS PRO LYS GLU LYS LYS PHE TYR ILE THR
SEQRES 4 A 967 VAL ALA PHE PRO TYR LEU SER GLY HIS LEU HIS VAL GLY
SEQRES 5 A 967 HIS ALA ARG THR TYR THR ILE PRO ASP VAL ILE ALA ARG
SEQRES 6 A 967 PHE LYS ARG MET GLN GLY TYR ASN VAL LEU PHE PRO MET
SEQRES 7 A 967 ALA TRP HIS ILE THR GLY SER PRO ILE VAL GLY ILE ALA
SEQRES 8 A 967 GLU ARG ILE LYS ASN ARG ASP PRO LYS THR ILE TRP ILE
SEQRES 9 A 967 TYR ARG ASP VAL TYR LYS VAL PRO GLU GLU ILE LEU TRP
SEQRES 10 A 967 THR PHE GLU ASP PRO ILE ASN ILE VAL LYS TYR PHE MET
SEQRES 11 A 967 LYS ALA ALA LYS GLU THR PHE ILE ARG ALA GLY PHE SER
SEQRES 12 A 967 VAL ASP TRP SER ARG GLU PHE TYR THR THR SER LEU PHE
SEQRES 13 A 967 PRO PRO PHE SER LYS PHE ILE GLU TRP GLN PHE TRP LYS
SEQRES 14 A 967 LEU LYS GLU LYS GLY TYR ILE VAL LYS GLY ALA HIS ARG
SEQRES 15 A 967 VAL ARG TRP ASP PRO VAL VAL GLY THR PRO LEU GLY ASP
SEQRES 16 A 967 HIS ASP LEU MET GLU GLY GLU ASP VAL PRO ILE LEU ASP
SEQRES 17 A 967 TYR ILE ILE ILE LYS PHE GLU LEU ARG GLU ASN GLY GLU
SEQRES 18 A 967 VAL ILE TYR LEU PRO ALA ALA THR LEU ARG PRO GLU THR
SEQRES 19 A 967 VAL TYR GLY VAL THR ASN MET TRP VAL ASN PRO ASN ALA
SEQRES 20 A 967 THR TYR VAL LYS ALA LYS VAL ARG ARG LYS ASP LYS GLU
SEQRES 21 A 967 GLU THR TRP ILE VAL SER LYS GLU ALA ALA TYR LYS LEU
SEQRES 22 A 967 SER PHE GLN ASP ARG GLU ILE GLU VAL ILE GLU GLU PHE
SEQRES 23 A 967 LYS GLY GLU LYS LEU ILE GLY LYS TYR VAL ARG ASN PRO
SEQRES 24 A 967 VAL SER GLY ASP GLU VAL ILE ILE LEU PRO ALA GLU PHE
SEQRES 25 A 967 VAL ASP PRO ASP ASN ALA THR GLY VAL VAL MET SER VAL
SEQRES 26 A 967 PRO ALA HIS ALA PRO PHE ASP HIS VAL ALA LEU GLU ASP
SEQRES 27 A 967 LEU LYS ARG GLU THR GLU ILE LEU GLU LYS TYR ASP ILE
SEQRES 28 A 967 ASP PRO ARG ILE VAL GLU ASN ILE THR TYR ILE SER LEU
SEQRES 29 A 967 ILE LYS LEU GLU GLY TYR GLY ASP PHE PRO ALA VAL GLU
SEQRES 30 A 967 GLU VAL ASN LYS LEU GLY ILE LYS SER GLN LYS ASP LYS
SEQRES 31 A 967 GLU LYS LEU GLU GLN ALA THR LYS THR ILE TYR LYS ALA
SEQRES 32 A 967 GLU TYR HIS LYS GLY ILE PHE LYS VAL PRO PRO TYR GLU
SEQRES 33 A 967 GLY LYS PRO VAL GLN GLU VAL LYS GLU ALA ILE ALA LYS
SEQRES 34 A 967 GLU MET LEU GLU LYS GLY ILE ALA GLU ILE MET TYR GLU
SEQRES 35 A 967 PHE ALA GLU LYS ASN VAL ILE SER ARG PHE GLY ASN ARG
SEQRES 36 A 967 ALA VAL ILE LYS ILE ILE HIS ASP GLN TRP PHE ILE ASP
SEQRES 37 A 967 TYR GLY ASN PRO GLU TRP LYS GLU LYS ALA ARG LYS ALA
SEQRES 38 A 967 LEU GLU ARG MET LYS ILE LEU PRO GLU THR ARG ARG ALA
SEQRES 39 A 967 GLN PHE GLU ALA ILE ILE ASP TRP LEU ASP LYS LYS ALA
SEQRES 40 A 967 CYS ALA ARG LYS ILE GLY LEU GLY THR PRO LEU PRO TRP
SEQRES 41 A 967 ASP PRO GLU TRP VAL ILE GLU SER LEU SER ASP SER THR
SEQRES 42 A 967 ILE TYR MET ALA TYR TYR THR ILE SER ARG HIS ILE ASN
SEQRES 43 A 967 LYS LEU ARG GLN GLU GLY LYS LEU ASP PRO GLU LYS LEU
SEQRES 44 A 967 THR PRO GLU PHE PHE ASP TYR ILE PHE LEU GLU GLU PHE
SEQRES 45 A 967 SER GLU ASP LYS GLU LYS GLU LEU GLU LYS LYS THR GLY
SEQRES 46 A 967 ILE PRO ALA GLU ILE ILE HIS GLU MET LYS GLU GLU PHE
SEQRES 47 A 967 GLU TYR TRP TYR PRO LEU ASP TRP ARG CYS SER GLY LYS
SEQRES 48 A 967 ASP LEU ILE PRO ASN HIS LEU THR PHE PHE ILE PHE ASN
SEQRES 49 A 967 HIS VAL ALA ILE PHE ARG GLU GLU HIS TRP PRO LYS GLY
SEQRES 50 A 967 ILE ALA VAL ASN GLY PHE GLY THR LEU GLU GLY GLN LYS
SEQRES 51 A 967 MET SER LYS SER LYS GLY ASN VAL LEU ASN PHE ILE ASP
SEQRES 52 A 967 ALA ILE GLU GLU ASN GLY ALA ASP VAL VAL ARG LEU TYR
SEQRES 53 A 967 ILE MET SER LEU ALA GLU HIS ASP SER ASP PHE ASP TRP
SEQRES 54 A 967 ARG ARG LYS GLU VAL GLY LYS LEU ARG LYS GLN ILE GLU
SEQRES 55 A 967 ARG PHE TYR GLU LEU ILE SER GLN PHE ALA GLU TYR GLU
SEQRES 56 A 967 VAL LYS GLY ASN VAL GLU LEU LYS ASP ILE ASP ARG TRP
SEQRES 57 A 967 MET LEU HIS ARG LEU ASN LYS ALA ILE LYS GLU THR THR
SEQRES 58 A 967 ASN ALA LEU GLU GLU PHE ARG THR ARG THR ALA VAL GLN
SEQRES 59 A 967 TRP ALA PHE TYR SER ILE MET ASN ASP LEU ARG TRP TYR
SEQRES 60 A 967 LEU ARG ARG THR GLU GLY ARG ASP ASP GLU ALA LYS ARG
SEQRES 61 A 967 TYR VAL LEU ARG THR LEU ALA ASP VAL TRP VAL ARG LEU
SEQRES 62 A 967 MET ALA PRO PHE THR PRO HIS ILE CYS GLU GLU LEU TRP
SEQRES 63 A 967 GLU LYS LEU GLY GLY GLU GLY PHE VAL SER LEU ALA LYS
SEQRES 64 A 967 TRP PRO GLU PRO VAL GLU GLU TRP TRP ASN GLU THR ILE
SEQRES 65 A 967 GLU ALA GLU GLU GLU PHE ILE ARG SER VAL MET GLU ASP
SEQRES 66 A 967 ILE LYS GLU ILE ILE GLU VAL ALA LYS ILE GLU ASN ALA
SEQRES 67 A 967 LYS ARG ALA TYR ILE TYR THR ALA GLU ASP TRP LYS TRP
SEQRES 68 A 967 LYS VAL ALA GLU VAL VAL SER GLU LYS ARG ASP PHE LYS
SEQRES 69 A 967 SER SER MET GLU GLU LEU MET LYS ASP SER GLU ILE ARG
SEQRES 70 A 967 LYS HIS GLY LYS GLU VAL ALA LYS ILE VAL GLN LYS LEU
SEQRES 71 A 967 ILE LYS GLU ARG THR PHE ASP VAL LYS ARG ILE ASN GLU
SEQRES 72 A 967 GLU LYS ALA LEU ARG GLU ALA LYS GLU PHE MET GLU LYS
SEQRES 73 A 967 GLU LEU GLY ILE GLU ILE ILE ILE ASN PRO THR GLU ASP
SEQRES 74 A 967 LYS GLY GLY LYS LYS LYS GLN ALA MET PRO LEU LYS PRO
SEQRES 75 A 967 ALA ILE PHE ILE GLU
SEQRES 1 B 967 MET ALA GLU LEU ASN PHE LYS ALA ILE GLU GLU LYS TRP
SEQRES 2 B 967 GLN LYS ARG TRP LEU GLU ALA LYS ILE PHE GLU PRO ASN
SEQRES 3 B 967 ILE ARG ASP LYS PRO LYS GLU LYS LYS PHE TYR ILE THR
SEQRES 4 B 967 VAL ALA PHE PRO TYR LEU SER GLY HIS LEU HIS VAL GLY
SEQRES 5 B 967 HIS ALA ARG THR TYR THR ILE PRO ASP VAL ILE ALA ARG
SEQRES 6 B 967 PHE LYS ARG MET GLN GLY TYR ASN VAL LEU PHE PRO MET
SEQRES 7 B 967 ALA TRP HIS ILE THR GLY SER PRO ILE VAL GLY ILE ALA
SEQRES 8 B 967 GLU ARG ILE LYS ASN ARG ASP PRO LYS THR ILE TRP ILE
SEQRES 9 B 967 TYR ARG ASP VAL TYR LYS VAL PRO GLU GLU ILE LEU TRP
SEQRES 10 B 967 THR PHE GLU ASP PRO ILE ASN ILE VAL LYS TYR PHE MET
SEQRES 11 B 967 LYS ALA ALA LYS GLU THR PHE ILE ARG ALA GLY PHE SER
SEQRES 12 B 967 VAL ASP TRP SER ARG GLU PHE TYR THR THR SER LEU PHE
SEQRES 13 B 967 PRO PRO PHE SER LYS PHE ILE GLU TRP GLN PHE TRP LYS
SEQRES 14 B 967 LEU LYS GLU LYS GLY TYR ILE VAL LYS GLY ALA HIS ARG
SEQRES 15 B 967 VAL ARG TRP ASP PRO VAL VAL GLY THR PRO LEU GLY ASP
SEQRES 16 B 967 HIS ASP LEU MET GLU GLY GLU ASP VAL PRO ILE LEU ASP
SEQRES 17 B 967 TYR ILE ILE ILE LYS PHE GLU LEU ARG GLU ASN GLY GLU
SEQRES 18 B 967 VAL ILE TYR LEU PRO ALA ALA THR LEU ARG PRO GLU THR
SEQRES 19 B 967 VAL TYR GLY VAL THR ASN MET TRP VAL ASN PRO ASN ALA
SEQRES 20 B 967 THR TYR VAL LYS ALA LYS VAL ARG ARG LYS ASP LYS GLU
SEQRES 21 B 967 GLU THR TRP ILE VAL SER LYS GLU ALA ALA TYR LYS LEU
SEQRES 22 B 967 SER PHE GLN ASP ARG GLU ILE GLU VAL ILE GLU GLU PHE
SEQRES 23 B 967 LYS GLY GLU LYS LEU ILE GLY LYS TYR VAL ARG ASN PRO
SEQRES 24 B 967 VAL SER GLY ASP GLU VAL ILE ILE LEU PRO ALA GLU PHE
SEQRES 25 B 967 VAL ASP PRO ASP ASN ALA THR GLY VAL VAL MET SER VAL
SEQRES 26 B 967 PRO ALA HIS ALA PRO PHE ASP HIS VAL ALA LEU GLU ASP
SEQRES 27 B 967 LEU LYS ARG GLU THR GLU ILE LEU GLU LYS TYR ASP ILE
SEQRES 28 B 967 ASP PRO ARG ILE VAL GLU ASN ILE THR TYR ILE SER LEU
SEQRES 29 B 967 ILE LYS LEU GLU GLY TYR GLY ASP PHE PRO ALA VAL GLU
SEQRES 30 B 967 GLU VAL ASN LYS LEU GLY ILE LYS SER GLN LYS ASP LYS
SEQRES 31 B 967 GLU LYS LEU GLU GLN ALA THR LYS THR ILE TYR LYS ALA
SEQRES 32 B 967 GLU TYR HIS LYS GLY ILE PHE LYS VAL PRO PRO TYR GLU
SEQRES 33 B 967 GLY LYS PRO VAL GLN GLU VAL LYS GLU ALA ILE ALA LYS
SEQRES 34 B 967 GLU MET LEU GLU LYS GLY ILE ALA GLU ILE MET TYR GLU
SEQRES 35 B 967 PHE ALA GLU LYS ASN VAL ILE SER ARG PHE GLY ASN ARG
SEQRES 36 B 967 ALA VAL ILE LYS ILE ILE HIS ASP GLN TRP PHE ILE ASP
SEQRES 37 B 967 TYR GLY ASN PRO GLU TRP LYS GLU LYS ALA ARG LYS ALA
SEQRES 38 B 967 LEU GLU ARG MET LYS ILE LEU PRO GLU THR ARG ARG ALA
SEQRES 39 B 967 GLN PHE GLU ALA ILE ILE ASP TRP LEU ASP LYS LYS ALA
SEQRES 40 B 967 CYS ALA ARG LYS ILE GLY LEU GLY THR PRO LEU PRO TRP
SEQRES 41 B 967 ASP PRO GLU TRP VAL ILE GLU SER LEU SER ASP SER THR
SEQRES 42 B 967 ILE TYR MET ALA TYR TYR THR ILE SER ARG HIS ILE ASN
SEQRES 43 B 967 LYS LEU ARG GLN GLU GLY LYS LEU ASP PRO GLU LYS LEU
SEQRES 44 B 967 THR PRO GLU PHE PHE ASP TYR ILE PHE LEU GLU GLU PHE
SEQRES 45 B 967 SER GLU ASP LYS GLU LYS GLU LEU GLU LYS LYS THR GLY
SEQRES 46 B 967 ILE PRO ALA GLU ILE ILE HIS GLU MET LYS GLU GLU PHE
SEQRES 47 B 967 GLU TYR TRP TYR PRO LEU ASP TRP ARG CYS SER GLY LYS
SEQRES 48 B 967 ASP LEU ILE PRO ASN HIS LEU THR PHE PHE ILE PHE ASN
SEQRES 49 B 967 HIS VAL ALA ILE PHE ARG GLU GLU HIS TRP PRO LYS GLY
SEQRES 50 B 967 ILE ALA VAL ASN GLY PHE GLY THR LEU GLU GLY GLN LYS
SEQRES 51 B 967 MET SER LYS SER LYS GLY ASN VAL LEU ASN PHE ILE ASP
SEQRES 52 B 967 ALA ILE GLU GLU ASN GLY ALA ASP VAL VAL ARG LEU TYR
SEQRES 53 B 967 ILE MET SER LEU ALA GLU HIS ASP SER ASP PHE ASP TRP
SEQRES 54 B 967 ARG ARG LYS GLU VAL GLY LYS LEU ARG LYS GLN ILE GLU
SEQRES 55 B 967 ARG PHE TYR GLU LEU ILE SER GLN PHE ALA GLU TYR GLU
SEQRES 56 B 967 VAL LYS GLY ASN VAL GLU LEU LYS ASP ILE ASP ARG TRP
SEQRES 57 B 967 MET LEU HIS ARG LEU ASN LYS ALA ILE LYS GLU THR THR
SEQRES 58 B 967 ASN ALA LEU GLU GLU PHE ARG THR ARG THR ALA VAL GLN
SEQRES 59 B 967 TRP ALA PHE TYR SER ILE MET ASN ASP LEU ARG TRP TYR
SEQRES 60 B 967 LEU ARG ARG THR GLU GLY ARG ASP ASP GLU ALA LYS ARG
SEQRES 61 B 967 TYR VAL LEU ARG THR LEU ALA ASP VAL TRP VAL ARG LEU
SEQRES 62 B 967 MET ALA PRO PHE THR PRO HIS ILE CYS GLU GLU LEU TRP
SEQRES 63 B 967 GLU LYS LEU GLY GLY GLU GLY PHE VAL SER LEU ALA LYS
SEQRES 64 B 967 TRP PRO GLU PRO VAL GLU GLU TRP TRP ASN GLU THR ILE
SEQRES 65 B 967 GLU ALA GLU GLU GLU PHE ILE ARG SER VAL MET GLU ASP
SEQRES 66 B 967 ILE LYS GLU ILE ILE GLU VAL ALA LYS ILE GLU ASN ALA
SEQRES 67 B 967 LYS ARG ALA TYR ILE TYR THR ALA GLU ASP TRP LYS TRP
SEQRES 68 B 967 LYS VAL ALA GLU VAL VAL SER GLU LYS ARG ASP PHE LYS
SEQRES 69 B 967 SER SER MET GLU GLU LEU MET LYS ASP SER GLU ILE ARG
SEQRES 70 B 967 LYS HIS GLY LYS GLU VAL ALA LYS ILE VAL GLN LYS LEU
SEQRES 71 B 967 ILE LYS GLU ARG THR PHE ASP VAL LYS ARG ILE ASN GLU
SEQRES 72 B 967 GLU LYS ALA LEU ARG GLU ALA LYS GLU PHE MET GLU LYS
SEQRES 73 B 967 GLU LEU GLY ILE GLU ILE ILE ILE ASN PRO THR GLU ASP
SEQRES 74 B 967 LYS GLY GLY LYS LYS LYS GLN ALA MET PRO LEU LYS PRO
SEQRES 75 B 967 ALA ILE PHE ILE GLU
HELIX 1 1 PHE A 6 LYS A 21 1 16
HELIX 2 2 ASN A 26 LYS A 30 5 5
HELIX 3 3 PRO A 31 LYS A 35 5 5
HELIX 4 4 HIS A 50 GLN A 70 1 21
HELIX 5 5 SER A 85 ASN A 96 1 12
HELIX 6 6 ASP A 98 ASP A 107 1 10
HELIX 7 7 PRO A 112 THR A 118 1 7
HELIX 8 8 ASP A 121 ARG A 139 1 19
HELIX 9 9 PHE A 156 LEU A 170 1 15
HELIX 10 10 ARG A 231 VAL A 238 5 8
HELIX 11 11 LYS A 267 GLN A 276 1 10
HELIX 12 12 LYS A 392 THR A 397 1 6
HELIX 13 13 LYS A 398 LYS A 407 1 10
HELIX 14 14 PRO A 419 LYS A 424 1 6
HELIX 15 15 ILE A 427 LYS A 434 1 8
HELIX 16 16 GLU A 473 GLU A 483 1 11
HELIX 17 17 ARG A 492 TRP A 502 1 11
HELIX 18 18 GLU A 527 SER A 532 1 6
HELIX 19 19 TYR A 535 GLU A 551 1 17
HELIX 20 20 ASP A 555 LEU A 559 5 5
HELIX 21 21 THR A 560 ILE A 567 1 8
HELIX 22 22 SER A 573 GLY A 585 1 13
HELIX 23 23 PRO A 587 TYR A 602 1 16
HELIX 24 24 ASP A 612 ILE A 614 5 3
HELIX 25 25 ASN A 616 PHE A 629 1 14
HELIX 26 26 ASN A 660 GLU A 667 1 8
HELIX 27 27 GLY A 669 ALA A 681 1 13
HELIX 28 28 ARG A 690 GLU A 713 1 24
HELIX 29 29 LYS A 723 GLU A 746 1 24
HELIX 30 30 ARG A 748 PHE A 757 1 10
HELIX 31 31 PHE A 757 THR A 771 1 15
HELIX 32 32 ASP A 776 ALA A 795 1 20
HELIX 33 33 THR A 798 LEU A 809 1 12
HELIX 34 34 PHE A 814 ALA A 818 5 5
HELIX 35 35 ASN A 829 VAL A 852 1 24
HELIX 36 36 VAL A 873 SER A 878 1 6
HELIX 37 37 LYS A 884 LYS A 892 1 9
HELIX 38 38 HIS A 899 VAL A 903 5 5
HELIX 39 39 ALA A 904 ILE A 911 1 8
HELIX 40 40 ILE A 921 ARG A 928 1 8
HELIX 41 41 ALA A 930 GLY A 939 1 10
HELIX 42 42 PHE B 6 LYS B 21 1 16
HELIX 43 43 PRO B 31 LYS B 35 5 5
HELIX 44 44 HIS B 50 GLN B 70 1 21
HELIX 45 45 SER B 85 ASN B 96 1 12
HELIX 46 46 ASP B 98 ASP B 107 1 10
HELIX 47 47 PRO B 112 THR B 118 1 7
HELIX 48 48 ASP B 121 ARG B 139 1 19
HELIX 49 49 PHE B 156 LEU B 170 1 15
HELIX 50 50 ARG B 231 VAL B 238 5 8
HELIX 51 51 LYS B 267 GLN B 276 1 10
HELIX 52 52 LYS B 392 THR B 397 1 6
HELIX 53 53 LYS B 398 LYS B 407 1 10
HELIX 54 54 PRO B 419 LYS B 424 1 6
HELIX 55 55 ILE B 427 LYS B 434 1 8
HELIX 56 56 GLU B 473 GLU B 483 1 11
HELIX 57 57 ARG B 492 TRP B 502 1 11
HELIX 58 58 GLU B 527 SER B 532 1 6
HELIX 59 59 TYR B 535 GLU B 551 1 17
HELIX 60 60 ASP B 555 LEU B 559 5 5
HELIX 61 61 THR B 560 ILE B 567 1 8
HELIX 62 62 SER B 573 GLY B 585 1 13
HELIX 63 63 PRO B 587 TYR B 602 1 16
HELIX 64 64 ASP B 612 ILE B 614 5 3
HELIX 65 65 ASN B 616 PHE B 629 1 14
HELIX 66 66 ASN B 660 GLU B 667 1 8
HELIX 67 67 GLY B 669 ALA B 681 1 13
HELIX 68 68 ARG B 690 GLU B 713 1 24
HELIX 69 69 LYS B 723 GLU B 746 1 24
HELIX 70 70 ARG B 748 PHE B 757 1 10
HELIX 71 71 PHE B 757 THR B 771 1 15
HELIX 72 72 ASP B 776 ALA B 795 1 20
HELIX 73 73 THR B 798 LEU B 809 1 12
HELIX 74 74 PHE B 814 ALA B 818 5 5
HELIX 75 75 ASN B 829 VAL B 852 1 24
HELIX 76 76 VAL B 873 SER B 878 1 6
HELIX 77 77 LYS B 884 LYS B 892 1 9
HELIX 78 78 HIS B 899 VAL B 903 5 5
HELIX 79 79 ALA B 904 ILE B 911 1 8
HELIX 80 80 ILE B 921 ARG B 928 1 8
HELIX 81 81 ALA B 930 GLY B 939 1 10
SHEET 1 A 4 ILE A 38 VAL A 40 0
SHEET 2 A 4 TRP A 606 GLY A 610 1 O CYS A 608 N THR A 39
SHEET 3 A 4 ILE A 638 ASN A 641 1 O ALA A 639 N ARG A 607
SHEET 4 A 4 ILE A 487 LEU A 488 1 N LEU A 488 O VAL A 640
SHEET 1 B 3 ILE A 176 LYS A 178 0
SHEET 2 B 3 TRP A 465 ASP A 468 -1 O PHE A 466 N VAL A 177
SHEET 3 B 3 LYS A 505 LYS A 506 -1 O LYS A 506 N ILE A 467
SHEET 1 C 2 ARG A 184 TRP A 185 0
SHEET 2 C 2 VAL A 457 ILE A 458 -1 O VAL A 457 N TRP A 185
SHEET 1 D 2 ILE A 206 LEU A 207 0
SHEET 2 D 2 GLU A 442 PHE A 443 -1 O GLU A 442 N LEU A 207
SHEET 1 E 3 TYR A 224 THR A 229 0
SHEET 2 E 3 ILE A 210 GLU A 215 -1 N ILE A 212 O ALA A 227
SHEET 3 E 3 ALA A 437 ILE A 439 -1 O GLU A 438 N ILE A 211
SHEET 1 F 4 TYR A 295 ARG A 297 0
SHEET 2 F 4 GLU A 304 PRO A 309 -1 O VAL A 305 N VAL A 296
SHEET 3 F 4 ASN A 240 VAL A 243 1 N MET A 241 O ILE A 306
SHEET 4 F 4 VAL A 322 SER A 324 -1 O VAL A 322 N TRP A 242
SHEET 1 G 3 GLU A 260 SER A 266 0
SHEET 2 G 3 TYR A 249 ARG A 255 -1 N VAL A 250 O VAL A 265
SHEET 3 G 3 GLU A 279 GLU A 285 -1 O GLU A 284 N LYS A 251
SHEET 1 H 2 THR A 516 PRO A 517 0
SHEET 2 H 2 VAL A 525 ILE A 526 -1 O ILE A 526 N THR A 516
SHEET 1 I 2 GLY A 644 LEU A 646 0
SHEET 2 I 2 PHE A 687 TRP A 689 1 O PHE A 687 N THR A 645
SHEET 1 J 2 ARG A 860 ILE A 863 0
SHEET 2 J 2 ALA A 963 ILE A 966 -1 O PHE A 965 N ALA A 861
SHEET 1 K 4 ILE B 38 VAL B 40 0
SHEET 2 K 4 TRP B 606 GLY B 610 1 O CYS B 608 N THR B 39
SHEET 3 K 4 ILE B 638 ASN B 641 1 O ALA B 639 N ARG B 607
SHEET 4 K 4 ILE B 487 LEU B 488 1 N LEU B 488 O VAL B 640
SHEET 1 L 3 ILE B 176 LYS B 178 0
SHEET 2 L 3 TRP B 465 ASP B 468 -1 O PHE B 466 N VAL B 177
SHEET 3 L 3 LYS B 505 LYS B 506 -1 O LYS B 506 N ILE B 467
SHEET 1 M 2 ARG B 184 TRP B 185 0
SHEET 2 M 2 VAL B 457 ILE B 458 -1 O VAL B 457 N TRP B 185
SHEET 1 N 2 ILE B 206 LEU B 207 0
SHEET 2 N 2 GLU B 442 PHE B 443 -1 O GLU B 442 N LEU B 207
SHEET 1 O 3 TYR B 224 THR B 229 0
SHEET 2 O 3 ILE B 210 GLU B 215 -1 N ILE B 212 O ALA B 227
SHEET 3 O 3 GLU B 438 ILE B 439 -1 O GLU B 438 N ILE B 211
SHEET 1 P 4 TYR B 295 ARG B 297 0
SHEET 2 P 4 GLU B 304 PRO B 309 -1 O VAL B 305 N VAL B 296
SHEET 3 P 4 ASN B 240 VAL B 243 1 N MET B 241 O ILE B 306
SHEET 4 P 4 VAL B 322 SER B 324 -1 O VAL B 322 N TRP B 242
SHEET 1 Q 3 GLU B 260 SER B 266 0
SHEET 2 Q 3 TYR B 249 ARG B 255 -1 N VAL B 254 O GLU B 261
SHEET 3 Q 3 GLU B 279 GLU B 285 -1 O GLU B 284 N LYS B 251
SHEET 1 R 2 THR B 516 PRO B 517 0
SHEET 2 R 2 VAL B 525 ILE B 526 -1 O ILE B 526 N THR B 516
SHEET 1 S 2 GLY B 644 LEU B 646 0
SHEET 2 S 2 PHE B 687 TRP B 689 1 O PHE B 687 N THR B 645
SHEET 1 T 2 ARG B 860 ILE B 863 0
SHEET 2 T 2 ALA B 963 ILE B 966 -1 O PHE B 965 N ALA B 861
CISPEP 1 LEU A 488 PRO A 489 0 -0.23
CISPEP 2 TYR A 602 PRO A 603 0 0.45
CISPEP 3 LEU B 488 PRO B 489 0 -0.01
CISPEP 4 TYR B 602 PRO B 603 0 0.14
CRYST1 120.546 231.127 118.181 90.00 90.00 90.00 P 21 21 2 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 0.008296 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004327 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008462 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
