HEADER HYDROLASE 11-DEC-18 6Q6J
TITLE HUMAN PHOSPHOSERINE PHOSPHATASE WITH SUBSTRATE ANALOGUE HOMO-CYSTEIC
TITLE 2 ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOSERINE PHOSPHATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PSPASE,L-3-PHOSPHOSERINE PHOSPHATASE,O-PHOSPHOSERINE
COMPND 5 PHOSPHOHYDROLASE;
COMPND 6 EC: 3.1.3.3;
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 GENE: PSPH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET 28 B
KEYWDS HUMAN PHOSPHOSERINE PHOSPHATASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WOUTERS,M.HAUFROID,M.MIRGAUX
REVDAT 3 24-JAN-24 6Q6J 1 LINK
REVDAT 2 26-JUN-19 6Q6J 1 JRNL
REVDAT 1 12-JUN-19 6Q6J 0
JRNL AUTH M.HAUFROID,M.MIRGAUX,L.LEHERTE,J.WOUTERS
JRNL TITL CRYSTAL STRUCTURES AND SNAPSHOTS ALONG THE REACTION PATHWAY
JRNL TITL 2 OF HUMAN PHOSPHOSERINE PHOSPHATASE.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 75 592 2019
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 31205021
JRNL DOI 10.1107/S2059798319006867
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 35467
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1774
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 40.9521 - 4.6646 1.00 2752 144 0.1731 0.2125
REMARK 3 2 4.6646 - 3.7032 1.00 2679 142 0.1616 0.2220
REMARK 3 3 3.7032 - 3.2353 1.00 2610 137 0.1789 0.2236
REMARK 3 4 3.2353 - 2.9396 1.00 2628 138 0.2017 0.2359
REMARK 3 5 2.9396 - 2.7289 1.00 2575 136 0.2247 0.2829
REMARK 3 6 2.7289 - 2.5681 1.00 2589 136 0.2205 0.2602
REMARK 3 7 2.5681 - 2.4395 1.00 2605 137 0.2217 0.2837
REMARK 3 8 2.4395 - 2.3333 1.00 2562 135 0.2242 0.3004
REMARK 3 9 2.3333 - 2.2435 1.00 2559 135 0.2281 0.2693
REMARK 3 10 2.2435 - 2.1661 1.00 2608 137 0.2384 0.2982
REMARK 3 11 2.1661 - 2.0983 1.00 2562 135 0.2498 0.2538
REMARK 3 12 2.0983 - 2.0384 1.00 2557 135 0.2931 0.3808
REMARK 3 13 2.0384 - 1.9847 0.94 2407 127 0.4101 0.4429
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.51
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.10
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6Q6J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1200013368.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-18
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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35482
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.985
REMARK 200 RESOLUTION RANGE LOW (A) : 40.943
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.01873
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.23310
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.290
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.1
REMARK 200 STARTING MODEL: 6HYY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE 0.1M PH6.5; CACL2
REMARK 280 0.3M; PEG 2000 20%; DMSO 4%, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.88000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.88000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 24.61500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.24500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.61500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.24500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.88000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.61500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.24500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 78.88000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.61500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.24500
REMARK 290 SMTRY3 8 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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 B 496 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 GLU B 222
REMARK 465 LEU B 223
REMARK 465 GLU B 224
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 B 50 CG CD NE CZ NH1 NH2
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 OG SER B 109 O3S HJT B 302 1.90
REMARK 500 O HOH A 415 O HOH A 470 1.96
REMARK 500 OE1 GLU B 185 O HOH B 401 2.00
REMARK 500 O HOH B 469 O HOH B 487 2.07
REMARK 500 O HOH B 480 O HOH B 487 2.11
REMARK 500 OE2 GLU A 148 O HOH A 401 2.12
REMARK 500 N SER B 5 O HOH B 402 2.13
REMARK 500 O HOH A 401 O HOH A 476 2.13
REMARK 500 OD2 ASP A 207 O HOH A 402 2.15
REMARK 500 O HOH A 452 O HOH A 464 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 VAL A 21 -66.59 -95.93
REMARK 500 THR A 24 -74.27 -117.23
REMARK 500 GLU A 222 7.29 -150.43
REMARK 500 VAL B 21 -68.25 -93.53
REMARK 500 THR B 24 -69.38 -121.99
REMARK 500 LYS B 36 -72.78 -54.88
REMARK 500 GLU B 46 89.49 -64.49
REMARK 500 MET B 47 -101.44 -89.03
REMARK 500 THR B 48 26.68 -141.59
REMARK 500 ALA B 55 -132.60 -78.74
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 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD2
REMARK 620 2 ASP A 22 O 84.5
REMARK 620 3 ASP A 179 OD2 73.3 93.1
REMARK 620 4 HOH A 409 O 86.0 170.5 84.4
REMARK 620 5 HOH A 473 O 165.5 84.8 97.6 104.6
REMARK 620 6 HOH A 483 O 114.6 103.1 162.4 80.7 77.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 185 O
REMARK 620 2 PRO A 188 O 85.6
REMARK 620 3 HOH A 458 O 77.2 161.6
REMARK 620 4 HOH B 413 O 78.5 85.2 97.5
REMARK 620 5 HOH B 466 O 110.5 91.4 88.7 170.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 20 OD1
REMARK 620 2 ASP B 20 OD2 43.7
REMARK 620 3 ASP B 22 O 90.2 76.6
REMARK 620 4 ASP B 179 OD1 113.3 70.7 84.0
REMARK 620 5 HOH B 414 O 75.4 86.2 162.6 92.7
REMARK 620 6 HOH B 438 O 77.8 121.4 107.8 164.3 79.0
REMARK 620 7 HOH B 463 O 143.8 157.9 82.2 101.1 115.1 71.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HJT B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 303
DBREF 6Q6J A 5 224 UNP P78330 SERB_HUMAN 5 224
DBREF 6Q6J B 5 224 UNP P78330 SERB_HUMAN 5 224
SEQRES 1 A 220 SER GLU LEU ARG LYS LEU PHE TYR SER ALA ASP ALA VAL
SEQRES 2 A 220 CYS PHE ASP VAL ASP SER THR VAL ILE ARG GLU GLU GLY
SEQRES 3 A 220 ILE ASP GLU LEU ALA LYS ILE CYS GLY VAL GLU ASP ALA
SEQRES 4 A 220 VAL SER GLU MET THR ARG ARG ALA MET GLY GLY ALA VAL
SEQRES 5 A 220 PRO PHE LYS ALA ALA LEU THR GLU ARG LEU ALA LEU ILE
SEQRES 6 A 220 GLN PRO SER ARG GLU GLN VAL GLN ARG LEU ILE ALA GLU
SEQRES 7 A 220 GLN PRO PRO HIS LEU THR PRO GLY ILE ARG GLU LEU VAL
SEQRES 8 A 220 SER ARG LEU GLN GLU ARG ASN VAL GLN VAL PHE LEU ILE
SEQRES 9 A 220 SER GLY GLY PHE ARG SER ILE VAL GLU HIS VAL ALA SER
SEQRES 10 A 220 LYS LEU ASN ILE PRO ALA THR ASN VAL PHE ALA ASN ARG
SEQRES 11 A 220 LEU LYS PHE TYR PHE ASN GLY GLU TYR ALA GLY PHE ASP
SEQRES 12 A 220 GLU THR GLN PRO THR ALA GLU SER GLY GLY LYS GLY LYS
SEQRES 13 A 220 VAL ILE LYS LEU LEU LYS GLU LYS PHE HIS PHE LYS LYS
SEQRES 14 A 220 ILE ILE MET ILE GLY ASP GLY ALA THR ASP MET GLU ALA
SEQRES 15 A 220 CYS PRO PRO ALA ASP ALA PHE ILE GLY PHE GLY GLY ASN
SEQRES 16 A 220 VAL ILE ARG GLN GLN VAL LYS ASP ASN ALA LYS TRP TYR
SEQRES 17 A 220 ILE THR ASP PHE VAL GLU LEU LEU GLY GLU LEU GLU
SEQRES 1 B 220 SER GLU LEU ARG LYS LEU PHE TYR SER ALA ASP ALA VAL
SEQRES 2 B 220 CYS PHE ASP VAL ASP SER THR VAL ILE ARG GLU GLU GLY
SEQRES 3 B 220 ILE ASP GLU LEU ALA LYS ILE CYS GLY VAL GLU ASP ALA
SEQRES 4 B 220 VAL SER GLU MET THR ARG ARG ALA MET GLY GLY ALA VAL
SEQRES 5 B 220 PRO PHE LYS ALA ALA LEU THR GLU ARG LEU ALA LEU ILE
SEQRES 6 B 220 GLN PRO SER ARG GLU GLN VAL GLN ARG LEU ILE ALA GLU
SEQRES 7 B 220 GLN PRO PRO HIS LEU THR PRO GLY ILE ARG GLU LEU VAL
SEQRES 8 B 220 SER ARG LEU GLN GLU ARG ASN VAL GLN VAL PHE LEU ILE
SEQRES 9 B 220 SER GLY GLY PHE ARG SER ILE VAL GLU HIS VAL ALA SER
SEQRES 10 B 220 LYS LEU ASN ILE PRO ALA THR ASN VAL PHE ALA ASN ARG
SEQRES 11 B 220 LEU LYS PHE TYR PHE ASN GLY GLU TYR ALA GLY PHE ASP
SEQRES 12 B 220 GLU THR GLN PRO THR ALA GLU SER GLY GLY LYS GLY LYS
SEQRES 13 B 220 VAL ILE LYS LEU LEU LYS GLU LYS PHE HIS PHE LYS LYS
SEQRES 14 B 220 ILE ILE MET ILE GLY ASP GLY ALA THR ASP MET GLU ALA
SEQRES 15 B 220 CYS PRO PRO ALA ASP ALA PHE ILE GLY PHE GLY GLY ASN
SEQRES 16 B 220 VAL ILE ARG GLN GLN VAL LYS ASP ASN ALA LYS TRP TYR
SEQRES 17 B 220 ILE THR ASP PHE VAL GLU LEU LEU GLY GLU LEU GLU
HET CA A 301 1
HET CA A 302 1
HET CA B 301 1
HET HJT B 302 11
HET CL B 303 1
HETNAM CA CALCIUM ION
HETNAM HJT (2~{S})-2-AZANYL-4-SULFO-BUTANOIC ACID
HETNAM CL CHLORIDE ION
FORMUL 3 CA 3(CA 2+)
FORMUL 6 HJT C4 H9 N O5 S
FORMUL 7 CL CL 1-
FORMUL 8 HOH *195(H2 O)
HELIX 1 AA1 SER A 5 SER A 13 1 9
HELIX 2 AA2 GLU A 29 GLY A 39 1 11
HELIX 3 AA3 VAL A 40 MET A 52 1 13
HELIX 4 AA4 PRO A 57 GLN A 70 1 14
HELIX 5 AA5 SER A 72 GLN A 83 1 12
HELIX 6 AA6 GLY A 90 ARG A 101 1 12
HELIX 7 AA7 ARG A 113 LEU A 123 1 11
HELIX 8 AA8 PRO A 126 THR A 128 5 3
HELIX 9 AA9 GLN A 150 GLU A 154 5 5
HELIX 10 AB1 GLY A 156 HIS A 170 1 15
HELIX 11 AB2 GLY A 180 GLU A 185 1 6
HELIX 12 AB3 ARG A 202 ALA A 209 1 8
HELIX 13 AB4 ASP A 215 LEU A 220 5 6
HELIX 14 AB5 GLU B 6 SER B 13 1 8
HELIX 15 AB6 GLU B 29 GLY B 39 1 11
HELIX 16 AB7 PRO B 57 GLN B 70 1 14
HELIX 17 AB8 SER B 72 GLN B 83 1 12
HELIX 18 AB9 GLY B 90 ARG B 101 1 12
HELIX 19 AC1 ARG B 113 LEU B 123 1 11
HELIX 20 AC2 PRO B 126 THR B 128 5 3
HELIX 21 AC3 GLN B 150 GLU B 154 5 5
HELIX 22 AC4 GLY B 156 HIS B 170 1 15
HELIX 23 AC5 GLY B 180 GLU B 185 1 6
HELIX 24 AC6 ARG B 202 ASP B 207 1 6
HELIX 25 AC7 ASP B 215 GLY B 221 1 7
SHEET 1 AA1 6 VAL A 130 ASN A 133 0
SHEET 2 AA1 6 GLN A 104 PHE A 112 1 N GLY A 111 O ASN A 133
SHEET 3 AA1 6 ALA A 16 ASP A 20 1 N VAL A 17 O PHE A 106
SHEET 4 AA1 6 ILE A 174 GLY A 178 1 O ILE A 175 N CYS A 18
SHEET 5 AA1 6 ALA A 192 PHE A 196 1 O ILE A 194 N MET A 176
SHEET 6 AA1 6 TRP A 211 ILE A 213 1 O TRP A 211 N GLY A 195
SHEET 1 AA2 2 LEU A 135 PHE A 137 0
SHEET 2 AA2 2 TYR A 143 PHE A 146 -1 O ALA A 144 N LYS A 136
SHEET 1 AA3 6 VAL B 130 ASN B 133 0
SHEET 2 AA3 6 GLN B 104 PHE B 112 1 N SER B 109 O PHE B 131
SHEET 3 AA3 6 ALA B 16 ASP B 20 1 N PHE B 19 O PHE B 106
SHEET 4 AA3 6 ILE B 174 GLY B 178 1 O ILE B 175 N CYS B 18
SHEET 5 AA3 6 ALA B 192 PHE B 196 1 O ALA B 192 N MET B 176
SHEET 6 AA3 6 TYR B 212 ILE B 213 1 O ILE B 213 N GLY B 195
SHEET 1 AA4 2 LEU B 135 PHE B 137 0
SHEET 2 AA4 2 TYR B 143 PHE B 146 -1 O GLY B 145 N LYS B 136
LINK OD2 ASP A 20 CA CA A 301 1555 1555 2.20
LINK O ASP A 22 CA CA A 301 1555 1555 2.28
LINK OD2 ASP A 179 CA CA A 301 1555 1555 2.25
LINK O GLU A 185 CA CA A 302 1555 1555 2.47
LINK O PRO A 188 CA CA A 302 1555 1555 2.53
LINK CA CA A 301 O HOH A 409 1555 1555 2.43
LINK CA CA A 301 O HOH A 473 1555 1555 2.34
LINK CA CA A 301 O HOH A 483 1555 1555 2.30
LINK CA CA A 302 O HOH A 458 1555 1555 2.26
LINK CA CA A 302 O HOH B 413 1555 3555 2.40
LINK CA CA A 302 O HOH B 466 1555 3555 2.40
LINK OD1 ASP B 20 CA CA B 301 1555 1555 3.18
LINK OD2 ASP B 20 CA CA B 301 1555 1555 2.36
LINK O ASP B 22 CA CA B 301 1555 1555 2.33
LINK OD1 ASP B 179 CA CA B 301 1555 1555 2.31
LINK CA CA B 301 O HOH B 414 1555 1555 2.64
LINK CA CA B 301 O HOH B 438 1555 1555 2.25
LINK CA CA B 301 O HOH B 463 1555 1555 2.55
CISPEP 1 CYS A 187 PRO A 188 0 -1.00
CISPEP 2 PRO A 188 PRO A 189 0 4.60
CISPEP 3 CYS B 187 PRO B 188 0 2.14
CISPEP 4 PRO B 188 PRO B 189 0 6.17
SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 179 HOH A 409
SITE 2 AC1 6 HOH A 473 HOH A 483
SITE 1 AC2 6 GLU A 185 PRO A 188 HOH A 458 GLU B 93
SITE 2 AC2 6 HOH B 413 HOH B 466
SITE 1 AC3 6 ASP B 20 ASP B 22 ASP B 179 HOH B 414
SITE 2 AC3 6 HOH B 438 HOH B 463
SITE 1 AC4 12 ASP B 20 VAL B 21 ASP B 22 PHE B 58
SITE 2 AC4 12 SER B 109 GLY B 110 GLY B 111 LYS B 158
SITE 3 AC4 12 THR B 182 HOH B 406 HOH B 410 HOH B 438
SITE 1 AC5 4 ARG B 113 SER B 114 LEU B 135 HOH B 437
CRYST1 49.230 130.490 157.760 90.00 90.00 90.00 C 2 2 21 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 0.020313 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007663 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006339 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
