HEADER OXIDOREDUCTASE 03-JUN-13 4BQX
TITLE HIF PROLYL HYDROXYLASE 2 (PHD2/ EGLN1) IN COMPLEX WITH MN(II) AND N-
TITLE 2 [(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE (IOX3/UN9)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EGL NINE HOMOLOG 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 181-426;
COMPND 5 SYNONYM: HYPOXIA-INDUCIBLE FACTOR PROLYL HYDROXYLASE 2, HIF-PH2, HIF-
COMPND 6 PROLYL HYDROXYLASE 2, HPH-2, PROLYL HYDROXYLASE DOMAIN-CONTAINING
COMPND 7 PROTEIN 2, PHD2, SM-20;
COMPND 8 EC: 1.14.11.-;
COMPND 9 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_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28A
KEYWDS OXIDOREDUCTASE, 2-OXOGLUTARATE, DIOXYGENASE, EGLN, OXYGENASE, DNA-
KEYWDS 2 BINDING, TRANSCRIPTION, DSBH, FACIAL TRIAD, ASPARAGINYL/ ASPARTYL
KEYWDS 3 HYDROXYLASE, TRANSCRIPTION AND EPIGENETIC REGULATION, SIGNALING,
KEYWDS 4 DEVELOPMENT, CELL STRUCTURE, ARD, BETA-HYDROXYLATION, TRANSCRIPTION
KEYWDS 5 ACTIVATOR/INHIBITOR, S-NITROSYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.CHOWDHURY,C.J.SCHOFIELD
REVDAT 6 20-DEC-23 4BQX 1 REMARK LINK
REVDAT 5 08-MAY-19 4BQX 1 REMARK
REVDAT 4 06-MAR-19 4BQX 1 REMARK
REVDAT 3 14-MAR-18 4BQX 1 JRNL
REVDAT 2 13-NOV-13 4BQX 1 JRNL
REVDAT 1 19-JUN-13 4BQX 0
JRNL AUTH R.CHOWDHURY,J.I.CANDELA-LENA,M.C.CHAN,D.J.GREENALD,K.K.YEOH,
JRNL AUTH 2 Y.M.TIAN,M.A.MCDONOUGH,A.TUMBER,N.R.ROSE,A.CONEJO-GARCIA,
JRNL AUTH 3 M.DEMETRIADES,S.MATHAVAN,A.KAWAMURA,M.K.LEE,F.VAN EEDEN,
JRNL AUTH 4 C.W.PUGH,P.J.RATCLIFFE,C.J.SCHOFIELD
JRNL TITL SELECTIVE SMALL MOLECULE PROBES FOR THE HYPOXIA INDUCIBLE
JRNL TITL 2 FACTOR (HIF) PROLYL HYDROXYLASES.
JRNL REF ACS CHEM. BIOL. V. 8 1488 2013
JRNL REFN ESSN 1554-8937
JRNL PMID 23683440
JRNL DOI 10.1021/CB400088Q
REMARK 2
REMARK 2 RESOLUTION. 1.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 377793.210
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 25470
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 SET) : 0.211
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1297
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.79
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3690
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1771
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1682
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 121
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.52000
REMARK 3 B22 (A**2) : 1.52000
REMARK 3 B33 (A**2) : -3.03000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.25
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.28
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 66.80
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : UN9.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : UN9.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4BQX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1290057122.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979500
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25470
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 54.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.86000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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 2G19
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH6.5, 1.7M AMMONIUM SULFATE,
REMARK 280 1% DIOXANE, 0.002M MNCL2, SITTING DROP, 293K, VAPOR DIFFUSION,
REMARK 280 SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 19.66500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 19.66500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 19.66500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 175
REMARK 465 SER A 176
REMARK 465 HIS A 177
REMARK 465 MET A 178
REMARK 465 ALA A 179
REMARK 465 SER A 180
REMARK 465 PRO A 181
REMARK 465 ASN A 182
REMARK 465 GLY A 183
REMARK 465 GLN A 184
REMARK 465 THR A 185
REMARK 465 LYS A 186
REMARK 465 PRO A 187
REMARK 465 THR A 405
REMARK 465 GLY A 406
REMARK 465 GLU A 407
REMARK 465 LYS A 408
REMARK 465 GLY A 409
REMARK 465 VAL A 410
REMARK 465 ARG A 411
REMARK 465 VAL A 412
REMARK 465 GLU A 413
REMARK 465 LEU A 414
REMARK 465 ASN A 415
REMARK 465 LYS A 416
REMARK 465 PRO A 417
REMARK 465 SER A 418
REMARK 465 ASP A 419
REMARK 465 SER A 420
REMARK 465 VAL A 421
REMARK 465 GLY A 422
REMARK 465 LYS A 423
REMARK 465 ASP A 424
REMARK 465 VAL A 425
REMARK 465 PHE A 426
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 GLN A 243 CG CD OE1 NE2
REMARK 470 LYS A 244 CG CD CE NZ
REMARK 470 SER A 245 OG
REMARK 470 SER A 247 OG
REMARK 470 LYS A 249 CG CD CE NZ
REMARK 470 ASP A 250 CG OD1 OD2
REMARK 470 LYS A 350 CE NZ
REMARK 470 GLN A 352 CG CD OE1 NE2
REMARK 470 LYS A 402 CG CD CE NZ
REMARK 470 TYR A 403 CG CD1 CD2 CE1 CE2 CZ OH
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 PHE A 346 77.19 -115.95
REMARK 500 ARG A 370 -9.12 -53.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 501 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 313 NE2
REMARK 620 2 ASP A 315 OD1 87.8
REMARK 620 3 HIS A 374 NE2 88.2 87.9
REMARK 620 4 UN9 A 601 N8 87.8 118.7 152.9
REMARK 620 5 UN9 A 601 O13 105.2 163.4 82.3 72.9
REMARK 620 6 HOH A2078 O 164.0 81.8 103.5 86.6 87.5
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UN9 A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BQW RELATED DB: PDB
REMARK 900 HIF PROLYL HYDROXYLASE 2 (PHD2/ EGLN1) IN COMPLEX WITH MN(II) AND 2-
REMARK 900 (4-HYDROXY-2-OXO-1,2- DIHYDROQUINOLINE-3-CARBOXAMIDO)ACETIC ACID
REMARK 900 RELATED ID: 4BQY RELATED DB: PDB
REMARK 900 HIF PROLYL HYDROXYLASE 2 (PHD2/ EGLN1) IN COMPLEX WITH FE(II) AND N-
REMARK 900 [(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL) CARBONYL]ALANINE
DBREF 4BQX A 181 426 UNP Q9GZT9 EGLN1_HUMAN 181 426
SEQADV 4BQX GLY A 175 UNP Q9GZT9 EXPRESSION TAG
SEQADV 4BQX SER A 176 UNP Q9GZT9 EXPRESSION TAG
SEQADV 4BQX HIS A 177 UNP Q9GZT9 EXPRESSION TAG
SEQADV 4BQX MET A 178 UNP Q9GZT9 EXPRESSION TAG
SEQADV 4BQX ALA A 179 UNP Q9GZT9 EXPRESSION TAG
SEQADV 4BQX SER A 180 UNP Q9GZT9 EXPRESSION TAG
SEQRES 1 A 252 GLY SER HIS MET ALA SER PRO ASN GLY GLN THR LYS PRO
SEQRES 2 A 252 LEU PRO ALA LEU LYS LEU ALA LEU GLU TYR ILE VAL PRO
SEQRES 3 A 252 CYS MET ASN LYS HIS GLY ILE CYS VAL VAL ASP ASP PHE
SEQRES 4 A 252 LEU GLY LYS GLU THR GLY GLN GLN ILE GLY ASP GLU VAL
SEQRES 5 A 252 ARG ALA LEU HIS ASP THR GLY LYS PHE THR ASP GLY GLN
SEQRES 6 A 252 LEU VAL SER GLN LYS SER ASP SER SER LYS ASP ILE ARG
SEQRES 7 A 252 GLY ASP LYS ILE THR TRP ILE GLU GLY LYS GLU PRO GLY
SEQRES 8 A 252 CYS GLU THR ILE GLY LEU LEU MET SER SER MET ASP ASP
SEQRES 9 A 252 LEU ILE ARG HIS CYS ASN GLY LYS LEU GLY SER TYR LYS
SEQRES 10 A 252 ILE ASN GLY ARG THR LYS ALA MET VAL ALA CYS TYR PRO
SEQRES 11 A 252 GLY ASN GLY THR GLY TYR VAL ARG HIS VAL ASP ASN PRO
SEQRES 12 A 252 ASN GLY ASP GLY ARG CYS VAL THR CYS ILE TYR TYR LEU
SEQRES 13 A 252 ASN LYS ASP TRP ASP ALA LYS VAL SER GLY GLY ILE LEU
SEQRES 14 A 252 ARG ILE PHE PRO GLU GLY LYS ALA GLN PHE ALA ASP ILE
SEQRES 15 A 252 GLU PRO LYS PHE ASP ARG LEU LEU PHE PHE TRP SER ASP
SEQRES 16 A 252 ARG ARG ASN PRO HIS GLU VAL GLN PRO ALA TYR ALA THR
SEQRES 17 A 252 ARG TYR ALA ILE THR VAL TRP TYR PHE ASP ALA ASP GLU
SEQRES 18 A 252 ARG ALA ARG ALA LYS VAL LYS TYR LEU THR GLY GLU LYS
SEQRES 19 A 252 GLY VAL ARG VAL GLU LEU ASN LYS PRO SER ASP SER VAL
SEQRES 20 A 252 GLY LYS ASP VAL PHE
HET MN A 501 1
HET UN9 A 601 19
HETNAM MN MANGANESE (II) ION
HETNAM UN9 N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE
FORMUL 2 MN MN 2+
FORMUL 3 UN9 C12 H9 CL N2 O4
FORMUL 4 HOH *121(H2 O)
HELIX 1 1 PRO A 189 TYR A 197 1 9
HELIX 2 2 TYR A 197 GLY A 206 1 10
HELIX 3 3 GLY A 215 THR A 232 1 18
HELIX 4 4 CYS A 266 HIS A 282 1 17
HELIX 5 5 ASP A 335 GLY A 340 1 6
HELIX 6 6 ALA A 393 TYR A 403 1 11
SHEET 1 AA 6 ILE A 207 VAL A 210 0
SHEET 2 AA 6 ARG A 362 TRP A 367 -1 O LEU A 363 N VAL A 210
SHEET 3 AA 6 ARG A 322 TYR A 329 -1 O THR A 325 N PHE A 366
SHEET 4 AA 6 ARG A 383 ASP A 392 -1 O ILE A 386 N TYR A 328
SHEET 5 AA 6 ALA A 298 TYR A 303 -1 O MET A 299 N THR A 387
SHEET 6 AA 6 LYS A 255 ILE A 259 -1 O LYS A 255 N CYS A 302
SHEET 1 AB 5 ILE A 207 VAL A 210 0
SHEET 2 AB 5 ARG A 362 TRP A 367 -1 O LEU A 363 N VAL A 210
SHEET 3 AB 5 ARG A 322 TYR A 329 -1 O THR A 325 N PHE A 366
SHEET 4 AB 5 ARG A 383 ASP A 392 -1 O ILE A 386 N TYR A 328
SHEET 5 AB 5 ILE A 292 ARG A 295 1 N ASN A 293 O PHE A 391
SHEET 1 AC 2 LEU A 240 SER A 242 0
SHEET 2 AC 2 ILE A 251 ARG A 252 -1 O ILE A 251 N VAL A 241
SHEET 1 AD 4 TYR A 310 HIS A 313 0
SHEET 2 AD 4 HIS A 374 VAL A 376 -1 O HIS A 374 N HIS A 313
SHEET 3 AD 4 LEU A 343 ILE A 345 -1 O ARG A 344 N GLU A 375
SHEET 4 AD 4 ALA A 354 ILE A 356 -1 O ALA A 354 N ILE A 345
SSBOND 1 CYS A 201 CYS A 208 1555 1555 2.07
LINK NE2 HIS A 313 MN MN A 501 1555 1555 2.30
LINK OD1 ASP A 315 MN MN A 501 1555 1555 2.25
LINK NE2 HIS A 374 MN MN A 501 1555 1555 2.27
LINK MN MN A 501 N8 UN9 A 601 1555 1555 2.35
LINK MN MN A 501 O13 UN9 A 601 1555 1555 2.26
LINK MN MN A 501 O HOH A2078 1555 1555 2.24
SITE 1 AC1 5 HIS A 313 ASP A 315 HIS A 374 UN9 A 601
SITE 2 AC1 5 HOH A2078
SITE 1 AC2 15 ASP A 254 ILE A 256 MET A 299 TYR A 303
SITE 2 AC2 15 TYR A 310 HIS A 313 ASP A 315 TYR A 329
SITE 3 AC2 15 LEU A 343 HIS A 374 VAL A 376 ARG A 383
SITE 4 AC2 15 ARG A 398 MN A 501 HOH A2121
CRYST1 109.600 109.600 39.330 90.00 90.00 120.00 P 63 6
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 0.009124 0.005268 0.000000 0.00000
SCALE2 0.000000 0.010536 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025426 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
