HEADER LYASE(CARBON-CARBON) 10-OCT-91 1RUS
TITLE CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-
TITLE 2 BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-
TITLE 3 GLYCERATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RUBISCO (RIBULOSE-1,5-BISPHOSPHATE
COMPND 3 CARBOXYLASE(SLASH)OXYGENASE);
COMPND 4 CHAIN: A, B;
COMPND 5 EC: 4.1.1.39;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOSPIRILLUM RUBRUM;
SOURCE 3 ORGANISM_TAXID: 1085
KEYWDS LYASE(CARBON-CARBON)
EXPDTA X-RAY DIFFRACTION
AUTHOR T.LUNDQVIST,G.SCHNEIDER
REVDAT 2 24-FEB-09 1RUS 1 VERSN
REVDAT 1 15-OCT-91 1RUS 0
JRNL AUTH T.LUNDQVIST,G.SCHNEIDER
JRNL TITL CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF
JRNL TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS
JRNL TITL 3 PRODUCT, 3-PHOSPHO-D-GLYCERATE.
JRNL REF J.BIOL.CHEM. V. 264 3643 1989
JRNL REFN ISSN 0021-9258
JRNL PMID 2492987
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.LUNDQVIST,G.SCHNEIDER
REMARK 1 TITL CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF
REMARK 1 TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE, MG(II), AND
REMARK 1 TITL 3 ACTIVATOR CO2 AT 2.3-ANGSTROMS RESOLUTION
REMARK 1 REF BIOCHEMISTRY V. 30 904 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.SCHNEIDER,Y.LINDQVIST,T.LUNDQVIST
REMARK 1 TITL CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE OF
REMARK 1 TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE FROM
REMARK 1 TITL 3 RHODOSPIRILLUM RUBRUM AT 1.7 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 211 989 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.LUNDQVIST,G.SCHNEIDER
REMARK 1 TITL CRYSTAL STRUCTURE OF THE COMPLEX OF
REMARK 1 TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND A
REMARK 1 TITL 3 TRANSITION STATE ANALOGUE, 2-CARBOXY-D-ARABINITOL
REMARK 1 TITL 4 1,5-BISPHOSPHATE
REMARK 1 REF J.BIOL.CHEM. V. 264 7078 1989
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 4
REMARK 1 AUTH I.ANDERSSON,S.KNIGHT,G.SCHNEIDER,Y.LINDQVIST,
REMARK 1 AUTH 2 T.LUNDQVIST,C.-I.BRANDEN,G.H.LORIMER
REMARK 1 TITL CRYSTAL STRUCTURE OF THE ACTIVE SITE OF
REMARK 1 TITL 2 RIBULOSE-BISPHOSPHATE CARBOXYLASE
REMARK 1 REF NATURE V. 337 229 1989
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 5
REMARK 1 AUTH G.SCHNEIDER,Y.LINDQVIST,C.-I.BRANDEN,G.LORIMER
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF
REMARK 1 TITL 2 RIBULOSE-1,5-BISPHOSPHATE
REMARK 1 TITL 3 CARBOXYLASE(SLASH)OXYGENASE FROM RHODOSPIRILLUM
REMARK 1 TITL 4 RUBRUM AT 2.9 ANGSTROMS RESOLUTION
REMARK 1 REF EMBO J. V. 5 3409 1986
REMARK 1 REFN ISSN 0261-4189
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6655
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.020 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.045 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.079 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.020 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.171 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.214 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.346 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.258 ; 0.300
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 10.500; 3.000
REMARK 3 STAGGERED (DEGREES) : 25.100; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS DETERMINED BY
REMARK 3 DIFFERENCE FOURIER TECHNIQUES WITH THE INITIAL PHASES DERIVED
REMARK 3 FROM THE NATIVE STRUCTURE.
REMARK 4
REMARK 4 1RUS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
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 (%): 45.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 35.30000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: 6750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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 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 THR A -23
REMARK 465 MET A -22
REMARK 465 ILE A -21
REMARK 465 THR A -20
REMARK 465 ASN A -19
REMARK 465 SER A -18
REMARK 465 PRO A -17
REMARK 465 ASP A -16
REMARK 465 ARG A -15
REMARK 465 TRP A -14
REMARK 465 GLY A -13
REMARK 465 TYR A -12
REMARK 465 SER A -11
REMARK 465 ALA A -10
REMARK 465 PRO A -9
REMARK 465 HIS A -8
REMARK 465 ARG A -7
REMARK 465 THR A -6
REMARK 465 SER A -5
REMARK 465 ARG A -4
REMARK 465 GLU A -3
REMARK 465 SER A -2
REMARK 465 PRO A -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 ASN A 54
REMARK 465 VAL A 55
REMARK 465 GLU A 56
REMARK 465 VAL A 57
REMARK 465 CYS A 58
REMARK 465 THR A 59
REMARK 465 THR A 60
REMARK 465 ASP A 61
REMARK 465 ASP A 62
REMARK 465 PHE A 63
REMARK 465 GLY A 326
REMARK 465 PHE A 327
REMARK 465 GLY A 328
REMARK 465 LYS A 329
REMARK 465 MET A 330
REMARK 465 GLU A 331
REMARK 465 GLY A 332
REMARK 465 GLU A 333
REMARK 465 GLU A 458
REMARK 465 ASP A 459
REMARK 465 THR A 460
REMARK 465 ARG A 461
REMARK 465 SER A 462
REMARK 465 ALA A 463
REMARK 465 LEU A 464
REMARK 465 PRO A 465
REMARK 465 ALA A 466
REMARK 465 THR B -23
REMARK 465 MET B -22
REMARK 465 ILE B -21
REMARK 465 THR B -20
REMARK 465 ASN B -19
REMARK 465 SER B -18
REMARK 465 PRO B -17
REMARK 465 ASP B -16
REMARK 465 ARG B -15
REMARK 465 TRP B -14
REMARK 465 GLY B -13
REMARK 465 TYR B -12
REMARK 465 SER B -11
REMARK 465 ALA B -10
REMARK 465 PRO B -9
REMARK 465 HIS B -8
REMARK 465 ARG B -7
REMARK 465 THR B -6
REMARK 465 SER B -5
REMARK 465 ARG B -4
REMARK 465 GLU B -3
REMARK 465 SER B -2
REMARK 465 PRO B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 ASN B 54
REMARK 465 VAL B 55
REMARK 465 GLU B 56
REMARK 465 VAL B 57
REMARK 465 CYS B 58
REMARK 465 THR B 59
REMARK 465 THR B 60
REMARK 465 ASP B 61
REMARK 465 ASP B 62
REMARK 465 PHE B 63
REMARK 465 THR B 64
REMARK 465 ARG B 65
REMARK 465 GLY B 326
REMARK 465 PHE B 327
REMARK 465 GLY B 328
REMARK 465 LYS B 329
REMARK 465 MET B 330
REMARK 465 GLU B 331
REMARK 465 GLY B 332
REMARK 465 GLU B 333
REMARK 465 GLU B 458
REMARK 465 ASP B 459
REMARK 465 THR B 460
REMARK 465 ARG B 461
REMARK 465 SER B 462
REMARK 465 ALA B 463
REMARK 465 LEU B 464
REMARK 465 PRO B 465
REMARK 465 ALA B 466
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 SER B 296 OG
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 GLY B 66
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 3 CG CD OE1 NE2
REMARK 480 SER A 296 OG
REMARK 480 VAL A 457 C O
REMARK 480 VAL B 67 N
REMARK 480 MET B 115 N
REMARK 480 GLN B 298 CG CD OE1 NE2
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 GLN A 196 ND2 ASN A 231 1.67
REMARK 500 O ALA A 293 OG SER A 299 1.86
REMARK 500 N GLY B 66 CG PRO B 86 1.89
REMARK 500 O SER B 335 CG1 ILE B 339 1.93
REMARK 500 O ALA A 293 CB SER A 299 2.03
REMARK 500 O ALA A 289 N ASN B 111 2.10
REMARK 500 O ALA B 270 OG1 THR B 274 2.18
REMARK 500 CB HIS B 321 O4P 3PG B 500 2.18
REMARK 500 O ALA A 340 OG1 THR A 344 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP A 346 NH2 ARG A 408 2646 1.89
REMARK 500 O GLY A 358 CD LYS A 431 2646 2.07
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 GLU B 14 CD GLU B 14 OE1 -0.070
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 ARG A 6 NH1 - CZ - NH2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ARG A 6 NE - CZ - NH2 ANGL. DEV. = -9.3 DEGREES
REMARK 500 ASP A 16 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 16 CB - CG - OD2 ANGL. DEV. = -11.3 DEGREES
REMARK 500 GLU A 22 CG - CD - OE1 ANGL. DEV. = 12.8 DEGREES
REMARK 500 LEU A 25 CA - CB - CG ANGL. DEV. = 22.7 DEGREES
REMARK 500 VAL A 24 CA - C - N ANGL. DEV. = 16.6 DEGREES
REMARK 500 VAL A 24 O - C - N ANGL. DEV. = -10.4 DEGREES
REMARK 500 CYS A 26 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 TYR A 28 CA - CB - CG ANGL. DEV. = 13.7 DEGREES
REMARK 500 TYR A 38 N - CA - CB ANGL. DEV. = 10.9 DEGREES
REMARK 500 TYR A 38 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 TYR A 38 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ALA A 42 CB - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 THR A 51 CA - C - N ANGL. DEV. = 14.0 DEGREES
REMARK 500 THR A 53 CA - C - O ANGL. DEV. = -13.2 DEGREES
REMARK 500 THR A 53 C - N - CA ANGL. DEV. = 20.6 DEGREES
REMARK 500 THR A 64 CA - CB - CG2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 GLU A 73 CA - CB - CG ANGL. DEV. = 16.7 DEGREES
REMARK 500 ASP A 75 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 75 CB - CG - OD2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 GLU A 76 CB - CG - CD ANGL. DEV. = 17.3 DEGREES
REMARK 500 GLU A 76 OE1 - CD - OE2 ANGL. DEV. = -12.5 DEGREES
REMARK 500 GLU A 76 CG - CD - OE1 ANGL. DEV. = 20.0 DEGREES
REMARK 500 GLU A 79 CA - CB - CG ANGL. DEV. = 13.4 DEGREES
REMARK 500 TYR A 85 C - N - CA ANGL. DEV. = 17.3 DEGREES
REMARK 500 ASP A 91 CB - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 ASP A 91 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP A 96 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 LYS A 98 CD - CE - NZ ANGL. DEV. = 16.0 DEGREES
REMARK 500 LYS A 98 C - N - CA ANGL. DEV. = 15.9 DEGREES
REMARK 500 ASN A 112 CA - C - O ANGL. DEV. = 13.7 DEGREES
REMARK 500 PHE A 126 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 VAL A 128 CA - CB - CG1 ANGL. DEV. = 10.0 DEGREES
REMARK 500 GLU A 130 CB - CG - CD ANGL. DEV. = 21.5 DEGREES
REMARK 500 GLU A 130 OE1 - CD - OE2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ARG A 133 NH1 - CZ - NH2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG A 133 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 LEU A 135 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 GLY A 138 CA - C - O ANGL. DEV. = -11.8 DEGREES
REMARK 500 GLY A 138 C - N - CA ANGL. DEV. = 17.4 DEGREES
REMARK 500 SER A 144 CB - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 SER A 144 CA - CB - OG ANGL. DEV. = 22.1 DEGREES
REMARK 500 ALA A 145 CB - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 ALA A 145 N - CA - CB ANGL. DEV. = -8.8 DEGREES
REMARK 500 TRP A 147 N - CA - CB ANGL. DEV. = 11.3 DEGREES
REMARK 500 ARG A 152 NH1 - CZ - NH2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ARG A 152 NE - CZ - NH2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 156 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 211 ANGLE DEVIATIONS.
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 4 -91.75 17.41
REMARK 500 LEU A 10 4.11 -58.37
REMARK 500 ALA A 34 102.77 -47.74
REMARK 500 SER A 50 -108.01 -88.24
REMARK 500 ARG A 65 39.31 -74.66
REMARK 500 GLU A 73 145.15 -171.77
REMARK 500 GLU A 76 -52.80 -27.22
REMARK 500 GLU A 79 37.06 70.48
REMARK 500 MET A 109 39.95 -145.32
REMARK 500 ASN A 111 45.44 -95.77
REMARK 500 MET A 115 167.11 -48.38
REMARK 500 GLU A 119 -76.01 -50.27
REMARK 500 ASN A 142 -142.48 -142.42
REMARK 500 TRP A 184 6.78 -60.07
REMARK 500 ALA A 202 67.39 -160.49
REMARK 500 ASP A 263 87.87 -67.69
REMARK 500 VAL A 294 -70.42 -85.06
REMARK 500 PRO A 297 -5.94 -45.55
REMARK 500 GLN A 298 57.38 108.75
REMARK 500 LYS A 300 12.99 -63.47
REMARK 500 HIS A 321 121.88 -38.27
REMARK 500 THR A 324 -72.66 -121.47
REMARK 500 SER A 335 165.70 157.12
REMARK 500 LYS A 361 142.39 -39.50
REMARK 500 ASN A 372 168.48 112.08
REMARK 500 ASN A 387 45.42 -83.25
REMARK 500 LYS A 431 -81.31 -30.03
REMARK 500 ALA A 444 -76.71 -58.43
REMARK 500 ASP A 445 -70.06 -30.03
REMARK 500 GLN A 446 -76.52 -29.10
REMARK 500 LEU A 455 131.89 105.09
REMARK 500 SER B 4 -143.39 22.07
REMARK 500 SER B 5 -44.63 5.07
REMARK 500 ARG B 6 -72.12 -63.19
REMARK 500 ASN B 9 82.82 -175.50
REMARK 500 LEU B 10 30.75 -81.83
REMARK 500 GLU B 22 34.22 -142.25
REMARK 500 ALA B 34 -86.34 21.30
REMARK 500 TYR B 38 -75.54 -62.98
REMARK 500 VAL B 39 -38.44 -38.83
REMARK 500 GLU B 48 -71.88 -53.05
REMARK 500 SER B 49 -79.23 -38.67
REMARK 500 SER B 50 -101.36 -44.15
REMARK 500 THR B 51 -80.14 -105.78
REMARK 500 VAL B 67 -41.87 -132.77
REMARK 500 ASP B 75 103.59 -165.35
REMARK 500 GLU B 79 56.72 76.49
REMARK 500 ASP B 117 -3.01 107.71
REMARK 500 PRO B 129 179.35 -54.76
REMARK 500 ASN B 142 -159.07 -160.29
REMARK 500 TRP B 184 2.93 -56.82
REMARK 500 GLU B 194 -47.86 -23.64
REMARK 500 ALA B 202 62.05 -174.42
REMARK 500 ARG B 288 40.31 -103.79
REMARK 500 HIS B 291 -53.77 41.56
REMARK 500 SER B 296 141.91 -38.62
REMARK 500 THR B 324 -74.11 -119.74
REMARK 500 SER B 335 -91.40 -69.68
REMARK 500 PHE B 352 -44.74 -135.22
REMARK 500 LYS B 361 153.87 -43.98
REMARK 500 ASN B 372 -178.94 -64.19
REMARK 500 THR B 391 75.81 -115.83
REMARK 500 ALA B 396 -73.80 -99.20
REMARK 500 PRO B 422 49.02 -85.12
REMARK 500 VAL B 423 -48.08 49.77
REMARK 500 ASP B 445 -65.62 -29.88
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, 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 ASN B 111 -13.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEETS PRESENTED AS *ACT* AND *BCT* ON SHEET RECORDS
REMARK 700 BELOW ARE ACTUALLY EIGHT-STRANDED BETA-BARRELS. THIS IS
REMARK 700 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND
REMARK 700 LAST STRANDS ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PG A 500
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PG B 500
DBREF 1RUS A 1 466 UNP P04718 RBL2_RHORU 1 466
DBREF 1RUS B 1 466 UNP P04718 RBL2_RHORU 1 466
SEQADV 1RUS ASP A 91 UNP P04718 HIS 91 CONFLICT
SEQADV 1RUS ASP B 91 UNP P04718 HIS 91 CONFLICT
SEQRES 1 A 490 THR MET ILE THR ASN SER PRO ASP ARG TRP GLY TYR SER
SEQRES 2 A 490 ALA PRO HIS ARG THR SER ARG GLU SER PRO PRO MET ASP
SEQRES 3 A 490 GLN SER SER ARG TYR VAL ASN LEU ALA LEU LYS GLU GLU
SEQRES 4 A 490 ASP LEU ILE ALA GLY GLY GLU HIS VAL LEU CYS ALA TYR
SEQRES 5 A 490 ILE MET LYS PRO LYS ALA GLY TYR GLY TYR VAL ALA THR
SEQRES 6 A 490 ALA ALA HIS PHE ALA ALA GLU SER SER THR GLY THR ASN
SEQRES 7 A 490 VAL GLU VAL CYS THR THR ASP ASP PHE THR ARG GLY VAL
SEQRES 8 A 490 ASP ALA LEU VAL TYR GLU VAL ASP GLU ALA ARG GLU LEU
SEQRES 9 A 490 THR LYS ILE ALA TYR PRO VAL ALA LEU PHE ASP ARG ASN
SEQRES 10 A 490 ILE THR ASP GLY LYS ALA MET ILE ALA SER PHE LEU THR
SEQRES 11 A 490 LEU THR MET GLY ASN ASN GLN GLY MET GLY ASP VAL GLU
SEQRES 12 A 490 TYR ALA LYS MET HIS ASP PHE TYR VAL PRO GLU ALA TYR
SEQRES 13 A 490 ARG ALA LEU PHE ASP GLY PRO SER VAL ASN ILE SER ALA
SEQRES 14 A 490 LEU TRP LYS VAL LEU GLY ARG PRO GLU VAL ASP GLY GLY
SEQRES 15 A 490 LEU VAL VAL GLY THR ILE ILE LYS PRO LYS LEU GLY LEU
SEQRES 16 A 490 ARG PRO LYS PRO PHE ALA GLU ALA CYS HIS ALA PHE TRP
SEQRES 17 A 490 LEU GLY GLY ASP PHE ILE LYS ASN ASP GLU PRO GLN GLY
SEQRES 18 A 490 ASN GLN PRO PHE ALA PRO LEU ARG ASP THR ILE ALA LEU
SEQRES 19 A 490 VAL ALA ASP ALA MET ARG ARG ALA GLN ASP GLU THR GLY
SEQRES 20 A 490 GLU ALA LYS LEU PHE SER ALA ASN ILE THR ALA ASP ASP
SEQRES 21 A 490 PRO PHE GLU ILE ILE ALA ARG GLY GLU TYR VAL LEU GLU
SEQRES 22 A 490 THR PHE GLY GLU ASN ALA SER HIS VAL ALA LEU LEU VAL
SEQRES 23 A 490 ASP GLY TYR VAL ALA GLY ALA ALA ALA ILE THR THR ALA
SEQRES 24 A 490 ARG ARG ARG PHE PRO ASP ASN PHE LEU HIS TYR HIS ARG
SEQRES 25 A 490 ALA GLY HIS GLY ALA VAL THR SER PRO GLN SER LYS ARG
SEQRES 26 A 490 GLY TYR THR ALA PHE VAL HIS CYS LYS MET ALA ARG LEU
SEQRES 27 A 490 GLN GLY ALA SER GLY ILE HIS THR GLY THR MET GLY PHE
SEQRES 28 A 490 GLY LYS MET GLU GLY GLU SER SER ASP ARG ALA ILE ALA
SEQRES 29 A 490 TYR MET LEU THR GLN ASP GLU ALA GLN GLY PRO PHE TYR
SEQRES 30 A 490 ARG GLN SER TRP GLY GLY MET LYS ALA CYS THR PRO ILE
SEQRES 31 A 490 ILE SER GLY GLY MET ASN ALA LEU ARG MET PRO GLY PHE
SEQRES 32 A 490 PHE GLU ASN LEU GLY ASN ALA ASN VAL ILE LEU THR ALA
SEQRES 33 A 490 GLY GLY GLY ALA PHE GLY HIS ILE ASP GLY PRO VAL ALA
SEQRES 34 A 490 GLY ALA ARG SER LEU ARG GLN ALA TRP GLN ALA TRP ARG
SEQRES 35 A 490 ASP GLY VAL PRO VAL LEU ASP TYR ALA ARG GLU HIS LYS
SEQRES 36 A 490 GLU LEU ALA ARG ALA PHE GLU SER PHE PRO GLY ASP ALA
SEQRES 37 A 490 ASP GLN ILE TYR PRO GLY TRP ARG LYS ALA LEU GLY VAL
SEQRES 38 A 490 GLU ASP THR ARG SER ALA LEU PRO ALA
SEQRES 1 B 490 THR MET ILE THR ASN SER PRO ASP ARG TRP GLY TYR SER
SEQRES 2 B 490 ALA PRO HIS ARG THR SER ARG GLU SER PRO PRO MET ASP
SEQRES 3 B 490 GLN SER SER ARG TYR VAL ASN LEU ALA LEU LYS GLU GLU
SEQRES 4 B 490 ASP LEU ILE ALA GLY GLY GLU HIS VAL LEU CYS ALA TYR
SEQRES 5 B 490 ILE MET LYS PRO LYS ALA GLY TYR GLY TYR VAL ALA THR
SEQRES 6 B 490 ALA ALA HIS PHE ALA ALA GLU SER SER THR GLY THR ASN
SEQRES 7 B 490 VAL GLU VAL CYS THR THR ASP ASP PHE THR ARG GLY VAL
SEQRES 8 B 490 ASP ALA LEU VAL TYR GLU VAL ASP GLU ALA ARG GLU LEU
SEQRES 9 B 490 THR LYS ILE ALA TYR PRO VAL ALA LEU PHE ASP ARG ASN
SEQRES 10 B 490 ILE THR ASP GLY LYS ALA MET ILE ALA SER PHE LEU THR
SEQRES 11 B 490 LEU THR MET GLY ASN ASN GLN GLY MET GLY ASP VAL GLU
SEQRES 12 B 490 TYR ALA LYS MET HIS ASP PHE TYR VAL PRO GLU ALA TYR
SEQRES 13 B 490 ARG ALA LEU PHE ASP GLY PRO SER VAL ASN ILE SER ALA
SEQRES 14 B 490 LEU TRP LYS VAL LEU GLY ARG PRO GLU VAL ASP GLY GLY
SEQRES 15 B 490 LEU VAL VAL GLY THR ILE ILE LYS PRO LYS LEU GLY LEU
SEQRES 16 B 490 ARG PRO LYS PRO PHE ALA GLU ALA CYS HIS ALA PHE TRP
SEQRES 17 B 490 LEU GLY GLY ASP PHE ILE LYS ASN ASP GLU PRO GLN GLY
SEQRES 18 B 490 ASN GLN PRO PHE ALA PRO LEU ARG ASP THR ILE ALA LEU
SEQRES 19 B 490 VAL ALA ASP ALA MET ARG ARG ALA GLN ASP GLU THR GLY
SEQRES 20 B 490 GLU ALA LYS LEU PHE SER ALA ASN ILE THR ALA ASP ASP
SEQRES 21 B 490 PRO PHE GLU ILE ILE ALA ARG GLY GLU TYR VAL LEU GLU
SEQRES 22 B 490 THR PHE GLY GLU ASN ALA SER HIS VAL ALA LEU LEU VAL
SEQRES 23 B 490 ASP GLY TYR VAL ALA GLY ALA ALA ALA ILE THR THR ALA
SEQRES 24 B 490 ARG ARG ARG PHE PRO ASP ASN PHE LEU HIS TYR HIS ARG
SEQRES 25 B 490 ALA GLY HIS GLY ALA VAL THR SER PRO GLN SER LYS ARG
SEQRES 26 B 490 GLY TYR THR ALA PHE VAL HIS CYS LYS MET ALA ARG LEU
SEQRES 27 B 490 GLN GLY ALA SER GLY ILE HIS THR GLY THR MET GLY PHE
SEQRES 28 B 490 GLY LYS MET GLU GLY GLU SER SER ASP ARG ALA ILE ALA
SEQRES 29 B 490 TYR MET LEU THR GLN ASP GLU ALA GLN GLY PRO PHE TYR
SEQRES 30 B 490 ARG GLN SER TRP GLY GLY MET LYS ALA CYS THR PRO ILE
SEQRES 31 B 490 ILE SER GLY GLY MET ASN ALA LEU ARG MET PRO GLY PHE
SEQRES 32 B 490 PHE GLU ASN LEU GLY ASN ALA ASN VAL ILE LEU THR ALA
SEQRES 33 B 490 GLY GLY GLY ALA PHE GLY HIS ILE ASP GLY PRO VAL ALA
SEQRES 34 B 490 GLY ALA ARG SER LEU ARG GLN ALA TRP GLN ALA TRP ARG
SEQRES 35 B 490 ASP GLY VAL PRO VAL LEU ASP TYR ALA ARG GLU HIS LYS
SEQRES 36 B 490 GLU LEU ALA ARG ALA PHE GLU SER PHE PRO GLY ASP ALA
SEQRES 37 B 490 ASP GLN ILE TYR PRO GLY TRP ARG LYS ALA LEU GLY VAL
SEQRES 38 B 490 GLU ASP THR ARG SER ALA LEU PRO ALA
HET 3PG A 500 11
HET 3PG B 500 11
HETNAM 3PG 3-PHOSPHOGLYCERIC ACID
FORMUL 3 3PG 2(C3 H7 O7 P)
HELIX 1 AHA GLU A 14 GLY A 20 1 7
HELIX 2 AHB TYR A 38 SER A 49 1 12
HELIX 3 AHC ILE A 101 MET A 109 1 9
HELIX 4 AHD GLU A 130 ARG A 133 1 4
HELIX 5 AHE SER A 144 LEU A 150 1 7
HELIX 6 AH1 PRO A 173 TRP A 184 1 12
HELIX 7 AH2 LEU A 204 THR A 222 1 19
HELIX 8 AH3 ASP A 235 PHE A 251 1 17
HELIX 9 AH4 ALA A 269 ARG A 278 1 10
HELIX 10 AHF GLY A 292 THR A 295 1 4
HELIX 11 AH5 ALA A 305 GLN A 315 1 11
HELIX 12 AH6 ARG A 337 THR A 344 1 8
HELIX 13 AH7 MET A 376 LEU A 383 1 8
HELIX 14 AH8 PRO A 403 ASP A 419 1 17
HELIX 15 AHG VAL A 423 GLU A 429 1 7
HELIX 16 AHH LYS A 431 PHE A 440 1 10
HELIX 17 AHI GLY A 442 TYR A 448 1 7
HELIX 18 AHJ TRP A 451 LEU A 455 1 5
HELIX 19 AHA GLU B 14 GLY B 20 1 7
HELIX 20 AHB TYR B 38 SER B 49 1 12
HELIX 21 AHC ILE B 101 MET B 109 1 9
HELIX 22 AHD GLU B 130 ARG B 133 1 4
HELIX 23 AHE SER B 144 LEU B 150 1 7
HELIX 24 AH1 PRO B 173 TRP B 184 1 12
HELIX 25 AH2 LEU B 204 THR B 222 1 19
HELIX 26 AH3 ASP B 235 PHE B 251 1 17
HELIX 27 AH4 ALA B 269 ARG B 278 1 10
HELIX 28 AHF GLY B 292 THR B 295 1 4
HELIX 29 AH5 ALA B 305 GLN B 315 1 11
HELIX 30 AH6 ARG B 337 THR B 344 1 8
HELIX 31 AH7 MET B 376 LEU B 383 1 8
HELIX 32 AH8 PRO B 403 ASP B 419 1 17
HELIX 33 AHG VAL B 423 GLU B 429 1 7
HELIX 34 AHH LYS B 431 PHE B 440 1 10
HELIX 35 AHI GLY B 442 TYR B 448 1 7
HELIX 36 AHJ TRP B 451 LEU B 455 1 5
SHEET 1 ANT 5 VAL A 8 LEU A 10 0
SHEET 2 ANT 5 LEU A 70 ASP A 75 1
SHEET 3 ANT 5 GLU A 79 PRO A 86 -1
SHEET 4 ANT 5 HIS A 23 PRO A 32 -1
SHEET 5 ANT 5 ASP A 117 TYR A 127 -1
SHEET 1 ACT 9 VAL A 160 ILE A 164 0
SHEET 2 ACT 9 PHE A 189 LYS A 191 1
SHEET 3 ACT 9 LEU A 227 ASN A 231 1
SHEET 4 ACT 9 VAL A 258 ASP A 263 1
SHEET 5 ACT 9 LEU A 284 HIS A 287 1
SHEET 6 ACT 9 GLY A 319 HIS A 321 1
SHEET 7 ACT 9 THR A 364 GLY A 369 1
SHEET 8 ACT 9 ILE A 389 ALA A 392 1
SHEET 9 ACT 9 VAL A 160 ILE A 164 1
SHEET 1 BNT 5 VAL B 8 LEU B 10 0
SHEET 2 BNT 5 LEU B 70 ASP B 75 1
SHEET 3 BNT 5 GLU B 79 PRO B 86 -1
SHEET 4 BNT 5 HIS B 23 PRO B 32 -1
SHEET 5 BNT 5 ASP B 117 TYR B 127 -1
SHEET 1 BCT 9 VAL B 160 ILE B 164 0
SHEET 2 BCT 9 PHE B 189 LYS B 191 1
SHEET 3 BCT 9 LEU B 227 ASN B 231 1
SHEET 4 BCT 9 VAL B 258 ASP B 263 1
SHEET 5 BCT 9 LEU B 284 HIS B 287 1
SHEET 6 BCT 9 GLY B 319 HIS B 321 1
SHEET 7 BCT 9 THR B 364 GLY B 369 1
SHEET 8 BCT 9 ILE B 389 ALA B 392 1
SHEET 9 BCT 9 VAL B 160 ILE B 164 1
CISPEP 1 LYS A 166 PRO A 167 0 0.59
CISPEP 2 LYS B 166 PRO B 167 0 1.55
SITE 1 AC1 8 ILE A 164 HIS A 287 ARG A 288 HIS A 321
SITE 2 AC1 8 THR A 322 GLY A 323 SER A 368 ASN B 111
SITE 1 AC2 5 ASN A 111 HIS B 287 ARG B 288 HIS B 321
SITE 2 AC2 5 GLY B 323
CRYST1 65.500 70.600 104.100 90.00 92.10 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.036668 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000672 0.00000
SCALE1 0.015267 0.000000 0.000560 0.00000
SCALE2 0.000000 0.014164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009613 0.00000
MTRIX1 1 0.373740 -0.056207 0.940855 6.14161 1
MTRIX2 1 -0.073400 -0.996800 -0.033512 17.87800 1
MTRIX3 1 0.909789 -0.054363 -0.376740 -7.57091 1
(ATOM LINES ARE NOT SHOWN.)
END
