HEADER HYDROLASE 08-NOV-17 5YR7
TITLE HUMAN METHIONINE AMINOPEPTIDASE TYPE 1B (F309L MUTANT)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHIONINE AMINOPEPTIDASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 81-386;
COMPND 5 SYNONYM: METAP 1,PEPTIDASE M 1;
COMPND 6 EC: 3.4.11.18;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: METAP1, KIAA0094;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS METAL BINDING PROTEIN, METHIONINE AMINOPEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.PILLALAMARRI,T.ARYA,A.ADDLAGATTA
REVDAT 5 22-NOV-23 5YR7 1 LINK
REVDAT 4 27-MAY-20 5YR7 1 REMARK
REVDAT 3 20-NOV-19 5YR7 1 LINK
REVDAT 2 26-JUN-19 5YR7 1 JRNL
REVDAT 1 14-NOV-18 5YR7 0
JRNL AUTH V.PILLALAMARRI,T.ARYA,A.ADDLAGATTA
JRNL TITL DIFFERENTIAL INHIBITION OF SUB-TYPE 1 METHIONINE
JRNL TITL 2 AMINOPEPTIDASES BY OVALICIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 79.3
REMARK 3 NUMBER OF REFLECTIONS : 16543
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 840
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1041
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.3200
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2392
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 70
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.272
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.233
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.164
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.464
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2481 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2262 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3370 ; 1.699 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5255 ; 1.027 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 309 ; 7.254 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 114 ;37.812 ;23.158
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 413 ;15.503 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;16.112 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 367 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2774 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 506 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5YR7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1300005573.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO 2.3.1
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK 2.2.0
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17388
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 79.9
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
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: MOLREP
REMARK 200 STARTING MODEL: 2B3K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BISTRIS PH-6.2, 19% PEG 3350, 5%
REMARK 280 GLYCEROL, PH 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 38.59650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 MET A 68
REMARK 465 GLY A 69
REMARK 465 SER A 70
REMARK 465 SER A 71
REMARK 465 HIS A 72
REMARK 465 HIS A 73
REMARK 465 HIS A 74
REMARK 465 HIS A 75
REMARK 465 HIS A 76
REMARK 465 HIS A 77
REMARK 465 SER A 78
REMARK 465 SER A 79
REMARK 465 GLY A 80
REMARK 465 LEU A 81
REMARK 465 VAL A 82
REMARK 465 PRO A 83
REMARK 465 ARG A 84
REMARK 465 GLY A 85
REMARK 465 SER A 86
REMARK 465 HIS A 87
REMARK 465 MET A 88
REMARK 465 PRO A 89
REMARK 465 GLN A 394
REMARK 465 PHE A 395
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 207 -97.02 52.17
REMARK 500 HIS A 306 -101.35 -174.42
REMARK 500 GLU A 336 55.37 -147.72
REMARK 500 TRP A 349 158.63 -49.01
REMARK 500 TRP A 353 -48.85 -130.35
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 CO A 404 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 99 NE2
REMARK 620 2 HOH A 564 O 112.7
REMARK 620 3 HOH A 568 O 152.0 90.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 207 O
REMARK 620 2 VAL A 209 O 96.9
REMARK 620 3 SER A 363 O 88.4 109.7
REMARK 620 4 HOH A 544 O 128.1 130.4 93.1
REMARK 620 5 HOH A 560 O 156.9 86.5 69.1 60.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 403 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 212 NE2
REMARK 620 2 MET A 406 OXT 149.2
REMARK 620 3 HOH A 545 O 85.8 92.2
REMARK 620 4 HOH A 561 O 86.2 87.9 164.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 401 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 229 OD1
REMARK 620 2 ASP A 229 OD2 54.8
REMARK 620 3 ASP A 240 OD1 93.3 147.7
REMARK 620 4 GLU A 367 OE1 113.0 98.3 89.3
REMARK 620 5 MET A 406 N 75.3 91.8 83.7 169.5
REMARK 620 6 MET A 406 O 146.5 105.8 104.6 95.6 78.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 402 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 240 OD2
REMARK 620 2 HIS A 303 NE2 86.7
REMARK 620 3 GLU A 336 OE1 163.3 90.5
REMARK 620 4 GLU A 367 OE2 84.2 124.7 83.9
REMARK 620 5 MET A 406 O 93.4 112.9 102.9 122.0
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 CO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MET A 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5YR6 RELATED DB: PDB
REMARK 900 RELATED ID: 5YR5 RELATED DB: PDB
REMARK 900 RELATED ID: 5YR4 RELATED DB: PDB
REMARK 900 RELATED ID: 5YKP RELATED DB: PDB
DBREF 5YR7 A 90 395 UNP P53582 MAP11_HUMAN 81 386
SEQADV 5YR7 MET A 68 UNP P53582 INITIATING METHIONINE
SEQADV 5YR7 GLY A 69 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 SER A 70 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 SER A 71 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 HIS A 72 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 HIS A 73 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 HIS A 74 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 HIS A 75 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 HIS A 76 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 HIS A 77 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 SER A 78 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 SER A 79 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 GLY A 80 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 LEU A 81 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 VAL A 82 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 PRO A 83 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 ARG A 84 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 GLY A 85 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 SER A 86 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 HIS A 87 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 MET A 88 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 PRO A 89 UNP P53582 EXPRESSION TAG
SEQADV 5YR7 LEU A 309 UNP P53582 PHE 300 ENGINEERED MUTATION
SEQRES 1 A 328 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 328 LEU VAL PRO ARG GLY SER HIS MET PRO TYR ARG TYR THR
SEQRES 3 A 328 GLY LYS LEU ARG PRO HIS TYR PRO LEU MET PRO THR ARG
SEQRES 4 A 328 PRO VAL PRO SER TYR ILE GLN ARG PRO ASP TYR ALA ASP
SEQRES 5 A 328 HIS PRO LEU GLY MET SER GLU SER GLU GLN ALA LEU LYS
SEQRES 6 A 328 GLY THR SER GLN ILE LYS LEU LEU SER SER GLU ASP ILE
SEQRES 7 A 328 GLU GLY MET ARG LEU VAL CYS ARG LEU ALA ARG GLU VAL
SEQRES 8 A 328 LEU ASP VAL ALA ALA GLY MET ILE LYS PRO GLY VAL THR
SEQRES 9 A 328 THR GLU GLU ILE ASP HIS ALA VAL HIS LEU ALA CYS ILE
SEQRES 10 A 328 ALA ARG ASN CYS TYR PRO SER PRO LEU ASN TYR TYR ASN
SEQRES 11 A 328 PHE PRO LYS SER CYS CYS THR SER VAL ASN GLU VAL ILE
SEQRES 12 A 328 CYS HIS GLY ILE PRO ASP ARG ARG PRO LEU GLN GLU GLY
SEQRES 13 A 328 ASP ILE VAL ASN VAL ASP ILE THR LEU TYR ARG ASN GLY
SEQRES 14 A 328 TYR HIS GLY ASP LEU ASN GLU THR PHE PHE VAL GLY GLU
SEQRES 15 A 328 VAL ASP ASP GLY ALA ARG LYS LEU VAL GLN THR THR TYR
SEQRES 16 A 328 GLU CYS LEU MET GLN ALA ILE ASP ALA VAL LYS PRO GLY
SEQRES 17 A 328 VAL ARG TYR ARG GLU LEU GLY ASN ILE ILE GLN LYS HIS
SEQRES 18 A 328 ALA GLN ALA ASN GLY PHE SER VAL VAL ARG SER TYR CYS
SEQRES 19 A 328 GLY HIS GLY ILE HIS LYS LEU LEU HIS THR ALA PRO ASN
SEQRES 20 A 328 VAL PRO HIS TYR ALA LYS ASN LYS ALA VAL GLY VAL MET
SEQRES 21 A 328 LYS SER GLY HIS VAL PHE THR ILE GLU PRO MET ILE CYS
SEQRES 22 A 328 GLU GLY GLY TRP GLN ASP GLU THR TRP PRO ASP GLY TRP
SEQRES 23 A 328 THR ALA VAL THR ARG ASP GLY LYS ARG SER ALA GLN PHE
SEQRES 24 A 328 GLU HIS THR LEU LEU VAL THR ASP THR GLY CYS GLU ILE
SEQRES 25 A 328 LEU THR ARG ARG LEU ASP SER ALA ARG PRO HIS PHE MET
SEQRES 26 A 328 SER GLN PHE
HET CO A 401 1
HET CO A 402 1
HET CO A 403 1
HET CO A 404 1
HET NA A 405 1
HET MET A 406 9
HETNAM CO COBALT (II) ION
HETNAM NA SODIUM ION
HETNAM MET METHIONINE
FORMUL 2 CO 4(CO 2+)
FORMUL 6 NA NA 1+
FORMUL 7 MET C5 H11 N O2 S
FORMUL 8 HOH *70(H2 O)
HELIX 1 AA1 PRO A 115 HIS A 120 5 6
HELIX 2 AA2 SER A 125 LEU A 131 1 7
HELIX 3 AA3 SER A 141 MET A 165 1 25
HELIX 4 AA4 THR A 171 ARG A 186 1 16
HELIX 5 AA5 ASN A 194 PHE A 198 5 5
HELIX 6 AA6 ASP A 251 ALA A 271 1 21
HELIX 7 AA7 ARG A 279 ALA A 291 1 13
HELIX 8 AA8 PRO A 389 SER A 393 5 5
SHEET 1 AA1 3 TYR A 189 PRO A 190 0
SHEET 2 AA1 3 ILE A 225 ARG A 234 -1 O TYR A 233 N TYR A 189
SHEET 3 AA1 3 CYS A 203 VAL A 206 -1 N SER A 205 O ASN A 227
SHEET 1 AA2 3 TYR A 189 PRO A 190 0
SHEET 2 AA2 3 ILE A 225 ARG A 234 -1 O TYR A 233 N TYR A 189
SHEET 3 AA2 3 TYR A 237 PHE A 246 -1 O TYR A 237 N ARG A 234
SHEET 1 AA3 3 VAL A 209 CYS A 211 0
SHEET 2 AA3 3 ALA A 355 THR A 357 -1 O ALA A 355 N ILE A 210
SHEET 3 AA3 3 ASP A 346 THR A 348 -1 N GLU A 347 O VAL A 356
SHEET 1 AA4 3 SER A 295 VAL A 296 0
SHEET 2 AA4 3 MET A 338 CYS A 340 -1 O CYS A 340 N SER A 295
SHEET 3 AA4 3 SER A 363 GLN A 365 -1 O ALA A 364 N ILE A 339
SHEET 1 AA5 2 GLY A 302 GLY A 304 0
SHEET 2 AA5 2 THR A 311 VAL A 315 -1 O VAL A 315 N GLY A 302
SHEET 1 AA6 3 VAL A 332 ILE A 335 0
SHEET 2 AA6 3 HIS A 368 VAL A 372 -1 O LEU A 370 N PHE A 333
SHEET 3 AA6 3 CYS A 377 ILE A 379 -1 O GLU A 378 N LEU A 371
LINK NE2 HIS A 99 CO CO A 404 1555 1555 2.19
LINK O ASN A 207 NA NA A 405 1555 1555 2.38
LINK O VAL A 209 NA NA A 405 1555 1555 2.35
LINK NE2 HIS A 212 CO CO A 403 1555 1555 2.15
LINK OD1 ASP A 229 CO CO A 401 1555 1555 2.20
LINK OD2 ASP A 229 CO CO A 401 1555 1555 2.35
LINK OD1 ASP A 240 CO CO A 401 1555 1555 2.02
LINK OD2 ASP A 240 CO CO A 402 1555 1555 2.08
LINK NE2 HIS A 303 CO CO A 402 1555 1555 2.22
LINK OE1 GLU A 336 CO CO A 402 1555 1555 1.95
LINK O SER A 363 NA NA A 405 1555 1555 2.27
LINK OE1 GLU A 367 CO CO A 401 1555 1555 1.99
LINK OE2 GLU A 367 CO CO A 402 1555 1555 1.99
LINK CO CO A 401 N MET A 406 1555 1555 2.27
LINK CO CO A 401 O MET A 406 1555 1555 2.26
LINK CO CO A 402 O MET A 406 1555 1555 1.83
LINK CO CO A 403 OXT MET A 406 1555 1555 2.49
LINK CO CO A 403 O HOH A 545 1555 1555 2.39
LINK CO CO A 403 O HOH A 561 1555 1555 2.41
LINK CO CO A 404 O HOH A 564 1555 1555 2.12
LINK CO CO A 404 O HOH A 568 1555 1555 2.26
LINK NA NA A 405 O HOH A 544 1555 1555 2.16
LINK NA NA A 405 O HOH A 560 1555 1555 3.08
CISPEP 1 TYR A 100 PRO A 101 0 4.13
CISPEP 2 ALA A 312 PRO A 313 0 0.89
SITE 1 AC1 5 ASP A 229 ASP A 240 GLU A 367 CO A 402
SITE 2 AC1 5 MET A 406
SITE 1 AC2 7 ASP A 240 HIS A 303 THR A 334 GLU A 336
SITE 2 AC2 7 GLU A 367 CO A 401 MET A 406
SITE 1 AC3 4 HIS A 212 MET A 406 HOH A 545 HOH A 561
SITE 1 AC4 3 HIS A 99 HOH A 564 HOH A 568
SITE 1 AC5 5 ASN A 207 VAL A 209 SER A 363 HOH A 544
SITE 2 AC5 5 HOH A 560
SITE 1 AC6 12 PHE A 198 ASP A 229 THR A 231 ASP A 240
SITE 2 AC6 12 HIS A 303 HIS A 310 GLU A 336 TRP A 353
SITE 3 AC6 12 GLU A 367 CO A 401 CO A 402 CO A 403
CRYST1 47.414 77.193 48.220 90.00 92.03 90.00 P 1 21 1 2
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 0.021091 0.000000 0.000747 0.00000
SCALE2 0.000000 0.012955 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020751 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
