HEADER HYDROLASE 19-NOV-14 4RUH
TITLE CRYSTAL STRUCTURE OF HUMAN CARNOSINASE-2 (CN2) IN COMPLEX WITH
TITLE 2 INHIBITOR, BESTATIN AT 2.25 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOSOLIC NON-SPECIFIC DIPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HUMAN CARNOSINASE-2 (CN-2);
COMPND 5 SYNONYM: CNDP DIPEPTIDASE 2, GLUTAMATE CARBOXYPEPTIDASE-LIKE PROTEIN
COMPND 6 1, PEPTIDASE A;
COMPND 7 EC: 3.4.13.18;
COMPND 8 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: CN2, CNDP DIPEPTIDASE 2 (METALLOPEPTIDASE M20 FAMILY) [ HOMO
SOURCE 6 SAPIENS (HUMAN), CNDP2, CPGL, PEPA;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET23A
KEYWDS STRUCTURAL GENOMICS, ENZYME FUNCTION INITIATIVE, CARBOXYPEPTIDASE,
KEYWDS 2 HYDROLASE, METALLOPROTEASE, PROTEASE, SUBSTRATE
KEYWDS 3 CARNOSINE(DIPEPTIDE), COFACTOR MANGANESE, CYTOSOLIC
EXPDTA X-RAY DIFFRACTION
AUTHOR V.PANDYA,A.KAUSHIK,A.K.SINGH,R.P.SINGH,S.KUMARAN
REVDAT 2 28-FEB-24 4RUH 1 REMARK LINK
REVDAT 1 25-NOV-15 4RUH 0
JRNL AUTH V.PANDYA,A.KAUSHIK,A.K.SINGH,R.P.SINGH,S.KUMARAN
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CARNOSINASE-2 (CN2) IN COMPLEX
JRNL TITL 2 WITH INHIBITOR, BESTATIN AT 2.25 A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.310
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.4
REMARK 3 NUMBER OF REFLECTIONS : 74921
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 3769
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 33.6274 - 6.7326 0.86 2575 117 0.2667 0.2724
REMARK 3 2 6.7326 - 5.3508 0.87 2589 151 0.2545 0.2337
REMARK 3 3 5.3508 - 4.6765 0.87 2604 119 0.2047 0.2547
REMARK 3 4 4.6765 - 4.2498 0.87 2581 155 0.1887 0.2296
REMARK 3 5 4.2498 - 3.9457 0.87 2578 151 0.2002 0.2014
REMARK 3 6 3.9457 - 3.7134 0.88 2593 157 0.2071 0.2715
REMARK 3 7 3.7134 - 3.5276 0.87 2630 112 0.2040 0.2372
REMARK 3 8 3.5276 - 3.3742 0.88 2630 138 0.2143 0.2887
REMARK 3 9 3.3742 - 3.2444 0.88 2588 155 0.2197 0.3150
REMARK 3 10 3.2444 - 3.1325 0.88 2654 124 0.2148 0.3035
REMARK 3 11 3.1325 - 3.0347 0.89 2603 165 0.2088 0.2799
REMARK 3 12 3.0347 - 2.9480 0.88 2640 130 0.2150 0.2663
REMARK 3 13 2.9480 - 2.8704 0.88 2642 139 0.2263 0.3312
REMARK 3 14 2.8704 - 2.8004 0.88 2626 142 0.2256 0.3222
REMARK 3 15 2.8004 - 2.7368 0.89 2661 142 0.2199 0.3019
REMARK 3 16 2.7368 - 2.6786 0.89 2670 136 0.2289 0.3164
REMARK 3 17 2.6786 - 2.6250 0.89 2667 132 0.2563 0.2642
REMARK 3 18 2.6250 - 2.5755 0.89 2618 140 0.2187 0.3396
REMARK 3 19 2.5755 - 2.5295 0.89 2676 156 0.2100 0.2901
REMARK 3 20 2.5295 - 2.4866 0.90 2649 141 0.2129 0.2934
REMARK 3 21 2.4866 - 2.4465 0.90 2678 134 0.2076 0.3209
REMARK 3 22 2.4465 - 2.4089 0.89 2676 122 0.2294 0.3341
REMARK 3 23 2.4089 - 2.3735 0.90 2692 142 0.2345 0.3313
REMARK 3 24 2.3735 - 2.3401 0.90 2645 160 0.2322 0.3474
REMARK 3 25 2.3401 - 2.3085 0.90 2702 125 0.2292 0.3240
REMARK 3 26 2.3085 - 2.2785 0.90 2708 136 0.2295 0.3222
REMARK 3 27 2.2785 - 2.2500 0.89 2577 148 0.2072 0.2970
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.73
REMARK 3 K_SOL : 0.42
REMARK 3 B_SOL : 46.58
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.06410
REMARK 3 B22 (A**2) : 10.20990
REMARK 3 B33 (A**2) : -4.14580
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 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 7250
REMARK 3 ANGLE : 1.163 9835
REMARK 3 CHIRALITY : 0.072 1074
REMARK 3 PLANARITY : 0.005 1256
REMARK 3 DIHEDRAL : 14.789 2631
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 4RUH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000087810.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97755
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 33.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 23.0
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.19200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M HEPES. 25% PPEG 4000, 100MM NACL,
REMARK 280 PH 8.0, LIQUID DIFFUSION, TEMPERATURE 293K
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 43.54500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.91500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.03500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.91500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.54500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.03500
REMARK 290 SMTRY3 4 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 300 REMARK: HOMODIMER
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: 10070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 265
REMARK 465 VAL A 266
REMARK 465 ALA A 267
REMARK 465 ALA A 268
REMARK 465 VAL A 269
REMARK 465 THR A 270
REMARK 465 GLU A 271
REMARK 465 GLU A 272
REMARK 465 GLU A 273
REMARK 465 HIS A 274
REMARK 465 LYS A 275
REMARK 465 LEU A 276
REMARK 465 TYR A 277
REMARK 465 ASP A 278
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 LYS B 202
REMARK 465 ASN B 263
REMARK 465 GLU B 264
REMARK 465 ALA B 265
REMARK 465 VAL B 266
REMARK 465 ALA B 267
REMARK 465 ALA B 268
REMARK 465 VAL B 269
REMARK 465 THR B 270
REMARK 465 GLU B 271
REMARK 465 GLU B 272
REMARK 465 GLU B 273
REMARK 465 HIS B 274
REMARK 465 LYS B 275
REMARK 465 LEU B 276
REMARK 465 TYR B 277
REMARK 465 ASP B 278
REMARK 465 ASP B 279
REMARK 465 ASN B 347
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 LYS A 9 CG CD CE NZ
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 LYS A 20 CG CD CE NZ
REMARK 470 GLU A 40 CG CD OE1 OE2
REMARK 470 ARG A 43 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 46 CG CD OE1 OE2
REMARK 470 LYS A 68 CG CD CE NZ
REMARK 470 PRO A 70 CG CD
REMARK 470 GLU A 153 CG CD OE1 OE2
REMARK 470 ASP A 174 CG OD1 OD2
REMARK 470 LYS A 201 CG CD CE NZ
REMARK 470 LYS A 253 CG CD CE NZ
REMARK 470 ARG A 254 CG CD NE CZ NH1 NH2
REMARK 470 TRP A 309 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 309 CZ3 CH2
REMARK 470 ASN A 347 CG OD1 ND2
REMARK 470 GLU A 351 CG CD OE1 OE2
REMARK 470 GLU A 408 CG CD OE1 OE2
REMARK 470 LYS A 474 CG CD CE NZ
REMARK 470 GLU B 13 CG CD OE1 OE2
REMARK 470 ARG B 17 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 20 CG CD CE NZ
REMARK 470 LEU B 69 CG CD1 CD2
REMARK 470 GLU B 74 CG CD OE1 OE2
REMARK 470 GLU B 114 CG CD OE1 OE2
REMARK 470 LYS B 186 CG CD CE NZ
REMARK 470 ARG B 254 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 289 CG CD CE NZ
REMARK 470 ARG B 310 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 408 CG CD OE1 OE2
REMARK 470 LYS B 474 CG CD CE NZ
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 71 33.74 -83.30
REMARK 500 SER A 87 55.44 -140.81
REMARK 500 ASP A 133 19.13 -141.52
REMARK 500 THR A 183 -85.18 -113.07
REMARK 500 ASP A 195 52.25 -151.90
REMARK 500 ASN A 196 -169.90 -161.51
REMARK 500 LYS A 202 -71.81 -88.73
REMARK 500 ILE A 262 72.20 -42.84
REMARK 500 ASN A 263 92.26 -162.80
REMARK 500 ASN A 347 -57.03 113.16
REMARK 500 SER B 30 58.33 -91.79
REMARK 500 GLU B 108 3.58 -66.60
REMARK 500 THR B 183 -95.48 -123.99
REMARK 500 ASP B 195 52.72 -166.78
REMARK 500 HIS B 380 163.94 178.99
REMARK 500 HIS B 445 -3.68 79.63
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 502 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 99 NE2
REMARK 620 2 ASP A 132 OD2 92.7
REMARK 620 3 ASP A 195 OD1 93.2 103.3
REMARK 620 4 ASP A 195 OD2 83.2 160.8 58.5
REMARK 620 5 BES A 501 O2 95.5 106.3 148.7 92.8
REMARK 620 6 BES A 501 N2 152.7 114.3 84.7 72.5 73.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 503 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 132 OD1
REMARK 620 2 GLU A 167 OE2 96.1
REMARK 620 3 GLU A 167 OE1 151.0 58.7
REMARK 620 4 HIS A 445 NE2 101.2 120.6 82.6
REMARK 620 5 BES A 501 O3 116.8 143.1 91.7 71.0
REMARK 620 6 BES A 501 O2 95.7 87.5 97.0 144.8 73.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 502 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 99 NE2
REMARK 620 2 ASP B 132 OD2 83.8
REMARK 620 3 ASP B 195 OD1 110.3 86.9
REMARK 620 4 ASP B 195 OD2 89.6 142.5 60.9
REMARK 620 5 BES B 501 O2 92.5 102.2 156.4 115.0
REMARK 620 6 BES B 501 N2 166.3 104.9 81.1 89.5 75.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 503 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 132 OD1
REMARK 620 2 GLU B 167 OE2 79.4
REMARK 620 3 GLU B 167 OE1 137.8 58.5
REMARK 620 4 HIS B 445 NE2 76.5 105.1 110.8
REMARK 620 5 BES B 501 O2 99.6 95.3 86.9 158.0
REMARK 620 6 BES B 501 O3 134.4 146.2 87.7 85.3 82.3
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 BES A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BES B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 505
DBREF 4RUH A 1 475 UNP Q96KP4 CNDP2_HUMAN 1 475
DBREF 4RUH B 1 475 UNP Q96KP4 CNDP2_HUMAN 1 475
SEQRES 1 A 475 MET ALA ALA LEU THR THR LEU PHE LYS TYR ILE ASP GLU
SEQRES 2 A 475 ASN GLN ASP ARG TYR ILE LYS LYS LEU ALA LYS TRP VAL
SEQRES 3 A 475 ALA ILE GLN SER VAL SER ALA TRP PRO GLU LYS ARG GLY
SEQRES 4 A 475 GLU ILE ARG ARG MET MET GLU VAL ALA ALA ALA ASP VAL
SEQRES 5 A 475 LYS GLN LEU GLY GLY SER VAL GLU LEU VAL ASP ILE GLY
SEQRES 6 A 475 LYS GLN LYS LEU PRO ASP GLY SER GLU ILE PRO LEU PRO
SEQRES 7 A 475 PRO ILE LEU LEU GLY ARG LEU GLY SER ASP PRO GLN LYS
SEQRES 8 A 475 LYS THR VAL CYS ILE TYR GLY HIS LEU ASP VAL GLN PRO
SEQRES 9 A 475 ALA ALA LEU GLU ASP GLY TRP ASP SER GLU PRO PHE THR
SEQRES 10 A 475 LEU VAL GLU ARG ASP GLY LYS LEU TYR GLY ARG GLY SER
SEQRES 11 A 475 THR ASP ASP LYS GLY PRO VAL ALA GLY TRP ILE ASN ALA
SEQRES 12 A 475 LEU GLU ALA TYR GLN LYS THR GLY GLN GLU ILE PRO VAL
SEQRES 13 A 475 ASN VAL ARG PHE CYS LEU GLU GLY MET GLU GLU SER GLY
SEQRES 14 A 475 SER GLU GLY LEU ASP GLU LEU ILE PHE ALA ARG LYS ASP
SEQRES 15 A 475 THR PHE PHE LYS ASP VAL ASP TYR VAL CYS ILE SER ASP
SEQRES 16 A 475 ASN TYR TRP LEU GLY LYS LYS LYS PRO CYS ILE THR TYR
SEQRES 17 A 475 GLY LEU ARG GLY ILE CYS TYR PHE PHE ILE GLU VAL GLU
SEQRES 18 A 475 CYS SER ASN LYS ASP LEU HIS SER GLY VAL TYR GLY GLY
SEQRES 19 A 475 SER VAL HIS GLU ALA MET THR ASP LEU ILE LEU LEU MET
SEQRES 20 A 475 GLY SER LEU VAL ASP LYS ARG GLY ASN ILE LEU ILE PRO
SEQRES 21 A 475 GLY ILE ASN GLU ALA VAL ALA ALA VAL THR GLU GLU GLU
SEQRES 22 A 475 HIS LYS LEU TYR ASP ASP ILE ASP PHE ASP ILE GLU GLU
SEQRES 23 A 475 PHE ALA LYS ASP VAL GLY ALA GLN ILE LEU LEU HIS SER
SEQRES 24 A 475 HIS LYS LYS ASP ILE LEU MET HIS ARG TRP ARG TYR PRO
SEQRES 25 A 475 SER LEU SER LEU HIS GLY ILE GLU GLY ALA PHE SER GLY
SEQRES 26 A 475 SER GLY ALA LYS THR VAL ILE PRO ARG LYS VAL VAL GLY
SEQRES 27 A 475 LYS PHE SER ILE ARG LEU VAL PRO ASN MET THR PRO GLU
SEQRES 28 A 475 VAL VAL GLY GLU GLN VAL THR SER TYR LEU THR LYS LYS
SEQRES 29 A 475 PHE ALA GLU LEU ARG SER PRO ASN GLU PHE LYS VAL TYR
SEQRES 30 A 475 MET GLY HIS GLY GLY LYS PRO TRP VAL SER ASP PHE SER
SEQRES 31 A 475 HIS PRO HIS TYR LEU ALA GLY ARG ARG ALA MET LYS THR
SEQRES 32 A 475 VAL PHE GLY VAL GLU PRO ASP LEU THR ARG GLU GLY GLY
SEQRES 33 A 475 SER ILE PRO VAL THR LEU THR PHE GLN GLU ALA THR GLY
SEQRES 34 A 475 LYS ASN VAL MET LEU LEU PRO VAL GLY SER ALA ASP ASP
SEQRES 35 A 475 GLY ALA HIS SER GLN ASN GLU LYS LEU ASN ARG TYR ASN
SEQRES 36 A 475 TYR ILE GLU GLY THR LYS MET LEU ALA ALA TYR LEU TYR
SEQRES 37 A 475 GLU VAL SER GLN LEU LYS ASP
SEQRES 1 B 475 MET ALA ALA LEU THR THR LEU PHE LYS TYR ILE ASP GLU
SEQRES 2 B 475 ASN GLN ASP ARG TYR ILE LYS LYS LEU ALA LYS TRP VAL
SEQRES 3 B 475 ALA ILE GLN SER VAL SER ALA TRP PRO GLU LYS ARG GLY
SEQRES 4 B 475 GLU ILE ARG ARG MET MET GLU VAL ALA ALA ALA ASP VAL
SEQRES 5 B 475 LYS GLN LEU GLY GLY SER VAL GLU LEU VAL ASP ILE GLY
SEQRES 6 B 475 LYS GLN LYS LEU PRO ASP GLY SER GLU ILE PRO LEU PRO
SEQRES 7 B 475 PRO ILE LEU LEU GLY ARG LEU GLY SER ASP PRO GLN LYS
SEQRES 8 B 475 LYS THR VAL CYS ILE TYR GLY HIS LEU ASP VAL GLN PRO
SEQRES 9 B 475 ALA ALA LEU GLU ASP GLY TRP ASP SER GLU PRO PHE THR
SEQRES 10 B 475 LEU VAL GLU ARG ASP GLY LYS LEU TYR GLY ARG GLY SER
SEQRES 11 B 475 THR ASP ASP LYS GLY PRO VAL ALA GLY TRP ILE ASN ALA
SEQRES 12 B 475 LEU GLU ALA TYR GLN LYS THR GLY GLN GLU ILE PRO VAL
SEQRES 13 B 475 ASN VAL ARG PHE CYS LEU GLU GLY MET GLU GLU SER GLY
SEQRES 14 B 475 SER GLU GLY LEU ASP GLU LEU ILE PHE ALA ARG LYS ASP
SEQRES 15 B 475 THR PHE PHE LYS ASP VAL ASP TYR VAL CYS ILE SER ASP
SEQRES 16 B 475 ASN TYR TRP LEU GLY LYS LYS LYS PRO CYS ILE THR TYR
SEQRES 17 B 475 GLY LEU ARG GLY ILE CYS TYR PHE PHE ILE GLU VAL GLU
SEQRES 18 B 475 CYS SER ASN LYS ASP LEU HIS SER GLY VAL TYR GLY GLY
SEQRES 19 B 475 SER VAL HIS GLU ALA MET THR ASP LEU ILE LEU LEU MET
SEQRES 20 B 475 GLY SER LEU VAL ASP LYS ARG GLY ASN ILE LEU ILE PRO
SEQRES 21 B 475 GLY ILE ASN GLU ALA VAL ALA ALA VAL THR GLU GLU GLU
SEQRES 22 B 475 HIS LYS LEU TYR ASP ASP ILE ASP PHE ASP ILE GLU GLU
SEQRES 23 B 475 PHE ALA LYS ASP VAL GLY ALA GLN ILE LEU LEU HIS SER
SEQRES 24 B 475 HIS LYS LYS ASP ILE LEU MET HIS ARG TRP ARG TYR PRO
SEQRES 25 B 475 SER LEU SER LEU HIS GLY ILE GLU GLY ALA PHE SER GLY
SEQRES 26 B 475 SER GLY ALA LYS THR VAL ILE PRO ARG LYS VAL VAL GLY
SEQRES 27 B 475 LYS PHE SER ILE ARG LEU VAL PRO ASN MET THR PRO GLU
SEQRES 28 B 475 VAL VAL GLY GLU GLN VAL THR SER TYR LEU THR LYS LYS
SEQRES 29 B 475 PHE ALA GLU LEU ARG SER PRO ASN GLU PHE LYS VAL TYR
SEQRES 30 B 475 MET GLY HIS GLY GLY LYS PRO TRP VAL SER ASP PHE SER
SEQRES 31 B 475 HIS PRO HIS TYR LEU ALA GLY ARG ARG ALA MET LYS THR
SEQRES 32 B 475 VAL PHE GLY VAL GLU PRO ASP LEU THR ARG GLU GLY GLY
SEQRES 33 B 475 SER ILE PRO VAL THR LEU THR PHE GLN GLU ALA THR GLY
SEQRES 34 B 475 LYS ASN VAL MET LEU LEU PRO VAL GLY SER ALA ASP ASP
SEQRES 35 B 475 GLY ALA HIS SER GLN ASN GLU LYS LEU ASN ARG TYR ASN
SEQRES 36 B 475 TYR ILE GLU GLY THR LYS MET LEU ALA ALA TYR LEU TYR
SEQRES 37 B 475 GLU VAL SER GLN LEU LYS ASP
HET BES A 501 22
HET MN A 502 1
HET MN A 503 1
HET BES B 501 22
HET MN B 502 1
HET MN B 503 1
HET GOL B 504 6
HET GOL B 505 6
HETNAM BES 2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-
HETNAM 2 BES PENTANOIC ACID
HETNAM MN MANGANESE (II) ION
HETNAM GOL GLYCEROL
HETSYN BES BESTATIN
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 BES 2(C16 H24 N2 O4)
FORMUL 4 MN 4(MN 2+)
FORMUL 9 GOL 2(C3 H8 O3)
FORMUL 11 HOH *228(H2 O)
HELIX 1 1 LEU A 4 ASN A 14 1 11
HELIX 2 2 ASN A 14 ILE A 28 1 15
HELIX 3 3 TRP A 34 GLU A 36 5 3
HELIX 4 4 LYS A 37 LEU A 55 1 19
HELIX 5 5 ALA A 106 GLY A 110 5 5
HELIX 6 6 ASP A 133 THR A 150 1 18
HELIX 7 7 MET A 165 GLY A 169 5 5
HELIX 8 8 GLY A 172 LYS A 181 1 10
HELIX 9 9 SER A 229 GLY A 233 1 5
HELIX 10 10 GLU A 238 GLY A 248 1 11
HELIX 11 11 ASP A 283 ASP A 290 1 8
HELIX 12 12 HIS A 300 ARG A 310 1 11
HELIX 13 13 THR A 349 ARG A 369 1 21
HELIX 14 14 HIS A 391 GLY A 406 1 16
HELIX 15 15 PRO A 419 GLY A 429 1 11
HELIX 16 16 ARG A 453 GLN A 472 1 20
HELIX 17 17 THR B 5 ASN B 14 1 10
HELIX 18 18 ASN B 14 ILE B 28 1 15
HELIX 19 19 TRP B 34 GLU B 36 5 3
HELIX 20 20 LYS B 37 LEU B 55 1 19
HELIX 21 21 ALA B 106 GLY B 110 5 5
HELIX 22 22 ASP B 133 THR B 150 1 18
HELIX 23 23 MET B 165 GLY B 169 5 5
HELIX 24 24 GLY B 172 ARG B 180 1 9
HELIX 25 25 SER B 229 GLY B 233 1 5
HELIX 26 26 GLU B 238 SER B 249 1 12
HELIX 27 27 ASP B 283 ASP B 290 1 8
HELIX 28 28 HIS B 300 ARG B 310 1 11
HELIX 29 29 THR B 349 LEU B 368 1 20
HELIX 30 30 HIS B 391 GLY B 406 1 16
HELIX 31 31 PRO B 419 GLY B 429 1 11
HELIX 32 32 ARG B 453 LEU B 473 1 21
SHEET 1 A 6 SER A 58 VAL A 62 0
SHEET 2 A 6 ILE A 80 LEU A 85 -1 O ARG A 84 N SER A 58
SHEET 3 A 6 ASN A 157 GLU A 163 -1 O VAL A 158 N LEU A 85
SHEET 4 A 6 THR A 93 HIS A 99 1 N VAL A 94 O ASN A 157
SHEET 5 A 6 TYR A 190 ILE A 193 1 O TYR A 190 N CYS A 95
SHEET 6 A 6 ASN A 431 LEU A 434 1 O ASN A 431 N VAL A 191
SHEET 1 B 2 LYS A 66 LYS A 68 0
SHEET 2 B 2 GLU A 74 PRO A 76 -1 O ILE A 75 N GLN A 67
SHEET 1 C 3 VAL A 119 ARG A 121 0
SHEET 2 C 3 LYS A 124 TYR A 126 -1 O TYR A 126 N VAL A 119
SHEET 3 C 3 LYS A 450 ASN A 452 -1 O LEU A 451 N LEU A 125
SHEET 1 D 3 TRP A 385 VAL A 386 0
SHEET 2 D 3 CYS A 205 LEU A 210 -1 N LEU A 210 O TRP A 385
SHEET 3 D 3 ASP A 410 GLU A 414 1 O ASP A 410 N ILE A 206
SHEET 1 E 4 SER A 313 GLU A 320 0
SHEET 2 E 4 LYS A 335 LEU A 344 -1 O LYS A 339 N HIS A 317
SHEET 3 E 4 GLY A 212 GLU A 221 -1 N GLY A 212 O LEU A 344
SHEET 4 E 4 GLU A 373 GLY A 382 -1 O LYS A 375 N GLU A 219
SHEET 1 F 2 LEU A 227 HIS A 228 0
SHEET 2 F 2 VAL A 331 ILE A 332 -1 O ILE A 332 N LEU A 227
SHEET 1 G 6 SER B 58 VAL B 62 0
SHEET 2 G 6 ILE B 80 LEU B 85 -1 O LEU B 82 N GLU B 60
SHEET 3 G 6 ASN B 157 GLU B 163 -1 O LEU B 162 N LEU B 81
SHEET 4 G 6 THR B 93 HIS B 99 1 N VAL B 94 O ARG B 159
SHEET 5 G 6 TYR B 190 ILE B 193 1 O TYR B 190 N CYS B 95
SHEET 6 G 6 ASN B 431 LEU B 434 1 O ASN B 431 N VAL B 191
SHEET 1 H 2 LYS B 66 LYS B 68 0
SHEET 2 H 2 GLU B 74 PRO B 76 -1 O ILE B 75 N GLN B 67
SHEET 1 I 3 VAL B 119 ARG B 121 0
SHEET 2 I 3 LYS B 124 TYR B 126 -1 O TYR B 126 N VAL B 119
SHEET 3 I 3 LYS B 450 ASN B 452 -1 O LEU B 451 N LEU B 125
SHEET 1 J 3 TRP B 385 VAL B 386 0
SHEET 2 J 3 CYS B 205 LEU B 210 -1 N LEU B 210 O TRP B 385
SHEET 3 J 3 ASP B 410 GLU B 414 1 O ASP B 410 N ILE B 206
SHEET 1 K 4 SER B 313 GLU B 320 0
SHEET 2 K 4 LYS B 335 LEU B 344 -1 O VAL B 337 N GLU B 320
SHEET 3 K 4 GLY B 212 GLU B 221 -1 N PHE B 216 O PHE B 340
SHEET 4 K 4 GLU B 373 GLY B 382 -1 O TYR B 377 N PHE B 217
SHEET 1 L 2 LEU B 227 HIS B 228 0
SHEET 2 L 2 VAL B 331 ILE B 332 -1 O ILE B 332 N LEU B 227
LINK NE2 HIS A 99 MN MN A 502 1555 1555 2.38
LINK OD2 ASP A 132 MN MN A 502 1555 1555 2.14
LINK OD1 ASP A 132 MN MN A 503 1555 1555 2.26
LINK OE2 GLU A 167 MN MN A 503 1555 1555 2.15
LINK OE1 GLU A 167 MN MN A 503 1555 1555 2.28
LINK OD1 ASP A 195 MN MN A 502 1555 1555 2.22
LINK OD2 ASP A 195 MN MN A 502 1555 1555 2.25
LINK NE2 HIS A 445 MN MN A 503 1555 1555 2.60
LINK O2 BES A 501 MN MN A 502 1555 1555 1.83
LINK N2 BES A 501 MN MN A 502 1555 1555 2.16
LINK O3 BES A 501 MN MN A 503 1555 1555 2.05
LINK O2 BES A 501 MN MN A 503 1555 1555 2.56
LINK NE2 HIS B 99 MN MN B 502 1555 1555 2.30
LINK OD2 ASP B 132 MN MN B 502 1555 1555 2.11
LINK OD1 ASP B 132 MN MN B 503 1555 1555 2.18
LINK OE2 GLU B 167 MN MN B 503 1555 1555 2.14
LINK OE1 GLU B 167 MN MN B 503 1555 1555 2.32
LINK OD1 ASP B 195 MN MN B 502 1555 1555 2.14
LINK OD2 ASP B 195 MN MN B 502 1555 1555 2.18
LINK NE2 HIS B 445 MN MN B 503 1555 1555 1.89
LINK O2 BES B 501 MN MN B 502 1555 1555 2.12
LINK N2 BES B 501 MN MN B 502 1555 1555 2.21
LINK O2 BES B 501 MN MN B 503 1555 1555 2.22
LINK O3 BES B 501 MN MN B 503 1555 1555 2.26
CISPEP 1 ASP A 132 ASP A 133 0 11.02
CISPEP 2 ASP B 132 ASP B 133 0 5.27
SITE 1 AC1 16 HIS A 99 ASP A 132 GLU A 166 GLU A 167
SITE 2 AC1 16 ASP A 195 ARG A 343 HIS A 380 GLU A 414
SITE 3 AC1 16 GLY A 416 SER A 417 HIS A 445 MN A 502
SITE 4 AC1 16 MN A 503 HIS B 228 VAL B 231 THR B 330
SITE 1 AC2 6 HIS A 99 ASP A 132 GLU A 167 ASP A 195
SITE 2 AC2 6 BES A 501 MN A 503
SITE 1 AC3 5 ASP A 132 GLU A 167 HIS A 445 BES A 501
SITE 2 AC3 5 MN A 502
SITE 1 AC4 18 HIS A 228 VAL A 231 THR A 330 HIS B 99
SITE 2 AC4 18 ASP B 132 GLU B 166 GLU B 167 ASP B 195
SITE 3 AC4 18 ASN B 196 TYR B 197 ARG B 343 GLU B 414
SITE 4 AC4 18 GLY B 416 SER B 417 ILE B 418 HIS B 445
SITE 5 AC4 18 MN B 502 MN B 503
SITE 1 AC5 6 HIS B 99 ASP B 132 GLU B 166 ASP B 195
SITE 2 AC5 6 BES B 501 MN B 503
SITE 1 AC6 5 ASP B 132 GLU B 167 HIS B 445 BES B 501
SITE 2 AC6 5 MN B 502
SITE 1 AC7 8 ASP B 226 GLY B 321 ALA B 322 PHE B 323
SITE 2 AC7 8 LYS B 329 VAL B 331 PRO B 333 HOH B 684
SITE 1 AC8 6 LYS B 181 PHE B 185 LYS B 186 VAL B 188
SITE 2 AC8 6 THR B 428 LYS B 430
CRYST1 87.090 100.070 105.830 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 0.011482 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009993 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009449 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
