HEADER HYDROLASE 17-JAN-15 4XPN
TITLE CRYSTAL STRUCTURE OF PROTEIN PHOSPHATE 1 COMPLEXED WITH PP1 BINDING
TITLE 2 DOMAIN OF GADD34
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC
COMPND 3 SUBUNIT;
COMPND 4 CHAIN: A, C;
COMPND 5 FRAGMENT: UNP RESIDUES 7-300;
COMPND 6 SYNONYM: PP-1A;
COMPND 7 EC: 3.1.3.16;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 15A;
COMPND 11 CHAIN: B, D;
COMPND 12 FRAGMENT: UNP RESIDUES 552-591;
COMPND 13 SYNONYM: GROWTH ARREST AND DNA DAMAGE-INDUCIBLE PROTEIN GADD34,
COMPND 14 MYELOID DIFFERENTIATION PRIMARY RESPONSE PROTEIN MYD116 HOMOLOG;
COMPND 15 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: PPP1CA, PPP1A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: PPP1R15A, GADD34;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EIF2ALPHA PHOSPHATASE, PP1 REGULATOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.S.CHOY,W.PETI,R.PAGE
REVDAT 6 27-SEP-23 4XPN 1 LINK
REVDAT 5 25-DEC-19 4XPN 1 REMARK
REVDAT 4 27-SEP-17 4XPN 1 SOURCE REMARK
REVDAT 3 15-JUL-15 4XPN 1 JRNL
REVDAT 2 08-JUL-15 4XPN 1 JRNL
REVDAT 1 01-JUL-15 4XPN 0
JRNL AUTH M.S.CHOY,P.YUSOFF,I.C.LEE,J.C.NEWTON,C.W.GOH,R.PAGE,
JRNL AUTH 2 S.SHENOLIKAR,W.PETI
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF THE GADD34:PP1 EIF2
JRNL TITL 2 ALPHA PHOSPHATASE.
JRNL REF CELL REP V. 11 1885 2015
JRNL REFN ESSN 2211-1247
JRNL PMID 26095357
JRNL DOI 10.1016/J.CELREP.2015.05.043
REMARK 2
REMARK 2 RESOLUTION. 2.29 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) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 40789
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2053
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 31.4308 - 5.6253 0.99 2807 161 0.1473 0.1808
REMARK 3 2 5.6253 - 4.4691 1.00 2729 139 0.1247 0.1646
REMARK 3 3 4.4691 - 3.9053 0.99 2640 142 0.1259 0.1585
REMARK 3 4 3.9053 - 3.5488 0.99 2680 116 0.1559 0.2093
REMARK 3 5 3.5488 - 3.2947 0.99 2661 135 0.1666 0.2189
REMARK 3 6 3.2947 - 3.1007 1.00 2640 131 0.1834 0.2178
REMARK 3 7 3.1007 - 2.9455 1.00 2625 151 0.1795 0.2351
REMARK 3 8 2.9455 - 2.8174 1.00 2621 141 0.1843 0.2150
REMARK 3 9 2.8174 - 2.7090 1.00 2634 147 0.1922 0.2509
REMARK 3 10 2.7090 - 2.6155 1.00 2627 135 0.1999 0.2824
REMARK 3 11 2.6155 - 2.5338 0.99 2593 139 0.1873 0.2206
REMARK 3 12 2.5338 - 2.4614 0.98 2549 131 0.1912 0.2440
REMARK 3 13 2.4614 - 2.3966 0.94 2474 138 0.1915 0.2714
REMARK 3 14 2.3966 - 2.3382 0.92 2407 135 0.2036 0.2851
REMARK 3 15 2.3382 - 2.2850 0.79 2049 112 0.2222 0.3062
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.98
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 : 0.011 5078
REMARK 3 ANGLE : 1.007 6836
REMARK 3 CHIRALITY : 0.041 742
REMARK 3 PLANARITY : 0.004 885
REMARK 3 DIHEDRAL : 13.638 1852
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 4:299
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8893 16.4702 -12.8947
REMARK 3 T TENSOR
REMARK 3 T11: 0.4587 T22: 0.3044
REMARK 3 T33: 0.2823 T12: -0.0477
REMARK 3 T13: -0.0077 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.4661 L22: 3.5629
REMARK 3 L33: 1.6354 L12: -0.6166
REMARK 3 L13: 0.3746 L23: 0.3501
REMARK 3 S TENSOR
REMARK 3 S11: 0.0574 S12: 0.0616 S13: -0.0987
REMARK 3 S21: -0.1535 S22: -0.0157 S23: 0.1513
REMARK 3 S31: 0.2558 S32: -0.0319 S33: -0.0330
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B AND RESID 553:568
REMARK 3 ORIGIN FOR THE GROUP (A): -24.0116 5.4067 -28.4403
REMARK 3 T TENSOR
REMARK 3 T11: 0.9344 T22: 0.4630
REMARK 3 T33: 0.5012 T12: -0.0599
REMARK 3 T13: -0.1788 T23: -0.1124
REMARK 3 L TENSOR
REMARK 3 L11: 3.5342 L22: 5.4629
REMARK 3 L33: 1.5698 L12: 2.4605
REMARK 3 L13: -2.1436 L23: -2.4970
REMARK 3 S TENSOR
REMARK 3 S11: 0.0503 S12: 0.3786 S13: 0.1117
REMARK 3 S21: -1.5460 S22: 0.1291 S23: 0.2277
REMARK 3 S31: 0.4631 S32: -0.2510 S33: -0.0101
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C AND RESID 6:299
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6285 -9.7962 9.1649
REMARK 3 T TENSOR
REMARK 3 T11: 0.7210 T22: 0.3332
REMARK 3 T33: 0.4154 T12: 0.0553
REMARK 3 T13: 0.0799 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 1.4835 L22: 3.5368
REMARK 3 L33: 2.1505 L12: 0.5962
REMARK 3 L13: -0.5762 L23: -0.7932
REMARK 3 S TENSOR
REMARK 3 S11: -0.1750 S12: -0.0932 S13: -0.3206
REMARK 3 S21: -0.1842 S22: -0.0169 S23: -0.3904
REMARK 3 S31: 0.8072 S32: 0.0390 S33: 0.0790
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D AND RESID 554:568
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0729 -20.9753 23.0865
REMARK 3 T TENSOR
REMARK 3 T11: 1.2272 T22: 0.5514
REMARK 3 T33: 0.5801 T12: -0.0042
REMARK 3 T13: 0.1048 T23: 0.0888
REMARK 3 L TENSOR
REMARK 3 L11: 6.6323 L22: 7.4438
REMARK 3 L33: 1.4885 L12: -6.8502
REMARK 3 L13: -2.6557 L23: 2.3476
REMARK 3 S TENSOR
REMARK 3 S11: -0.5995 S12: -0.3669 S13: -1.1950
REMARK 3 S21: 0.9033 S22: 0.2387 S23: 1.1368
REMARK 3 S31: 0.6974 S32: 0.2962 S33: 0.3193
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 2734
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 128
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4XPN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000205419.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49300
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.96500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.3
REMARK 200 STARTING MODEL: 3E7A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM PHOSPHATE DIBASIC, 20%
REMARK 280 W/V POLYETHYLENE GLYCOL 3,350, PH 6.8, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277K
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 32.15550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.50650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.42650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.50650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.15550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.42650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 GLY A 2
REMARK 465 HIS A 3
REMARK 465 ASP A 300
REMARK 465 GLY B 549
REMARK 465 HIS B 550
REMARK 465 MET B 551
REMARK 465 LYS B 552
REMARK 465 VAL B 569
REMARK 465 TRP B 570
REMARK 465 ALA B 571
REMARK 465 GLY B 572
REMARK 465 PRO B 573
REMARK 465 ALA B 574
REMARK 465 GLN B 575
REMARK 465 ALA B 576
REMARK 465 ALA B 577
REMARK 465 ARG B 578
REMARK 465 GLN B 579
REMARK 465 GLY B 580
REMARK 465 PRO B 581
REMARK 465 TRP B 582
REMARK 465 GLU B 583
REMARK 465 GLN B 584
REMARK 465 LEU B 585
REMARK 465 ALA B 586
REMARK 465 ARG B 587
REMARK 465 ASP B 588
REMARK 465 ARG B 589
REMARK 465 SER B 590
REMARK 465 ARG B 591
REMARK 465 GLY C 2
REMARK 465 HIS C 3
REMARK 465 MET C 4
REMARK 465 GLY C 5
REMARK 465 ASP C 300
REMARK 465 GLY D 549
REMARK 465 HIS D 550
REMARK 465 MET D 551
REMARK 465 LYS D 552
REMARK 465 ALA D 553
REMARK 465 ALA D 568
REMARK 465 VAL D 569
REMARK 465 TRP D 570
REMARK 465 ALA D 571
REMARK 465 GLY D 572
REMARK 465 PRO D 573
REMARK 465 ALA D 574
REMARK 465 GLN D 575
REMARK 465 ALA D 576
REMARK 465 ALA D 577
REMARK 465 ARG D 578
REMARK 465 GLN D 579
REMARK 465 GLY D 580
REMARK 465 PRO D 581
REMARK 465 TRP D 582
REMARK 465 GLU D 583
REMARK 465 GLN D 584
REMARK 465 LEU D 585
REMARK 465 ALA D 586
REMARK 465 ARG D 587
REMARK 465 ASP D 588
REMARK 465 ARG D 589
REMARK 465 SER D 590
REMARK 465 ARG D 591
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 ARG A 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 26 NZ
REMARK 470 LYS A 98 CE NZ
REMARK 470 LYS A 211 CE NZ
REMARK 470 GLN A 214 CG CD OE1 NE2
REMARK 470 LYS A 260 CD CE NZ
REMARK 470 GLU A 275 CG CD OE1 OE2
REMARK 470 GLU A 287 CG CD OE1 OE2
REMARK 470 ARG C 23 CZ NH1 NH2
REMARK 470 LYS C 26 NZ
REMARK 470 LYS C 41 CD CE NZ
REMARK 470 LYS C 98 NZ
REMARK 470 LYS C 147 CE NZ
REMARK 470 LYS C 168 CD CE NZ
REMARK 470 ARG C 188 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 211 CG CD CE NZ
REMARK 470 GLN C 214 CG CD OE1 NE2
REMARK 470 GLU C 218 CG CD OE1 OE2
REMARK 470 ASP C 220 CG OD1 OD2
REMARK 470 GLU C 230 CG CD OE1 OE2
REMARK 470 LYS C 234 CG CD CE NZ
REMARK 470 LYS C 260 CD CE NZ
REMARK 470 GLU C 287 CG CD OE1 OE2
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 O2 PO4 A 403 O HOH A 624 1.71
REMARK 500 O1 PO4 C 403 O HOH C 588 1.85
REMARK 500 NH1 ARG A 36 O HOH A 501 2.10
REMARK 500 O HOH C 537 O HOH C 568 2.15
REMARK 500 ND2 ASN A 271 O PHE A 276 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 95 154.35 78.34
REMARK 500 ARG A 96 -43.79 72.03
REMARK 500 TYR A 144 -113.71 -140.33
REMARK 500 SER A 224 -147.83 61.21
REMARK 500 ALA A 247 -126.19 -137.50
REMARK 500 HIS A 248 -15.02 72.88
REMARK 500 ASP C 95 155.47 78.14
REMARK 500 ARG C 96 -44.77 72.51
REMARK 500 TYR C 144 -113.60 -139.05
REMARK 500 SER C 224 -147.67 60.07
REMARK 500 ALA C 247 -124.05 -139.24
REMARK 500 HIS C 248 -17.90 71.49
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 A 619 DISTANCE = 7.04 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 MN A 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD2
REMARK 620 2 HIS A 66 NE2 127.3
REMARK 620 3 ASP A 92 OD2 102.3 103.8
REMARK 620 4 PO4 A 403 O2 126.8 96.0 93.9
REMARK 620 5 HOH A 624 O 87.6 142.8 76.7 47.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 92 OD2
REMARK 620 2 ASN A 124 OD1 96.0
REMARK 620 3 HIS A 173 NE2 79.4 91.6
REMARK 620 4 HIS A 248 ND1 165.8 97.7 96.6
REMARK 620 5 PO4 A 403 O4 98.1 88.3 177.5 85.8
REMARK 620 6 HOH A 624 O 74.7 147.7 116.1 95.2 63.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 64 OD2
REMARK 620 2 HIS C 66 NE2 113.1
REMARK 620 3 ASP C 92 OD2 93.6 99.9
REMARK 620 4 HOH C 588 O 107.6 139.2 80.3
REMARK 620 5 HOH C 589 O 103.8 94.0 151.4 72.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 92 OD2
REMARK 620 2 ASN C 124 OD1 102.7
REMARK 620 3 HIS C 173 NE2 82.2 88.7
REMARK 620 4 HIS C 248 ND1 162.7 94.6 97.4
REMARK 620 5 PO4 C 403 O1 91.5 84.4 169.4 91.2
REMARK 620 6 HOH C 588 O 79.5 129.6 140.3 90.3 45.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 404
DBREF 4XPN A 7 300 UNP P62136 PP1A_HUMAN 7 300
DBREF 4XPN B 552 591 UNP O75807 PR15A_HUMAN 552 591
DBREF 4XPN C 7 300 UNP P62136 PP1A_HUMAN 7 300
DBREF 4XPN D 552 591 UNP O75807 PR15A_HUMAN 552 591
SEQADV 4XPN GLY A 2 UNP P62136 EXPRESSION TAG
SEQADV 4XPN HIS A 3 UNP P62136 EXPRESSION TAG
SEQADV 4XPN MET A 4 UNP P62136 EXPRESSION TAG
SEQADV 4XPN GLY A 5 UNP P62136 EXPRESSION TAG
SEQADV 4XPN SER A 6 UNP P62136 EXPRESSION TAG
SEQADV 4XPN GLY B 549 UNP O75807 EXPRESSION TAG
SEQADV 4XPN HIS B 550 UNP O75807 EXPRESSION TAG
SEQADV 4XPN MET B 551 UNP O75807 EXPRESSION TAG
SEQADV 4XPN GLY C 2 UNP P62136 EXPRESSION TAG
SEQADV 4XPN HIS C 3 UNP P62136 EXPRESSION TAG
SEQADV 4XPN MET C 4 UNP P62136 EXPRESSION TAG
SEQADV 4XPN GLY C 5 UNP P62136 EXPRESSION TAG
SEQADV 4XPN SER C 6 UNP P62136 EXPRESSION TAG
SEQADV 4XPN GLY D 549 UNP O75807 EXPRESSION TAG
SEQADV 4XPN HIS D 550 UNP O75807 EXPRESSION TAG
SEQADV 4XPN MET D 551 UNP O75807 EXPRESSION TAG
SEQRES 1 A 299 GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY
SEQRES 2 A 299 ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN
SEQRES 3 A 299 VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU
SEQRES 4 A 299 LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU
SEQRES 5 A 299 GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS
SEQRES 6 A 299 GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY
SEQRES 7 A 299 GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP
SEQRES 8 A 299 TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS
SEQRES 9 A 299 LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE
SEQRES 10 A 299 PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN
SEQRES 11 A 299 ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR
SEQRES 12 A 299 ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN
SEQRES 13 A 299 CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE
SEQRES 14 A 299 CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET
SEQRES 15 A 299 GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO
SEQRES 16 A 299 ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO
SEQRES 17 A 299 ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY
SEQRES 18 A 299 VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE
SEQRES 19 A 299 LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS
SEQRES 20 A 299 GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG
SEQRES 21 A 299 GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY
SEQRES 22 A 299 GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU
SEQRES 23 A 299 THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP
SEQRES 1 B 43 GLY HIS MET LYS ALA ARG LYS VAL ARG PHE SER GLU LYS
SEQRES 2 B 43 VAL THR VAL HIS PHE LEU ALA VAL TRP ALA GLY PRO ALA
SEQRES 3 B 43 GLN ALA ALA ARG GLN GLY PRO TRP GLU GLN LEU ALA ARG
SEQRES 4 B 43 ASP ARG SER ARG
SEQRES 1 C 299 GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY
SEQRES 2 C 299 ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN
SEQRES 3 C 299 VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU
SEQRES 4 C 299 LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU
SEQRES 5 C 299 GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS
SEQRES 6 C 299 GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY
SEQRES 7 C 299 GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP
SEQRES 8 C 299 TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS
SEQRES 9 C 299 LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE
SEQRES 10 C 299 PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN
SEQRES 11 C 299 ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR
SEQRES 12 C 299 ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN
SEQRES 13 C 299 CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE
SEQRES 14 C 299 CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET
SEQRES 15 C 299 GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO
SEQRES 16 C 299 ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO
SEQRES 17 C 299 ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY
SEQRES 18 C 299 VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE
SEQRES 19 C 299 LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS
SEQRES 20 C 299 GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG
SEQRES 21 C 299 GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY
SEQRES 22 C 299 GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU
SEQRES 23 C 299 THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP
SEQRES 1 D 43 GLY HIS MET LYS ALA ARG LYS VAL ARG PHE SER GLU LYS
SEQRES 2 D 43 VAL THR VAL HIS PHE LEU ALA VAL TRP ALA GLY PRO ALA
SEQRES 3 D 43 GLN ALA ALA ARG GLN GLY PRO TRP GLU GLN LEU ALA ARG
SEQRES 4 D 43 ASP ARG SER ARG
HET MN A 401 1
HET MN A 402 1
HET PO4 A 403 5
HET GOL A 404 6
HET MN C 401 1
HET MN C 402 1
HET PO4 C 403 5
HET GOL C 404 6
HETNAM MN MANGANESE (II) ION
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 MN 4(MN 2+)
FORMUL 7 PO4 2(O4 P 3-)
FORMUL 8 GOL 2(C3 H8 O3)
FORMUL 13 HOH *223(H2 O)
HELIX 1 AA1 ASN A 8 GLU A 18 1 11
HELIX 2 AA2 THR A 31 GLN A 49 1 19
HELIX 3 AA3 GLN A 68 GLY A 80 1 13
HELIX 4 AA4 GLN A 99 TYR A 114 1 16
HELIX 5 AA5 CYS A 127 ARG A 132 1 6
HELIX 6 AA6 GLY A 135 TYR A 144 1 10
HELIX 7 AA7 ASN A 145 ASN A 157 1 13
HELIX 8 AA8 MET A 183 ARG A 188 1 6
HELIX 9 AA9 GLY A 199 SER A 207 1 9
HELIX 10 AB1 GLY A 228 HIS A 239 1 12
HELIX 11 AB2 ASN A 271 GLU A 275 5 5
HELIX 12 AB3 ASN C 8 VAL C 19 1 12
HELIX 13 AB4 THR C 31 GLN C 49 1 19
HELIX 14 AB5 GLN C 68 GLY C 80 1 13
HELIX 15 AB6 GLN C 99 TYR C 114 1 16
HELIX 16 AB7 CYS C 127 ARG C 132 1 6
HELIX 17 AB8 GLY C 135 TYR C 144 1 10
HELIX 18 AB9 ASN C 145 ASN C 157 1 13
HELIX 19 AC1 MET C 183 ARG C 188 1 6
HELIX 20 AC2 GLY C 199 SER C 207 1 9
HELIX 21 AC3 GLY C 228 HIS C 239 1 12
HELIX 22 AC4 ASN C 271 GLU C 275 5 5
SHEET 1 AA1 6 LEU A 52 LEU A 55 0
SHEET 2 AA1 6 ALA A 162 VAL A 165 1 O ALA A 162 N LEU A 53
SHEET 3 AA1 6 ILE A 169 CYS A 172 -1 O CYS A 171 N ALA A 163
SHEET 4 AA1 6 LEU A 243 ARG A 246 1 O CYS A 245 N PHE A 170
SHEET 5 AA1 6 LEU A 263 LEU A 266 1 O VAL A 264 N ILE A 244
SHEET 6 AA1 6 TYR A 255 PHE A 258 -1 N PHE A 258 O LEU A 263
SHEET 1 AA2 6 PHE A 118 LEU A 120 0
SHEET 2 AA2 6 TYR A 87 PHE A 89 1 N PHE A 89 O PHE A 119
SHEET 3 AA2 6 LEU A 59 CYS A 62 1 N LYS A 60 O LEU A 88
SHEET 4 AA2 6 GLY A 280 VAL A 285 -1 O MET A 283 N ILE A 61
SHEET 5 AA2 6 MET A 290 LEU A 296 -1 O LEU A 296 N GLY A 280
SHEET 6 AA2 6 ARG B 557 PHE B 558 1 O ARG B 557 N CYS A 291
SHEET 1 AA3 6 PHE A 118 LEU A 120 0
SHEET 2 AA3 6 TYR A 87 PHE A 89 1 N PHE A 89 O PHE A 119
SHEET 3 AA3 6 LEU A 59 CYS A 62 1 N LYS A 60 O LEU A 88
SHEET 4 AA3 6 GLY A 280 VAL A 285 -1 O MET A 283 N ILE A 61
SHEET 5 AA3 6 MET A 290 LEU A 296 -1 O LEU A 296 N GLY A 280
SHEET 6 AA3 6 THR B 563 HIS B 565 1 O THR B 563 N ILE A 295
SHEET 1 AA4 3 ASP A 208 PRO A 209 0
SHEET 2 AA4 3 PHE A 225 PHE A 227 1 O PHE A 227 N ASP A 208
SHEET 3 AA4 3 TRP A 216 GLU A 218 -1 N GLY A 217 O THR A 226
SHEET 1 AA5 6 LEU C 52 LEU C 55 0
SHEET 2 AA5 6 ALA C 162 VAL C 165 1 O ALA C 162 N LEU C 53
SHEET 3 AA5 6 ILE C 169 CYS C 172 -1 O CYS C 171 N ALA C 163
SHEET 4 AA5 6 LEU C 243 ARG C 246 1 O CYS C 245 N PHE C 170
SHEET 5 AA5 6 LEU C 263 LEU C 266 1 O LEU C 266 N ARG C 246
SHEET 6 AA5 6 TYR C 255 PHE C 258 -1 N PHE C 258 O LEU C 263
SHEET 1 AA6 6 PHE C 118 LEU C 120 0
SHEET 2 AA6 6 TYR C 87 PHE C 89 1 N PHE C 89 O PHE C 119
SHEET 3 AA6 6 LEU C 59 CYS C 62 1 N LYS C 60 O LEU C 88
SHEET 4 AA6 6 GLY C 280 VAL C 285 -1 O MET C 283 N ILE C 61
SHEET 5 AA6 6 MET C 290 LEU C 296 -1 O LEU C 296 N GLY C 280
SHEET 6 AA6 6 ARG D 557 PHE D 558 1 O ARG D 557 N CYS C 291
SHEET 1 AA7 6 PHE C 118 LEU C 120 0
SHEET 2 AA7 6 TYR C 87 PHE C 89 1 N PHE C 89 O PHE C 119
SHEET 3 AA7 6 LEU C 59 CYS C 62 1 N LYS C 60 O LEU C 88
SHEET 4 AA7 6 GLY C 280 VAL C 285 -1 O MET C 283 N ILE C 61
SHEET 5 AA7 6 MET C 290 LEU C 296 -1 O LEU C 296 N GLY C 280
SHEET 6 AA7 6 THR D 563 HIS D 565 1 O THR D 563 N ILE C 295
SHEET 1 AA8 3 ASP C 208 PRO C 209 0
SHEET 2 AA8 3 PHE C 225 PHE C 227 1 O PHE C 227 N ASP C 208
SHEET 3 AA8 3 TRP C 216 GLU C 218 -1 N GLY C 217 O THR C 226
LINK OD2 ASP A 64 MN MN A 401 1555 1555 2.12
LINK NE2 HIS A 66 MN MN A 401 1555 1555 2.09
LINK OD2 ASP A 92 MN MN A 401 1555 1555 2.16
LINK OD2 ASP A 92 MN MN A 402 1555 1555 2.23
LINK OD1 ASN A 124 MN MN A 402 1555 1555 2.09
LINK NE2 HIS A 173 MN MN A 402 1555 1555 1.97
LINK ND1 HIS A 248 MN MN A 402 1555 1555 2.20
LINK MN MN A 401 O2 PO4 A 403 1555 1555 2.07
LINK MN MN A 401 O HOH A 624 1555 1555 2.17
LINK MN MN A 402 O4 PO4 A 403 1555 1555 2.08
LINK MN MN A 402 O HOH A 624 1555 1555 2.19
LINK OD2 ASP C 64 MN MN C 402 1555 1555 2.05
LINK NE2 HIS C 66 MN MN C 402 1555 1555 2.13
LINK OD2 ASP C 92 MN MN C 401 1555 1555 2.26
LINK OD2 ASP C 92 MN MN C 402 1555 1555 2.03
LINK OD1 ASN C 124 MN MN C 401 1555 1555 2.07
LINK NE2 HIS C 173 MN MN C 401 1555 1555 1.99
LINK ND1 HIS C 248 MN MN C 401 1555 1555 2.19
LINK MN MN C 401 O1 PO4 C 403 1555 1555 2.58
LINK MN MN C 401 O HOH C 588 1555 1555 2.08
LINK MN MN C 402 O HOH C 588 1555 1555 2.26
LINK MN MN C 402 O HOH C 589 1555 1555 2.03
CISPEP 1 MET A 4 GLY A 5 0 -4.64
CISPEP 2 ALA A 57 PRO A 58 0 4.21
CISPEP 3 PRO A 82 PRO A 83 0 5.58
CISPEP 4 ARG A 191 PRO A 192 0 2.47
CISPEP 5 ALA C 57 PRO C 58 0 2.86
CISPEP 6 PRO C 82 PRO C 83 0 4.53
CISPEP 7 ARG C 191 PRO C 192 0 2.10
SITE 1 AC1 6 ASP A 64 HIS A 66 ASP A 92 MN A 402
SITE 2 AC1 6 PO4 A 403 HOH A 624
SITE 1 AC2 7 ASP A 92 ASN A 124 HIS A 173 HIS A 248
SITE 2 AC2 7 MN A 401 PO4 A 403 HOH A 624
SITE 1 AC3 9 HIS A 66 ASP A 92 ASN A 124 HIS A 125
SITE 2 AC3 9 ARG A 221 HIS A 248 MN A 401 MN A 402
SITE 3 AC3 9 HOH A 624
SITE 1 AC4 3 PRO A 50 GLU A 54 GLU A 116
SITE 1 AC5 7 ASP C 92 ASN C 124 HIS C 173 HIS C 248
SITE 2 AC5 7 MN C 402 PO4 C 403 HOH C 588
SITE 1 AC6 7 ASP C 64 HIS C 66 ASP C 92 MN C 401
SITE 2 AC6 7 PO4 C 403 HOH C 588 HOH C 589
SITE 1 AC7 13 HIS C 66 ASP C 92 ASN C 124 HIS C 125
SITE 2 AC7 13 ARG C 221 HIS C 248 TYR C 272 MN C 401
SITE 3 AC7 13 MN C 402 HOH C 560 HOH C 561 HOH C 588
SITE 4 AC7 13 HOH C 589
SITE 1 AC8 4 SER C 129 VAL C 195 VAL C 223 HOH C 558
CRYST1 64.311 112.853 125.013 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 0.015549 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008861 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007999 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
