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HEADER HYDROLASE 29-SEP-17 5YHP
TITLE PROLINE IMINOPEPTIDASE FROM PSYCHROPHILIC YEAST GLACIOZYMA ANTARCTICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COLD ACTIVE PROLINE IMINOPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.11.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GLACIOZYMA ANTARCTICA;
SOURCE 3 ORGANISM_TAXID: 105987;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COLD ACTIVE ENZYME, PROTEASE, AMINOPEPTIDASE, SERINE PEPTIDASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.A.RODZLI,S.KAMARUDDIN,A.JONET,W.M.K.W.SEMAN,M.M.TAB,N.MINOR,
AUTHOR 2 N.R.JAAFAR,N.M.MAHADI,A.M.A.MURAD,F.D.A.BAKAR,R.M.D.ILLIAS
REVDAT 1 25-OCT-17 5YHP 0
JRNL AUTH S.KAMARUDDIN,N.A.RODZLI,A.JONET,W.M.K.W.SEMAN,M.M.TAB,
JRNL AUTH 2 N.MINOR,N.R.JAAFAR,N.M.MAHADI,A.M.A.MURAD,F.D.A.BAKAR
JRNL TITL PROLINE IMINOPEPTIDASE FROM PSYCHROPHILIC YEAST GLACIOZYMA
JRNL TITL 2 ANTARCTICA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 3 NUMBER OF REFLECTIONS : 28744
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1997
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 27.6958 - 5.7514 0.96 2183 164 0.1475 0.1499
REMARK 3 2 5.7514 - 4.5717 0.99 2129 158 0.1421 0.1551
REMARK 3 3 4.5717 - 3.9958 0.99 2098 157 0.1504 0.1891
REMARK 3 4 3.9958 - 3.6313 0.99 2111 158 0.1735 0.2147
REMARK 3 5 3.6313 - 3.3715 0.99 2096 157 0.2137 0.2411
REMARK 3 6 3.3715 - 3.1730 0.99 2063 154 0.2330 0.2946
REMARK 3 7 3.1730 - 3.0143 0.97 2025 151 0.2448 0.2840
REMARK 3 8 3.0143 - 2.8833 0.93 1944 145 0.2647 0.3028
REMARK 3 9 2.8833 - 2.7724 0.89 1837 138 0.2586 0.3101
REMARK 3 10 2.7724 - 2.6768 0.86 1787 133 0.2632 0.3484
REMARK 3 11 2.6768 - 2.5931 0.83 1734 130 0.2562 0.3126
REMARK 3 12 2.5931 - 2.5191 0.81 1668 123 0.2740 0.3058
REMARK 3 13 2.5191 - 2.4528 0.76 1600 120 0.2733 0.3535
REMARK 3 14 2.4528 - 2.3930 0.72 1472 109 0.2639 0.3138
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.950
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 64.04
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 : 0.008 5174
REMARK 3 ANGLE : 1.128 7029
REMARK 3 CHIRALITY : 0.090 741
REMARK 3 PLANARITY : 0.005 918
REMARK 3 DIHEDRAL : 15.622 1910
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 104 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.2643 -21.5668 -21.8631
REMARK 3 T TENSOR
REMARK 3 T11: 0.6326 T22: 0.6780
REMARK 3 T33: 0.7304 T12: -0.0178
REMARK 3 T13: 0.0622 T23: -0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 0.1111 L22: 0.7955
REMARK 3 L33: 0.2293 L12: 0.1194
REMARK 3 L13: -0.1015 L23: 0.1972
REMARK 3 S TENSOR
REMARK 3 S11: 0.0148 S12: -0.2012 S13: 0.2785
REMARK 3 S21: 0.1178 S22: 0.0635 S23: -0.1479
REMARK 3 S31: -0.0794 S32: 0.0260 S33: 0.0002
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 105 THROUGH 206 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9191 -36.1223 -26.0440
REMARK 3 T TENSOR
REMARK 3 T11: 0.6121 T22: 0.6329
REMARK 3 T33: 0.6129 T12: -0.0037
REMARK 3 T13: 0.0241 T23: 0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 0.3918 L22: 0.4142
REMARK 3 L33: 0.0367 L12: -0.0750
REMARK 3 L13: 0.0331 L23: 0.1107
REMARK 3 S TENSOR
REMARK 3 S11: 0.1083 S12: -0.1000 S13: 0.1381
REMARK 3 S21: -0.0017 S22: -0.0314 S23: 0.0093
REMARK 3 S31: -0.0400 S32: -0.0008 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 207 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5598 -34.0045 -26.0120
REMARK 3 T TENSOR
REMARK 3 T11: 0.6887 T22: 0.6658
REMARK 3 T33: 0.6412 T12: 0.0185
REMARK 3 T13: 0.0000 T23: -0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 0.1575 L22: 0.4876
REMARK 3 L33: 0.1343 L12: -0.0423
REMARK 3 L13: -0.0781 L23: -0.2056
REMARK 3 S TENSOR
REMARK 3 S11: 0.1426 S12: 0.0614 S13: 0.2344
REMARK 3 S21: 0.0606 S22: 0.1397 S23: -0.0988
REMARK 3 S31: -0.2764 S32: 0.0919 S33: 0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 256 THROUGH 319 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.3313 -42.6411 -25.0424
REMARK 3 T TENSOR
REMARK 3 T11: 0.6117 T22: 0.6435
REMARK 3 T33: 0.6439 T12: 0.0264
REMARK 3 T13: 0.0471 T23: 0.0571
REMARK 3 L TENSOR
REMARK 3 L11: 0.2511 L22: 0.3985
REMARK 3 L33: 0.2519 L12: -0.3061
REMARK 3 L13: -0.0086 L23: -0.0671
REMARK 3 S TENSOR
REMARK 3 S11: -0.0548 S12: 0.0719 S13: 0.0728
REMARK 3 S21: 0.0005 S22: -0.0233 S23: -0.1153
REMARK 3 S31: -0.0377 S32: 0.0479 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2562 -82.3230 -11.3297
REMARK 3 T TENSOR
REMARK 3 T11: 0.6782 T22: 0.6775
REMARK 3 T33: 0.6565 T12: 0.0252
REMARK 3 T13: 0.0382 T23: 0.0626
REMARK 3 L TENSOR
REMARK 3 L11: 0.5922 L22: 0.3195
REMARK 3 L33: 0.0970 L12: -0.0788
REMARK 3 L13: -0.1035 L23: -0.1418
REMARK 3 S TENSOR
REMARK 3 S11: -0.1330 S12: -0.2209 S13: -0.1918
REMARK 3 S21: -0.0390 S22: 0.1176 S23: -0.1133
REMARK 3 S31: 0.0888 S32: 0.2014 S33: -0.0001
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 67 THROUGH 319 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8991 -68.5525 -22.5508
REMARK 3 T TENSOR
REMARK 3 T11: 0.5813 T22: 0.5792
REMARK 3 T33: 0.5821 T12: 0.0240
REMARK 3 T13: 0.0322 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 0.4804 L22: 0.7598
REMARK 3 L33: 0.5938 L12: 0.4938
REMARK 3 L13: -0.3918 L23: -0.1069
REMARK 3 S TENSOR
REMARK 3 S11: -0.0535 S12: 0.0148 S13: -0.0214
REMARK 3 S21: -0.0561 S22: 0.0173 S23: 0.0447
REMARK 3 S31: 0.0653 S32: 0.0347 S33: -0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 2:319 )
REMARK 3 SELECTION : CHAIN 'B' AND (RESSEQ 2:319 )
REMARK 3 ATOM PAIRS NUMBER : 2495
REMARK 3 RMSD : 0.069
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5YHP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1300004891.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.6
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) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 200K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28758
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.393
REMARK 200 RESOLUTION RANGE LOW (A) : 27.694
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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
REMARK 200 STARTING MODEL: 1AZW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.2M AMMONIUM ACETATE,
REMARK 280 0.1M SODIUM CITRATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277.1K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,-Y,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 27.69400
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.50250
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 27.69400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 85.50250
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 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 -35
REMARK 465 ARG A -34
REMARK 465 GLY A -33
REMARK 465 SER A -32
REMARK 465 HIS A -31
REMARK 465 HIS A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 GLY A -25
REMARK 465 MET A -24
REMARK 465 ALA A -23
REMARK 465 SER A -22
REMARK 465 MET A -21
REMARK 465 THR A -20
REMARK 465 GLY A -19
REMARK 465 GLY A -18
REMARK 465 GLN A -17
REMARK 465 GLN A -16
REMARK 465 MET A -15
REMARK 465 GLY A -14
REMARK 465 ARG A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 TYR A -10
REMARK 465 ASP A -9
REMARK 465 ASP A -8
REMARK 465 ASP A -7
REMARK 465 ASP A -6
REMARK 465 LYS A -5
REMARK 465 ASP A -4
REMARK 465 HIS A -3
REMARK 465 PRO A -2
REMARK 465 PHE A -1
REMARK 465 THR A 0
REMARK 465 MET A 1
REMARK 465 MET B -35
REMARK 465 ARG B -34
REMARK 465 GLY B -33
REMARK 465 SER B -32
REMARK 465 HIS B -31
REMARK 465 HIS B -30
REMARK 465 HIS B -29
REMARK 465 HIS B -28
REMARK 465 HIS B -27
REMARK 465 HIS B -26
REMARK 465 GLY B -25
REMARK 465 MET B -24
REMARK 465 ALA B -23
REMARK 465 SER B -22
REMARK 465 MET B -21
REMARK 465 THR B -20
REMARK 465 GLY B -19
REMARK 465 GLY B -18
REMARK 465 GLN B -17
REMARK 465 GLN B -16
REMARK 465 MET B -15
REMARK 465 GLY B -14
REMARK 465 ARG B -13
REMARK 465 ASP B -12
REMARK 465 LEU B -11
REMARK 465 TYR B -10
REMARK 465 ASP B -9
REMARK 465 ASP B -8
REMARK 465 ASP B -7
REMARK 465 ASP B -6
REMARK 465 LYS B -5
REMARK 465 ASP B -4
REMARK 465 HIS B -3
REMARK 465 PRO B -2
REMARK 465 PHE B -1
REMARK 465 THR B 0
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 NH1 ARG B 23 OG2 FLC A 401 1545 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 23 NE - CZ - NH1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 23 NE - CZ - NH2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 127 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG B 23 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG B 23 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG B 127 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG B 127 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
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 SER A 111 -122.96 62.47
REMARK 500 LEU A 139 17.88 59.51
REMARK 500 SER B 111 -122.54 62.91
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 B 568 DISTANCE = 5.94 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC B 401
DBREF 5YHP A -35 319 PDB 5YHP 5YHP -35 319
DBREF 5YHP B -35 319 PDB 5YHP 5YHP -35 319
SEQRES 1 A 355 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 A 355 SER MET THR GLY GLY GLN GLN MET GLY ARG ASP LEU TYR
SEQRES 3 A 355 ASP ASP ASP ASP LYS ASP HIS PRO PHE THR MET THR SER
SEQRES 4 A 355 LEU PHE ALA ALA ILE GLN PRO TYR LYS THR HIS LEU LEU
SEQRES 5 A 355 ARG VAL SER PRO LEU HIS ARG LEU SER ILE LYS GLU TYR
SEQRES 6 A 355 GLY ASN PRO GLN GLY LYS PRO VAL VAL PHE LEU HIS GLY
SEQRES 7 A 355 GLY PRO GLY GLY GLY ALA SER ASP SER ASP ALA ARG ARG
SEQRES 8 A 355 PHE ASN PRO THR THR TYR ARG ILE VAL LEU PHE ASP GLN
SEQRES 9 A 355 ARG GLY SER GLY GLU SER THR PRO ALA SER CYS LEU GLU
SEQRES 10 A 355 ASP ASN THR THR GLN ALA LEU VAL GLU ASP ILE GLU LYS
SEQRES 11 A 355 ILE ARG GLU PHE LEU GLN VAL GLY ALA ALA TRP HIS VAL
SEQRES 12 A 355 PHE GLY GLY SER TRP GLY SER THR LEU ALA LEU ALA TYR
SEQRES 13 A 355 ALA GLN ALA HIS PRO ALA ARG VAL LYS SER LEU THR LEU
SEQRES 14 A 355 ARG GLY ILE PHE THR LEU ARG LYS LYS GLU LEU ASP PHE
SEQRES 15 A 355 PHE TYR GLN GLY PRO GLY SER SER PHE VAL PHE PRO GLU
SEQRES 16 A 355 TYR TRP GLU GLU TYR LEU ASP PRO ILE PRO VAL ALA GLU
SEQRES 17 A 355 ARG GLY ASP MET VAL LYS ALA TYR TYR GLU ARG LEU THR
SEQRES 18 A 355 GLY SER ASP GLU LYS VAL ARG ALA GLU ALA GLY ARG ALA
SEQRES 19 A 355 TRP SER ARG TRP GLU MET ALA THR SER ARG LEU HIS VAL
SEQRES 20 A 355 ASP PRO ASP TYR ILE SER LYS ALA ASP ALA PRO GLY PHE
SEQRES 21 A 355 ALA ASP ALA PHE ALA ARG ILE GLU SER HIS TYR PHE VAL
SEQRES 22 A 355 ASN GLY GLY PHE MET PRO GLU GLY GLU LEU LEU LYS PRO
SEQRES 23 A 355 GLU ASN ILE ALA LYS ILE SER HIS ILE PRO ALA VAL ILE
SEQRES 24 A 355 VAL GLN GLY ARG TYR ASP MET VAL CYS PRO ILE THR THR
SEQRES 25 A 355 ALA TYR GLU LEU THR LYS LEU TRP PRO GLU ALA LYS PHE
SEQRES 26 A 355 VAL VAL ILE PRO ASP ALA GLY HIS SER ALA ILE GLU ALA
SEQRES 27 A 355 GLY THR GLU LYS ALA LEU VAL GLU ALA THR GLU GLU PHE
SEQRES 28 A 355 ALA LYS LEU ALA
SEQRES 1 B 355 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 B 355 SER MET THR GLY GLY GLN GLN MET GLY ARG ASP LEU TYR
SEQRES 3 B 355 ASP ASP ASP ASP LYS ASP HIS PRO PHE THR MET THR SER
SEQRES 4 B 355 LEU PHE ALA ALA ILE GLN PRO TYR LYS THR HIS LEU LEU
SEQRES 5 B 355 ARG VAL SER PRO LEU HIS ARG LEU SER ILE LYS GLU TYR
SEQRES 6 B 355 GLY ASN PRO GLN GLY LYS PRO VAL VAL PHE LEU HIS GLY
SEQRES 7 B 355 GLY PRO GLY GLY GLY ALA SER ASP SER ASP ALA ARG ARG
SEQRES 8 B 355 PHE ASN PRO THR THR TYR ARG ILE VAL LEU PHE ASP GLN
SEQRES 9 B 355 ARG GLY SER GLY GLU SER THR PRO ALA SER CYS LEU GLU
SEQRES 10 B 355 ASP ASN THR THR GLN ALA LEU VAL GLU ASP ILE GLU LYS
SEQRES 11 B 355 ILE ARG GLU PHE LEU GLN VAL GLY ALA ALA TRP HIS VAL
SEQRES 12 B 355 PHE GLY GLY SER TRP GLY SER THR LEU ALA LEU ALA TYR
SEQRES 13 B 355 ALA GLN ALA HIS PRO ALA ARG VAL LYS SER LEU THR LEU
SEQRES 14 B 355 ARG GLY ILE PHE THR LEU ARG LYS LYS GLU LEU ASP PHE
SEQRES 15 B 355 PHE TYR GLN GLY PRO GLY SER SER PHE VAL PHE PRO GLU
SEQRES 16 B 355 TYR TRP GLU GLU TYR LEU ASP PRO ILE PRO VAL ALA GLU
SEQRES 17 B 355 ARG GLY ASP MET VAL LYS ALA TYR TYR GLU ARG LEU THR
SEQRES 18 B 355 GLY SER ASP GLU LYS VAL ARG ALA GLU ALA GLY ARG ALA
SEQRES 19 B 355 TRP SER ARG TRP GLU MET ALA THR SER ARG LEU HIS VAL
SEQRES 20 B 355 ASP PRO ASP TYR ILE SER LYS ALA ASP ALA PRO GLY PHE
SEQRES 21 B 355 ALA ASP ALA PHE ALA ARG ILE GLU SER HIS TYR PHE VAL
SEQRES 22 B 355 ASN GLY GLY PHE MET PRO GLU GLY GLU LEU LEU LYS PRO
SEQRES 23 B 355 GLU ASN ILE ALA LYS ILE SER HIS ILE PRO ALA VAL ILE
SEQRES 24 B 355 VAL GLN GLY ARG TYR ASP MET VAL CYS PRO ILE THR THR
SEQRES 25 B 355 ALA TYR GLU LEU THR LYS LEU TRP PRO GLU ALA LYS PHE
SEQRES 26 B 355 VAL VAL ILE PRO ASP ALA GLY HIS SER ALA ILE GLU ALA
SEQRES 27 B 355 GLY THR GLU LYS ALA LEU VAL GLU ALA THR GLU GLU PHE
SEQRES 28 B 355 ALA LYS LEU ALA
HET FLC A 401 13
HET FLC A 402 13
HET FLC B 401 13
HETNAM FLC CITRATE ANION
FORMUL 3 FLC 3(C6 H5 O7 3-)
FORMUL 6 HOH *140(H2 O)
HELIX 1 AA1 SER A 49 PHE A 56 5 8
HELIX 2 AA2 THR A 84 LEU A 99 1 16
HELIX 3 AA3 SER A 111 HIS A 124 1 14
HELIX 4 AA4 ARG A 140 GLN A 149 1 10
HELIX 5 AA5 GLY A 152 VAL A 156 5 5
HELIX 6 AA6 PHE A 157 ASP A 166 1 10
HELIX 7 AA7 PRO A 169 ARG A 173 5 5
HELIX 8 AA8 ASP A 175 THR A 185 1 11
HELIX 9 AA9 ASP A 188 THR A 206 1 19
HELIX 10 AB1 ASP A 212 SER A 217 1 6
HELIX 11 AB2 LYS A 218 ASP A 220 5 3
HELIX 12 AB3 ALA A 221 VAL A 237 1 17
HELIX 13 AB4 ASN A 238 MET A 242 5 5
HELIX 14 AB5 GLY A 245 LEU A 248 5 4
HELIX 15 AB6 LYS A 249 ALA A 254 1 6
HELIX 16 AB7 PRO A 273 TRP A 284 1 12
HELIX 17 AB8 GLU A 301 ALA A 316 1 16
HELIX 18 AB9 SER B 49 PHE B 56 5 8
HELIX 19 AC1 THR B 84 LEU B 99 1 16
HELIX 20 AC2 SER B 111 HIS B 124 1 14
HELIX 21 AC3 ARG B 140 GLN B 149 1 10
HELIX 22 AC4 GLY B 152 VAL B 156 5 5
HELIX 23 AC5 PHE B 157 ASP B 166 1 10
HELIX 24 AC6 PRO B 169 ARG B 173 5 5
HELIX 25 AC7 ASP B 175 THR B 185 1 11
HELIX 26 AC8 ASP B 188 THR B 206 1 19
HELIX 27 AC9 ASP B 212 SER B 217 1 6
HELIX 28 AD1 LYS B 218 ASP B 220 5 3
HELIX 29 AD2 ALA B 221 ASN B 238 1 18
HELIX 30 AD3 GLY B 239 MET B 242 5 4
HELIX 31 AD4 GLY B 245 LEU B 248 5 4
HELIX 32 AD5 LYS B 249 ALA B 254 1 6
HELIX 33 AD6 PRO B 273 TRP B 284 1 12
HELIX 34 AD7 GLU B 301 ALA B 316 1 16
SHEET 1 AA1 8 LYS A 12 ARG A 17 0
SHEET 2 AA1 8 ARG A 23 GLY A 30 -1 O ILE A 26 N HIS A 14
SHEET 3 AA1 8 TYR A 61 PHE A 66 -1 O LEU A 65 N LYS A 27
SHEET 4 AA1 8 LYS A 35 LEU A 40 1 N LYS A 35 O ARG A 62
SHEET 5 AA1 8 TRP A 105 GLY A 110 1 O PHE A 108 N LEU A 40
SHEET 6 AA1 8 VAL A 128 ARG A 134 1 O LYS A 129 N TRP A 105
SHEET 7 AA1 8 ALA A 261 GLY A 266 1 O VAL A 262 N LEU A 133
SHEET 8 AA1 8 LYS A 288 ILE A 292 1 O LYS A 288 N ILE A 263
SHEET 1 AA2 8 LYS B 12 ARG B 17 0
SHEET 2 AA2 8 ARG B 23 GLY B 30 -1 O LEU B 24 N LEU B 16
SHEET 3 AA2 8 TYR B 61 PHE B 66 -1 O LEU B 65 N LYS B 27
SHEET 4 AA2 8 LYS B 35 LEU B 40 1 N LYS B 35 O ARG B 62
SHEET 5 AA2 8 TRP B 105 GLY B 110 1 O PHE B 108 N LEU B 40
SHEET 6 AA2 8 VAL B 128 ARG B 134 1 O THR B 132 N GLY B 109
SHEET 7 AA2 8 ALA B 261 GLY B 266 1 O VAL B 262 N LEU B 133
SHEET 8 AA2 8 LYS B 288 ILE B 292 1 O LYS B 288 N ILE B 263
CISPEP 1 GLY A 43 PRO A 44 0 1.93
CISPEP 2 THR A 75 PRO A 76 0 -4.89
CISPEP 3 GLY A 150 PRO A 151 0 1.39
CISPEP 4 GLY B 43 PRO B 44 0 2.11
CISPEP 5 THR B 75 PRO B 76 0 -4.42
CISPEP 6 GLY B 150 PRO B 151 0 0.30
SITE 1 AC1 5 CYS A 79 ARG A 192 ARG A 230 ARG B 17
SITE 2 AC1 5 ARG B 23
SITE 1 AC2 9 GLY A 43 SER A 111 ARG A 134 GLU A 203
SITE 2 AC2 9 TYR A 215 HIS A 297 SER A 298 ALA A 299
SITE 3 AC2 9 HOH A 524
SITE 1 AC3 10 GLY B 42 GLY B 43 GLY B 110 SER B 111
SITE 2 AC3 10 ARG B 134 GLU B 203 HIS B 297 HOH B 509
SITE 3 AC3 10 HOH B 540 HOH B 543
CRYST1 55.388 82.269 171.005 90.00 90.00 90.00 P 21 2 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 0.018054 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012155 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005848 0.00000
TER 2496 ALA A 319
TER 5000 ALA B 319
MASTER 474 0 3 34 16 0 8 6 5177 2 39 56
END |