HEADER ISOMERASE 02-MAR-95 3PMG
TITLE STRUCTURE OF RABBIT MUSCLE PHOSPHOGLUCOMUTASE AT 2.4 ANGSTROMS
TITLE 2 RESOLUTION. USE OF FREEZING POINT DEPRESSANT AND REDUCED TEMPERATURE
TITLE 3 TO ENHANCE DIFFRACTIVITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOGLUCOMUTASE-1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHOGLUCOMUTASE;
COMPND 5 EC: 5.4.2.2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 TISSUE: MUSCLE
KEYWDS PHOSPHOTRANSFERASE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.J.RAY JUNIOR,Y.LIU,S.BARANIDHARAN
REVDAT 4 20-NOV-19 3PMG 1 LINK
REVDAT 3 24-JUL-19 3PMG 1 HEADER COMPND KEYWDS LINK
REVDAT 2 24-FEB-09 3PMG 1 VERSN
REVDAT 1 07-DEC-95 3PMG 0
SPRSDE 07-DEC-95 3PMG 2PMG
JRNL AUTH Y.LIU,W.J.RAY,S.BARANIDHARAN
JRNL TITL STRUCTURE OF RABBIT MUSCLE PHOSPHOGLUCOMUTASE REFINED AT 2.4
JRNL TITL 2 A RESOLUTION.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 53 392 1997
JRNL REFN ISSN 0907-4449
JRNL PMID 15299905
JRNL DOI 10.1107/S0907444997000875
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.J.RAY JUNIOR,C.B.POST,Y.LIU,G.I.RHYU
REMARK 1 TITL STRUCTURAL CHANGES AT THE METAL ION BINDING SITE DURING THE
REMARK 1 TITL 2 PHOSPHOGLUCOMUTASE REACTION
REMARK 1 REF BIOCHEMISTRY V. 32 48 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.B.DAI,Y.LIU,W.J.RAY,M.KONNO
REMARK 1 TITL THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOMUTASE REFINED AT 2.7
REMARK 1 TITL 2 ANGSTROMS RESOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 267 6322 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH W.J.RAY JUNIOR
REMARK 1 TITL THE CATALYTIC ACTIVITY OF MUSCLE PHOSPHOGLUCOMUTASE IN THE
REMARK 1 TITL 2 CRYSTALLINE PHASE
REMARK 1 REF J.BIOL.CHEM. V. 261 275 1986
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 4
REMARK 1 AUTH Z.-J.LIN,M.KONNO,C.ABAD-ZAPATERO,R.WIERENGA,M.R.N.MURTHY,
REMARK 1 AUTH 2 W.J.RAY JUNIOR,M.G.ROSSMANN
REMARK 1 TITL THE STRUCTURE OF RABBIT MUSCLE PHOSPHOGLUCOMUTASE AT
REMARK 1 TITL 2 INTERMEDIATE RESOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 261 264 1986
REMARK 1 REFN ISSN 0021-9258
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) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.0
REMARK 3 NUMBER OF REFLECTIONS : 49694
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 SET) : 0.163
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
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 : 8666
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 494
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.00
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) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : 3.230
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.940
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:
REMARK 3 THE MODEL CONTAINS FIVE RESIDUES OUT OF 1122 THAT FALL IN
REMARK 3 THE GENEROUSLY ALLOWED REGION OF A RAMACHANDRAN PLOT AS
REMARK 3 DEFINED IN PROCHECK AND ONE RESIDUE IN THE DISALLOWED
REMARK 3 REGION. TWO OF THE FIVE ARE ACTIVE SITE RESIDUES IN CHAIN
REMARK 3 A AND B AND THE OTHER FOUR ARE INVOLVED IN
REMARK 3 CRYSTALLOGRAPHIC CONTACTS. THE RESIDUES ARE ARG A 216,
REMARK 3 SER A 116, ASN A 461, SER B 116, AND ASN B 461.
REMARK 4
REMARK 4 3PMG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179109.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : OCT-93
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
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 : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN MULTIWIRE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XTS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54770
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 13.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.05400
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: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.56000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 87.21000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 87.21000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 25.28000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 87.21000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 87.21000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 75.84000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 87.21000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 87.21000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 25.28000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 87.21000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 87.21000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 75.84000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 50.56000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: MTRIX
REMARK 300 THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
REMARK 300 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
REMARK 300 VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE
REMARK 300 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
REMARK 300 SECOND.
REMARK 300
REMARK 300 APPLIED TO TRANSFORMED TO
REMARK 300 MTRIX RESIDUES RESIDUES RMSD
REMARK 300 M1 B 1 .. B 420 A 1 .. A 420 0.426
REMARK 300 M2 B 421 .. B 561 A 421 .. A 561 1.117
REMARK 300
REMARK 300 M1 SUPERIMPOSES DOMAINS I - III OF MONOMER B ON THE
REMARK 300 CORRESPONDING DOMAINS OF MONOMER A, BASED ON A LEAST
REMARK 300 SQUARES PROCEDURE (HOMOLOGY, ROSSMANN AND ARGOS,1975) USING
REMARK 300 301 SELECTED ALPHA-CARBON ATOMS IN THESE DOMAINS.
REMARK 300
REMARK 300 M2 SUPERIMPOSES DOMAIN IV OF MONOMER B ON DOMAIN IV OF
REMARK 300 MONOMER A, USING 35 SELECTED ALPHA-CARBON ATOMS FROM THE
REMARK 300 CENTRAL PART OF THE BETA-SHEET IN THESE DOMAINS.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 HD22 ASN A 37 H2 HOH A 567 1.25
REMARK 500 HD22 ASN B 37 H2 HOH B 616 1.27
REMARK 500 H1 HOH B 845 O HOH B 848 1.54
REMARK 500 HH11 ARG A 554 O HOH A 763 1.57
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 HIS A 117 NE2 HIS A 117 CD2 -0.068
REMARK 500 HIS A 260 NE2 HIS A 260 CD2 -0.070
REMARK 500 HIS A 384 NE2 HIS A 384 CD2 -0.073
REMARK 500 HIS B 117 NE2 HIS B 117 CD2 -0.070
REMARK 500 HIS B 225 NE2 HIS B 225 CD2 -0.076
REMARK 500 HIS B 280 NE2 HIS B 280 CD2 -0.071
REMARK 500 HIS B 384 NE2 HIS B 384 CD2 -0.067
REMARK 500 HIS B 417 NE2 HIS B 417 CD2 -0.066
REMARK 500 HIS B 476 NE2 HIS B 476 CD2 -0.066
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 SER A 30 N - CA - C ANGL. DEV. = 16.5 DEGREES
REMARK 500 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 51 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 63 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 75 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 VAL A 188 N - CA - CB ANGL. DEV. = -14.6 DEGREES
REMARK 500 ARG A 199 NE - CZ - NH1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG A 199 NE - CZ - NH2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 LEU A 210 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 ARG A 220 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 220 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 MET A 224 CG - SD - CE ANGL. DEV. = -10.4 DEGREES
REMARK 500 VAL A 309 CB - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 ARG A 328 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 328 NE - CZ - NH2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ARG A 342 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 TYR A 352 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 TRP A 358 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 386 NH1 - CZ - NH2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ARG A 386 NE - CZ - NH1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 386 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 TRP A 392 CD1 - CG - CD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 TRP A 392 CE2 - CD2 - CG ANGL. DEV. = -6.7 DEGREES
REMARK 500 TRP A 397 CD1 - CG - CD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 TRP A 397 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP A 397 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG A 404 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 LEU A 412 CA - CB - CG ANGL. DEV. = -15.5 DEGREES
REMARK 500 TRP A 416 CD1 - CG - CD2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 426 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 426 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 490 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 498 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 502 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 514 CG - CD - NE ANGL. DEV. = -13.4 DEGREES
REMARK 500 ARG A 514 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 LYS A 544 CA - CB - CG ANGL. DEV. = 13.3 DEGREES
REMARK 500 ARG A 554 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG B 22 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG B 24 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 VAL B 25 CG1 - CB - CG2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 ARG B 51 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG B 75 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG B 199 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 199 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG B 216 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 220 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG B 220 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 MET B 224 CG - SD - CE ANGL. DEV. = -14.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 86 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 PRO A 48 -52.74 -28.69
REMARK 500 TYR A 65 -4.62 74.38
REMARK 500 SEP A 116 -125.73 40.79
REMARK 500 ASN A 178 52.99 39.06
REMARK 500 ARG A 216 101.28 18.20
REMARK 500 PRO A 263 67.11 -60.48
REMARK 500 THR A 266 -72.53 -74.08
REMARK 500 ALA A 268 50.76 -108.68
REMARK 500 HIS A 299 -1.36 80.06
REMARK 500 ASN A 461 -137.98 47.28
REMARK 500 SER A 508 -57.27 -143.07
REMARK 500 ALA A 509 -43.65 -132.49
REMARK 500 THR B 32 124.79 -38.34
REMARK 500 TYR B 65 -9.45 73.98
REMARK 500 SEP B 116 -122.86 44.03
REMARK 500 ILE B 132 -169.42 -104.45
REMARK 500 GLU B 177 121.02 -34.69
REMARK 500 ASN B 178 -11.68 63.60
REMARK 500 ASN B 215 47.79 -102.59
REMARK 500 ALA B 268 45.80 -108.78
REMARK 500 ALA B 460 20.93 -158.59
REMARK 500 ASN B 461 -116.18 168.28
REMARK 500 VAL B 479 -66.16 -96.78
REMARK 500 SER B 482 150.56 -44.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 194 0.06 SIDE CHAIN
REMARK 500 ARG A 386 0.13 SIDE CHAIN
REMARK 500 ARG B 514 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 562 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SEP A 116 OG
REMARK 620 2 SEP A 116 O2P 62.2
REMARK 620 3 ASP A 287 OD2 76.3 81.8
REMARK 620 4 ASP A 289 OD1 87.7 149.8 93.0
REMARK 620 5 ASP A 291 OD1 168.0 107.2 108.9 102.6
REMARK 620 6 HOH A 733 O 75.1 75.6 149.4 96.3 97.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 562 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SEP B 116 OG
REMARK 620 2 SEP B 116 O2P 71.3
REMARK 620 3 ASP B 287 OD2 94.1 94.6
REMARK 620 4 ASP B 289 OD2 93.3 164.0 81.9
REMARK 620 5 ASP B 291 OD2 173.9 104.7 81.5 90.3
REMARK 620 6 HOH B 758 O 101.3 96.3 163.4 90.9 83.6
REMARK 620 N 1 2 3 4 5
REMARK 650
REMARK 650 HELIX
REMARK 650 THE MONOMER CAN BE SUBDIVIDED INTO FOUR SEQUENCE DOMAINS:
REMARK 650 THE FINAL COLUMN OF THE HELIX IDENTIFIER, 1 - 4, DESIGNATES
REMARK 650 THE DOMAINS; FOR STRANDS, THE DOMAINS ARE DESIGNATED BY THE
REMARK 650 NUMBERS IN THE SECOND COLUMN, 1 - 4, FOLLOWED BY EITHER B
REMARK 650 OR S. A SPATIAL RELATIONSHIP EXISTS BETWEEN GROUPS OF
REMARK 650 HELICES/STRANDS IN DOMAINS 1 - 3. IN ORDER TO EMPHASIZE
REMARK 650 THIS RELATIONSHIP, A PORTION OF THE MAIN SHEET IN DOMAIN 1,
REMARK 650 1 B - 7 B, IS REPEATED AS 4 S - 1 S. THUS, A SPATIAL
REMARK 650 DOMAIN-DOMAIN RELATIONSHIP EXISTS AMONG STRANDS/HELICES
REMARK 650 WHOSE DESIGNATOR CONTAINS 1 S - 4 S IN THE SECOND COLUMN OR
REMARK 650 ENDS WITH 1 - 4, RESPECTIVELY. DOMAINS 1, 2, 3 IN MONOMER
REMARK 650 1 AND MONOMER 2 ARE RELATED BY A ROTATION MATRIX GIVEN AS
REMARK 650 MTRIX 1. DOMAIN 4 IN MONOMER 1 AND MONOMER 2 ARE RELATED
REMARK 650 BY A DIFFERENT ROTATION MATRIX GIVEN AS MTRIX 2.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: MBA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: METAL BINDING SITE IN MONOMER A
REMARK 800
REMARK 800 SITE_IDENTIFIER: MBB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: METAL BINDING SITE IN MONOMER B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 562
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 562
DBREF 3PMG A 1 561 UNP P00949 PGMU_RABIT 1 561
DBREF 3PMG B 1 561 UNP P00949 PGMU_RABIT 1 561
SEQRES 1 A 561 VAL LYS ILE VAL THR VAL LYS THR LYS ALA TYR PRO ASP
SEQRES 2 A 561 GLN LYS PRO GLY THR SER GLY LEU ARG LYS ARG VAL LYS
SEQRES 3 A 561 VAL PHE GLN SER SER THR ASN TYR ALA GLU ASN PHE ILE
SEQRES 4 A 561 GLN SER ILE ILE SER THR VAL GLU PRO ALA GLN ARG GLN
SEQRES 5 A 561 GLU ALA THR LEU VAL VAL GLY GLY ASP GLY ARG PHE TYR
SEQRES 6 A 561 MET LYS GLU ALA ILE GLN LEU ILE VAL ARG ILE ALA ALA
SEQRES 7 A 561 ALA ASN GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN GLY
SEQRES 8 A 561 ILE LEU SER THR PRO ALA VAL SER CYS ILE ILE ARG LYS
SEQRES 9 A 561 ILE LYS ALA ILE GLY GLY ILE ILE LEU THR ALA SEP HIS
SEQRES 10 A 561 ASN PRO GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS PHE
SEQRES 11 A 561 ASN ILE SER ASN GLY GLY PRO ALA PRO GLU ALA ILE THR
SEQRES 12 A 561 ASP LYS ILE PHE GLN ILE SER LYS THR ILE GLU GLU TYR
SEQRES 13 A 561 ALA ILE CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL LEU
SEQRES 14 A 561 GLY LYS GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS PRO
SEQRES 15 A 561 PHE THR VAL GLU ILE VAL ASP SER VAL GLU ALA TYR ALA
SEQRES 16 A 561 THR MET LEU ARG ASN ILE PHE ASP PHE ASN ALA LEU LYS
SEQRES 17 A 561 GLU LEU LEU SER GLY PRO ASN ARG LEU LYS ILE ARG ILE
SEQRES 18 A 561 ASP ALA MET HIS GLY VAL VAL GLY PRO TYR VAL LYS LYS
SEQRES 19 A 561 ILE LEU CYS GLU GLU LEU GLY ALA PRO ALA ASN SER ALA
SEQRES 20 A 561 VAL ASN CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS HIS
SEQRES 21 A 561 PRO ASP PRO ASN LEU THR TYR ALA ALA ASP LEU VAL GLU
SEQRES 22 A 561 THR MET LYS SER GLY GLU HIS ASP PHE GLY ALA ALA PHE
SEQRES 23 A 561 ASP GLY ASP GLY ASP ARG ASN MET ILE LEU GLY LYS HIS
SEQRES 24 A 561 GLY PHE PHE VAL ASN PRO SER ASP SER VAL ALA VAL ILE
SEQRES 25 A 561 ALA ALA ASN ILE PHE SER ILE PRO TYR PHE GLN GLN THR
SEQRES 26 A 561 GLY VAL ARG GLY PHE ALA ARG SER MET PRO THR SER GLY
SEQRES 27 A 561 ALA LEU ASP ARG VAL ALA ASN ALA THR LYS ILE ALA LEU
SEQRES 28 A 561 TYR GLU THR PRO THR GLY TRP LYS PHE PHE GLY ASN LEU
SEQRES 29 A 561 MET ASP ALA SER LYS LEU SER LEU CYS GLY GLU GLU SER
SEQRES 30 A 561 PHE GLY THR GLY SER ASP HIS ILE ARG GLU LYS ASP GLY
SEQRES 31 A 561 LEU TRP ALA VAL LEU ALA TRP LEU SER ILE LEU ALA THR
SEQRES 32 A 561 ARG LYS GLN SER VAL GLU ASP ILE LEU LYS ASP HIS TRP
SEQRES 33 A 561 HIS LYS PHE GLY ARG ASN PHE PHE THR ARG TYR ASP TYR
SEQRES 34 A 561 GLU GLU VAL GLU ALA GLU GLY ALA THR LYS MET MET LYS
SEQRES 35 A 561 ASP LEU GLU ALA LEU MET PHE ASP ARG SER PHE VAL GLY
SEQRES 36 A 561 LYS GLN PHE SER ALA ASN ASP LYS VAL TYR THR VAL GLU
SEQRES 37 A 561 LYS ALA ASP ASN PHE GLU TYR HIS ASP PRO VAL ASP GLY
SEQRES 38 A 561 SER VAL SER LYS ASN GLN GLY LEU ARG LEU ILE PHE ALA
SEQRES 39 A 561 ASP GLY SER ARG ILE ILE PHE ARG LEU SER GLY THR GLY
SEQRES 40 A 561 SER ALA GLY ALA THR ILE ARG LEU TYR ILE ASP SER TYR
SEQRES 41 A 561 GLU LYS ASP ASN ALA LYS ILE ASN GLN ASP PRO GLN VAL
SEQRES 42 A 561 MET LEU ALA PRO LEU ILE SER ILE ALA LEU LYS VAL SER
SEQRES 43 A 561 GLN LEU GLN GLU ARG THR GLY ARG THR ALA PRO THR VAL
SEQRES 44 A 561 ILE THR
SEQRES 1 B 561 VAL LYS ILE VAL THR VAL LYS THR LYS ALA TYR PRO ASP
SEQRES 2 B 561 GLN LYS PRO GLY THR SER GLY LEU ARG LYS ARG VAL LYS
SEQRES 3 B 561 VAL PHE GLN SER SER THR ASN TYR ALA GLU ASN PHE ILE
SEQRES 4 B 561 GLN SER ILE ILE SER THR VAL GLU PRO ALA GLN ARG GLN
SEQRES 5 B 561 GLU ALA THR LEU VAL VAL GLY GLY ASP GLY ARG PHE TYR
SEQRES 6 B 561 MET LYS GLU ALA ILE GLN LEU ILE VAL ARG ILE ALA ALA
SEQRES 7 B 561 ALA ASN GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN GLY
SEQRES 8 B 561 ILE LEU SER THR PRO ALA VAL SER CYS ILE ILE ARG LYS
SEQRES 9 B 561 ILE LYS ALA ILE GLY GLY ILE ILE LEU THR ALA SEP HIS
SEQRES 10 B 561 ASN PRO GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS PHE
SEQRES 11 B 561 ASN ILE SER ASN GLY GLY PRO ALA PRO GLU ALA ILE THR
SEQRES 12 B 561 ASP LYS ILE PHE GLN ILE SER LYS THR ILE GLU GLU TYR
SEQRES 13 B 561 ALA ILE CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL LEU
SEQRES 14 B 561 GLY LYS GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS PRO
SEQRES 15 B 561 PHE THR VAL GLU ILE VAL ASP SER VAL GLU ALA TYR ALA
SEQRES 16 B 561 THR MET LEU ARG ASN ILE PHE ASP PHE ASN ALA LEU LYS
SEQRES 17 B 561 GLU LEU LEU SER GLY PRO ASN ARG LEU LYS ILE ARG ILE
SEQRES 18 B 561 ASP ALA MET HIS GLY VAL VAL GLY PRO TYR VAL LYS LYS
SEQRES 19 B 561 ILE LEU CYS GLU GLU LEU GLY ALA PRO ALA ASN SER ALA
SEQRES 20 B 561 VAL ASN CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS HIS
SEQRES 21 B 561 PRO ASP PRO ASN LEU THR TYR ALA ALA ASP LEU VAL GLU
SEQRES 22 B 561 THR MET LYS SER GLY GLU HIS ASP PHE GLY ALA ALA PHE
SEQRES 23 B 561 ASP GLY ASP GLY ASP ARG ASN MET ILE LEU GLY LYS HIS
SEQRES 24 B 561 GLY PHE PHE VAL ASN PRO SER ASP SER VAL ALA VAL ILE
SEQRES 25 B 561 ALA ALA ASN ILE PHE SER ILE PRO TYR PHE GLN GLN THR
SEQRES 26 B 561 GLY VAL ARG GLY PHE ALA ARG SER MET PRO THR SER GLY
SEQRES 27 B 561 ALA LEU ASP ARG VAL ALA ASN ALA THR LYS ILE ALA LEU
SEQRES 28 B 561 TYR GLU THR PRO THR GLY TRP LYS PHE PHE GLY ASN LEU
SEQRES 29 B 561 MET ASP ALA SER LYS LEU SER LEU CYS GLY GLU GLU SER
SEQRES 30 B 561 PHE GLY THR GLY SER ASP HIS ILE ARG GLU LYS ASP GLY
SEQRES 31 B 561 LEU TRP ALA VAL LEU ALA TRP LEU SER ILE LEU ALA THR
SEQRES 32 B 561 ARG LYS GLN SER VAL GLU ASP ILE LEU LYS ASP HIS TRP
SEQRES 33 B 561 HIS LYS PHE GLY ARG ASN PHE PHE THR ARG TYR ASP TYR
SEQRES 34 B 561 GLU GLU VAL GLU ALA GLU GLY ALA THR LYS MET MET LYS
SEQRES 35 B 561 ASP LEU GLU ALA LEU MET PHE ASP ARG SER PHE VAL GLY
SEQRES 36 B 561 LYS GLN PHE SER ALA ASN ASP LYS VAL TYR THR VAL GLU
SEQRES 37 B 561 LYS ALA ASP ASN PHE GLU TYR HIS ASP PRO VAL ASP GLY
SEQRES 38 B 561 SER VAL SER LYS ASN GLN GLY LEU ARG LEU ILE PHE ALA
SEQRES 39 B 561 ASP GLY SER ARG ILE ILE PHE ARG LEU SER GLY THR GLY
SEQRES 40 B 561 SER ALA GLY ALA THR ILE ARG LEU TYR ILE ASP SER TYR
SEQRES 41 B 561 GLU LYS ASP ASN ALA LYS ILE ASN GLN ASP PRO GLN VAL
SEQRES 42 B 561 MET LEU ALA PRO LEU ILE SER ILE ALA LEU LYS VAL SER
SEQRES 43 B 561 GLN LEU GLN GLU ARG THR GLY ARG THR ALA PRO THR VAL
SEQRES 44 B 561 ILE THR
MODRES 3PMG SEP A 116 SER PHOSPHOSERINE
MODRES 3PMG SEP B 116 SER PHOSPHOSERINE
HET SEP A 116 11
HET SEP B 116 11
HET MG A 562 1
HET MG B 562 1
HETNAM SEP PHOSPHOSERINE
HETNAM MG MAGNESIUM ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *494(H2 O)
HELIX 1 1 VAL A 25 SER A 30 1 6
HELIX 2 2 TYR A 34 THR A 45 1 12
HELIX 3 3 PRO A 48 GLN A 50 5 3
HELIX 4 4 MET A 66 ALA A 79 1 14
HELIX 5 5 GLN A 89 GLY A 91 5 3
HELIX 6 6 THR A 95 ILE A 105 1 11
HELIX 7 7 GLU A 140 THR A 152 1 13
HELIX 8 8 GLU A 192 ARG A 199 1 8
HELIX 9 9 PHE A 204 SER A 212 1 9
HELIX 10 10 GLY A 229 LEU A 236 1 8
HELIX 11 11 ALA A 244 SER A 246 5 3
HELIX 12 12 PHE A 256 GLY A 258 5 3
HELIX 13 13 ALA A 269 SER A 277 1 9
HELIX 14 14 LYS A 298 GLY A 300 5 3
HELIX 15 15 PRO A 305 ALA A 314 1 10
HELIX 16 16 ILE A 316 SER A 318 5 3
HELIX 17 17 PRO A 320 THR A 325 1 6
HELIX 18 18 ALA A 339 ALA A 346 1 8
HELIX 19 19 TRP A 358 ASP A 366 1 9
HELIX 20 20 GLY A 390 ARG A 404 1 15
HELIX 21 21 VAL A 408 PHE A 419 1 12
HELIX 22 22 ALA A 434 PHE A 449 1 16
HELIX 23 23 PRO A 531 SER A 546 1 16
HELIX 24 24 LEU A 548 THR A 552 1 5
HELIX 25 25 VAL B 25 SER B 30 1 6
HELIX 26 26 TYR B 34 THR B 45 1 12
HELIX 27 27 PRO B 48 GLN B 50 5 3
HELIX 28 28 MET B 66 ALA B 79 1 14
HELIX 29 29 GLN B 89 GLY B 91 5 3
HELIX 30 30 THR B 95 ILE B 105 1 11
HELIX 31 31 GLU B 140 THR B 152 1 13
HELIX 32 32 GLU B 192 ILE B 201 1 10
HELIX 33 33 PHE B 204 SER B 212 1 9
HELIX 34 34 VAL B 227 LEU B 236 5 10
HELIX 35 35 ALA B 244 SER B 246 5 3
HELIX 36 36 PHE B 256 GLY B 258 5 3
HELIX 37 37 ALA B 269 LYS B 276 1 8
HELIX 38 38 LYS B 298 GLY B 300 5 3
HELIX 39 39 PRO B 305 SER B 318 1 14
HELIX 40 40 PRO B 320 THR B 325 1 6
HELIX 41 41 GLY B 338 THR B 347 5 10
HELIX 42 42 LYS B 359 ASP B 366 1 8
HELIX 43 43 GLY B 390 ARG B 404 1 15
HELIX 44 44 VAL B 408 PHE B 419 1 12
HELIX 45 45 ALA B 434 MET B 448 1 15
HELIX 46 46 PRO B 531 SER B 546 1 16
HELIX 47 47 LEU B 548 THR B 552 1 5
SHEET 1 A 2 VAL A 4 LYS A 7 0
SHEET 2 A 2 GLU A 155 ILE A 158 -1 N ILE A 158 O VAL A 4
SHEET 1 B 7 LEU A 21 ARG A 24 0
SHEET 2 B 7 ASP A 125 ILE A 132 -1 N ILE A 128 O LEU A 21
SHEET 3 B 7 GLY A 109 LEU A 113 -1 N ILE A 112 O LYS A 129
SHEET 4 B 7 THR A 55 GLY A 60 1 N VAL A 57 O GLY A 109
SHEET 5 B 7 ARG A 84 GLY A 88 1 N ARG A 84 O LEU A 56
SHEET 6 B 7 PHE A 183 VAL A 188 1 N THR A 184 O LEU A 85
SHEET 7 B 7 GLY A 170 PHE A 174 -1 N PHE A 174 O PHE A 183
SHEET 1 C 3 ILE A 219 ASP A 222 0
SHEET 2 C 3 PHE A 282 PHE A 286 1 N PHE A 282 O ARG A 220
SHEET 3 C 3 ASN A 293 GLY A 297 -1 N LEU A 296 O GLY A 283
SHEET 1 D 4 LEU A 351 THR A 354 0
SHEET 2 D 4 PHE A 330 SER A 333 1 N PHE A 330 O TYR A 352
SHEET 3 D 4 LEU A 372 GLU A 375 1 N LEU A 372 O ALA A 331
SHEET 4 D 4 GLY A 379 SER A 382 -1 N GLY A 381 O CYS A 373
SHEET 1 E 6 VAL A 559 THR A 561 0
SHEET 2 E 6 ARG A 421 TYR A 429 -1 N ASP A 428 O VAL A 559
SHEET 3 E 6 ALA A 511 GLU A 521 -1 N GLU A 521 O ARG A 421
SHEET 4 E 6 ARG A 498 GLY A 505 -1 N SER A 504 O THR A 512
SHEET 5 E 6 LEU A 489 PHE A 493 -1 N LEU A 491 O ILE A 499
SHEET 6 E 6 VAL A 467 ASN A 472 -1 N ASP A 471 O ARG A 490
SHEET 1 F 2 GLN A 457 ALA A 460 0
SHEET 2 F 2 LYS A 463 THR A 466 -1 N TYR A 465 O PHE A 458
SHEET 1 G 2 VAL B 4 LYS B 7 0
SHEET 2 G 2 GLU B 155 ILE B 158 -1 N ILE B 158 O VAL B 4
SHEET 1 H 7 LEU B 21 ARG B 24 0
SHEET 2 H 7 ASP B 125 ILE B 132 -1 N ILE B 128 O LEU B 21
SHEET 3 H 7 GLY B 109 LEU B 113 -1 N ILE B 112 O LYS B 129
SHEET 4 H 7 THR B 55 GLY B 60 1 N VAL B 57 O GLY B 109
SHEET 5 H 7 ARG B 84 GLY B 88 1 N ARG B 84 O LEU B 56
SHEET 6 H 7 PHE B 183 VAL B 188 1 N THR B 184 O LEU B 85
SHEET 7 H 7 GLY B 170 PHE B 174 -1 N PHE B 174 O PHE B 183
SHEET 1 I 3 ILE B 219 ASP B 222 0
SHEET 2 I 3 PHE B 282 PHE B 286 1 N PHE B 282 O ARG B 220
SHEET 3 I 3 ASN B 293 GLY B 297 -1 N LEU B 296 O GLY B 283
SHEET 1 J 4 LEU B 351 THR B 354 0
SHEET 2 J 4 PHE B 330 SER B 333 1 N PHE B 330 O TYR B 352
SHEET 3 J 4 LEU B 372 GLU B 375 1 N LEU B 372 O ALA B 331
SHEET 4 J 4 GLY B 379 SER B 382 -1 N GLY B 381 O CYS B 373
SHEET 1 K 6 VAL B 559 THR B 561 0
SHEET 2 K 6 ARG B 421 TYR B 429 -1 N ASP B 428 O VAL B 559
SHEET 3 K 6 ILE B 513 GLU B 521 -1 N GLU B 521 O ARG B 421
SHEET 4 K 6 ARG B 498 LEU B 503 -1 N ARG B 502 O ARG B 514
SHEET 5 K 6 LEU B 489 PHE B 493 -1 N LEU B 491 O ILE B 499
SHEET 6 K 6 VAL B 467 ASN B 472 -1 N ASP B 471 O ARG B 490
SHEET 1 L 2 GLN B 457 SER B 459 0
SHEET 2 L 2 VAL B 464 THR B 466 -1 N TYR B 465 O PHE B 458
LINK C ALA A 115 N SEP A 116 1555 1555 1.34
LINK OG SEP A 116 MG MG A 562 1555 1555 2.56
LINK C SEP A 116 N HIS A 117 1555 1555 1.33
LINK O2P SEP A 116 MG MG A 562 1555 1555 2.10
LINK OD2 ASP A 287 MG MG A 562 1555 1555 1.86
LINK OD1 ASP A 289 MG MG A 562 1555 1555 1.78
LINK OD1 ASP A 291 MG MG A 562 1555 1555 1.71
LINK C ALA B 115 N SEP B 116 1555 1555 1.35
LINK OG SEP B 116 MG MG B 562 1555 1555 2.14
LINK C SEP B 116 N HIS B 117 1555 1555 1.34
LINK O2P SEP B 116 MG MG B 562 1555 1555 2.02
LINK OD2 ASP B 287 MG MG B 562 1555 1555 2.13
LINK OD2 ASP B 289 MG MG B 562 1555 1555 2.15
LINK OD2 ASP B 291 MG MG B 562 1555 1555 2.09
LINK MG MG A 562 O HOH A 733 1555 1555 1.94
LINK MG MG B 562 O HOH B 758 1555 1555 2.05
SITE 1 MBA 4 ASP A 287 ASP A 289 ASP A 291 SEP A 116
SITE 1 MBB 4 ASP B 287 ASP B 289 ASP B 291 SEP B 116
SITE 1 AC1 5 SEP A 116 ASP A 287 ASP A 289 ASP A 291
SITE 2 AC1 5 HOH A 733
SITE 1 AC2 5 SEP B 116 ASP B 287 ASP B 289 ASP B 291
SITE 2 AC2 5 HOH B 758
CRYST1 174.420 174.420 101.120 90.00 90.00 90.00 P 41 21 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005733 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005733 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009889 0.00000
MTRIX1 1 0.263000 -0.964800 0.008700 83.54550 1
MTRIX2 1 -0.964000 -0.263100 -0.039300 111.24200 1
MTRIX3 1 0.040200 0.002000 -0.999200 84.64360 1
MTRIX1 2 0.252500 -0.967500 -0.011900 84.17520 1
MTRIX2 2 -0.965800 -0.251300 -0.004300 111.43300 1
MTRIX3 2 0.059200 0.027800 -0.997900 83.05350 1
(ATOM LINES ARE NOT SHOWN.)
END
