HEADER TRANSFERASE 12-JUL-00 1FA9
TITLE HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH AMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN PHOSPHORYLASE, LIVER FORM;
COMPND 3 CHAIN: A;
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 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKK2332
KEYWDS PROTEIN-LIGAND COMPLEX, ALLOSTERIC PROTEIN, PHOSPHORYLATED PROTEIN,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.L.RATH,M.AMMIRATI,P.K.LEMOTTE,K.F.FENNELL,M.N.MANSOUR,D.E.DANLEY,
AUTHOR 2 T.R.HYNES,G.K.SCHULTE,D.J.WASILKO,J.PANDIT
REVDAT 7 09-AUG-23 1FA9 1 HETSYN
REVDAT 6 29-JUL-20 1FA9 1 COMPND REMARK SEQADV HETNAM
REVDAT 6 2 1 LINK SITE
REVDAT 5 31-JAN-18 1FA9 1 REMARK
REVDAT 4 13-JUL-11 1FA9 1 VERSN
REVDAT 3 24-FEB-09 1FA9 1 VERSN
REVDAT 2 01-APR-03 1FA9 1 JRNL
REVDAT 1 25-AUG-00 1FA9 0
JRNL AUTH V.L.RATH,M.AMMIRATI,P.K.LEMOTTE,K.F.FENNELL,M.N.MANSOUR,
JRNL AUTH 2 D.E.DANLEY,T.R.HYNES,G.K.SCHULTE,D.J.WASILKO,J.PANDIT
JRNL TITL ACTIVATION OF HUMAN LIVER GLYCOGEN PHOSPHORYLASE BY
JRNL TITL 2 ALTERATION OF THE SECONDARY STRUCTURE AND PACKING OF THE
JRNL TITL 3 CATALYTIC CORE.
JRNL REF MOL.CELL V. 6 139 2000
JRNL REFN ISSN 1097-2765
JRNL PMID 10949035
JRNL DOI 10.1016/S1097-2765(00)00015-0
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 43732
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : X-PLOR
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4101
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.42
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3530
REMARK 3 BIN FREE R VALUE : 0.4760
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6750
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 242
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FA9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000011436.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-94
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43732
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 9.000
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.49500
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: X-PLOR
REMARK 200 STARTING MODEL: 1GPA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, TRIS/HCL, AMP, GLUCOSE, PH
REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 25K, TEMPERATURE
REMARK 280 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 42.56000
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 85.12000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 85.12000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 42.56000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER CONSTRUCTED FROM CHAIN A
REMARK 300 A SYMMETRY PARTNER GENERATED BY THE TWO-FOLD.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 10080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 61620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 127.68000
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 ALA A 1
REMARK 465 LYS A 2
REMARK 465 PRO A 3
REMARK 465 LEU A 4
REMARK 465 GLU A 839
REMARK 465 SER A 840
REMARK 465 ASN A 841
REMARK 465 LYS A 842
REMARK 465 VAL A 843
REMARK 465 ASN A 844
REMARK 465 GLY A 845
REMARK 465 ASN A 846
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR A 5 OG1 CG2
REMARK 470 SER A 837 OG
REMARK 470 ASN A 838 CG OD1 ND2
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 SER A 318 N THR A 319 1.41
REMARK 500 O SER A 318 OG1 THR A 319 1.56
REMARK 500 CA GLY A 321 N ALA A 322 1.63
REMARK 500 N GLY A 321 N ALA A 322 1.75
REMARK 500 NH1 ARG A 320 CA GLY A 323 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CG2 THR A 319 CD2 LEU A 543 5665 1.53
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 THR A 319 C ARG A 320 N -0.173
REMARK 500 ARG A 320 C GLY A 321 N -0.145
REMARK 500 GLY A 321 N GLY A 321 CA -0.101
REMARK 500 GLY A 321 C ALA A 322 N -0.586
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 THR A 319 CA - C - N ANGL. DEV. = -16.6 DEGREES
REMARK 500 THR A 319 O - C - N ANGL. DEV. = 15.3 DEGREES
REMARK 500 ARG A 320 CA - C - N ANGL. DEV. = -19.0 DEGREES
REMARK 500 ARG A 320 O - C - N ANGL. DEV. = 18.4 DEGREES
REMARK 500 GLY A 321 C - N - CA ANGL. DEV. = 12.7 DEGREES
REMARK 500 GLY A 321 N - CA - C ANGL. DEV. = -25.8 DEGREES
REMARK 500 GLY A 321 CA - C - N ANGL. DEV. = -30.2 DEGREES
REMARK 500 GLY A 321 O - C - N ANGL. DEV. = 24.3 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 6 -103.71 -153.05
REMARK 500 GLN A 7 179.79 77.69
REMARK 500 ILE A 18 23.61 -76.78
REMARK 500 LEU A 95 -72.15 -50.19
REMARK 500 PHE A 166 159.44 159.59
REMARK 500 TYR A 203 -140.74 57.27
REMARK 500 MET A 234 28.41 45.97
REMARK 500 ASN A 282 108.90 -49.16
REMARK 500 ASN A 284 6.34 -64.99
REMARK 500 ASP A 339 -166.49 74.50
REMARK 500 LEU A 417 -18.38 -159.34
REMARK 500 SER A 436 114.59 139.70
REMARK 500 LYS A 466 -79.07 -75.54
REMARK 500 ASP A 477 -9.75 -59.62
REMARK 500 LEU A 492 -69.46 -142.21
REMARK 500 PHE A 563 77.78 79.23
REMARK 500 LYS A 568 172.46 178.67
REMARK 500 ARG A 575 -101.76 74.71
REMARK 500 GLN A 576 -15.42 55.71
REMARK 500 ASP A 593 133.95 168.58
REMARK 500 PRO A 594 -157.78 -65.03
REMARK 500 LYS A 595 -37.23 68.62
REMARK 500 SER A 638 39.14 -68.54
REMARK 500 GLN A 665 55.08 -118.86
REMARK 500 ILE A 666 37.99 -91.86
REMARK 500 SER A 674 -159.31 -133.78
REMARK 500 ASP A 722 34.98 -82.65
REMARK 500 LYS A 723 -18.33 -142.69
REMARK 500 LYS A 724 -61.30 -106.27
REMARK 500 PRO A 736 -70.77 -64.21
REMARK 500 PHE A 766 -93.21 -78.34
REMARK 500 HIS A 768 22.14 -141.57
REMARK 500 ASP A 769 -175.08 -64.92
REMARK 500 ARG A 770 -21.33 -163.78
REMARK 500 LYS A 772 72.38 49.44
REMARK 500 ILE A 824 -52.03 -122.36
REMARK 500 SER A 837 73.60 -110.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG A 320 10.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FC0 RELATED DB: PDB
REMARK 900 1FC0 CONTAINS THE SAME PROTEIN COMPLEXED WITH N-ACETYL-BETA-D-
REMARK 900 GLUCOPYRANOSYLAMINE
DBREF 1FA9 A 1 846 UNP P06737 PHS1_HUMAN 2 847
SEQADV 1FA9 SEP A 14 UNP P06737 SER 15 MODIFIED RESIDUE
SEQRES 1 A 846 ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN ILE
SEQRES 2 A 846 SEP ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA GLU
SEQRES 3 A 846 LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR LEU
SEQRES 4 A 846 VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR TYR
SEQRES 5 A 846 PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY
SEQRES 6 A 846 ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS CYS
SEQRES 7 A 846 PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR MET
SEQRES 8 A 846 GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY LEU
SEQRES 9 A 846 GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY LEU
SEQRES 10 A 846 ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY
SEQRES 11 A 846 LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE
SEQRES 12 A 846 LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY
SEQRES 13 A 846 TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN LYS
SEQRES 14 A 846 ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP TRP
SEQRES 15 A 846 LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO GLU
SEQRES 16 A 846 PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU HIS
SEQRES 17 A 846 THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL VAL
SEQRES 18 A 846 LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR MET
SEQRES 19 A 846 ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA ARG
SEQRES 20 A 846 ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL GLY
SEQRES 21 A 846 ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU
SEQRES 22 A 846 ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE
SEQRES 23 A 846 GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL
SEQRES 24 A 846 VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS
SEQRES 25 A 846 ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR VAL
SEQRES 26 A 846 PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU ASN
SEQRES 27 A 846 ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET ARG
SEQRES 28 A 846 ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS ALA
SEQRES 29 A 846 TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN HIS
SEQRES 30 A 846 THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL ASP
SEQRES 31 A 846 LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE ILE
SEQRES 32 A 846 TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL ALA
SEQRES 33 A 846 LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET SER
SEQRES 34 A 846 LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET ALA
SEQRES 35 A 846 HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY VAL
SEQRES 36 A 846 ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL PHE
SEQRES 37 A 846 LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN ASN
SEQRES 38 A 846 LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU LEU
SEQRES 39 A 846 CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS ILE
SEQRES 40 A 846 GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR LYS
SEQRES 41 A 846 LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG GLU
SEQRES 42 A 846 LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE SER
SEQRES 43 A 846 GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN PRO
SEQRES 44 A 846 SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU
SEQRES 45 A 846 TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR
SEQRES 46 A 846 MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU PHE
SEQRES 47 A 846 VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA PRO
SEQRES 48 A 846 GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR
SEQRES 49 A 846 SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL GLY
SEQRES 50 A 846 SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG VAL
SEQRES 51 A 846 SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU SER
SEQRES 52 A 846 GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR
SEQRES 53 A 846 GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE
SEQRES 54 A 846 GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU
SEQRES 55 A 846 ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG ILE
SEQRES 56 A 846 ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU ALA
SEQRES 57 A 846 LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU VAL
SEQRES 58 A 846 ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS GLN
SEQRES 59 A 846 PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE TYR
SEQRES 60 A 846 HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA TYR
SEQRES 61 A 846 VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET ASN
SEQRES 62 A 846 PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE ALA
SEQRES 63 A 846 ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS GLU
SEQRES 64 A 846 TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP LEU
SEQRES 65 A 846 LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN GLY
SEQRES 66 A 846 ASN
MODRES 1FA9 SEP A 14 SER PHOSPHOSERINE
HET SEP A 14 10
HET GLC A 998 12
HET AMP A 997 23
HET PLP A 999 15
HETNAM SEP PHOSPHOSERINE
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN SEP PHOSPHONOSERINE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 GLC C6 H12 O6
FORMUL 3 AMP C10 H14 N5 O7 P
FORMUL 4 PLP C8 H10 N O6 P
FORMUL 5 HOH *242(H2 O)
HELIX 1 1 LYS A 9 ILE A 13 5 5
HELIX 2 2 ASN A 23 PHE A 37 1 15
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 124 1 7
HELIX 7 7 GLY A 134 LEU A 150 1 17
HELIX 8 8 ASN A 253 GLY A 260 1 8
HELIX 9 9 ILE A 263 ALA A 265 5 3
HELIX 10 10 VAL A 266 ILE A 275 1 10
HELIX 11 11 PHE A 285 SER A 314 1 30
HELIX 12 12 ALA A 328 GLN A 332 1 5
HELIX 13 13 LEU A 344 ILE A 356 1 13
HELIX 14 14 PRO A 360 THR A 371 1 12
HELIX 15 15 LEU A 380 LEU A 384 5 5
HELIX 16 16 VAL A 389 LEU A 396 1 8
HELIX 17 17 LEU A 396 VAL A 415 1 20
HELIX 18 18 ASP A 421 SER A 429 1 9
HELIX 19 19 MET A 441 SER A 449 1 9
HELIX 20 20 ALA A 456 LYS A 466 1 11
HELIX 21 21 PHE A 468 GLU A 473 1 6
HELIX 22 22 GLU A 475 ASP A 477 5 3
HELIX 23 23 ASN A 496 GLY A 508 1 13
HELIX 24 24 ASP A 514 LEU A 525 5 12
HELIX 25 25 ASP A 527 LYS A 554 1 28
HELIX 26 26 GLN A 576 ASP A 593 1 18
HELIX 27 27 TYR A 613 ASP A 633 1 21
HELIX 28 28 ARG A 649 ILE A 657 1 9
HELIX 29 29 PRO A 658 THR A 660 5 3
HELIX 30 30 GLY A 675 GLY A 685 1 11
HELIX 31 31 GLY A 694 GLY A 704 1 11
HELIX 32 32 GLU A 705 LEU A 708 5 4
HELIX 33 33 ARG A 714 ASP A 722 1 9
HELIX 34 34 ALA A 728 LEU A 735 1 8
HELIX 35 35 LEU A 735 GLY A 748 1 14
HELIX 36 36 GLN A 754 LEU A 757 5 4
HELIX 37 37 PHE A 758 PHE A 766 1 9
HELIX 38 38 LYS A 772 MET A 792 1 21
HELIX 39 39 ASN A 793 ALA A 806 1 14
HELIX 40 40 ALA A 807 PHE A 811 5 5
HELIX 41 41 SER A 812 ILE A 824 1 13
SHEET 1 A 9 PHE A 479 ASN A 481 0
SHEET 2 A 9 ALA A 451 GLY A 454 1 O VAL A 452 N GLN A 480
SHEET 3 A 9 PHE A 372 THR A 375 1 O PHE A 372 N ALA A 451
SHEET 4 A 9 VAL A 333 ASN A 338 1 O ILE A 335 N ALA A 373
SHEET 5 A 9 ARG A 81 LEU A 85 1 O ARG A 81 N ALA A 334
SHEET 6 A 9 ALA A 154 ILE A 159 1 O TYR A 155 N TYR A 84
SHEET 7 A 9 VAL A 238 ARG A 247 1 O THR A 240 N GLY A 156
SHEET 8 A 9 GLN A 219 PRO A 231 -1 N LEU A 222 O ARG A 247
SHEET 9 A 9 LYS A 191 SER A 192 -1 O LYS A 191 N ASP A 227
SHEET 1 B 9 PHE A 479 ASN A 481 0
SHEET 2 B 9 ALA A 451 GLY A 454 1 O VAL A 452 N GLN A 480
SHEET 3 B 9 PHE A 372 THR A 375 1 O PHE A 372 N ALA A 451
SHEET 4 B 9 VAL A 333 ASN A 338 1 O ILE A 335 N ALA A 373
SHEET 5 B 9 ARG A 81 LEU A 85 1 O ARG A 81 N ALA A 334
SHEET 6 B 9 ALA A 154 ILE A 159 1 O TYR A 155 N TYR A 84
SHEET 7 B 9 VAL A 238 ARG A 247 1 O THR A 240 N GLY A 156
SHEET 8 B 9 GLN A 219 PRO A 231 -1 N LEU A 222 O ARG A 247
SHEET 9 B 9 LEU A 198 PHE A 202 -1 O LEU A 198 N ALA A 223
SHEET 1 C 2 ASN A 167 ARG A 171 0
SHEET 2 C 2 TRP A 174 GLU A 178 -1 O TRP A 174 N ARG A 171
SHEET 1 D 2 LYS A 205 THR A 209 0
SHEET 2 D 2 GLY A 212 ILE A 216 -1 O GLY A 212 N THR A 209
SHEET 1 E 3 ARG A 386 PRO A 388 0
SHEET 2 E 3 ARG A 438 ASN A 440 -1 N ILE A 439 O TRP A 387
SHEET 3 E 3 ILE A 431 GLU A 432 -1 N GLU A 432 O ARG A 438
SHEET 1 F 6 LEU A 640 LEU A 645 0
SHEET 2 F 6 ARG A 601 GLY A 606 1 O ARG A 601 N LYS A 641
SHEET 3 F 6 ASP A 564 VAL A 567 1 N ASP A 564 O THR A 602
SHEET 4 F 6 LEU A 662 GLN A 665 1 O LEU A 662 N VAL A 565
SHEET 5 F 6 LEU A 687 GLY A 690 1 O LEU A 687 N SER A 663
SHEET 6 F 6 PHE A 709 ILE A 710 1 N PHE A 709 O THR A 688
LINK C ILE A 13 N SEP A 14 1555 1555 1.33
LINK C SEP A 14 N ILE A 15 1555 1555 1.34
LINK NZ LYS A 680 C4A PLP A 999 1555 1555 1.45
CRYST1 123.910 123.910 127.680 90.00 90.00 120.00 P 31 2 1 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008070 0.004659 0.000000 0.00000
SCALE2 0.000000 0.009319 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007832 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
