HEADER LIGASE 08-JUL-08 2VXO
TITLE HUMAN GMP SYNTHETASE IN COMPLEX WITH XMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GMP SYNTHASE [GLUTAMINE-HYDROLYZING];
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 20-693;
COMPND 5 SYNONYM: GLUTAMINE AMIDOTRANSFERASE, GMP SYNTHETASE;
COMPND 6 EC: 6.3.5.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3 PRARE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PNIC-BSA4
KEYWDS PROTO-ONCOGENE, PHOSPHOPROTEIN, GUANINE MONOPHOSPHATE SYNTHETASE, GMP
KEYWDS 2 BIOSYNTHESIS, NUCLEOTIDE-BINDING, PURINE BIOSYNTHESIS, NUCLEOTIDE
KEYWDS 3 METABOLISM, GMPS, CASP8, LIGASE, ATP-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WELIN,L.LEHTIO,J.ANDERSSON,C.H.ARROWSMITH,H.BERGLUND,R.COLLINS,
AUTHOR 2 L.G.DAHLGREN,A.M.EDWARDS,S.FLODIN,A.FLORES,S.GRASLUND,M.HAMMARSTROM,
AUTHOR 3 A.JOHANSSON,I.JOHANSSON,T.KARLBERG,T.KOTENYOVA,M.MOCHE,M.E.NILSSON,
AUTHOR 4 T.NYMAN,K.OLESEN,C.PERSSON,J.SAGEMARK,H.SCHUELER,A.G.THORSELL,
AUTHOR 5 L.TRESAUGUES,S.VAN DEN BERG,M.WISNIEWSKA,M.WIKSTROM,P.NORDLUND
REVDAT 6 13-DEC-23 2VXO 1 REMARK
REVDAT 5 16-OCT-19 2VXO 1 REMARK
REVDAT 4 13-NOV-13 2VXO 1 JRNL
REVDAT 3 10-JUL-13 2VXO 1 SOURCE KEYWDS JRNL REMARK
REVDAT 3 2 1 VERSN FORMUL
REVDAT 2 24-FEB-09 2VXO 1 VERSN
REVDAT 1 12-AUG-08 2VXO 0
JRNL AUTH M.WELIN,L.LEHTIO,A.JOHANSSON,S.FLODIN,T.NYMAN,L.TRESAUGUES,
JRNL AUTH 2 M.HAMMARSTROM,S.GRASLUND,P.NORDLUND
JRNL TITL SUBSTRATE SPECIFICITY AND OLIGOMERIZATION OF HUMAN GMP
JRNL TITL 2 SYNTHETASE
JRNL REF J.MOL.BIOL. V. 425 4323 2013
JRNL REFN ISSN 0022-2836
JRNL PMID 23816837
JRNL DOI 10.1016/J.JMB.2013.06.032
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0036
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 51746
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2724
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3728
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 196
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10019
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 125
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.37000
REMARK 3 B22 (A**2) : 0.64000
REMARK 3 B33 (A**2) : -1.01000
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): 0.504
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.290
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.202
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.944
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10313 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14002 ; 1.203 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1301 ; 5.568 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 417 ;36.048 ;24.388
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1798 ;16.314 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;20.238 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1637 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7608 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 6490 ; 0.863 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10560 ; 1.679 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3823 ; 2.178 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3438 ; 3.698 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 2VXO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1290036804.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAY-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97968
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54472
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.80
REMARK 200 R MERGE FOR SHELL (I) : 0.58700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.120
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2YWC
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NAAC,PH 5.2,1.6M AMSO4, 0.2M
REMARK 280 NACL, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 49.26000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.98000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.71000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.98000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.26000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.71000
REMARK 290 SMTRY3 4 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: 9960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -128.5 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 MET A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 SER A 4
REMARK 465 SER A 5
REMARK 465 GLY A 6
REMARK 465 VAL A 7
REMARK 465 ASP A 8
REMARK 465 LEU A 9
REMARK 465 GLY A 10
REMARK 465 THR A 11
REMARK 465 GLU A 12
REMARK 465 ASN A 13
REMARK 465 LEU A 14
REMARK 465 TYR A 15
REMARK 465 PHE A 16
REMARK 465 GLN A 17
REMARK 465 SER A 18
REMARK 465 MET A 19
REMARK 465 GLY A 20
REMARK 465 HIS A 21
REMARK 465 HIS A 22
REMARK 465 HIS A 23
REMARK 465 TYR A 24
REMARK 465 ALA A 35
REMARK 465 GLN A 36
REMARK 465 ASN A 79
REMARK 465 SER A 80
REMARK 465 VAL A 81
REMARK 465 TYR A 82
REMARK 465 ALA A 83
REMARK 465 GLU A 84
REMARK 465 ASP A 85
REMARK 465 LYS A 121
REMARK 465 SER A 122
REMARK 465 VAL A 123
REMARK 465 ARG A 124
REMARK 465 GLU A 125
REMARK 465 ASP A 126
REMARK 465 GLY A 127
REMARK 465 ILE A 312
REMARK 465 SER A 313
REMARK 465 ASP A 314
REMARK 465 GLU A 315
REMARK 465 ASP A 316
REMARK 465 ARG A 317
REMARK 465 THR A 318
REMARK 465 PRO A 319
REMARK 465 ARG A 320
REMARK 465 LYS A 321
REMARK 465 MET B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 HIS B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 SER B 4
REMARK 465 SER B 5
REMARK 465 GLY B 6
REMARK 465 VAL B 7
REMARK 465 ASP B 8
REMARK 465 LEU B 9
REMARK 465 GLY B 10
REMARK 465 THR B 11
REMARK 465 GLU B 12
REMARK 465 ASN B 13
REMARK 465 LEU B 14
REMARK 465 TYR B 15
REMARK 465 PHE B 16
REMARK 465 GLN B 17
REMARK 465 SER B 18
REMARK 465 MET B 19
REMARK 465 GLY B 20
REMARK 465 HIS B 21
REMARK 465 HIS B 22
REMARK 465 VAL B 123
REMARK 465 ARG B 124
REMARK 465 GLU B 125
REMARK 465 ILE B 312
REMARK 465 SER B 313
REMARK 465 ASP B 314
REMARK 465 GLU B 315
REMARK 465 ASP B 316
REMARK 465 ARG B 317
REMARK 465 THR B 318
REMARK 465 PRO B 319
REMARK 465 ARG B 320
REMARK 465 LYS B 321
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 GLU A 25 CG CD OE1 OE2
REMARK 470 LYS A 39 CD CE NZ
REMARK 470 ARG A 43 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 66 CG CD OE1 OE2
REMARK 470 LYS A 120 CG CD CE NZ
REMARK 470 ARG A 278 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 281 CG CD OE1 NE2
REMARK 470 LYS A 289 CG CD CE NZ
REMARK 470 ARG A 322 CD NE CZ NH1 NH2
REMARK 470 ASN A 356 CG OD1 ND2
REMARK 470 LYS A 358 CD CE NZ
REMARK 470 LYS A 569 CG CD CE NZ
REMARK 470 LYS A 627 CG CD CE NZ
REMARK 470 HIS B 23 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 ARG B 43 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 120 CG CD CE NZ
REMARK 470 LYS B 121 CG CD CE NZ
REMARK 470 ARG B 278 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 289 CG CD CE NZ
REMARK 470 ARG B 322 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 360 CG CD OE1 OE2
REMARK 470 GLU B 361 CG CD OE1 OE2
REMARK 470 LYS B 569 CG CD CE NZ
REMARK 470 LYS B 627 CG CD CE NZ
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 ND2 ASN B 135 O LEU B 143 2.13
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 ALA A 33 57.97 -112.93
REMARK 500 CYS A 104 -105.55 73.30
REMARK 500 HIS A 119 -165.81 -127.11
REMARK 500 ASP A 158 -91.23 -108.43
REMARK 500 ARG A 278 -4.53 69.34
REMARK 500 PRO A 617 40.64 -79.21
REMARK 500 ASN A 655 -90.08 -111.32
REMARK 500 SER A 676 -82.78 -78.02
REMARK 500 ALA B 86 122.28 -37.48
REMARK 500 CYS B 104 -98.65 55.18
REMARK 500 ASP B 158 -85.87 -90.36
REMARK 500 TYR B 208 -71.02 -97.01
REMARK 500 LYS B 277 109.09 -55.22
REMARK 500 GLN B 610 142.54 -172.45
REMARK 500 PRO B 617 46.71 -74.68
REMARK 500 GLN B 626 -17.06 -160.82
REMARK 500 ASN B 655 -85.57 -123.58
REMARK 500 SER B 676 -84.55 -74.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XMP A 1694
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XMP B 1694
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1695
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1696
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1695
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1696
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1697
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1697
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VPI RELATED DB: PDB
REMARK 900 HUMAN GMP SYNTHETASE - GLUTAMINASE DOMAIN
DBREF 2VXO A -3 19 PDB 2VXO 2VXO -3 19
DBREF 2VXO A 20 693 UNP P49915 GUAA_HUMAN 20 693
DBREF 2VXO B -3 19 PDB 2VXO 2VXO -3 19
DBREF 2VXO B 20 693 UNP P49915 GUAA_HUMAN 20 693
SEQRES 1 A 697 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 697 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY HIS HIS
SEQRES 3 A 697 HIS TYR GLU GLY ALA VAL VAL ILE LEU ASP ALA GLY ALA
SEQRES 4 A 697 GLN TYR GLY LYS VAL ILE ASP ARG ARG VAL ARG GLU LEU
SEQRES 5 A 697 PHE VAL GLN SER GLU ILE PHE PRO LEU GLU THR PRO ALA
SEQRES 6 A 697 PHE ALA ILE LYS GLU GLN GLY PHE ARG ALA ILE ILE ILE
SEQRES 7 A 697 SER GLY GLY PRO ASN SER VAL TYR ALA GLU ASP ALA PRO
SEQRES 8 A 697 TRP PHE ASP PRO ALA ILE PHE THR ILE GLY LYS PRO VAL
SEQRES 9 A 697 LEU GLY ILE CYS TYR GLY MET GLN MET MET ASN LYS VAL
SEQRES 10 A 697 PHE GLY GLY THR VAL HIS LYS LYS SER VAL ARG GLU ASP
SEQRES 11 A 697 GLY VAL PHE ASN ILE SER VAL ASP ASN THR CYS SER LEU
SEQRES 12 A 697 PHE ARG GLY LEU GLN LYS GLU GLU VAL VAL LEU LEU THR
SEQRES 13 A 697 HIS GLY ASP SER VAL ASP LYS VAL ALA ASP GLY PHE LYS
SEQRES 14 A 697 VAL VAL ALA ARG SER GLY ASN ILE VAL ALA GLY ILE ALA
SEQRES 15 A 697 ASN GLU SER LYS LYS LEU TYR GLY ALA GLN PHE HIS PRO
SEQRES 16 A 697 GLU VAL GLY LEU THR GLU ASN GLY LYS VAL ILE LEU LYS
SEQRES 17 A 697 ASN PHE LEU TYR ASP ILE ALA GLY CYS SER GLY THR PHE
SEQRES 18 A 697 THR VAL GLN ASN ARG GLU LEU GLU CYS ILE ARG GLU ILE
SEQRES 19 A 697 LYS GLU ARG VAL GLY THR SER LYS VAL LEU VAL LEU LEU
SEQRES 20 A 697 SER GLY GLY VAL ASP SER THR VAL CYS THR ALA LEU LEU
SEQRES 21 A 697 ASN ARG ALA LEU ASN GLN GLU GLN VAL ILE ALA VAL HIS
SEQRES 22 A 697 ILE ASP ASN GLY PHE MET ARG LYS ARG GLU SER GLN SER
SEQRES 23 A 697 VAL GLU GLU ALA LEU LYS LYS LEU GLY ILE GLN VAL LYS
SEQRES 24 A 697 VAL ILE ASN ALA ALA HIS SER PHE TYR ASN GLY THR THR
SEQRES 25 A 697 THR LEU PRO ILE SER ASP GLU ASP ARG THR PRO ARG LYS
SEQRES 26 A 697 ARG ILE SER LYS THR LEU ASN MET THR THR SER PRO GLU
SEQRES 27 A 697 GLU LYS ARG LYS ILE ILE GLY ASP THR PHE VAL LYS ILE
SEQRES 28 A 697 ALA ASN GLU VAL ILE GLY GLU MET ASN LEU LYS PRO GLU
SEQRES 29 A 697 GLU VAL PHE LEU ALA GLN GLY THR LEU ARG PRO ASP LEU
SEQRES 30 A 697 ILE GLU SER ALA SER LEU VAL ALA SER GLY LYS ALA GLU
SEQRES 31 A 697 LEU ILE LYS THR HIS HIS ASN ASP THR GLU LEU ILE ARG
SEQRES 32 A 697 LYS LEU ARG GLU GLU GLY LYS VAL ILE GLU PRO LEU LYS
SEQRES 33 A 697 ASP PHE HIS LYS ASP GLU VAL ARG ILE LEU GLY ARG GLU
SEQRES 34 A 697 LEU GLY LEU PRO GLU GLU LEU VAL SER ARG HIS PRO PHE
SEQRES 35 A 697 PRO GLY PRO GLY LEU ALA ILE ARG VAL ILE CYS ALA GLU
SEQRES 36 A 697 GLU PRO TYR ILE CYS LYS ASP PHE PRO GLU THR ASN ASN
SEQRES 37 A 697 ILE LEU LYS ILE VAL ALA ASP PHE SER ALA SER VAL LYS
SEQRES 38 A 697 LYS PRO HIS THR LEU LEU GLN ARG VAL LYS ALA CYS THR
SEQRES 39 A 697 THR GLU GLU ASP GLN GLU LYS LEU MET GLN ILE THR SER
SEQRES 40 A 697 LEU HIS SER LEU ASN ALA PHE LEU LEU PRO ILE LYS THR
SEQRES 41 A 697 VAL GLY VAL GLN GLY ASP CYS ARG SER TYR SER TYR VAL
SEQRES 42 A 697 CYS GLY ILE SER SER LYS ASP GLU PRO ASP TRP GLU SER
SEQRES 43 A 697 LEU ILE PHE LEU ALA ARG LEU ILE PRO ARG MET CYS HIS
SEQRES 44 A 697 ASN VAL ASN ARG VAL VAL TYR ILE PHE GLY PRO PRO VAL
SEQRES 45 A 697 LYS GLU PRO PRO THR ASP VAL THR PRO THR PHE LEU THR
SEQRES 46 A 697 THR GLY VAL LEU SER THR LEU ARG GLN ALA ASP PHE GLU
SEQRES 47 A 697 ALA HIS ASN ILE LEU ARG GLU SER GLY TYR ALA GLY LYS
SEQRES 48 A 697 ILE SER GLN MET PRO VAL ILE LEU THR PRO LEU HIS PHE
SEQRES 49 A 697 ASP ARG ASP PRO LEU GLN LYS GLN PRO SER CYS GLN ARG
SEQRES 50 A 697 SER VAL VAL ILE ARG THR PHE ILE THR SER ASP PHE MET
SEQRES 51 A 697 THR GLY ILE PRO ALA THR PRO GLY ASN GLU ILE PRO VAL
SEQRES 52 A 697 GLU VAL VAL LEU LYS MET VAL THR GLU ILE LYS LYS ILE
SEQRES 53 A 697 PRO GLY ILE SER ARG ILE MET TYR ASP LEU THR SER LYS
SEQRES 54 A 697 PRO PRO GLY THR THR GLU TRP GLU
SEQRES 1 B 697 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 697 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY HIS HIS
SEQRES 3 B 697 HIS TYR GLU GLY ALA VAL VAL ILE LEU ASP ALA GLY ALA
SEQRES 4 B 697 GLN TYR GLY LYS VAL ILE ASP ARG ARG VAL ARG GLU LEU
SEQRES 5 B 697 PHE VAL GLN SER GLU ILE PHE PRO LEU GLU THR PRO ALA
SEQRES 6 B 697 PHE ALA ILE LYS GLU GLN GLY PHE ARG ALA ILE ILE ILE
SEQRES 7 B 697 SER GLY GLY PRO ASN SER VAL TYR ALA GLU ASP ALA PRO
SEQRES 8 B 697 TRP PHE ASP PRO ALA ILE PHE THR ILE GLY LYS PRO VAL
SEQRES 9 B 697 LEU GLY ILE CYS TYR GLY MET GLN MET MET ASN LYS VAL
SEQRES 10 B 697 PHE GLY GLY THR VAL HIS LYS LYS SER VAL ARG GLU ASP
SEQRES 11 B 697 GLY VAL PHE ASN ILE SER VAL ASP ASN THR CYS SER LEU
SEQRES 12 B 697 PHE ARG GLY LEU GLN LYS GLU GLU VAL VAL LEU LEU THR
SEQRES 13 B 697 HIS GLY ASP SER VAL ASP LYS VAL ALA ASP GLY PHE LYS
SEQRES 14 B 697 VAL VAL ALA ARG SER GLY ASN ILE VAL ALA GLY ILE ALA
SEQRES 15 B 697 ASN GLU SER LYS LYS LEU TYR GLY ALA GLN PHE HIS PRO
SEQRES 16 B 697 GLU VAL GLY LEU THR GLU ASN GLY LYS VAL ILE LEU LYS
SEQRES 17 B 697 ASN PHE LEU TYR ASP ILE ALA GLY CYS SER GLY THR PHE
SEQRES 18 B 697 THR VAL GLN ASN ARG GLU LEU GLU CYS ILE ARG GLU ILE
SEQRES 19 B 697 LYS GLU ARG VAL GLY THR SER LYS VAL LEU VAL LEU LEU
SEQRES 20 B 697 SER GLY GLY VAL ASP SER THR VAL CYS THR ALA LEU LEU
SEQRES 21 B 697 ASN ARG ALA LEU ASN GLN GLU GLN VAL ILE ALA VAL HIS
SEQRES 22 B 697 ILE ASP ASN GLY PHE MET ARG LYS ARG GLU SER GLN SER
SEQRES 23 B 697 VAL GLU GLU ALA LEU LYS LYS LEU GLY ILE GLN VAL LYS
SEQRES 24 B 697 VAL ILE ASN ALA ALA HIS SER PHE TYR ASN GLY THR THR
SEQRES 25 B 697 THR LEU PRO ILE SER ASP GLU ASP ARG THR PRO ARG LYS
SEQRES 26 B 697 ARG ILE SER LYS THR LEU ASN MET THR THR SER PRO GLU
SEQRES 27 B 697 GLU LYS ARG LYS ILE ILE GLY ASP THR PHE VAL LYS ILE
SEQRES 28 B 697 ALA ASN GLU VAL ILE GLY GLU MET ASN LEU LYS PRO GLU
SEQRES 29 B 697 GLU VAL PHE LEU ALA GLN GLY THR LEU ARG PRO ASP LEU
SEQRES 30 B 697 ILE GLU SER ALA SER LEU VAL ALA SER GLY LYS ALA GLU
SEQRES 31 B 697 LEU ILE LYS THR HIS HIS ASN ASP THR GLU LEU ILE ARG
SEQRES 32 B 697 LYS LEU ARG GLU GLU GLY LYS VAL ILE GLU PRO LEU LYS
SEQRES 33 B 697 ASP PHE HIS LYS ASP GLU VAL ARG ILE LEU GLY ARG GLU
SEQRES 34 B 697 LEU GLY LEU PRO GLU GLU LEU VAL SER ARG HIS PRO PHE
SEQRES 35 B 697 PRO GLY PRO GLY LEU ALA ILE ARG VAL ILE CYS ALA GLU
SEQRES 36 B 697 GLU PRO TYR ILE CYS LYS ASP PHE PRO GLU THR ASN ASN
SEQRES 37 B 697 ILE LEU LYS ILE VAL ALA ASP PHE SER ALA SER VAL LYS
SEQRES 38 B 697 LYS PRO HIS THR LEU LEU GLN ARG VAL LYS ALA CYS THR
SEQRES 39 B 697 THR GLU GLU ASP GLN GLU LYS LEU MET GLN ILE THR SER
SEQRES 40 B 697 LEU HIS SER LEU ASN ALA PHE LEU LEU PRO ILE LYS THR
SEQRES 41 B 697 VAL GLY VAL GLN GLY ASP CYS ARG SER TYR SER TYR VAL
SEQRES 42 B 697 CYS GLY ILE SER SER LYS ASP GLU PRO ASP TRP GLU SER
SEQRES 43 B 697 LEU ILE PHE LEU ALA ARG LEU ILE PRO ARG MET CYS HIS
SEQRES 44 B 697 ASN VAL ASN ARG VAL VAL TYR ILE PHE GLY PRO PRO VAL
SEQRES 45 B 697 LYS GLU PRO PRO THR ASP VAL THR PRO THR PHE LEU THR
SEQRES 46 B 697 THR GLY VAL LEU SER THR LEU ARG GLN ALA ASP PHE GLU
SEQRES 47 B 697 ALA HIS ASN ILE LEU ARG GLU SER GLY TYR ALA GLY LYS
SEQRES 48 B 697 ILE SER GLN MET PRO VAL ILE LEU THR PRO LEU HIS PHE
SEQRES 49 B 697 ASP ARG ASP PRO LEU GLN LYS GLN PRO SER CYS GLN ARG
SEQRES 50 B 697 SER VAL VAL ILE ARG THR PHE ILE THR SER ASP PHE MET
SEQRES 51 B 697 THR GLY ILE PRO ALA THR PRO GLY ASN GLU ILE PRO VAL
SEQRES 52 B 697 GLU VAL VAL LEU LYS MET VAL THR GLU ILE LYS LYS ILE
SEQRES 53 B 697 PRO GLY ILE SER ARG ILE MET TYR ASP LEU THR SER LYS
SEQRES 54 B 697 PRO PRO GLY THR THR GLU TRP GLU
HET XMP A1694 24
HET SO4 A1695 5
HET SO4 A1696 5
HET SO4 A1697 5
HET XMP B1694 24
HET SO4 B1695 5
HET SO4 B1696 5
HET SO4 B1697 5
HETNAM XMP XANTHOSINE-5'-MONOPHOSPHATE
HETNAM SO4 SULFATE ION
HETSYN XMP 5-MONOPHOSPHATE-9-BETA-D-RIBOFURANOSYL XANTHINE
FORMUL 3 XMP 2(C10 H14 N4 O9 P 1+)
FORMUL 4 SO4 6(O4 S 2-)
FORMUL 11 HOH *125(H2 O)
HELIX 1 1 TYR A 37 LEU A 48 1 12
HELIX 2 2 PRO A 60 GLY A 68 1 9
HELIX 3 3 ASP A 90 PHE A 94 5 5
HELIX 4 4 CYS A 104 PHE A 114 1 11
HELIX 5 5 CYS A 137 ARG A 141 5 5
HELIX 6 6 ASN A 198 TYR A 208 1 11
HELIX 7 7 THR A 218 GLY A 235 1 18
HELIX 8 8 GLY A 246 LEU A 260 1 15
HELIX 9 9 ASN A 261 GLU A 263 5 3
HELIX 10 10 SER A 280 LEU A 290 1 11
HELIX 11 11 ALA A 299 ASN A 305 1 7
HELIX 12 12 THR A 326 THR A 330 5 5
HELIX 13 13 SER A 332 MET A 355 1 24
HELIX 14 14 SER A 376 GLY A 383 1 8
HELIX 15 15 GLU A 386 THR A 390 5 5
HELIX 16 16 THR A 395 GLU A 404 1 10
HELIX 17 17 GLU A 409 PHE A 414 5 6
HELIX 18 18 HIS A 415 LEU A 426 1 12
HELIX 19 19 PRO A 429 SER A 434 1 6
HELIX 20 20 PRO A 441 ARG A 446 5 6
HELIX 21 21 ASP A 458 ASP A 471 1 14
HELIX 22 22 ASP A 471 VAL A 476 1 6
HELIX 23 23 HIS A 480 THR A 490 1 11
HELIX 24 24 THR A 491 HIS A 505 1 15
HELIX 25 25 ASP A 539 CYS A 554 1 16
HELIX 26 26 THR A 581 SER A 602 1 22
HELIX 27 27 TYR A 604 ILE A 608 5 5
HELIX 28 28 ASP A 623 LYS A 627 5 5
HELIX 29 29 PRO A 658 ILE A 672 1 15
HELIX 30 30 GLN B 36 LEU B 48 1 13
HELIX 31 31 PRO B 60 GLY B 68 1 9
HELIX 32 32 ASP B 90 THR B 95 5 6
HELIX 33 33 CYS B 104 PHE B 114 1 11
HELIX 34 34 CYS B 137 ARG B 141 5 5
HELIX 35 35 ASN B 198 TYR B 208 1 11
HELIX 36 36 THR B 218 GLY B 235 1 18
HELIX 37 37 GLY B 246 LEU B 260 1 15
HELIX 38 38 GLN B 281 LEU B 290 1 10
HELIX 39 39 ALA B 299 ASN B 305 1 7
HELIX 40 40 THR B 326 THR B 330 5 5
HELIX 41 41 SER B 332 MET B 355 1 24
HELIX 42 42 LYS B 358 GLU B 360 5 3
HELIX 43 43 SER B 376 GLY B 383 1 8
HELIX 44 44 GLU B 386 THR B 390 5 5
HELIX 45 45 THR B 395 GLU B 404 1 10
HELIX 46 46 GLU B 409 PHE B 414 5 6
HELIX 47 47 HIS B 415 LEU B 426 1 12
HELIX 48 48 PRO B 429 SER B 434 1 6
HELIX 49 49 PRO B 441 ARG B 446 5 6
HELIX 50 50 ASP B 458 ASP B 471 1 14
HELIX 51 51 ASP B 471 LYS B 478 1 8
HELIX 52 52 HIS B 480 THR B 490 1 11
HELIX 53 53 THR B 491 HIS B 505 1 15
HELIX 54 54 ASP B 539 CYS B 554 1 16
HELIX 55 55 THR B 581 SER B 602 1 22
HELIX 56 56 TYR B 604 ILE B 608 5 5
HELIX 57 57 PRO B 658 LYS B 671 1 14
SHEET 1 AA 9 SER A 52 PRO A 56 0
SHEET 2 AA 9 VAL A 28 ALA A 33 1 O VAL A 28 N GLU A 53
SHEET 3 AA 9 ALA A 71 GLY A 76 1 O ALA A 71 N VAL A 29
SHEET 4 AA 9 VAL A 100 ILE A 103 1 O LEU A 101 N ILE A 74
SHEET 5 AA 9 LEU A 184 ALA A 187 1 O TYR A 185 N GLY A 102
SHEET 6 AA 9 ILE A 173 ASN A 179 -1 O ILE A 177 N GLY A 186
SHEET 7 AA 9 LYS A 165 SER A 170 -1 O LYS A 165 N ALA A 178
SHEET 8 AA 9 PHE A 129 VAL A 133 -1 O SER A 132 N ARG A 169
SHEET 9 AA 9 GLU A 146 VAL A 149 -1 O GLU A 147 N ILE A 131
SHEET 1 AB 5 VAL A 294 ASN A 298 0
SHEET 2 AB 5 VAL A 265 ASP A 271 1 O ALA A 267 N LYS A 295
SHEET 3 AB 5 LYS A 238 LEU A 242 1 O VAL A 239 N ILE A 266
SHEET 4 AB 5 VAL A 362 ALA A 365 1 O PHE A 363 N LEU A 240
SHEET 5 AB 5 VAL A 407 ILE A 408 1 N ILE A 408 O LEU A 364
SHEET 1 AC 6 LEU A 507 GLN A 520 0
SHEET 2 AC 6 CYS A 523 SER A 534 -1 O CYS A 523 N GLN A 520
SHEET 3 AC 6 VAL A 557 ILE A 563 1 N ASN A 558 O TYR A 528
SHEET 4 AC 6 ILE A 675 ASP A 681 -1 O TYR A 680 N TYR A 562
SHEET 5 AC 6 ARG A 633 ILE A 637 1 O ARG A 633 N SER A 676
SHEET 6 AC 6 VAL A 613 THR A 616 -1 O ILE A 614 N VAL A 636
SHEET 1 BA 9 SER B 52 PRO B 56 0
SHEET 2 BA 9 VAL B 28 ASP B 32 1 O VAL B 28 N GLU B 53
SHEET 3 BA 9 ALA B 71 SER B 75 1 O ALA B 71 N VAL B 29
SHEET 4 BA 9 VAL B 100 ILE B 103 1 O LEU B 101 N ILE B 74
SHEET 5 BA 9 LEU B 184 ALA B 187 1 O TYR B 185 N GLY B 102
SHEET 6 BA 9 ILE B 173 ASN B 179 -1 O ILE B 177 N GLY B 186
SHEET 7 BA 9 LYS B 165 SER B 170 -1 O LYS B 165 N ALA B 178
SHEET 8 BA 9 VAL B 128 VAL B 133 -1 O SER B 132 N ARG B 169
SHEET 9 BA 9 GLU B 146 LEU B 150 -1 O GLU B 147 N ILE B 131
SHEET 1 BB 5 VAL B 294 ASN B 298 0
SHEET 2 BB 5 VAL B 265 ASP B 271 1 O ALA B 267 N LYS B 295
SHEET 3 BB 5 LYS B 238 LEU B 242 1 O VAL B 239 N ILE B 266
SHEET 4 BB 5 VAL B 362 ALA B 365 1 O PHE B 363 N LEU B 240
SHEET 5 BB 5 VAL B 407 ILE B 408 1 N ILE B 408 O LEU B 364
SHEET 1 BC 6 LEU B 507 GLN B 520 0
SHEET 2 BC 6 CYS B 523 SER B 534 -1 O CYS B 523 N GLN B 520
SHEET 3 BC 6 VAL B 557 ILE B 563 1 N ASN B 558 O TYR B 528
SHEET 4 BC 6 ILE B 675 ASP B 681 -1 O TYR B 680 N TYR B 562
SHEET 5 BC 6 ARG B 633 ILE B 637 1 O ARG B 633 N SER B 676
SHEET 6 BC 6 VAL B 613 THR B 616 -1 O ILE B 614 N VAL B 636
CISPEP 1 LYS A 685 PRO A 686 0 -6.34
CISPEP 2 PRO A 686 PRO A 687 0 -4.03
CISPEP 3 LYS B 685 PRO B 686 0 -6.20
CISPEP 4 PRO B 686 PRO B 687 0 2.86
SITE 1 AC1 15 ARG A 337 GLY A 383 LYS A 384 PRO A 439
SITE 2 AC1 15 GLY A 440 PRO A 441 GLN A 610 PHE A 645
SITE 3 AC1 15 LYS A 685 THR A 689 THR A 690 GLU A 691
SITE 4 AC1 15 HOH A2066 HOH A2067 ASP B 522
SITE 1 AC2 16 ASP A 522 ARG B 337 GLY B 383 LYS B 384
SITE 2 AC2 16 PRO B 439 GLY B 440 PRO B 441 ARG B 524
SITE 3 AC2 16 GLN B 610 PHE B 645 LYS B 685 THR B 689
SITE 4 AC2 16 THR B 690 GLU B 691 HOH B2029 HOH B2057
SITE 1 AC3 6 ARG A 276 GLU A 279 ARG A 435 HIS A 436
SITE 2 AC3 6 HIS A 596 ARG A 600
SITE 1 AC4 3 THR A 581 GLY A 583 VAL A 584
SITE 1 AC5 3 THR B 581 GLY B 583 VAL B 584
SITE 1 AC6 5 ARG B 276 ARG B 435 HIS B 436 HIS B 596
SITE 2 AC6 5 ARG B 600
SITE 1 AC7 5 SER A 244 GLY A 246 VAL A 247 ASP A 248
SITE 2 AC7 5 SER A 249
SITE 1 AC8 4 SER B 244 GLY B 246 ASP B 248 SER B 249
CRYST1 98.520 123.420 127.960 90.00 90.00 90.00 P 21 21 21 8
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 0.010150 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008102 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007815 0.00000
MTRIX1 1 -1.000000 -0.009850 -0.001055 24.64000 1
MTRIX2 1 -0.000966 0.202900 -0.979200 -24.04000 1
MTRIX3 1 0.009859 -0.979100 -0.202900 -29.46000 1
(ATOM LINES ARE NOT SHOWN.)
END