HEADER TRANSFERASE 29-FEB-08 3CEH
TITLE HUMAN LIVER GLYCOGEN PHOSPHORYLASE (TENSE STATE) IN COMPLEX WITH THE
TITLE 2 ALLOSTERIC INHIBITOR AVE5688
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN PHOSPHORYLASE, LIVER FORM;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.4.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: PYGL;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS PROTEIN LIGAND COMPLEX, TENSE STATE, ALLOSTERIC INHIBITOR, ALLOSTERIC
KEYWDS 2 ENZYME, CARBOHYDRATE METABOLISM, DISEASE MUTATION, GLYCOGEN
KEYWDS 3 METABOLISM, GLYCOGEN STORAGE DISEASE, GLYCOSYLTRANSFERASE,
KEYWDS 4 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, PYRIDOXAL PHOSPHATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.U.WENDT,M.K.DREYER,O.ANDERKA,T.KLABUNDE,P.LOENZE,E.DEFOSSA,
AUTHOR 2 D.SCHMOLL
REVDAT 4 13-JUL-11 3CEH 1 VERSN
REVDAT 3 24-FEB-09 3CEH 1 VERSN
REVDAT 2 03-JUN-08 3CEH 1 JRNL
REVDAT 1 27-MAY-08 3CEH 0
JRNL AUTH O.ANDERKA,P.LOENZE,T.KLABUNDE,M.K.DREYER,E.DEFOSSA,
JRNL AUTH 2 K.U.WENDT,D.SCHMOLL
JRNL TITL THERMODYNAMIC CHARACTERIZATION OF ALLOSTERIC GLYCOGEN
JRNL TITL 2 PHOSPHORYLASE INHIBITORS.
JRNL REF BIOCHEMISTRY V. 47 4683 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18373353
JRNL DOI 10.1021/BI702397D
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 51525
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2618
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3620
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.02
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 204
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12898
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 142
REMARK 3 SOLVENT ATOMS : 508
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.373
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.269
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.906
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.877
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13375 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18108 ; 1.599 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1590 ; 6.800 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 648 ;37.826 ;24.275
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2376 ;19.033 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 80 ;16.734 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1969 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10112 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7080 ; 0.235 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 9117 ; 0.322 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 777 ; 0.175 ; 0.200
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): 58 ; 0.252 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.224 ; 0.200
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): 8140 ; 0.679 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12846 ; 1.173 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5973 ; 1.630 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5262 ; 2.680 ; 4.500
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3CEH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-08.
REMARK 100 THE RCSB ID CODE IS RCSB046677.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51974
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 43.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
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: NULL
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 (%): 57.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7 MG/ML IN 20 MM BES, 1 MM EDTA, 0.5
REMARK 280 MM DTT, PH 6.5, 50 MM NBG, 2.5 MM AVE5688, VAPOR DIFFUSION,
REMARK 280 HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,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 40.83033
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 81.66067
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASN A 253
REMARK 465 LEU A 254
REMARK 465 ARG A 255
REMARK 465 ASP A 256
REMARK 465 PHE A 257
REMARK 465 ASN A 258
REMARK 465 VAL A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 317
REMARK 465 SER A 318
REMARK 465 THR A 319
REMARK 465 ARG A 320
REMARK 465 GLY A 321
REMARK 465 ALA A 322
REMARK 465 GLY A 323
REMARK 465 ASN B 253
REMARK 465 LEU B 254
REMARK 465 ARG B 255
REMARK 465 ASP B 256
REMARK 465 PHE B 257
REMARK 465 ASN B 258
REMARK 465 VAL B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 317
REMARK 465 SER B 318
REMARK 465 THR B 319
REMARK 465 ARG B 320
REMARK 465 GLY B 321
REMARK 465 ALA B 322
REMARK 465 GLY B 323
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 OD2 ASP A 128 OG SER A 651 2.12
REMARK 500 ND2 ASN B 274 NH1 ARG B 277 2.13
REMARK 500 ND2 ASN A 274 NH1 ARG A 277 2.15
REMARK 500 NZ LYS A 680 O4A PLP A 832 2.15
REMARK 500 N THR A 324 O HOH A 995 2.17
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 LEU B 384 CA - CB - CG ANGL. DEV. = 17.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 76 -79.52 -76.13
REMARK 500 LEU A 131 50.43 -99.19
REMARK 500 TYR A 203 -141.56 62.13
REMARK 500 ASP A 217 53.86 37.96
REMARK 500 ASN A 235 -158.76 -128.16
REMARK 500 ASN A 250 -77.95 15.89
REMARK 500 LYS A 315 49.87 -106.74
REMARK 500 ASN A 338 96.05 -68.20
REMARK 500 ASP A 339 -159.88 56.00
REMARK 500 LEU A 344 -16.18 -49.59
REMARK 500 LYS A 358 12.98 58.32
REMARK 500 HIS A 410 -74.12 -49.34
REMARK 500 ARG A 413 0.25 -69.99
REMARK 500 LYS A 466 -75.46 -106.02
REMARK 500 ARG A 489 -73.04 -86.79
REMARK 500 LEU A 492 -74.54 -128.11
REMARK 500 GLU A 552 -73.35 -99.70
REMARK 500 VAL A 555 129.75 -175.50
REMARK 500 LYS A 568 164.19 166.12
REMARK 500 THR A 585 -61.89 -28.46
REMARK 500 ASP A 593 68.10 -151.93
REMARK 500 SER A 674 -56.31 -145.07
REMARK 500 GLU A 701 -51.88 -28.50
REMARK 500 LYS A 753 -5.98 -58.26
REMARK 500 GLN A 754 81.83 -157.19
REMARK 500 PRO A 755 10.88 -69.82
REMARK 500 HIS A 768 -15.62 -150.54
REMARK 500 ASP A 769 95.43 -64.04
REMARK 500 PRO A 794 -50.58 -26.90
REMARK 500 ILE A 824 -54.33 -121.13
REMARK 500 PRO A 829 55.96 -59.53
REMARK 500 CYS B 78 56.05 34.84
REMARK 500 LEU B 131 43.34 -92.26
REMARK 500 ASP B 181 43.94 -80.81
REMARK 500 TYR B 203 -139.41 66.92
REMARK 500 HIS B 208 75.02 -105.16
REMARK 500 ASN B 235 -151.79 -133.04
REMARK 500 ASP B 251 106.07 78.99
REMARK 500 SER B 276 34.12 -91.01
REMARK 500 LYS B 315 -62.37 -3.61
REMARK 500 ASP B 339 -170.98 70.10
REMARK 500 PRO B 342 40.98 -90.91
REMARK 500 PRO B 381 -49.59 -28.83
REMARK 500 PHE B 418 58.33 -156.12
REMARK 500 LEU B 425 -72.80 -60.58
REMARK 500 LYS B 437 112.15 78.54
REMARK 500 LYS B 466 -83.66 -109.18
REMARK 500 GLU B 475 75.55 -158.50
REMARK 500 ARG B 489 -76.03 -71.03
REMARK 500 LEU B 492 -72.83 -130.86
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 249 ASN A 250 141.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP A 42 22.5 L L OUTSIDE RANGE
REMARK 500 VAL B 447 24.9 L L OUTSIDE RANGE
REMARK 500 ASP B 756 23.5 L L OUTSIDE RANGE
REMARK 500 ASP B 831 21.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B1040 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH B1104 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH B1105 DISTANCE = 7.38 ANGSTROMS
REMARK 525 HOH B1106 DISTANCE = 5.44 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBG A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBG B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 832
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 832
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AVE A 833
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AVE B 833
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CEJ RELATED DB: PDB
REMARK 900 RELATED ID: 3CEM RELATED DB: PDB
DBREF 3CEH A 23 831 UNP P06737 PYGL_HUMAN 24 832
DBREF 3CEH B 23 831 UNP P06737 PYGL_HUMAN 24 832
SEQRES 1 A 809 ASN VAL ALA GLU LEU LYS LYS SER PHE ASN ARG HIS LEU
SEQRES 2 A 809 HIS PHE THR LEU VAL LYS ASP ARG ASN VAL ALA THR THR
SEQRES 3 A 809 ARG ASP TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP
SEQRES 4 A 809 HIS LEU VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR
SEQRES 5 A 809 TYR ASP LYS CYS PRO LYS ARG VAL TYR TYR LEU SER LEU
SEQRES 6 A 809 GLU PHE TYR MET GLY ARG THR LEU GLN ASN THR MET ILE
SEQRES 7 A 809 ASN LEU GLY LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR
SEQRES 8 A 809 GLN LEU GLY LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU
SEQRES 9 A 809 GLU ASP ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU
SEQRES 10 A 809 ALA ALA CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU
SEQRES 11 A 809 ALA ALA TYR GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE
SEQRES 12 A 809 PHE ASN GLN LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU
SEQRES 13 A 809 ALA ASP ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS
SEQRES 14 A 809 SER ARG PRO GLU PHE MET LEU PRO VAL HIS PHE TYR GLY
SEQRES 15 A 809 LYS VAL GLU HIS THR ASN THR GLY THR LYS TRP ILE ASP
SEQRES 16 A 809 THR GLN VAL VAL LEU ALA LEU PRO TYR ASP THR PRO VAL
SEQRES 17 A 809 PRO GLY TYR MET ASN ASN THR VAL ASN THR MET ARG LEU
SEQRES 18 A 809 TRP SER ALA ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP
SEQRES 19 A 809 PHE ASN VAL GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG
SEQRES 20 A 809 ASN LEU ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN
SEQRES 21 A 809 ASP ASN PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN
SEQRES 22 A 809 GLU TYR PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE
SEQRES 23 A 809 ARG ARG PHE LYS ALA SER LYS PHE GLY SER THR ARG GLY
SEQRES 24 A 809 ALA GLY THR VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA
SEQRES 25 A 809 ILE GLN LEU ASN ASP THR HIS PRO ALA LEU ALA ILE PRO
SEQRES 26 A 809 GLU LEU MET ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO
SEQRES 27 A 809 TRP SER LYS ALA TRP GLU LEU THR GLN LYS THR PHE ALA
SEQRES 28 A 809 TYR THR ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG
SEQRES 29 A 809 TRP PRO VAL ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS
SEQRES 30 A 809 LEU GLU ILE ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP
SEQRES 31 A 809 ARG ILE VAL ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU
SEQRES 32 A 809 ARG ARG MET SER LEU ILE GLU GLU GLU GLY SER LYS ARG
SEQRES 33 A 809 ILE ASN MET ALA HIS LEU CYS ILE VAL GLY SER HIS ALA
SEQRES 34 A 809 VAL ASN GLY VAL ALA LYS ILE HIS SER ASP ILE VAL LYS
SEQRES 35 A 809 THR LYS VAL PHE LYS ASP PHE SER GLU LEU GLU PRO ASP
SEQRES 36 A 809 LYS PHE GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG
SEQRES 37 A 809 TRP LEU LEU LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE
SEQRES 38 A 809 ALA GLU LYS ILE GLY GLU ASP TYR VAL LYS ASP LEU SER
SEQRES 39 A 809 GLN LEU THR LYS LEU HIS SER PHE LEU GLY ASP ASP VAL
SEQRES 40 A 809 PHE LEU ARG GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS
SEQRES 41 A 809 LEU LYS PHE SER GLN PHE LEU GLU THR GLU TYR LYS VAL
SEQRES 42 A 809 LYS ILE ASN PRO SER SER MET PHE ASP VAL GLN VAL LYS
SEQRES 43 A 809 ARG ILE HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU
SEQRES 44 A 809 HIS VAL ILE THR MET TYR ASN ARG ILE LYS LYS ASP PRO
SEQRES 45 A 809 LYS LYS LEU PHE VAL PRO ARG THR VAL ILE ILE GLY GLY
SEQRES 46 A 809 LYS ALA ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE
SEQRES 47 A 809 LYS LEU ILE THR SER VAL ALA ASP VAL VAL ASN ASN ASP
SEQRES 48 A 809 PRO MET VAL GLY SER LYS LEU LYS VAL ILE PHE LEU GLU
SEQRES 49 A 809 ASN TYR ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA
SEQRES 50 A 809 THR ASP LEU SER GLU GLN ILE SER THR ALA GLY THR GLU
SEQRES 51 A 809 ALA SER GLY THR GLY ASN MET LYS PHE MET LEU ASN GLY
SEQRES 52 A 809 ALA LEU THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU
SEQRES 53 A 809 MET ALA GLU GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE
SEQRES 54 A 809 GLY MET ARG ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS
SEQRES 55 A 809 GLY TYR GLU ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU
SEQRES 56 A 809 LEU LYS LEU VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE
SEQRES 57 A 809 SER PRO LYS GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN
SEQRES 58 A 809 MET LEU PHE TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP
SEQRES 59 A 809 TYR GLU ALA TYR VAL LYS CYS GLN ASP LYS VAL SER GLN
SEQRES 60 A 809 LEU TYR MET ASN PRO LYS ALA TRP ASN THR MET VAL LEU
SEQRES 61 A 809 LYS ASN ILE ALA ALA SER GLY LYS PHE SER SER ASP ARG
SEQRES 62 A 809 THR ILE LYS GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU
SEQRES 63 A 809 PRO SER ASP
SEQRES 1 B 809 ASN VAL ALA GLU LEU LYS LYS SER PHE ASN ARG HIS LEU
SEQRES 2 B 809 HIS PHE THR LEU VAL LYS ASP ARG ASN VAL ALA THR THR
SEQRES 3 B 809 ARG ASP TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP
SEQRES 4 B 809 HIS LEU VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR
SEQRES 5 B 809 TYR ASP LYS CYS PRO LYS ARG VAL TYR TYR LEU SER LEU
SEQRES 6 B 809 GLU PHE TYR MET GLY ARG THR LEU GLN ASN THR MET ILE
SEQRES 7 B 809 ASN LEU GLY LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR
SEQRES 8 B 809 GLN LEU GLY LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU
SEQRES 9 B 809 GLU ASP ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU
SEQRES 10 B 809 ALA ALA CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU
SEQRES 11 B 809 ALA ALA TYR GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE
SEQRES 12 B 809 PHE ASN GLN LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU
SEQRES 13 B 809 ALA ASP ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS
SEQRES 14 B 809 SER ARG PRO GLU PHE MET LEU PRO VAL HIS PHE TYR GLY
SEQRES 15 B 809 LYS VAL GLU HIS THR ASN THR GLY THR LYS TRP ILE ASP
SEQRES 16 B 809 THR GLN VAL VAL LEU ALA LEU PRO TYR ASP THR PRO VAL
SEQRES 17 B 809 PRO GLY TYR MET ASN ASN THR VAL ASN THR MET ARG LEU
SEQRES 18 B 809 TRP SER ALA ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP
SEQRES 19 B 809 PHE ASN VAL GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG
SEQRES 20 B 809 ASN LEU ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN
SEQRES 21 B 809 ASP ASN PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN
SEQRES 22 B 809 GLU TYR PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE
SEQRES 23 B 809 ARG ARG PHE LYS ALA SER LYS PHE GLY SER THR ARG GLY
SEQRES 24 B 809 ALA GLY THR VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA
SEQRES 25 B 809 ILE GLN LEU ASN ASP THR HIS PRO ALA LEU ALA ILE PRO
SEQRES 26 B 809 GLU LEU MET ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO
SEQRES 27 B 809 TRP SER LYS ALA TRP GLU LEU THR GLN LYS THR PHE ALA
SEQRES 28 B 809 TYR THR ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG
SEQRES 29 B 809 TRP PRO VAL ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS
SEQRES 30 B 809 LEU GLU ILE ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP
SEQRES 31 B 809 ARG ILE VAL ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU
SEQRES 32 B 809 ARG ARG MET SER LEU ILE GLU GLU GLU GLY SER LYS ARG
SEQRES 33 B 809 ILE ASN MET ALA HIS LEU CYS ILE VAL GLY SER HIS ALA
SEQRES 34 B 809 VAL ASN GLY VAL ALA LYS ILE HIS SER ASP ILE VAL LYS
SEQRES 35 B 809 THR LYS VAL PHE LYS ASP PHE SER GLU LEU GLU PRO ASP
SEQRES 36 B 809 LYS PHE GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG
SEQRES 37 B 809 TRP LEU LEU LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE
SEQRES 38 B 809 ALA GLU LYS ILE GLY GLU ASP TYR VAL LYS ASP LEU SER
SEQRES 39 B 809 GLN LEU THR LYS LEU HIS SER PHE LEU GLY ASP ASP VAL
SEQRES 40 B 809 PHE LEU ARG GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS
SEQRES 41 B 809 LEU LYS PHE SER GLN PHE LEU GLU THR GLU TYR LYS VAL
SEQRES 42 B 809 LYS ILE ASN PRO SER SER MET PHE ASP VAL GLN VAL LYS
SEQRES 43 B 809 ARG ILE HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU
SEQRES 44 B 809 HIS VAL ILE THR MET TYR ASN ARG ILE LYS LYS ASP PRO
SEQRES 45 B 809 LYS LYS LEU PHE VAL PRO ARG THR VAL ILE ILE GLY GLY
SEQRES 46 B 809 LYS ALA ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE
SEQRES 47 B 809 LYS LEU ILE THR SER VAL ALA ASP VAL VAL ASN ASN ASP
SEQRES 48 B 809 PRO MET VAL GLY SER LYS LEU LYS VAL ILE PHE LEU GLU
SEQRES 49 B 809 ASN TYR ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA
SEQRES 50 B 809 THR ASP LEU SER GLU GLN ILE SER THR ALA GLY THR GLU
SEQRES 51 B 809 ALA SER GLY THR GLY ASN MET LYS PHE MET LEU ASN GLY
SEQRES 52 B 809 ALA LEU THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU
SEQRES 53 B 809 MET ALA GLU GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE
SEQRES 54 B 809 GLY MET ARG ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS
SEQRES 55 B 809 GLY TYR GLU ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU
SEQRES 56 B 809 LEU LYS LEU VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE
SEQRES 57 B 809 SER PRO LYS GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN
SEQRES 58 B 809 MET LEU PHE TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP
SEQRES 59 B 809 TYR GLU ALA TYR VAL LYS CYS GLN ASP LYS VAL SER GLN
SEQRES 60 B 809 LEU TYR MET ASN PRO LYS ALA TRP ASN THR MET VAL LEU
SEQRES 61 B 809 LYS ASN ILE ALA ALA SER GLY LYS PHE SER SER ASP ARG
SEQRES 62 B 809 THR ILE LYS GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU
SEQRES 63 B 809 PRO SER ASP
HET NBG A 1 15
HET NBG B 2 15
HET PO4 A 3 5
HET PO4 B 4 5
HET PLP A 832 16
HET AVE A 833 29
HET MES B 1 12
HET PLP B 832 16
HET AVE B 833 29
HETNAM NBG 1-N-ACETYL-BETA-D-GLUCOSAMINE
HETNAM PO4 PHOSPHATE ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM AVE 4-[3-(2-CHLORO-4,5-DIFLUORO-BENZOYL)UREIDO]-3-
HETNAM 2 AVE TRIFLUOROMETHOXYBENZOIC ACID
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETSYN PLP VITAMIN B6 PHOSPHATE
HETSYN AVE 4-({[(2-CHLORO-4,5-DIFLUOROPHENYL)
HETSYN 2 AVE CARBONYL]CARBAMOYL}AMINO)-3-(TRIFLUOROMETHOXY)BENZOIC
HETSYN 3 AVE ACID
FORMUL 3 NBG 2(C8 H15 N O6)
FORMUL 5 PO4 2(O4 P 3-)
FORMUL 7 PLP 2(C8 H10 N O6 P)
FORMUL 8 AVE 2(C16 H8 CL F5 N2 O5)
FORMUL 9 MES C6 H13 N O4 S
FORMUL 12 HOH *508(H2 O)
HELIX 1 1 ASN A 23 THR A 38 1 16
HELIX 2 2 ASP A 42 ALA A 46 5 5
HELIX 3 3 THR A 47 CYS A 78 1 32
HELIX 4 4 THR A 94 LEU A 102 1 9
HELIX 5 5 LEU A 104 LEU A 115 1 12
HELIX 6 6 ASP A 118 GLU A 126 1 9
HELIX 7 7 GLY A 134 LEU A 150 1 17
HELIX 8 8 PRO A 194 MET A 197 5 4
HELIX 9 9 ASP A 261 ASP A 268 1 8
HELIX 10 10 ASP A 268 ASN A 274 1 7
HELIX 11 11 ILE A 275 ARG A 277 5 3
HELIX 12 12 LYS A 289 SER A 314 1 26
HELIX 13 13 ALA A 328 GLN A 332 1 5
HELIX 14 14 LEU A 344 ILE A 356 1 13
HELIX 15 15 PRO A 360 THR A 371 1 12
HELIX 16 16 LEU A 380 LEU A 384 5 5
HELIX 17 17 VAL A 389 LEU A 396 1 8
HELIX 18 18 LEU A 396 ALA A 416 1 21
HELIX 19 19 ASP A 421 SER A 429 1 9
HELIX 20 20 MET A 441 GLY A 448 1 8
HELIX 21 21 ALA A 456 LYS A 466 1 11
HELIX 22 22 PHE A 468 GLU A 473 1 6
HELIX 23 23 GLU A 475 ASP A 477 5 3
HELIX 24 24 ASN A 496 GLY A 508 1 13
HELIX 25 25 GLU A 509 LYS A 513 5 5
HELIX 26 26 ASP A 514 GLY A 526 5 13
HELIX 27 27 ASP A 527 THR A 551 1 25
HELIX 28 28 ARG A 575 LYS A 592 1 18
HELIX 29 29 TYR A 613 ASN A 631 1 19
HELIX 30 30 ARG A 649 ILE A 657 1 9
HELIX 31 31 PRO A 658 THR A 660 5 3
HELIX 32 32 THR A 676 ASN A 684 1 9
HELIX 33 33 ASP A 693 GLY A 704 1 12
HELIX 34 34 GLU A 705 LEU A 708 5 4
HELIX 35 35 ARG A 714 GLY A 725 1 12
HELIX 36 36 ALA A 728 LEU A 735 1 8
HELIX 37 37 LEU A 735 GLY A 748 1 14
HELIX 38 38 PHE A 758 HIS A 768 1 11
HELIX 39 39 VAL A 773 ALA A 775 5 3
HELIX 40 40 ASP A 776 MET A 792 1 17
HELIX 41 41 ASN A 793 ALA A 806 1 14
HELIX 42 42 ALA A 807 PHE A 811 5 5
HELIX 43 43 SER A 812 ILE A 824 1 13
HELIX 44 44 ASN B 23 THR B 38 1 16
HELIX 45 45 ASP B 42 ALA B 46 5 5
HELIX 46 46 THR B 47 HIS B 62 1 16
HELIX 47 47 LEU B 63 CYS B 78 1 16
HELIX 48 48 THR B 94 LEU B 102 1 9
HELIX 49 49 LEU B 104 LEU B 115 1 12
HELIX 50 50 ASP B 118 GLU B 126 1 9
HELIX 51 51 GLY B 134 LEU B 150 1 17
HELIX 52 52 PRO B 194 MET B 197 5 4
HELIX 53 53 ASP B 261 ARG B 269 1 9
HELIX 54 54 ARG B 269 ASN B 274 1 6
HELIX 55 55 LYS B 289 ALA B 313 1 25
HELIX 56 56 THR B 324 ASP B 327 5 4
HELIX 57 57 ALA B 328 GLN B 332 1 5
HELIX 58 58 LEU B 344 ILE B 356 1 13
HELIX 59 59 PRO B 360 THR B 371 1 12
HELIX 60 60 LEU B 380 LEU B 384 5 5
HELIX 61 61 VAL B 389 LEU B 396 1 8
HELIX 62 62 LEU B 396 PHE B 418 1 23
HELIX 63 63 ASP B 421 SER B 429 1 9
HELIX 64 64 MET B 441 SER B 449 1 9
HELIX 65 65 ALA B 456 LYS B 466 1 11
HELIX 66 66 PHE B 468 GLU B 475 1 8
HELIX 67 67 ASN B 496 GLY B 508 1 13
HELIX 68 68 GLU B 509 LYS B 513 5 5
HELIX 69 69 ASP B 514 LEU B 525 5 12
HELIX 70 70 ASP B 527 TYR B 553 1 27
HELIX 71 71 ARG B 575 ASP B 593 1 19
HELIX 72 72 TYR B 613 ASP B 633 1 21
HELIX 73 73 VAL B 636 SER B 638 5 3
HELIX 74 74 ARG B 649 ILE B 657 1 9
HELIX 75 75 PRO B 658 THR B 660 5 3
HELIX 76 76 THR B 676 ASN B 684 1 9
HELIX 77 77 ALA B 695 GLY B 704 1 10
HELIX 78 78 GLU B 705 LEU B 708 5 4
HELIX 79 79 ARG B 714 GLY B 725 1 12
HELIX 80 80 GLU B 727 LEU B 735 1 9
HELIX 81 81 LEU B 735 ASN B 747 1 13
HELIX 82 82 PHE B 758 HIS B 768 1 11
HELIX 83 83 LYS B 772 MET B 792 1 21
HELIX 84 84 ASN B 793 ALA B 806 1 14
HELIX 85 85 ALA B 807 PHE B 811 5 5
HELIX 86 86 SER B 812 ILE B 824 1 13
SHEET 1 A 3 LYS A 191 SER A 192 0
SHEET 2 A 3 GLN A 219 PRO A 231 -1 O ASP A 227 N LYS A 191
SHEET 3 A 3 LEU A 198 PHE A 202 -1 N VAL A 200 O VAL A 221
SHEET 1 B 9 LYS A 191 SER A 192 0
SHEET 2 B 9 GLN A 219 PRO A 231 -1 O ASP A 227 N LYS A 191
SHEET 3 B 9 VAL A 238 ARG A 247 -1 O ARG A 247 N LEU A 222
SHEET 4 B 9 ALA A 154 ILE A 159 1 N GLY A 156 O ARG A 242
SHEET 5 B 9 ARG A 81 LEU A 85 1 N TYR A 84 O TYR A 155
SHEET 6 B 9 VAL A 333 ASN A 338 1 O ALA A 334 N ARG A 81
SHEET 7 B 9 PHE A 372 THR A 375 1 O ALA A 373 N LEU A 337
SHEET 8 B 9 ALA A 451 GLY A 454 1 O ALA A 451 N TYR A 374
SHEET 9 B 9 PHE A 479 ASN A 481 1 O GLN A 480 N VAL A 452
SHEET 1 C 2 PHE A 89 GLY A 92 0
SHEET 2 C 2 ALA A 129 LEU A 131 -1 O LEU A 131 N PHE A 89
SHEET 1 D 2 ASN A 167 ARG A 171 0
SHEET 2 D 2 TRP A 174 GLU A 178 -1 O VAL A 176 N LYS A 169
SHEET 1 E 2 LYS A 205 THR A 209 0
SHEET 2 E 2 GLY A 212 ILE A 216 -1 O LYS A 214 N GLU A 207
SHEET 1 F 3 ARG A 386 PRO A 388 0
SHEET 2 F 3 ARG A 438 ASN A 440 -1 O ILE A 439 N TRP A 387
SHEET 3 F 3 ILE A 431 GLU A 432 -1 N GLU A 432 O ARG A 438
SHEET 1 G 6 LEU A 640 LEU A 645 0
SHEET 2 G 6 ARG A 601 GLY A 606 1 N VAL A 603 O ILE A 643
SHEET 3 G 6 MET A 562 VAL A 567 1 N ASP A 564 O THR A 602
SHEET 4 G 6 LEU A 662 GLN A 665 1 O LEU A 662 N PHE A 563
SHEET 5 G 6 LEU A 687 GLY A 690 1 O ILE A 689 N GLN A 665
SHEET 6 G 6 PHE A 709 ILE A 710 1 O PHE A 709 N THR A 688
SHEET 1 H 3 LYS B 191 SER B 192 0
SHEET 2 H 3 GLN B 219 PRO B 231 -1 O ASP B 227 N LYS B 191
SHEET 3 H 3 LEU B 198 PHE B 202 -1 N PHE B 202 O GLN B 219
SHEET 1 I 9 LYS B 191 SER B 192 0
SHEET 2 I 9 GLN B 219 PRO B 231 -1 O ASP B 227 N LYS B 191
SHEET 3 I 9 VAL B 238 ARG B 247 -1 O ARG B 247 N LEU B 222
SHEET 4 I 9 ALA B 154 ILE B 159 1 N GLY B 156 O ARG B 242
SHEET 5 I 9 ARG B 81 LEU B 85 1 N VAL B 82 O TYR B 155
SHEET 6 I 9 VAL B 333 ASN B 338 1 O ALA B 334 N TYR B 83
SHEET 7 I 9 PHE B 372 THR B 375 1 O ALA B 373 N LEU B 337
SHEET 8 I 9 ALA B 451 GLY B 454 1 O ALA B 451 N TYR B 374
SHEET 9 I 9 PHE B 479 ASN B 481 1 O GLN B 480 N VAL B 452
SHEET 1 J 2 PHE B 89 TYR B 90 0
SHEET 2 J 2 GLY B 130 LEU B 131 -1 O LEU B 131 N PHE B 89
SHEET 1 K 2 ASN B 167 ILE B 170 0
SHEET 2 K 2 GLN B 175 GLU B 178 -1 O VAL B 176 N LYS B 169
SHEET 1 L 2 LYS B 205 THR B 209 0
SHEET 2 L 2 GLY B 212 ILE B 216 -1 O LYS B 214 N GLU B 207
SHEET 1 M 3 ARG B 386 PRO B 388 0
SHEET 2 M 3 ARG B 438 ASN B 440 -1 O ILE B 439 N TRP B 387
SHEET 3 M 3 ILE B 431 GLU B 432 -1 N GLU B 432 O ARG B 438
SHEET 1 N 6 LEU B 640 LEU B 645 0
SHEET 2 N 6 ARG B 601 GLY B 606 1 N ILE B 605 O LEU B 645
SHEET 3 N 6 MET B 562 VAL B 567 1 N GLN B 566 O ILE B 604
SHEET 4 N 6 LEU B 662 GLN B 665 1 O LEU B 662 N VAL B 565
SHEET 5 N 6 LEU B 687 GLY B 690 1 O LEU B 687 N SER B 663
SHEET 6 N 6 PHE B 709 ILE B 710 1 O PHE B 709 N THR B 688
LINK NZ LYS A 680 C4A PLP A 832 1555 1555 1.61
LINK NZ LYS B 680 C4A PLP B 832 1555 1555 1.45
SITE 1 AC1 9 GLY A 135 LEU A 136 ASN A 284 HIS A 377
SITE 2 AC1 9 ASN A 484 TYR A 573 GLU A 672 SER A 674
SITE 3 AC1 9 GLY A 675
SITE 1 AC2 11 GLY B 135 LEU B 136 ASN B 284 HIS B 377
SITE 2 AC2 11 THR B 378 ASN B 484 TYR B 573 GLU B 672
SITE 3 AC2 11 ALA B 673 SER B 674 GLY B 675
SITE 1 AC3 5 ARG A 193 PHE A 196 ARG A 242 ARG A 309
SITE 2 AC3 5 ARG A 310
SITE 1 AC4 4 PHE B 196 ARG B 242 ARG B 309 ARG B 310
SITE 1 AC5 11 GLY A 134 GLY A 135 TRP A 491 LYS A 568
SITE 2 AC5 11 LYS A 574 TYR A 648 ARG A 649 GLY A 675
SITE 3 AC5 11 THR A 676 GLY A 677 LYS A 680
SITE 1 AC6 11 GLY B 134 GLY B 135 TRP B 491 LYS B 568
SITE 2 AC6 11 LYS B 574 TYR B 648 ARG B 649 GLY B 675
SITE 3 AC6 11 THR B 676 GLY B 677 LYS B 680
SITE 1 AC7 7 ARG B 49 ARG B 93 GLU B 124 ILE B 125
SITE 2 AC7 7 GLU B 126 GLU B 127 ARG B 649
SITE 1 AC8 12 TRP A 67 ILE A 68 GLN A 71 GLN A 72
SITE 2 AC8 12 TYR A 75 LYS A 191 ARG A 193 ASP A 227
SITE 3 AC8 12 LEU B 39 LYS B 41 ASP B 42 ASN B 44
SITE 1 AC9 12 LEU A 39 LYS A 41 ASP A 42 ASN A 44
SITE 2 AC9 12 TRP B 67 ILE B 68 GLN B 71 GLN B 72
SITE 3 AC9 12 TYR B 75 LYS B 191 ARG B 193 ASP B 227
CRYST1 124.115 124.115 122.491 90.00 90.00 120.00 P 31 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 0.008057 0.004652 0.000000 0.00000
SCALE2 0.000000 0.009303 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008164 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
