HEADER ISOMERASE 11-NOV-15 5EPC
TITLE CRYSTAL STRUCTURE OF WILD-TYPE HUMAN PHOSPHOGLUCOMUTASE 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOGLUCOMUTASE-1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PGM 1,GLUCOSE PHOSPHOMUTASE 1;
COMPND 5 EC: 5.4.2.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PGM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS ISOMERASE METABOLISM, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.J.BEAMER
REVDAT 1 27-APR-16 5EPC 0
JRNL AUTH K.M.STIERS,B.N.KAIN,A.C.GRAHAM,L.J.BEAMER
JRNL TITL INDUCED STRUCTURAL DISORDER AS A MOLECULAR MECHANISM FOR
JRNL TITL 2 ENZYME DYSFUNCTION IN PHOSPHOGLUCOMUTASE 1 DEFICIENCY.
JRNL REF J.MOL.BIOL. V. 428 1493 2016
JRNL REFN ESSN 1089-8638
JRNL PMID 26972339
JRNL DOI 10.1016/J.JMB.2016.02.032
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.05
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.920
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 127879
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 6404
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 61.0840 - 5.7468 1.00 4374 229 0.1762 0.1958
REMARK 3 2 5.7468 - 4.5619 1.00 4171 227 0.1451 0.1750
REMARK 3 3 4.5619 - 3.9854 1.00 4138 207 0.1329 0.1490
REMARK 3 4 3.9854 - 3.6210 1.00 4108 227 0.1346 0.1620
REMARK 3 5 3.6210 - 3.3615 1.00 4091 220 0.1509 0.1610
REMARK 3 6 3.3615 - 3.1633 1.00 4074 209 0.1633 0.2077
REMARK 3 7 3.1633 - 3.0049 1.00 4071 217 0.1710 0.2006
REMARK 3 8 3.0049 - 2.8741 1.00 4053 215 0.1792 0.2084
REMARK 3 9 2.8741 - 2.7635 1.00 4078 198 0.1682 0.2023
REMARK 3 10 2.7635 - 2.6681 1.00 4023 231 0.1657 0.1977
REMARK 3 11 2.6681 - 2.5847 1.00 3993 237 0.1697 0.2028
REMARK 3 12 2.5847 - 2.5108 1.00 4054 201 0.1706 0.2073
REMARK 3 13 2.5108 - 2.4447 1.00 4009 244 0.1674 0.2087
REMARK 3 14 2.4447 - 2.3851 1.00 4063 197 0.1732 0.2210
REMARK 3 15 2.3851 - 2.3308 1.00 4024 195 0.1734 0.1991
REMARK 3 16 2.3308 - 2.2812 1.00 4032 225 0.1700 0.2233
REMARK 3 17 2.2812 - 2.2356 1.00 4006 221 0.1781 0.2087
REMARK 3 18 2.2356 - 2.1934 1.00 3978 232 0.1810 0.2063
REMARK 3 19 2.1934 - 2.1542 1.00 4054 205 0.1816 0.2150
REMARK 3 20 2.1542 - 2.1177 1.00 4009 202 0.1938 0.2212
REMARK 3 21 2.1177 - 2.0836 1.00 3993 237 0.1987 0.2113
REMARK 3 22 2.0836 - 2.0515 1.00 3995 221 0.2029 0.2375
REMARK 3 23 2.0515 - 2.0213 1.00 4034 192 0.2090 0.1962
REMARK 3 24 2.0213 - 1.9929 1.00 4000 199 0.2111 0.2424
REMARK 3 25 1.9929 - 1.9659 1.00 4029 201 0.2189 0.2370
REMARK 3 26 1.9659 - 1.9404 1.00 3979 198 0.2346 0.2767
REMARK 3 27 1.9404 - 1.9161 1.00 4020 208 0.2436 0.3017
REMARK 3 28 1.9161 - 1.8930 1.00 4015 219 0.2514 0.2763
REMARK 3 29 1.8930 - 1.8710 1.00 3994 207 0.2802 0.3180
REMARK 3 30 1.8710 - 1.8500 1.00 4013 183 0.3087 0.3512
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.40
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 8754
REMARK 3 ANGLE : 0.998 11884
REMARK 3 CHIRALITY : 0.043 1344
REMARK 3 PLANARITY : 0.005 1543
REMARK 3 DIHEDRAL : 12.381 3149
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.5064 -73.5023 5.4307
REMARK 3 T TENSOR
REMARK 3 T11: 0.3668 T22: 0.1739
REMARK 3 T33: 0.1951 T12: 0.0335
REMARK 3 T13: 0.0154 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 2.8485 L22: 3.5741
REMARK 3 L33: 2.1581 L12: -0.1059
REMARK 3 L13: 0.0615 L23: -0.1659
REMARK 3 S TENSOR
REMARK 3 S11: -0.0617 S12: -0.0994 S13: -0.2010
REMARK 3 S21: 0.2343 S22: 0.1234 S23: -0.0458
REMARK 3 S31: 0.5642 S32: 0.1731 S33: -0.0609
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 82 THROUGH 405 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2354 -53.5527 -0.1390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1658 T22: 0.1711
REMARK 3 T33: 0.1833 T12: -0.0634
REMARK 3 T13: 0.0049 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.7125 L22: 1.2354
REMARK 3 L33: 1.4819 L12: -0.3764
REMARK 3 L13: -0.1070 L23: 0.6518
REMARK 3 S TENSOR
REMARK 3 S11: -0.0478 S12: 0.0097 S13: -0.0033
REMARK 3 S21: -0.1047 S22: 0.0681 S23: -0.0488
REMARK 3 S31: 0.0572 S32: -0.0328 S33: -0.0142
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 406 THROUGH 562 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7381 -40.6069 23.9638
REMARK 3 T TENSOR
REMARK 3 T11: 0.1431 T22: 0.2523
REMARK 3 T33: 0.2202 T12: 0.0236
REMARK 3 T13: -0.0102 T23: -0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 1.7132 L22: 1.2084
REMARK 3 L33: 2.7930 L12: 0.5851
REMARK 3 L13: 0.5092 L23: 0.0209
REMARK 3 S TENSOR
REMARK 3 S11: 0.0118 S12: -0.3803 S13: 0.0580
REMARK 3 S21: 0.0893 S22: -0.0439 S23: 0.0896
REMARK 3 S31: -0.0223 S32: -0.3858 S33: 0.0129
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 405 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9489 -50.7931 -11.2099
REMARK 3 T TENSOR
REMARK 3 T11: 0.2024 T22: 0.5008
REMARK 3 T33: 0.2295 T12: 0.0685
REMARK 3 T13: -0.0651 T23: 0.0939
REMARK 3 L TENSOR
REMARK 3 L11: 1.8472 L22: 1.8909
REMARK 3 L33: 3.0365 L12: 1.2051
REMARK 3 L13: -1.4603 L23: -1.5716
REMARK 3 S TENSOR
REMARK 3 S11: -0.1214 S12: 0.5224 S13: 0.2241
REMARK 3 S21: -0.1436 S22: 0.4984 S23: 0.2588
REMARK 3 S31: 0.0623 S32: -0.6936 S33: -0.1608
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 406 THROUGH 562 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1031 -37.1641 -33.9869
REMARK 3 T TENSOR
REMARK 3 T11: 0.3556 T22: 0.6006
REMARK 3 T33: 0.3207 T12: 0.0186
REMARK 3 T13: 0.0299 T23: 0.1120
REMARK 3 L TENSOR
REMARK 3 L11: 1.3254 L22: 2.8937
REMARK 3 L33: 4.9075 L12: -0.0428
REMARK 3 L13: 0.3060 L23: 0.9392
REMARK 3 S TENSOR
REMARK 3 S11: 0.1133 S12: 0.5879 S13: 0.1909
REMARK 3 S21: -0.4496 S22: 0.1020 S23: -0.0416
REMARK 3 S31: -0.4510 S32: -0.2351 S33: -0.1408
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5EPC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215225.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5-8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00001
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CMOS
REMARK 200 DETECTOR MANUFACTURER : RDI CMOS_8M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 150855
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 61.051
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 32.50
REMARK 200 R MERGE (I) : 0.16300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 27.70
REMARK 200 R MERGE FOR SHELL (I) : 3.51000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3PMG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM OR AMMONIUM SULFATE (1.35 -
REMARK 280 1.85 M) WITH 0.1 M TRIS, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 49.89000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 86.29500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 86.29500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 24.94500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 86.29500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 86.29500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 74.83500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 86.29500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 86.29500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 24.94500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 86.29500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 86.29500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 74.83500
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 49.89000
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 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: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1218 LIES ON A SPECIAL POSITION.
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 -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 SER A -15
REMARK 465 SER A -14
REMARK 465 GLY A -13
REMARK 465 VAL A -12
REMARK 465 ASP A -11
REMARK 465 LEU A -10
REMARK 465 GLY A -9
REMARK 465 THR A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 THR A 507
REMARK 465 GLY A 508
REMARK 465 SER A 509
REMARK 465 MET B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 SER B -15
REMARK 465 SER B -14
REMARK 465 GLY B -13
REMARK 465 VAL B -12
REMARK 465 ASP B -11
REMARK 465 LEU B -10
REMARK 465 GLY B -9
REMARK 465 THR B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 SER B -1
REMARK 465 GLY B 506
REMARK 465 THR B 507
REMARK 465 GLY B 508
REMARK 465 SER B 509
REMARK 465 ALA B 510
REMARK 465 GLY B 511
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 A -1 OG
REMARK 470 LYS A 3 CG CD CE NZ
REMARK 470 GLN A 149 CG CD OE1 NE2
REMARK 470 LYS A 182 CG CD CE NZ
REMARK 470 PRO A 215 CG CD
REMARK 470 GLU A 274 CG CD OE1 OE2
REMARK 470 GLU A 280 CG CD OE1 OE2
REMARK 470 GLN A 325 CG CD OE1 NE2
REMARK 470 GLU A 434 CG CD OE1 OE2
REMARK 470 GLU A 436 CG CD OE1 OE2
REMARK 470 LYS A 443 CG CD CE NZ
REMARK 470 ARG A 452 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 457 CG CD CE NZ
REMARK 470 ASP A 463 CG OD1 OD2
REMARK 470 ASN B 0 CG OD1 ND2
REMARK 470 MET B 1 CG SD CE
REMARK 470 LYS B 3 CG CD CE NZ
REMARK 470 LYS B 8 CG CD CE NZ
REMARK 470 GLN B 10 CG CD OE1 NE2
REMARK 470 LYS B 16 CG CD CE NZ
REMARK 470 ARG B 23 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 25 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 27 CG CD CE NZ
REMARK 470 GLU B 48 CG CD OE1 OE2
REMARK 470 GLU B 54 CG CD OE1 OE2
REMARK 470 LYS B 146 CG CD CE NZ
REMARK 470 GLU B 155 CG CD OE1 OE2
REMARK 470 LYS B 164 CG CD CE NZ
REMARK 470 ASN B 179 CG OD1 ND2
REMARK 470 LYS B 180 CG CD CE NZ
REMARK 470 LYS B 182 CG CD CE NZ
REMARK 470 PRO B 215 CG CD
REMARK 470 ASN B 216 CG OD1 ND2
REMARK 470 LYS B 219 CG CD CE NZ
REMARK 470 GLU B 274 CG CD OE1 OE2
REMARK 470 GLU B 280 CG CD OE1 OE2
REMARK 470 GLU B 432 CG CD OE1 OE2
REMARK 470 GLU B 434 CG CD OE1 OE2
REMARK 470 GLU B 436 CG CD OE1 OE2
REMARK 470 LYS B 440 CG CD CE NZ
REMARK 470 LYS B 443 CG CD CE NZ
REMARK 470 ARG B 452 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 457 CG CD CE NZ
REMARK 470 ASP B 463 CG OD1 OD2
REMARK 470 LYS B 464 CG CD CE NZ
REMARK 470 VAL B 465 CG1 CG2
REMARK 470 LYS B 523 CG CD CE NZ
REMARK 470 LYS B 527 CG CD CE NZ
REMARK 470 GLN B 533 CG CD OE1 NE2
REMARK 470 LYS B 545 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 O HOH A 1028 O HOH B 918 1.81
REMARK 500 O HOH B 947 O HOH B 954 1.87
REMARK 500 O HOH B 853 O HOH B 952 1.89
REMARK 500 O HOH A 863 O HOH A 893 1.90
REMARK 500 O HOH B 741 O HOH B 945 1.94
REMARK 500 O HOH A 856 O HOH A 1115 1.95
REMARK 500 O HOH B 939 O HOH B 943 1.95
REMARK 500 O HOH A 1019 O HOH A 1177 1.98
REMARK 500 OE1 GLN A 324 O HOH A 701 2.01
REMARK 500 O HOH B 762 O HOH B 766 2.02
REMARK 500 O HOH B 949 O HOH B 972 2.06
REMARK 500 O3 GOL A 607 O HOH A 702 2.06
REMARK 500 O HOH B 830 O HOH B 894 2.09
REMARK 500 O HOH A 1056 O HOH A 1212 2.12
REMARK 500 O TYR B 268 O HOH B 701 2.14
REMARK 500 O HOH B 842 O HOH B 936 2.14
REMARK 500 O HOH A 802 O HOH A 1039 2.15
REMARK 500 OG1 THR B 495 O HOH B 702 2.15
REMARK 500 O ALA A 461 O HOH A 703 2.15
REMARK 500 O HOH B 846 O HOH B 887 2.15
REMARK 500 O HOH B 855 O HOH B 948 2.16
REMARK 500 OE2 GLU B 376 O HOH B 703 2.16
REMARK 500 O HOH A 1195 O HOH A 1237 2.17
REMARK 500 O HOH A 1150 O HOH A 1187 2.17
REMARK 500 NZ LYS B 370 O HOH B 704 2.17
REMARK 500 OD1 ASP A 176 O HOH A 704 2.17
REMARK 500 O GLY A 511 O HOH A 705 2.18
REMARK 500 O HOH A 763 O HOH A 1172 2.18
REMARK 500 OE1 GLU B 475 O HOH B 705 2.18
REMARK 500 O HOH A 1201 O HOH A 1204 2.19
REMARK 500 O HOH A 948 O HOH A 1099 2.19
REMARK 500 O HOH B 886 O HOH B 940 2.19
REMARK 500 O HOH A 978 O HOH B 934 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 O HOH A 866 O HOH A 1016 8555 2.05
REMARK 500 O HOH B 732 O HOH B 759 3445 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 ASN A 34 19.45 59.53
REMARK 500 TYR A 66 -6.60 85.35
REMARK 500 ASN A 91 15.62 59.80
REMARK 500 SER A 117 -113.22 57.88
REMARK 500 ILE A 133 -164.26 -108.92
REMARK 500 ALA A 269 41.20 -104.11
REMARK 500 SER A 378 47.59 -82.82
REMARK 500 ASN A 462 -169.72 -109.66
REMARK 500 ASP A 463 -56.02 70.36
REMARK 500 MET B 1 49.54 -103.70
REMARK 500 TYR B 66 -10.43 84.02
REMARK 500 SER B 117 -110.02 60.72
REMARK 500 ILE B 133 -167.73 -106.29
REMARK 500 ILE B 236 -62.00 -91.21
REMARK 500 SER B 378 49.23 -82.68
REMARK 500 ASN B 462 -124.16 60.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1241 DISTANCE = 6.17 ANGSTROMS
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 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 117 OG
REMARK 620 2 ASP A 288 OD2 89.7
REMARK 620 3 ASP A 290 OD1 89.9 98.4
REMARK 620 4 ASP A 292 OD1 165.5 97.5 101.4
REMARK 620 5 HOH A 771 O 80.6 167.7 89.2 90.5
REMARK 620 6 HOH A 878 O 79.2 94.6 163.1 87.6 76.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 117 OG
REMARK 620 2 ASP B 288 OD2 93.5
REMARK 620 3 ASP B 290 OD1 93.6 88.1
REMARK 620 4 ASP B 292 OD1 167.3 92.6 97.7
REMARK 620 5 HOH B 851 O 82.5 93.9 175.7 86.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 608
DBREF 5EPC A 1 562 UNP P36871 PGM1_HUMAN 1 562
DBREF 5EPC B 1 562 UNP P36871 PGM1_HUMAN 1 562
SEQADV 5EPC MET A -22 UNP P36871 INITIATING METHIONINE
SEQADV 5EPC HIS A -21 UNP P36871 EXPRESSION TAG
SEQADV 5EPC HIS A -20 UNP P36871 EXPRESSION TAG
SEQADV 5EPC HIS A -19 UNP P36871 EXPRESSION TAG
SEQADV 5EPC HIS A -18 UNP P36871 EXPRESSION TAG
SEQADV 5EPC HIS A -17 UNP P36871 EXPRESSION TAG
SEQADV 5EPC HIS A -16 UNP P36871 EXPRESSION TAG
SEQADV 5EPC SER A -15 UNP P36871 EXPRESSION TAG
SEQADV 5EPC SER A -14 UNP P36871 EXPRESSION TAG
SEQADV 5EPC GLY A -13 UNP P36871 EXPRESSION TAG
SEQADV 5EPC VAL A -12 UNP P36871 EXPRESSION TAG
SEQADV 5EPC ASP A -11 UNP P36871 EXPRESSION TAG
SEQADV 5EPC LEU A -10 UNP P36871 EXPRESSION TAG
SEQADV 5EPC GLY A -9 UNP P36871 EXPRESSION TAG
SEQADV 5EPC THR A -8 UNP P36871 EXPRESSION TAG
SEQADV 5EPC GLU A -7 UNP P36871 EXPRESSION TAG
SEQADV 5EPC ASN A -6 UNP P36871 EXPRESSION TAG
SEQADV 5EPC LEU A -5 UNP P36871 EXPRESSION TAG
SEQADV 5EPC TYR A -4 UNP P36871 EXPRESSION TAG
SEQADV 5EPC PHE A -3 UNP P36871 EXPRESSION TAG
SEQADV 5EPC GLN A -2 UNP P36871 EXPRESSION TAG
SEQADV 5EPC SER A -1 UNP P36871 EXPRESSION TAG
SEQADV 5EPC ASN A 0 UNP P36871 EXPRESSION TAG
SEQADV 5EPC MET B -22 UNP P36871 INITIATING METHIONINE
SEQADV 5EPC HIS B -21 UNP P36871 EXPRESSION TAG
SEQADV 5EPC HIS B -20 UNP P36871 EXPRESSION TAG
SEQADV 5EPC HIS B -19 UNP P36871 EXPRESSION TAG
SEQADV 5EPC HIS B -18 UNP P36871 EXPRESSION TAG
SEQADV 5EPC HIS B -17 UNP P36871 EXPRESSION TAG
SEQADV 5EPC HIS B -16 UNP P36871 EXPRESSION TAG
SEQADV 5EPC SER B -15 UNP P36871 EXPRESSION TAG
SEQADV 5EPC SER B -14 UNP P36871 EXPRESSION TAG
SEQADV 5EPC GLY B -13 UNP P36871 EXPRESSION TAG
SEQADV 5EPC VAL B -12 UNP P36871 EXPRESSION TAG
SEQADV 5EPC ASP B -11 UNP P36871 EXPRESSION TAG
SEQADV 5EPC LEU B -10 UNP P36871 EXPRESSION TAG
SEQADV 5EPC GLY B -9 UNP P36871 EXPRESSION TAG
SEQADV 5EPC THR B -8 UNP P36871 EXPRESSION TAG
SEQADV 5EPC GLU B -7 UNP P36871 EXPRESSION TAG
SEQADV 5EPC ASN B -6 UNP P36871 EXPRESSION TAG
SEQADV 5EPC LEU B -5 UNP P36871 EXPRESSION TAG
SEQADV 5EPC TYR B -4 UNP P36871 EXPRESSION TAG
SEQADV 5EPC PHE B -3 UNP P36871 EXPRESSION TAG
SEQADV 5EPC GLN B -2 UNP P36871 EXPRESSION TAG
SEQADV 5EPC SER B -1 UNP P36871 EXPRESSION TAG
SEQADV 5EPC ASN B 0 UNP P36871 EXPRESSION TAG
SEQRES 1 A 585 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 585 GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET VAL LYS
SEQRES 3 A 585 ILE VAL THR VAL LYS THR GLN ALA TYR GLN ASP GLN LYS
SEQRES 4 A 585 PRO GLY THR SER GLY LEU ARG LYS ARG VAL LYS VAL PHE
SEQRES 5 A 585 GLN SER SER ALA ASN TYR ALA GLU ASN PHE ILE GLN SER
SEQRES 6 A 585 ILE ILE SER THR VAL GLU PRO ALA GLN ARG GLN GLU ALA
SEQRES 7 A 585 THR LEU VAL VAL GLY GLY ASP GLY ARG PHE TYR MET LYS
SEQRES 8 A 585 GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA ALA ALA ASN
SEQRES 9 A 585 GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN GLY ILE LEU
SEQRES 10 A 585 SER THR PRO ALA VAL SER CYS ILE ILE ARG LYS ILE LYS
SEQRES 11 A 585 ALA ILE GLY GLY ILE ILE LEU THR ALA SER HIS ASN PRO
SEQRES 12 A 585 GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS PHE ASN ILE
SEQRES 13 A 585 SER ASN GLY GLY PRO ALA PRO GLU ALA ILE THR ASP LYS
SEQRES 14 A 585 ILE PHE GLN ILE SER LYS THR ILE GLU GLU TYR ALA VAL
SEQRES 15 A 585 CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL LEU GLY LYS
SEQRES 16 A 585 GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS PRO PHE THR
SEQRES 17 A 585 VAL GLU ILE VAL ASP SER VAL GLU ALA TYR ALA THR MET
SEQRES 18 A 585 LEU ARG SER ILE PHE ASP PHE SER ALA LEU LYS GLU LEU
SEQRES 19 A 585 LEU SER GLY PRO ASN ARG LEU LYS ILE ARG ILE ASP ALA
SEQRES 20 A 585 MET HIS GLY VAL VAL GLY PRO TYR VAL LYS LYS ILE LEU
SEQRES 21 A 585 CYS GLU GLU LEU GLY ALA PRO ALA ASN SER ALA VAL ASN
SEQRES 22 A 585 CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS HIS PRO ASP
SEQRES 23 A 585 PRO ASN LEU THR TYR ALA ALA ASP LEU VAL GLU THR MET
SEQRES 24 A 585 LYS SER GLY GLU HIS ASP PHE GLY ALA ALA PHE ASP GLY
SEQRES 25 A 585 ASP GLY ASP ARG ASN MET ILE LEU GLY LYS HIS GLY PHE
SEQRES 26 A 585 PHE VAL ASN PRO SER ASP SER VAL ALA VAL ILE ALA ALA
SEQRES 27 A 585 ASN ILE PHE SER ILE PRO TYR PHE GLN GLN THR GLY VAL
SEQRES 28 A 585 ARG GLY PHE ALA ARG SER MET PRO THR SER GLY ALA LEU
SEQRES 29 A 585 ASP ARG VAL ALA SER ALA THR LYS ILE ALA LEU TYR GLU
SEQRES 30 A 585 THR PRO THR GLY TRP LYS PHE PHE GLY ASN LEU MET ASP
SEQRES 31 A 585 ALA SER LYS LEU SER LEU CYS GLY GLU GLU SER PHE GLY
SEQRES 32 A 585 THR GLY SER ASP HIS ILE ARG GLU LYS ASP GLY LEU TRP
SEQRES 33 A 585 ALA VAL LEU ALA TRP LEU SER ILE LEU ALA THR ARG LYS
SEQRES 34 A 585 GLN SER VAL GLU ASP ILE LEU LYS ASP HIS TRP GLN LYS
SEQRES 35 A 585 TYR GLY ARG ASN PHE PHE THR ARG TYR ASP TYR GLU GLU
SEQRES 36 A 585 VAL GLU ALA GLU GLY ALA ASN LYS MET MET LYS ASP LEU
SEQRES 37 A 585 GLU ALA LEU MET PHE ASP ARG SER PHE VAL GLY LYS GLN
SEQRES 38 A 585 PHE SER ALA ASN ASP LYS VAL TYR THR VAL GLU LYS ALA
SEQRES 39 A 585 ASP ASN PHE GLU TYR SER ASP PRO VAL ASP GLY SER ILE
SEQRES 40 A 585 SER ARG ASN GLN GLY LEU ARG LEU ILE PHE THR ASP GLY
SEQRES 41 A 585 SER ARG ILE VAL PHE ARG LEU SER GLY THR GLY SER ALA
SEQRES 42 A 585 GLY ALA THR ILE ARG LEU TYR ILE ASP SER TYR GLU LYS
SEQRES 43 A 585 ASP VAL ALA LYS ILE ASN GLN ASP PRO GLN VAL MET LEU
SEQRES 44 A 585 ALA PRO LEU ILE SER ILE ALA LEU LYS VAL SER GLN LEU
SEQRES 45 A 585 GLN GLU ARG THR GLY ARG THR ALA PRO THR VAL ILE THR
SEQRES 1 B 585 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 585 GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET VAL LYS
SEQRES 3 B 585 ILE VAL THR VAL LYS THR GLN ALA TYR GLN ASP GLN LYS
SEQRES 4 B 585 PRO GLY THR SER GLY LEU ARG LYS ARG VAL LYS VAL PHE
SEQRES 5 B 585 GLN SER SER ALA ASN TYR ALA GLU ASN PHE ILE GLN SER
SEQRES 6 B 585 ILE ILE SER THR VAL GLU PRO ALA GLN ARG GLN GLU ALA
SEQRES 7 B 585 THR LEU VAL VAL GLY GLY ASP GLY ARG PHE TYR MET LYS
SEQRES 8 B 585 GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA ALA ALA ASN
SEQRES 9 B 585 GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN GLY ILE LEU
SEQRES 10 B 585 SER THR PRO ALA VAL SER CYS ILE ILE ARG LYS ILE LYS
SEQRES 11 B 585 ALA ILE GLY GLY ILE ILE LEU THR ALA SER HIS ASN PRO
SEQRES 12 B 585 GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS PHE ASN ILE
SEQRES 13 B 585 SER ASN GLY GLY PRO ALA PRO GLU ALA ILE THR ASP LYS
SEQRES 14 B 585 ILE PHE GLN ILE SER LYS THR ILE GLU GLU TYR ALA VAL
SEQRES 15 B 585 CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL LEU GLY LYS
SEQRES 16 B 585 GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS PRO PHE THR
SEQRES 17 B 585 VAL GLU ILE VAL ASP SER VAL GLU ALA TYR ALA THR MET
SEQRES 18 B 585 LEU ARG SER ILE PHE ASP PHE SER ALA LEU LYS GLU LEU
SEQRES 19 B 585 LEU SER GLY PRO ASN ARG LEU LYS ILE ARG ILE ASP ALA
SEQRES 20 B 585 MET HIS GLY VAL VAL GLY PRO TYR VAL LYS LYS ILE LEU
SEQRES 21 B 585 CYS GLU GLU LEU GLY ALA PRO ALA ASN SER ALA VAL ASN
SEQRES 22 B 585 CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS HIS PRO ASP
SEQRES 23 B 585 PRO ASN LEU THR TYR ALA ALA ASP LEU VAL GLU THR MET
SEQRES 24 B 585 LYS SER GLY GLU HIS ASP PHE GLY ALA ALA PHE ASP GLY
SEQRES 25 B 585 ASP GLY ASP ARG ASN MET ILE LEU GLY LYS HIS GLY PHE
SEQRES 26 B 585 PHE VAL ASN PRO SER ASP SER VAL ALA VAL ILE ALA ALA
SEQRES 27 B 585 ASN ILE PHE SER ILE PRO TYR PHE GLN GLN THR GLY VAL
SEQRES 28 B 585 ARG GLY PHE ALA ARG SER MET PRO THR SER GLY ALA LEU
SEQRES 29 B 585 ASP ARG VAL ALA SER ALA THR LYS ILE ALA LEU TYR GLU
SEQRES 30 B 585 THR PRO THR GLY TRP LYS PHE PHE GLY ASN LEU MET ASP
SEQRES 31 B 585 ALA SER LYS LEU SER LEU CYS GLY GLU GLU SER PHE GLY
SEQRES 32 B 585 THR GLY SER ASP HIS ILE ARG GLU LYS ASP GLY LEU TRP
SEQRES 33 B 585 ALA VAL LEU ALA TRP LEU SER ILE LEU ALA THR ARG LYS
SEQRES 34 B 585 GLN SER VAL GLU ASP ILE LEU LYS ASP HIS TRP GLN LYS
SEQRES 35 B 585 TYR GLY ARG ASN PHE PHE THR ARG TYR ASP TYR GLU GLU
SEQRES 36 B 585 VAL GLU ALA GLU GLY ALA ASN LYS MET MET LYS ASP LEU
SEQRES 37 B 585 GLU ALA LEU MET PHE ASP ARG SER PHE VAL GLY LYS GLN
SEQRES 38 B 585 PHE SER ALA ASN ASP LYS VAL TYR THR VAL GLU LYS ALA
SEQRES 39 B 585 ASP ASN PHE GLU TYR SER ASP PRO VAL ASP GLY SER ILE
SEQRES 40 B 585 SER ARG ASN GLN GLY LEU ARG LEU ILE PHE THR ASP GLY
SEQRES 41 B 585 SER ARG ILE VAL PHE ARG LEU SER GLY THR GLY SER ALA
SEQRES 42 B 585 GLY ALA THR ILE ARG LEU TYR ILE ASP SER TYR GLU LYS
SEQRES 43 B 585 ASP VAL ALA LYS ILE ASN GLN ASP PRO GLN VAL MET LEU
SEQRES 44 B 585 ALA PRO LEU ILE SER ILE ALA LEU LYS VAL SER GLN LEU
SEQRES 45 B 585 GLN GLU ARG THR GLY ARG THR ALA PRO THR VAL ILE THR
HET MG A 601 1
HET SO4 A 602 5
HET SO4 A 603 5
HET SO4 A 604 5
HET SO4 A 605 5
HET SO4 A 606 5
HET GOL A 607 6
HET GOL A 608 6
HET GOL A 609 6
HET GOL A 610 6
HET GOL A 611 6
HET MG B 601 1
HET SO4 B 602 5
HET SO4 B 603 5
HET SO4 B 604 5
HET GOL B 605 6
HET GOL B 606 6
HET GOL B 607 6
HET GOL B 608 6
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MG 2(MG 2+)
FORMUL 4 SO4 8(O4 S 2-)
FORMUL 9 GOL 9(C3 H8 O3)
FORMUL 22 HOH *819(H2 O)
HELIX 1 AA1 VAL A 26 SER A 32 1 7
HELIX 2 AA2 ASN A 34 SER A 45 1 12
HELIX 3 AA3 THR A 46 VAL A 47 5 2
HELIX 4 AA4 GLU A 48 ARG A 52 5 5
HELIX 5 AA5 TYR A 66 ASN A 81 1 16
HELIX 6 AA6 SER A 95 LYS A 107 1 13
HELIX 7 AA7 PRO A 140 ILE A 154 1 15
HELIX 8 AA8 VAL A 192 PHE A 203 1 12
HELIX 9 AA9 ASP A 204 SER A 213 1 10
HELIX 10 AB1 VAL A 229 LEU A 237 1 9
HELIX 11 AB2 PRO A 244 ASN A 246 5 3
HELIX 12 AB3 ASP A 256 HIS A 260 5 5
HELIX 13 AB4 ALA A 269 SER A 278 1 10
HELIX 14 AB5 ASN A 305 ASN A 316 1 12
HELIX 15 AB6 ILE A 317 SER A 319 5 3
HELIX 16 AB7 ILE A 320 GLY A 327 1 8
HELIX 17 AB8 GLY A 339 LYS A 349 1 11
HELIX 18 AB9 GLY A 358 ALA A 368 1 11
HELIX 19 AC1 ASP A 390 LYS A 406 1 17
HELIX 20 AC2 SER A 408 GLY A 421 1 14
HELIX 21 AC3 GLU A 434 ASP A 451 1 18
HELIX 22 AC4 ASP A 524 ASN A 529 1 6
HELIX 23 AC5 ASP A 531 GLN A 548 1 18
HELIX 24 AC6 GLN A 548 GLY A 554 1 7
HELIX 25 AC7 VAL B 26 SER B 32 1 7
HELIX 26 AC8 ASN B 34 SER B 45 1 12
HELIX 27 AC9 THR B 46 VAL B 47 5 2
HELIX 28 AD1 GLU B 48 ARG B 52 5 5
HELIX 29 AD2 TYR B 66 ASN B 81 1 16
HELIX 30 AD3 SER B 95 LYS B 107 1 13
HELIX 31 AD4 PRO B 140 THR B 153 1 14
HELIX 32 AD5 VAL B 192 PHE B 203 1 12
HELIX 33 AD6 ASP B 204 SER B 213 1 10
HELIX 34 AD7 VAL B 229 LEU B 237 1 9
HELIX 35 AD8 PRO B 244 ASN B 246 5 3
HELIX 36 AD9 ASP B 256 HIS B 260 5 5
HELIX 37 AE1 ALA B 269 SER B 278 1 10
HELIX 38 AE2 ASN B 305 ASN B 316 1 12
HELIX 39 AE3 ILE B 317 SER B 319 5 3
HELIX 40 AE4 ILE B 320 GLY B 327 1 8
HELIX 41 AE5 GLY B 339 ALA B 347 1 9
HELIX 42 AE6 GLY B 358 ALA B 368 1 11
HELIX 43 AE7 ASP B 390 LYS B 406 1 17
HELIX 44 AE8 SER B 408 GLY B 421 1 14
HELIX 45 AE9 GLU B 434 ASP B 451 1 18
HELIX 46 AF1 ASP B 524 ASN B 529 1 6
HELIX 47 AF2 ASP B 531 GLN B 548 1 18
HELIX 48 AF3 GLN B 548 GLY B 554 1 7
SHEET 1 AA1 8 MET A 1 VAL A 2 0
SHEET 2 AA1 8 GLY A 171 LEU A 177 1 O ASP A 176 N VAL A 2
SHEET 3 AA1 8 PHE A 184 VAL A 189 -1 O VAL A 186 N GLN A 173
SHEET 4 AA1 8 ARG A 85 ILE A 93 1 N ILE A 88 O GLU A 187
SHEET 5 AA1 8 THR A 56 GLY A 61 1 N VAL A 59 O VAL A 87
SHEET 6 AA1 8 GLY A 110 LEU A 114 1 O GLY A 110 N VAL A 58
SHEET 7 AA1 8 ASP A 126 ILE A 133 -1 O ASN A 132 N GLY A 111
SHEET 8 AA1 8 LEU A 22 ARG A 25 -1 N LYS A 24 O PHE A 127
SHEET 1 AA2 2 VAL A 5 LYS A 8 0
SHEET 2 AA2 2 GLU A 156 VAL A 159 -1 O TYR A 157 N VAL A 7
SHEET 1 AA3 5 ALA A 248 VAL A 249 0
SHEET 2 AA3 5 ILE A 220 ASP A 223 1 N ILE A 222 O VAL A 249
SHEET 3 AA3 5 PHE A 283 PHE A 287 1 O ALA A 285 N ASP A 223
SHEET 4 AA3 5 ASN A 294 GLY A 298 -1 O LEU A 297 N GLY A 284
SHEET 5 AA3 5 PHE A 303 VAL A 304 -1 O VAL A 304 N ILE A 296
SHEET 1 AA4 4 LEU A 352 THR A 355 0
SHEET 2 AA4 4 PHE A 331 SER A 334 1 N PHE A 331 O TYR A 353
SHEET 3 AA4 4 LEU A 373 GLU A 376 1 O LEU A 373 N ALA A 332
SHEET 4 AA4 4 GLY A 380 SER A 383 -1 O GLY A 382 N CYS A 374
SHEET 1 AA5 7 GLN A 458 SER A 460 0
SHEET 2 AA5 7 VAL A 465 ASN A 473 -1 O TYR A 466 N PHE A 459
SHEET 3 AA5 7 LEU A 490 PHE A 494 -1 O ILE A 493 N LYS A 470
SHEET 4 AA5 7 ARG A 499 LEU A 504 -1 O ILE A 500 N LEU A 492
SHEET 5 AA5 7 ALA A 512 GLU A 522 -1 O ARG A 515 N ARG A 503
SHEET 6 AA5 7 ARG A 422 VAL A 433 -1 N ARG A 422 O GLU A 522
SHEET 7 AA5 7 VAL A 560 THR A 562 -1 O VAL A 560 N ASP A 429
SHEET 1 AA6 2 TYR A 476 SER A 477 0
SHEET 2 AA6 2 ILE A 484 SER A 485 -1 O SER A 485 N TYR A 476
SHEET 1 AA7 2 VAL B 5 LYS B 8 0
SHEET 2 AA7 2 GLU B 156 VAL B 159 -1 O TYR B 157 N VAL B 7
SHEET 1 AA8 7 LEU B 22 ARG B 25 0
SHEET 2 AA8 7 ASP B 126 ILE B 133 -1 O PHE B 127 N LYS B 24
SHEET 3 AA8 7 GLY B 110 LEU B 114 -1 N ILE B 113 O LYS B 130
SHEET 4 AA8 7 THR B 56 GLY B 61 1 N VAL B 58 O ILE B 112
SHEET 5 AA8 7 ARG B 85 ILE B 93 1 O VAL B 87 N VAL B 59
SHEET 6 AA8 7 PHE B 184 VAL B 189 1 O GLU B 187 N LEU B 86
SHEET 7 AA8 7 GLY B 171 PHE B 175 -1 N PHE B 175 O PHE B 184
SHEET 1 AA9 5 ALA B 248 VAL B 249 0
SHEET 2 AA9 5 ILE B 220 ASP B 223 1 N ILE B 222 O VAL B 249
SHEET 3 AA9 5 PHE B 283 PHE B 287 1 O ALA B 285 N ASP B 223
SHEET 4 AA9 5 ASN B 294 GLY B 298 -1 O LEU B 297 N GLY B 284
SHEET 5 AA9 5 PHE B 303 VAL B 304 -1 O VAL B 304 N ILE B 296
SHEET 1 AB1 4 LEU B 352 THR B 355 0
SHEET 2 AB1 4 PHE B 331 SER B 334 1 N PHE B 331 O TYR B 353
SHEET 3 AB1 4 LEU B 373 GLU B 376 1 O LEU B 373 N ALA B 332
SHEET 4 AB1 4 GLY B 380 SER B 383 -1 O GLY B 380 N GLU B 376
SHEET 1 AB2 7 GLN B 458 ALA B 461 0
SHEET 2 AB2 7 LYS B 464 ASN B 473 -1 O TYR B 466 N PHE B 459
SHEET 3 AB2 7 LEU B 490 PHE B 494 -1 O ILE B 493 N GLU B 469
SHEET 4 AB2 7 ARG B 499 LEU B 504 -1 O ILE B 500 N LEU B 492
SHEET 5 AB2 7 ILE B 514 GLU B 522 -1 O TYR B 517 N VAL B 501
SHEET 6 AB2 7 ARG B 422 TYR B 430 -1 N TYR B 428 O LEU B 516
SHEET 7 AB2 7 VAL B 560 THR B 562 -1 O VAL B 560 N ASP B 429
SHEET 1 AB3 2 TYR B 476 SER B 477 0
SHEET 2 AB3 2 ILE B 484 SER B 485 -1 O SER B 485 N TYR B 476
LINK OG SER A 117 MG MG A 601 1555 1555 2.16
LINK OD2 ASP A 288 MG MG A 601 1555 1555 1.95
LINK OD1 ASP A 290 MG MG A 601 1555 1555 2.03
LINK OD1 ASP A 292 MG MG A 601 1555 1555 1.98
LINK OG SER B 117 MG MG B 601 1555 1555 2.26
LINK OD2 ASP B 288 MG MG B 601 1555 1555 1.94
LINK OD1 ASP B 290 MG MG B 601 1555 1555 2.12
LINK OD1 ASP B 292 MG MG B 601 1555 1555 2.02
LINK MG MG A 601 O HOH A 771 1555 1555 2.39
LINK MG MG A 601 O HOH A 878 1555 1555 2.18
LINK MG MG B 601 O HOH B 851 1555 1555 2.21
CISPEP 1 ALA A 461 ASN A 462 0 5.66
SITE 1 AC1 6 SER A 117 ASP A 288 ASP A 290 ASP A 292
SITE 2 AC1 6 HOH A 771 HOH A 878
SITE 1 AC2 5 ARG A 503 SER A 505 GLY A 506 ARG A 515
SITE 2 AC2 5 GOL A 611
SITE 1 AC3 6 ASN A 179 LYS A 470 ARG A 491 HOH A 819
SITE 2 AC3 6 HOH A 925 HOH A1020
SITE 1 AC4 7 SER A 20 ARG A 23 SER A 117 HIS A 118
SITE 2 AC4 7 ARG A 293 HOH A 724 HOH A 878
SITE 1 AC5 3 ARG A 85 ILE A 106 HOH A 706
SITE 1 AC6 7 ARG A 217 ARG A 221 PRO A 244 ASN A 246
SITE 2 AC6 7 HOH A 711 HOH A 734 HOH A 980
SITE 1 AC7 8 TYR A 66 MET A 67 LYS A 68 GLU A 69
SITE 2 AC7 8 GLU A 255 HOH A 702 HOH A 714 HOH A 972
SITE 1 AC8 7 PHE A 303 ASN A 305 ARG A 422 PHE A 424
SITE 2 AC8 7 PHE A 425 HOH A 762 HOH A 851
SITE 1 AC9 9 ASN A 135 PRO A 140 LYS A 360 GLY A 363
SITE 2 AC9 9 ASN A 364 ASP A 367 HOH A 767 HOH A 786
SITE 3 AC9 9 HOH A 836
SITE 1 AD1 6 TYR A 428 GLN A 533 THR A 556 PRO A 558
SITE 2 AD1 6 HOH A 782 HOH A 810
SITE 1 AD2 5 GLU A 377 ARG A 427 ARG A 515 TYR A 517
SITE 2 AD2 5 SO4 A 602
SITE 1 AD3 5 SER B 117 ASP B 288 ASP B 290 ASP B 292
SITE 2 AD3 5 HOH B 851
SITE 1 AD4 3 ARG B 503 SER B 505 ARG B 515
SITE 1 AD5 3 ARG B 85 ILE B 106 HOH B 862
SITE 1 AD6 5 SER B 20 SER B 117 HIS B 118 ARG B 293
SITE 2 AD6 5 HOH B 706
SITE 1 AD7 7 ARG B 64 PHE B 65 TYR B 66 MET B 67
SITE 2 AD7 7 LYS B 68 GLU B 69 GLU B 255
SITE 1 AD8 6 GLN B 90 ASN B 91 ASP B 190 SER B 191
SITE 2 AD8 6 PRO B 231 LYS B 235
SITE 1 AD9 6 PHE B 303 ASN B 305 ARG B 422 PHE B 424
SITE 2 AD9 6 PHE B 425 HOH B 787
SITE 1 AE1 3 ASP A 14 VAL A 28 TYR A 35
CRYST1 172.590 172.590 99.780 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 0.005794 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005794 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010022 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
