HEADER ISOMERASE 02-JUL-01 1JIQ
TITLE CRYSTAL STRUCTURE OF HUMAN AUTOCRINE MOTILITY FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AUTOCRINE MOTILITY FACTOR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: GLUCOSE PHOSPHATE ISOMERASE;
COMPND 5 EC: 5.3.1.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-6P
KEYWDS CYTOKINE, AUTOCRINE MOTILITY FACTOR, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.TANAKA,A.HAGA,H.UEMURA,H.AKIYAMA,T.FUNASAKA,H.NAGASE,A.RAZ,
AUTHOR 2 K.T.NAKAMURA
REVDAT 4 25-OCT-23 1JIQ 1 REMARK
REVDAT 3 24-FEB-09 1JIQ 1 VERSN
REVDAT 2 18-DEC-02 1JIQ 1 REMARK
REVDAT 1 19-JUN-02 1JIQ 0
JRNL AUTH N.TANAKA,A.HAGA,H.UEMURA,H.AKIYAMA,T.FUNASAKA,H.NAGASE,
JRNL AUTH 2 A.RAZ,K.T.NAKAMURA
JRNL TITL INHIBITION MECHANISM OF CYTOKINE ACTIVITY OF HUMAN AUTOCRINE
JRNL TITL 2 MOTILITY FACTOR EXAMINED BY CRYSTAL STRUCTURE ANALYSES AND
JRNL TITL 3 SITE-DIRECTED MUTAGENESIS STUDIES.
JRNL REF J.MOL.BIOL. V. 318 985 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12054796
JRNL DOI 10.1016/S0022-2836(02)00186-9
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 174100
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9195
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11476
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 593
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17780
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1475
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.36000
REMARK 3 B22 (A**2) : 0.68000
REMARK 3 B33 (A**2) : -1.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.145
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.128
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.125
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.203
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 18216 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 16316 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 24660 ; 1.321 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): 38000 ; 0.759 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2224 ; 4.131 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3297 ;17.320 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2680 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 20268 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 3760 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4209 ; 0.228 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 16429 ; 0.196 ; 0.300
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): 1395 ; 0.137 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 10 ; 0.151 ; 0.500
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): 14 ; 0.284 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 37 ; 0.174 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 33 ; 0.209 ; 0.500
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): 11064 ; 0.590 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17832 ; 1.089 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7152 ; 1.747 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6828 ; 2.866 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1JIQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013817.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-18B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 183404
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.30500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1DQR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CACODYLATE, SODIUM ACETATE, PEG8000,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 40.38500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 135.35000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 135.35000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.38500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.70000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER.
REMARK 300 TWO DIMERS EXIST IN AN ASYMMETRIC UNIT.
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: 12920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 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
REMARK 350 BIOMOLECULE: 2
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: 12960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLN A 558
REMARK 465 GLN B 558
REMARK 465 GLN C 558
REMARK 465 GLN D 558
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 874 O HOH A 920 2.06
REMARK 500 OE1 GLU A 121 O HOH A 815 2.13
REMARK 500 NH2 ARG C 83 O HOH C 873 2.16
REMARK 500 OD1 ASN A 38 O HOH A 827 2.16
REMARK 500 O HOH B 847 O HOH B 864 2.16
REMARK 500 OD1 ASP D 35 O HOH D 870 2.19
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 ASP A 63 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 140 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 161 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 235 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 35 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP C 140 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP D 511 CB - CG - OD2 ANGL. DEV. = 5.6 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 SER A 22 0.90 -68.96
REMARK 500 ASN A 47 -7.16 78.04
REMARK 500 LYS A 57 38.04 -87.28
REMARK 500 ASP A 161 -53.52 -122.63
REMARK 500 SER A 210 117.74 -167.18
REMARK 500 LYS A 234 -51.29 73.42
REMARK 500 ASP A 342 114.26 -168.51
REMARK 500 TYR A 363 -0.43 -143.05
REMARK 500 THR A 375 -139.23 -119.61
REMARK 500 ALA A 390 -63.81 -104.32
REMARK 500 GLN A 512 59.49 -163.86
REMARK 500 HIS A 538 -168.81 -118.95
REMARK 500 ASN B 47 -4.61 74.27
REMARK 500 LYS B 57 33.74 -92.22
REMARK 500 ASP B 161 -54.68 -123.19
REMARK 500 SER B 185 -41.75 -131.79
REMARK 500 SER B 210 114.60 -160.99
REMARK 500 LYS B 234 -48.33 70.08
REMARK 500 ASP B 342 113.10 -169.65
REMARK 500 THR B 375 -140.66 -116.73
REMARK 500 GLN B 512 58.33 -162.26
REMARK 500 ASN C 47 -7.95 77.29
REMARK 500 LYS C 57 34.70 -86.46
REMARK 500 ASP C 161 -55.63 -121.10
REMARK 500 SER C 185 -43.58 -131.11
REMARK 500 SER C 210 112.68 -164.65
REMARK 500 LYS C 234 -39.16 68.42
REMARK 500 ASP C 342 112.52 -169.31
REMARK 500 THR C 375 -140.19 -116.66
REMARK 500 ALA C 390 -63.71 -107.38
REMARK 500 GLU C 457 -71.78 -51.32
REMARK 500 GLN C 512 58.28 -162.76
REMARK 500 ASN D 47 -7.32 72.24
REMARK 500 LYS D 57 34.47 -91.66
REMARK 500 ASP D 161 -54.13 -121.81
REMARK 500 SER D 185 -41.84 -131.85
REMARK 500 SER D 210 115.54 -161.19
REMARK 500 ALA D 233 101.09 -176.43
REMARK 500 LYS D 234 93.96 -56.56
REMARK 500 ASP D 235 94.57 -161.24
REMARK 500 PRO D 260 -9.28 -59.14
REMARK 500 SER D 278 -158.85 -100.69
REMARK 500 ASP D 342 112.30 -165.34
REMARK 500 THR D 375 -136.84 -116.37
REMARK 500 GLN D 512 58.71 -162.23
REMARK 500 HIS D 538 -169.78 -118.33
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JIQ A 1 558 UNP P06744 G6PI_HUMAN 1 558
DBREF 1JIQ B 1 558 UNP P06744 G6PI_HUMAN 1 558
DBREF 1JIQ C 1 558 UNP P06744 G6PI_HUMAN 1 558
DBREF 1JIQ D 1 558 UNP P06744 G6PI_HUMAN 1 558
SEQRES 1 A 558 MET ALA ALA LEU THR ARG ASP PRO GLN PHE GLN LYS LEU
SEQRES 2 A 558 GLN GLN TRP TYR ARG GLU HIS ARG SER GLU LEU ASN LEU
SEQRES 3 A 558 ARG ARG LEU PHE ASP ALA ASN LYS ASP ARG PHE ASN HIS
SEQRES 4 A 558 PHE SER LEU THR LEU ASN THR ASN HIS GLY HIS ILE LEU
SEQRES 5 A 558 VAL ASP TYR SER LYS ASN LEU VAL THR GLU ASP VAL MET
SEQRES 6 A 558 ARG MET LEU VAL ASP LEU ALA LYS SER ARG GLY VAL GLU
SEQRES 7 A 558 ALA ALA ARG GLU ARG MET PHE ASN GLY GLU LYS ILE ASN
SEQRES 8 A 558 TYR THR GLU GLY ARG ALA VAL LEU HIS VAL ALA LEU ARG
SEQRES 9 A 558 ASN ARG SER ASN THR PRO ILE LEU VAL ASP GLY LYS ASP
SEQRES 10 A 558 VAL MET PRO GLU VAL ASN LYS VAL LEU ASP LYS MET LYS
SEQRES 11 A 558 SER PHE CYS GLN ARG VAL ARG SER GLY ASP TRP LYS GLY
SEQRES 12 A 558 TYR THR GLY LYS THR ILE THR ASP VAL ILE ASN ILE GLY
SEQRES 13 A 558 ILE GLY GLY SER ASP LEU GLY PRO LEU MET VAL THR GLU
SEQRES 14 A 558 ALA LEU LYS PRO TYR SER SER GLY GLY PRO ARG VAL TRP
SEQRES 15 A 558 TYR VAL SER ASN ILE ASP GLY THR HIS ILE ALA LYS THR
SEQRES 16 A 558 LEU ALA GLN LEU ASN PRO GLU SER SER LEU PHE ILE ILE
SEQRES 17 A 558 ALA SER LYS THR PHE THR THR GLN GLU THR ILE THR ASN
SEQRES 18 A 558 ALA GLU THR ALA LYS GLU TRP PHE LEU GLN ALA ALA LYS
SEQRES 19 A 558 ASP PRO SER ALA VAL ALA LYS HIS PHE VAL ALA LEU SER
SEQRES 20 A 558 THR ASN THR THR LYS VAL LYS GLU PHE GLY ILE ASP PRO
SEQRES 21 A 558 GLN ASN MET PHE GLU PHE TRP ASP TRP VAL GLY GLY ARG
SEQRES 22 A 558 TYR SER LEU TRP SER ALA ILE GLY LEU SER ILE ALA LEU
SEQRES 23 A 558 HIS VAL GLY PHE ASP ASN PHE GLU GLN LEU LEU SER GLY
SEQRES 24 A 558 ALA HIS TRP MET ASP GLN HIS PHE ARG THR THR PRO LEU
SEQRES 25 A 558 GLU LYS ASN ALA PRO VAL LEU LEU ALA LEU LEU GLY ILE
SEQRES 26 A 558 TRP TYR ILE ASN CYS PHE GLY CYS GLU THR HIS ALA MET
SEQRES 27 A 558 LEU PRO TYR ASP GLN TYR LEU HIS ARG PHE ALA ALA TYR
SEQRES 28 A 558 PHE GLN GLN GLY ASP MET GLU SER ASN GLY LYS TYR ILE
SEQRES 29 A 558 THR LYS SER GLY THR ARG VAL ASP HIS GLN THR GLY PRO
SEQRES 30 A 558 ILE VAL TRP GLY GLU PRO GLY THR ASN GLY GLN HIS ALA
SEQRES 31 A 558 PHE TYR GLN LEU ILE HIS GLN GLY THR LYS MET ILE PRO
SEQRES 32 A 558 CYS ASP PHE LEU ILE PRO VAL GLN THR GLN HIS PRO ILE
SEQRES 33 A 558 ARG LYS GLY LEU HIS HIS LYS ILE LEU LEU ALA ASN PHE
SEQRES 34 A 558 LEU ALA GLN THR GLU ALA LEU MET ARG GLY LYS SER THR
SEQRES 35 A 558 GLU GLU ALA ARG LYS GLU LEU GLN ALA ALA GLY LYS SER
SEQRES 36 A 558 PRO GLU ASP LEU GLU ARG LEU LEU PRO HIS LYS VAL PHE
SEQRES 37 A 558 GLU GLY ASN ARG PRO THR ASN SER ILE VAL PHE THR LYS
SEQRES 38 A 558 LEU THR PRO PHE MET LEU GLY ALA LEU VAL ALA MET TYR
SEQRES 39 A 558 GLU HIS LYS ILE PHE VAL GLN GLY ILE ILE TRP ASP ILE
SEQRES 40 A 558 ASN SER PHE ASP GLN TRP GLY VAL GLU LEU GLY LYS GLN
SEQRES 41 A 558 LEU ALA LYS LYS ILE GLU PRO GLU LEU ASP GLY SER ALA
SEQRES 42 A 558 GLN VAL THR SER HIS ASP ALA SER THR ASN GLY LEU ILE
SEQRES 43 A 558 ASN PHE ILE LYS GLN GLN ARG GLU ALA ARG VAL GLN
SEQRES 1 B 558 MET ALA ALA LEU THR ARG ASP PRO GLN PHE GLN LYS LEU
SEQRES 2 B 558 GLN GLN TRP TYR ARG GLU HIS ARG SER GLU LEU ASN LEU
SEQRES 3 B 558 ARG ARG LEU PHE ASP ALA ASN LYS ASP ARG PHE ASN HIS
SEQRES 4 B 558 PHE SER LEU THR LEU ASN THR ASN HIS GLY HIS ILE LEU
SEQRES 5 B 558 VAL ASP TYR SER LYS ASN LEU VAL THR GLU ASP VAL MET
SEQRES 6 B 558 ARG MET LEU VAL ASP LEU ALA LYS SER ARG GLY VAL GLU
SEQRES 7 B 558 ALA ALA ARG GLU ARG MET PHE ASN GLY GLU LYS ILE ASN
SEQRES 8 B 558 TYR THR GLU GLY ARG ALA VAL LEU HIS VAL ALA LEU ARG
SEQRES 9 B 558 ASN ARG SER ASN THR PRO ILE LEU VAL ASP GLY LYS ASP
SEQRES 10 B 558 VAL MET PRO GLU VAL ASN LYS VAL LEU ASP LYS MET LYS
SEQRES 11 B 558 SER PHE CYS GLN ARG VAL ARG SER GLY ASP TRP LYS GLY
SEQRES 12 B 558 TYR THR GLY LYS THR ILE THR ASP VAL ILE ASN ILE GLY
SEQRES 13 B 558 ILE GLY GLY SER ASP LEU GLY PRO LEU MET VAL THR GLU
SEQRES 14 B 558 ALA LEU LYS PRO TYR SER SER GLY GLY PRO ARG VAL TRP
SEQRES 15 B 558 TYR VAL SER ASN ILE ASP GLY THR HIS ILE ALA LYS THR
SEQRES 16 B 558 LEU ALA GLN LEU ASN PRO GLU SER SER LEU PHE ILE ILE
SEQRES 17 B 558 ALA SER LYS THR PHE THR THR GLN GLU THR ILE THR ASN
SEQRES 18 B 558 ALA GLU THR ALA LYS GLU TRP PHE LEU GLN ALA ALA LYS
SEQRES 19 B 558 ASP PRO SER ALA VAL ALA LYS HIS PHE VAL ALA LEU SER
SEQRES 20 B 558 THR ASN THR THR LYS VAL LYS GLU PHE GLY ILE ASP PRO
SEQRES 21 B 558 GLN ASN MET PHE GLU PHE TRP ASP TRP VAL GLY GLY ARG
SEQRES 22 B 558 TYR SER LEU TRP SER ALA ILE GLY LEU SER ILE ALA LEU
SEQRES 23 B 558 HIS VAL GLY PHE ASP ASN PHE GLU GLN LEU LEU SER GLY
SEQRES 24 B 558 ALA HIS TRP MET ASP GLN HIS PHE ARG THR THR PRO LEU
SEQRES 25 B 558 GLU LYS ASN ALA PRO VAL LEU LEU ALA LEU LEU GLY ILE
SEQRES 26 B 558 TRP TYR ILE ASN CYS PHE GLY CYS GLU THR HIS ALA MET
SEQRES 27 B 558 LEU PRO TYR ASP GLN TYR LEU HIS ARG PHE ALA ALA TYR
SEQRES 28 B 558 PHE GLN GLN GLY ASP MET GLU SER ASN GLY LYS TYR ILE
SEQRES 29 B 558 THR LYS SER GLY THR ARG VAL ASP HIS GLN THR GLY PRO
SEQRES 30 B 558 ILE VAL TRP GLY GLU PRO GLY THR ASN GLY GLN HIS ALA
SEQRES 31 B 558 PHE TYR GLN LEU ILE HIS GLN GLY THR LYS MET ILE PRO
SEQRES 32 B 558 CYS ASP PHE LEU ILE PRO VAL GLN THR GLN HIS PRO ILE
SEQRES 33 B 558 ARG LYS GLY LEU HIS HIS LYS ILE LEU LEU ALA ASN PHE
SEQRES 34 B 558 LEU ALA GLN THR GLU ALA LEU MET ARG GLY LYS SER THR
SEQRES 35 B 558 GLU GLU ALA ARG LYS GLU LEU GLN ALA ALA GLY LYS SER
SEQRES 36 B 558 PRO GLU ASP LEU GLU ARG LEU LEU PRO HIS LYS VAL PHE
SEQRES 37 B 558 GLU GLY ASN ARG PRO THR ASN SER ILE VAL PHE THR LYS
SEQRES 38 B 558 LEU THR PRO PHE MET LEU GLY ALA LEU VAL ALA MET TYR
SEQRES 39 B 558 GLU HIS LYS ILE PHE VAL GLN GLY ILE ILE TRP ASP ILE
SEQRES 40 B 558 ASN SER PHE ASP GLN TRP GLY VAL GLU LEU GLY LYS GLN
SEQRES 41 B 558 LEU ALA LYS LYS ILE GLU PRO GLU LEU ASP GLY SER ALA
SEQRES 42 B 558 GLN VAL THR SER HIS ASP ALA SER THR ASN GLY LEU ILE
SEQRES 43 B 558 ASN PHE ILE LYS GLN GLN ARG GLU ALA ARG VAL GLN
SEQRES 1 C 558 MET ALA ALA LEU THR ARG ASP PRO GLN PHE GLN LYS LEU
SEQRES 2 C 558 GLN GLN TRP TYR ARG GLU HIS ARG SER GLU LEU ASN LEU
SEQRES 3 C 558 ARG ARG LEU PHE ASP ALA ASN LYS ASP ARG PHE ASN HIS
SEQRES 4 C 558 PHE SER LEU THR LEU ASN THR ASN HIS GLY HIS ILE LEU
SEQRES 5 C 558 VAL ASP TYR SER LYS ASN LEU VAL THR GLU ASP VAL MET
SEQRES 6 C 558 ARG MET LEU VAL ASP LEU ALA LYS SER ARG GLY VAL GLU
SEQRES 7 C 558 ALA ALA ARG GLU ARG MET PHE ASN GLY GLU LYS ILE ASN
SEQRES 8 C 558 TYR THR GLU GLY ARG ALA VAL LEU HIS VAL ALA LEU ARG
SEQRES 9 C 558 ASN ARG SER ASN THR PRO ILE LEU VAL ASP GLY LYS ASP
SEQRES 10 C 558 VAL MET PRO GLU VAL ASN LYS VAL LEU ASP LYS MET LYS
SEQRES 11 C 558 SER PHE CYS GLN ARG VAL ARG SER GLY ASP TRP LYS GLY
SEQRES 12 C 558 TYR THR GLY LYS THR ILE THR ASP VAL ILE ASN ILE GLY
SEQRES 13 C 558 ILE GLY GLY SER ASP LEU GLY PRO LEU MET VAL THR GLU
SEQRES 14 C 558 ALA LEU LYS PRO TYR SER SER GLY GLY PRO ARG VAL TRP
SEQRES 15 C 558 TYR VAL SER ASN ILE ASP GLY THR HIS ILE ALA LYS THR
SEQRES 16 C 558 LEU ALA GLN LEU ASN PRO GLU SER SER LEU PHE ILE ILE
SEQRES 17 C 558 ALA SER LYS THR PHE THR THR GLN GLU THR ILE THR ASN
SEQRES 18 C 558 ALA GLU THR ALA LYS GLU TRP PHE LEU GLN ALA ALA LYS
SEQRES 19 C 558 ASP PRO SER ALA VAL ALA LYS HIS PHE VAL ALA LEU SER
SEQRES 20 C 558 THR ASN THR THR LYS VAL LYS GLU PHE GLY ILE ASP PRO
SEQRES 21 C 558 GLN ASN MET PHE GLU PHE TRP ASP TRP VAL GLY GLY ARG
SEQRES 22 C 558 TYR SER LEU TRP SER ALA ILE GLY LEU SER ILE ALA LEU
SEQRES 23 C 558 HIS VAL GLY PHE ASP ASN PHE GLU GLN LEU LEU SER GLY
SEQRES 24 C 558 ALA HIS TRP MET ASP GLN HIS PHE ARG THR THR PRO LEU
SEQRES 25 C 558 GLU LYS ASN ALA PRO VAL LEU LEU ALA LEU LEU GLY ILE
SEQRES 26 C 558 TRP TYR ILE ASN CYS PHE GLY CYS GLU THR HIS ALA MET
SEQRES 27 C 558 LEU PRO TYR ASP GLN TYR LEU HIS ARG PHE ALA ALA TYR
SEQRES 28 C 558 PHE GLN GLN GLY ASP MET GLU SER ASN GLY LYS TYR ILE
SEQRES 29 C 558 THR LYS SER GLY THR ARG VAL ASP HIS GLN THR GLY PRO
SEQRES 30 C 558 ILE VAL TRP GLY GLU PRO GLY THR ASN GLY GLN HIS ALA
SEQRES 31 C 558 PHE TYR GLN LEU ILE HIS GLN GLY THR LYS MET ILE PRO
SEQRES 32 C 558 CYS ASP PHE LEU ILE PRO VAL GLN THR GLN HIS PRO ILE
SEQRES 33 C 558 ARG LYS GLY LEU HIS HIS LYS ILE LEU LEU ALA ASN PHE
SEQRES 34 C 558 LEU ALA GLN THR GLU ALA LEU MET ARG GLY LYS SER THR
SEQRES 35 C 558 GLU GLU ALA ARG LYS GLU LEU GLN ALA ALA GLY LYS SER
SEQRES 36 C 558 PRO GLU ASP LEU GLU ARG LEU LEU PRO HIS LYS VAL PHE
SEQRES 37 C 558 GLU GLY ASN ARG PRO THR ASN SER ILE VAL PHE THR LYS
SEQRES 38 C 558 LEU THR PRO PHE MET LEU GLY ALA LEU VAL ALA MET TYR
SEQRES 39 C 558 GLU HIS LYS ILE PHE VAL GLN GLY ILE ILE TRP ASP ILE
SEQRES 40 C 558 ASN SER PHE ASP GLN TRP GLY VAL GLU LEU GLY LYS GLN
SEQRES 41 C 558 LEU ALA LYS LYS ILE GLU PRO GLU LEU ASP GLY SER ALA
SEQRES 42 C 558 GLN VAL THR SER HIS ASP ALA SER THR ASN GLY LEU ILE
SEQRES 43 C 558 ASN PHE ILE LYS GLN GLN ARG GLU ALA ARG VAL GLN
SEQRES 1 D 558 MET ALA ALA LEU THR ARG ASP PRO GLN PHE GLN LYS LEU
SEQRES 2 D 558 GLN GLN TRP TYR ARG GLU HIS ARG SER GLU LEU ASN LEU
SEQRES 3 D 558 ARG ARG LEU PHE ASP ALA ASN LYS ASP ARG PHE ASN HIS
SEQRES 4 D 558 PHE SER LEU THR LEU ASN THR ASN HIS GLY HIS ILE LEU
SEQRES 5 D 558 VAL ASP TYR SER LYS ASN LEU VAL THR GLU ASP VAL MET
SEQRES 6 D 558 ARG MET LEU VAL ASP LEU ALA LYS SER ARG GLY VAL GLU
SEQRES 7 D 558 ALA ALA ARG GLU ARG MET PHE ASN GLY GLU LYS ILE ASN
SEQRES 8 D 558 TYR THR GLU GLY ARG ALA VAL LEU HIS VAL ALA LEU ARG
SEQRES 9 D 558 ASN ARG SER ASN THR PRO ILE LEU VAL ASP GLY LYS ASP
SEQRES 10 D 558 VAL MET PRO GLU VAL ASN LYS VAL LEU ASP LYS MET LYS
SEQRES 11 D 558 SER PHE CYS GLN ARG VAL ARG SER GLY ASP TRP LYS GLY
SEQRES 12 D 558 TYR THR GLY LYS THR ILE THR ASP VAL ILE ASN ILE GLY
SEQRES 13 D 558 ILE GLY GLY SER ASP LEU GLY PRO LEU MET VAL THR GLU
SEQRES 14 D 558 ALA LEU LYS PRO TYR SER SER GLY GLY PRO ARG VAL TRP
SEQRES 15 D 558 TYR VAL SER ASN ILE ASP GLY THR HIS ILE ALA LYS THR
SEQRES 16 D 558 LEU ALA GLN LEU ASN PRO GLU SER SER LEU PHE ILE ILE
SEQRES 17 D 558 ALA SER LYS THR PHE THR THR GLN GLU THR ILE THR ASN
SEQRES 18 D 558 ALA GLU THR ALA LYS GLU TRP PHE LEU GLN ALA ALA LYS
SEQRES 19 D 558 ASP PRO SER ALA VAL ALA LYS HIS PHE VAL ALA LEU SER
SEQRES 20 D 558 THR ASN THR THR LYS VAL LYS GLU PHE GLY ILE ASP PRO
SEQRES 21 D 558 GLN ASN MET PHE GLU PHE TRP ASP TRP VAL GLY GLY ARG
SEQRES 22 D 558 TYR SER LEU TRP SER ALA ILE GLY LEU SER ILE ALA LEU
SEQRES 23 D 558 HIS VAL GLY PHE ASP ASN PHE GLU GLN LEU LEU SER GLY
SEQRES 24 D 558 ALA HIS TRP MET ASP GLN HIS PHE ARG THR THR PRO LEU
SEQRES 25 D 558 GLU LYS ASN ALA PRO VAL LEU LEU ALA LEU LEU GLY ILE
SEQRES 26 D 558 TRP TYR ILE ASN CYS PHE GLY CYS GLU THR HIS ALA MET
SEQRES 27 D 558 LEU PRO TYR ASP GLN TYR LEU HIS ARG PHE ALA ALA TYR
SEQRES 28 D 558 PHE GLN GLN GLY ASP MET GLU SER ASN GLY LYS TYR ILE
SEQRES 29 D 558 THR LYS SER GLY THR ARG VAL ASP HIS GLN THR GLY PRO
SEQRES 30 D 558 ILE VAL TRP GLY GLU PRO GLY THR ASN GLY GLN HIS ALA
SEQRES 31 D 558 PHE TYR GLN LEU ILE HIS GLN GLY THR LYS MET ILE PRO
SEQRES 32 D 558 CYS ASP PHE LEU ILE PRO VAL GLN THR GLN HIS PRO ILE
SEQRES 33 D 558 ARG LYS GLY LEU HIS HIS LYS ILE LEU LEU ALA ASN PHE
SEQRES 34 D 558 LEU ALA GLN THR GLU ALA LEU MET ARG GLY LYS SER THR
SEQRES 35 D 558 GLU GLU ALA ARG LYS GLU LEU GLN ALA ALA GLY LYS SER
SEQRES 36 D 558 PRO GLU ASP LEU GLU ARG LEU LEU PRO HIS LYS VAL PHE
SEQRES 37 D 558 GLU GLY ASN ARG PRO THR ASN SER ILE VAL PHE THR LYS
SEQRES 38 D 558 LEU THR PRO PHE MET LEU GLY ALA LEU VAL ALA MET TYR
SEQRES 39 D 558 GLU HIS LYS ILE PHE VAL GLN GLY ILE ILE TRP ASP ILE
SEQRES 40 D 558 ASN SER PHE ASP GLN TRP GLY VAL GLU LEU GLY LYS GLN
SEQRES 41 D 558 LEU ALA LYS LYS ILE GLU PRO GLU LEU ASP GLY SER ALA
SEQRES 42 D 558 GLN VAL THR SER HIS ASP ALA SER THR ASN GLY LEU ILE
SEQRES 43 D 558 ASN PHE ILE LYS GLN GLN ARG GLU ALA ARG VAL GLN
FORMUL 5 HOH *1475(H2 O)
HELIX 1 1 ALA A 2 ASP A 7 1 6
HELIX 2 2 ASP A 7 ARG A 21 1 15
HELIX 3 3 SER A 22 LEU A 24 5 3
HELIX 4 4 ASN A 25 ASN A 33 1 9
HELIX 5 5 ASP A 35 PHE A 40 1 6
HELIX 6 6 THR A 61 ARG A 75 1 15
HELIX 7 7 GLY A 76 ASN A 86 1 11
HELIX 8 8 LEU A 99 ARG A 104 1 6
HELIX 9 9 VAL A 118 SER A 138 1 21
HELIX 10 10 ILE A 157 SER A 160 5 4
HELIX 11 11 ASP A 161 LEU A 171 1 11
HELIX 12 12 LYS A 172 SER A 175 5 4
HELIX 13 13 ASP A 188 ALA A 197 1 10
HELIX 14 14 GLN A 198 LEU A 199 5 2
HELIX 15 15 ASN A 200 GLU A 202 5 3
HELIX 16 16 THR A 215 LYS A 234 1 20
HELIX 17 17 ASP A 235 SER A 237 5 3
HELIX 18 18 ALA A 238 HIS A 242 1 5
HELIX 19 19 ASN A 249 GLY A 257 1 9
HELIX 20 20 ASP A 259 ASN A 262 5 4
HELIX 21 21 GLY A 271 SER A 275 5 5
HELIX 22 22 SER A 278 ILE A 280 5 3
HELIX 23 23 GLY A 281 GLY A 289 1 9
HELIX 24 24 GLY A 289 THR A 310 1 22
HELIX 25 25 PRO A 311 LYS A 314 5 4
HELIX 26 26 ASN A 315 CYS A 330 1 16
HELIX 27 27 ASP A 342 HIS A 346 5 5
HELIX 28 28 ARG A 347 GLY A 361 1 15
HELIX 29 29 ASN A 386 ALA A 390 5 5
HELIX 30 30 PHE A 391 GLY A 398 1 8
HELIX 31 31 ILE A 416 LYS A 418 5 3
HELIX 32 32 GLY A 419 GLY A 439 1 21
HELIX 33 33 SER A 441 ALA A 452 1 12
HELIX 34 34 SER A 455 LEU A 463 1 9
HELIX 35 35 PRO A 464 VAL A 467 5 4
HELIX 36 36 THR A 483 ASP A 506 1 24
HELIX 37 37 GLN A 512 GLY A 514 5 3
HELIX 38 38 VAL A 515 GLU A 526 1 12
HELIX 39 39 PRO A 527 ASP A 530 5 4
HELIX 40 40 ASP A 539 GLU A 554 1 16
HELIX 41 41 ALA B 2 ASP B 7 1 6
HELIX 42 42 ASP B 7 ARG B 21 1 15
HELIX 43 43 SER B 22 LEU B 24 5 3
HELIX 44 44 ASN B 25 ASN B 33 1 9
HELIX 45 45 ASP B 35 PHE B 40 1 6
HELIX 46 46 THR B 61 ARG B 75 1 15
HELIX 47 47 GLY B 76 GLY B 87 1 12
HELIX 48 48 LEU B 99 ARG B 104 1 6
HELIX 49 49 VAL B 118 SER B 138 1 21
HELIX 50 50 ILE B 157 SER B 160 5 4
HELIX 51 51 ASP B 161 LEU B 171 1 11
HELIX 52 52 LYS B 172 SER B 175 5 4
HELIX 53 53 ASP B 188 ALA B 197 1 10
HELIX 54 54 GLN B 198 LEU B 199 5 2
HELIX 55 55 ASN B 200 GLU B 202 5 3
HELIX 56 56 THR B 215 LYS B 234 1 20
HELIX 57 57 ASP B 235 LYS B 241 5 7
HELIX 58 58 ASN B 249 GLY B 257 1 9
HELIX 59 59 ASP B 259 GLN B 261 5 3
HELIX 60 60 GLY B 271 SER B 275 5 5
HELIX 61 61 SER B 278 ILE B 280 5 3
HELIX 62 62 GLY B 281 GLY B 289 1 9
HELIX 63 63 GLY B 289 THR B 310 1 22
HELIX 64 64 PRO B 311 LYS B 314 5 4
HELIX 65 65 ASN B 315 CYS B 330 1 16
HELIX 66 66 ASP B 342 HIS B 346 5 5
HELIX 67 67 ARG B 347 GLY B 361 1 15
HELIX 68 68 ASN B 386 ALA B 390 5 5
HELIX 69 69 PHE B 391 GLY B 398 1 8
HELIX 70 70 ILE B 416 LYS B 418 5 3
HELIX 71 71 GLY B 419 GLY B 439 1 21
HELIX 72 72 SER B 441 ALA B 452 1 12
HELIX 73 73 SER B 455 LEU B 463 1 9
HELIX 74 74 PRO B 464 VAL B 467 5 4
HELIX 75 75 THR B 483 ASP B 506 1 24
HELIX 76 76 GLN B 512 GLY B 514 5 3
HELIX 77 77 VAL B 515 LEU B 529 1 15
HELIX 78 78 ASP B 539 ARG B 553 1 15
HELIX 79 79 ASP C 7 ARG C 21 1 15
HELIX 80 80 SER C 22 LEU C 24 5 3
HELIX 81 81 ASN C 25 ASN C 33 1 9
HELIX 82 82 ASP C 35 PHE C 40 1 6
HELIX 83 83 THR C 61 ARG C 75 1 15
HELIX 84 84 GLY C 76 ASN C 86 1 11
HELIX 85 85 LEU C 99 ARG C 104 1 6
HELIX 86 86 VAL C 118 SER C 138 1 21
HELIX 87 87 ILE C 157 SER C 160 5 4
HELIX 88 88 ASP C 161 LEU C 171 1 11
HELIX 89 89 LYS C 172 SER C 176 5 5
HELIX 90 90 ASP C 188 ALA C 197 1 10
HELIX 91 91 GLN C 198 LEU C 199 5 2
HELIX 92 92 ASN C 200 GLU C 202 5 3
HELIX 93 93 THR C 215 LYS C 234 1 20
HELIX 94 94 ASP C 235 LYS C 241 5 7
HELIX 95 95 ASN C 249 GLY C 257 1 9
HELIX 96 96 ASP C 259 GLN C 261 5 3
HELIX 97 97 GLY C 271 SER C 275 5 5
HELIX 98 98 SER C 278 ILE C 280 5 3
HELIX 99 99 GLY C 281 GLY C 289 1 9
HELIX 100 100 GLY C 289 THR C 310 1 22
HELIX 101 101 PRO C 311 LYS C 314 5 4
HELIX 102 102 ASN C 315 CYS C 330 1 16
HELIX 103 103 ASP C 342 HIS C 346 5 5
HELIX 104 104 ARG C 347 GLY C 361 1 15
HELIX 105 105 ASN C 386 ALA C 390 5 5
HELIX 106 106 PHE C 391 GLY C 398 1 8
HELIX 107 107 ILE C 416 LYS C 418 5 3
HELIX 108 108 GLY C 419 GLY C 439 1 21
HELIX 109 109 SER C 441 GLY C 453 1 13
HELIX 110 110 SER C 455 LEU C 463 1 9
HELIX 111 111 PRO C 464 VAL C 467 5 4
HELIX 112 112 THR C 483 ASP C 506 1 24
HELIX 113 113 GLN C 512 GLY C 514 5 3
HELIX 114 114 VAL C 515 LEU C 529 1 15
HELIX 115 115 ASP C 539 GLU C 554 1 16
HELIX 116 116 ASP D 7 ARG D 21 1 15
HELIX 117 117 SER D 22 LEU D 24 5 3
HELIX 118 118 ASN D 25 ASN D 33 1 9
HELIX 119 119 ASP D 35 PHE D 40 1 6
HELIX 120 120 THR D 61 ARG D 75 1 15
HELIX 121 121 GLY D 76 GLY D 87 1 12
HELIX 122 122 LEU D 99 ARG D 104 1 6
HELIX 123 123 VAL D 118 SER D 138 1 21
HELIX 124 124 ILE D 157 SER D 160 5 4
HELIX 125 125 ASP D 161 LEU D 171 1 11
HELIX 126 126 LYS D 172 SER D 175 5 4
HELIX 127 127 ASP D 188 ALA D 197 1 10
HELIX 128 128 THR D 215 GLN D 231 1 17
HELIX 129 129 SER D 237 LYS D 241 5 5
HELIX 130 130 ASN D 249 GLY D 257 1 9
HELIX 131 131 ASP D 259 GLN D 261 5 3
HELIX 132 132 GLY D 271 SER D 275 5 5
HELIX 133 133 SER D 278 ILE D 280 5 3
HELIX 134 134 GLY D 281 GLY D 289 1 9
HELIX 135 135 GLY D 289 THR D 310 1 22
HELIX 136 136 PRO D 311 LYS D 314 5 4
HELIX 137 137 ASN D 315 CYS D 330 1 16
HELIX 138 138 ASP D 342 HIS D 346 5 5
HELIX 139 139 ARG D 347 ASP D 356 1 10
HELIX 140 140 ASP D 356 GLY D 361 1 6
HELIX 141 141 ASN D 386 ALA D 390 5 5
HELIX 142 142 PHE D 391 GLY D 398 1 8
HELIX 143 143 PRO D 415 LYS D 418 5 4
HELIX 144 144 GLY D 419 GLY D 439 1 21
HELIX 145 145 SER D 441 GLY D 453 1 13
HELIX 146 146 SER D 455 LEU D 463 1 9
HELIX 147 147 PRO D 464 VAL D 467 5 4
HELIX 148 148 THR D 483 ASP D 506 1 24
HELIX 149 149 GLN D 512 GLY D 514 5 3
HELIX 150 150 VAL D 515 LEU D 529 1 15
HELIX 151 151 ASP D 539 GLU D 554 1 16
SHEET 1 A 6 SER A 41 ASN A 45 0
SHEET 2 A 6 HIS A 50 ASP A 54 -1 O ILE A 51 N LEU A 44
SHEET 3 A 6 THR A 474 LYS A 481 -1 N SER A 476 O ASP A 54
SHEET 4 A 6 CYS A 404 GLN A 411 1 O CYS A 404 N ASN A 475
SHEET 5 A 6 THR A 335 PRO A 340 1 O ALA A 337 N ASP A 405
SHEET 6 A 6 ILE A 378 TRP A 380 1 O ILE A 378 N HIS A 336
SHEET 1 B 2 LEU A 112 VAL A 113 0
SHEET 2 B 2 LYS A 116 ASP A 117 -1 N LYS A 116 O VAL A 113
SHEET 1 C 4 ARG A 180 VAL A 184 0
SHEET 2 C 4 ASP A 151 ILE A 155 1 O VAL A 152 N TRP A 182
SHEET 3 C 4 SER A 204 ALA A 209 1 N LEU A 205 O ASP A 151
SHEET 4 C 4 PHE A 243 LEU A 246 1 O VAL A 244 N ILE A 208
SHEET 1 D 6 SER B 41 ASN B 45 0
SHEET 2 D 6 HIS B 50 ASP B 54 -1 O ILE B 51 N LEU B 44
SHEET 3 D 6 THR B 474 LYS B 481 -1 O SER B 476 N ASP B 54
SHEET 4 D 6 CYS B 404 GLN B 411 1 O CYS B 404 N ASN B 475
SHEET 5 D 6 THR B 335 PRO B 340 1 O ALA B 337 N ASP B 405
SHEET 6 D 6 ILE B 378 TRP B 380 1 O ILE B 378 N HIS B 336
SHEET 1 E 2 LEU B 112 VAL B 113 0
SHEET 2 E 2 LYS B 116 ASP B 117 -1 O LYS B 116 N VAL B 113
SHEET 1 F 5 ARG B 180 VAL B 184 0
SHEET 2 F 5 ASP B 151 ILE B 155 1 N VAL B 152 O ARG B 180
SHEET 3 F 5 SER B 204 ALA B 209 1 O LEU B 205 N ILE B 153
SHEET 4 F 5 PHE B 243 LEU B 246 1 O VAL B 244 N ILE B 208
SHEET 5 F 5 MET B 263 PHE B 264 1 N PHE B 264 O ALA B 245
SHEET 1 G 6 SER C 41 ASN C 45 0
SHEET 2 G 6 HIS C 50 ASP C 54 -1 O ILE C 51 N LEU C 44
SHEET 3 G 6 THR C 474 LYS C 481 -1 O SER C 476 N ASP C 54
SHEET 4 G 6 CYS C 404 GLN C 411 1 O CYS C 404 N ASN C 475
SHEET 5 G 6 THR C 335 PRO C 340 1 O ALA C 337 N ASP C 405
SHEET 6 G 6 ILE C 378 TRP C 380 1 O ILE C 378 N HIS C 336
SHEET 1 H 2 LEU C 112 VAL C 113 0
SHEET 2 H 2 LYS C 116 ASP C 117 -1 O LYS C 116 N VAL C 113
SHEET 1 I 5 ARG C 180 VAL C 184 0
SHEET 2 I 5 ASP C 151 ILE C 155 1 N VAL C 152 O ARG C 180
SHEET 3 I 5 SER C 204 ALA C 209 1 O LEU C 205 N ILE C 153
SHEET 4 I 5 PHE C 243 LEU C 246 1 O VAL C 244 N ILE C 208
SHEET 5 I 5 MET C 263 PHE C 264 1 N PHE C 264 O ALA C 245
SHEET 1 J 6 SER D 41 ASN D 45 0
SHEET 2 J 6 HIS D 50 LYS D 57 -1 O ILE D 51 N LEU D 44
SHEET 3 J 6 THR D 474 LYS D 481 -1 N THR D 474 O LYS D 57
SHEET 4 J 6 CYS D 404 GLN D 411 1 O CYS D 404 N ASN D 475
SHEET 5 J 6 THR D 335 PRO D 340 1 O ALA D 337 N ASP D 405
SHEET 6 J 6 ILE D 378 TRP D 380 1 O ILE D 378 N HIS D 336
SHEET 1 K 2 LEU D 112 VAL D 113 0
SHEET 2 K 2 LYS D 116 ASP D 117 -1 O LYS D 116 N VAL D 113
SHEET 1 L 5 ARG D 180 VAL D 184 0
SHEET 2 L 5 ASP D 151 ILE D 155 1 N VAL D 152 O ARG D 180
SHEET 3 L 5 SER D 204 ALA D 209 1 N LEU D 205 O ASP D 151
SHEET 4 L 5 PHE D 243 LEU D 246 1 O VAL D 244 N ILE D 208
SHEET 5 L 5 MET D 263 PHE D 264 1 N PHE D 264 O ALA D 245
CISPEP 1 GLY A 384 THR A 385 0 0.19
CISPEP 2 GLY B 384 THR B 385 0 2.66
CISPEP 3 GLY C 384 THR C 385 0 3.68
CISPEP 4 GLY D 384 THR D 385 0 2.08
CRYST1 80.770 107.400 270.700 90.00 90.00 90.00 P 21 21 21 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 0.012380 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009310 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003690 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
